HGNC approved symbol | HGNC ID | HGNC approved name | Entrez gene ID | UniProt AC (human) | UniProt ID (human) | Pfam domains | MGI symbol | MGI ID | UniProt AC (mouse) | UniProt ID (mouse) | HGNC gene family tag | HGNC gene family description | Function | Modification | PMID for information on function | Protein complex | Target molecule | Target entity | Product | PMID for information on target | Comment | Status of entry |
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
A1CF
(details) |
24086 | APOBEC1 complementation factor | 29974 | Q9NQ94 | A1CF_HUMAN | RRM_1 PF00076 58-126 138-199 233-297, DND1_DSRM PF14709 447-522 | A1cf | 1917115 | Q5YD48 | A1CF_MOUSE | RBM | RNA binding motif (RRM) containing | RNA modification | RNA deamination | 10781591 | APOB_mRNA_editosome | RNA | mRNA, mC | U | 10781591 | ASP=A1CF has three RNA-binding domains with homologies to poly(A)-binding proteins. Recombinant ASP complements recombinant APOBEC-1 to edit apoB RNA in vitro. Therefore, APOBEC-1 and ASP represent the minimal requirements for apoB mRNA editing in vitro. | # |
ACINU
(details) |
17066 | Apoptotic chromatin condensation inducer in the nucleus (Acinus) | 22985 | Q9UKV3 | ACINU_HUMAN | SAP PF02037 72-106, RSB_motif PF16294 1171-1247 | Acin1 | 1891824 | Q9JIX8 | ACINU_MOUSE | # | # | RNA modification | Alternative splicing | 22203037 | # | RNA | mRNA | # | 22203037 | Production of the proapoptotic Bcl-x(S) splice variant. | New |
ACTB
(details) |
132 | actin, beta | 60 | P60709 | ACTB_HUMAN | Actin PF00022 4-375 | Actb | 87904 | P60710 | ACTB_MOUSE | # | # | Chromatin remodeling cofactor | # | 10966108 | BAF, nBAF, npBAF, PBAF, SWI/SNF-like EPAFB, bBAF, SWI/SNF BRM-BRG1, NuA4, NuA4-related complex | chromatin | # | # | 10966108 | β-actin=ACTB and actin-related proteins appear to have weak ATPase activities, which contribute ∼1% of the total activity in the BAF remodeling complex (Zhao et al. 1998). Results of experiments using the actin monomer sequestering product latrunculin B suggest that β-actin and BAF53 are required for stimulation of the ATPase activity of the BAF complex by chromatin | # |
ACTL6A
(details) |
24124 | actin-like 6A | 86 | O96019 | ACL6A_HUMAN | Actin PF00022 10-428 | Actl6a | 1861453 | Q9Z2N8 | ACL6A_MOUSE | INO80 | INO80 complex subunits | Chromatin remodeling cofactor | # | 9845365 | BAF, npBAF, PBAF, SWI/SNF_Brg1(I), SWI/SNF_Brg1(II), SWI/SNF_Brm, SWI/SNF-like_EPAFa, WINAC, SWI/SNF-like EPAFB, SWI/SNF BRM-BRG1, Ino80, NuA4, NuA4-related complex, SRCAP | chromatin | # | # | 9845365 | β-actin and BAF53 =ACTL6A are required for maximal ATPase activity of BRG1 and are also required with BRG1 for association of the complex with chromatin/matrix. | # |
ACTL6B
(details) |
160 | actin-like 6B | 51412 | O94805 | ACL6B_HUMAN | Actin PF00022 9-425 | Actl6b | 1933548 | Q99MR0 | ACL6B_MOUSE | # | # | Chromatin remodeling cofactor | # | 11726552 | BAF, nBAF, PBAF, SWI/SNF_Brg1(I), SWI/SNF_Brg1(II), SWI/SNF_Brm, SWI/SNF BRM-BRG1 | chromatin | # | # | 11726552 | Belongs to the chromatin remodeling brain-specific BAF (bBAF) complex, as such plays a role in remodeling mononucleosomes in an ATP-dependent fashion. | # |
ACTR3B
(details) |
17256 | ARP3 actin-related protein 3 homolog B (yeast) | 57180 | Q9P1U1 | ARP3B_HUMAN | Actin PF00022 5-237 | Actr3b | 2661120 | Q641P0 | ARP3B_MOUSE | # | # | Chromatin remodeling | # | 10911987 | # | histone | H2A, H3, H4 | # | 10911987 | Act3/Arp4 can interact through the N-terminal domains of histones H3, H4, and H2A. Since Esa1 can only acetylate nucleosomal histones as part of theNuA4 complex, it has been proposed that the Act3/Arp4 subunit functions by promoting the binding of NuA4 to chromatin. | # |
ACTR5
(details) |
14671 | ARP5 actin-related protein 5 homolog (yeast) | 79913 | Q9H9F9 | ARP5_HUMAN | Actin PF00022 32-230 427-567 | Actr5 | 1924748 | Q80US4 | ARP5_MOUSE | INO80 | INO80 complex subunits | Chromatin remodeling | # | 19014934 | Ino80 | chromatin | # | # | 19014934 | hArp5 binds to chromatin as a component of the hINO80 complex in a DSB-independent manner. | # |
ACTR6
(details) |
24025 | ARP6 actin-related protein 6 homolog (yeast) | 64431 | Q9GZN1 | ARP6_HUMAN | Actin PF00022 2-394 | Actr6 | 1914269 | Q9D864 | ARP6_MOUSE | # | # | Chromatin remodeling cofactor | # | 11368909 | SRCAP | chromatin | # | # | 11368909 | The Arp6 subfamily might regulate heterochromatin formation induced by the HP1 family. | # |
ACTR8
(details) |
14672 | ARP8 actin-related protein 8 homolog (yeast) | 93973 | Q9H981 | ARP8_HUMAN | Actin PF00022 48-325 506-619 | Actr8 | 1860775 | Q8R2S9 | ARP8_MOUSE | INO80 | INO80 complex subunits | Histone modification read | # | 22977180 | Ino80 | histone | # | # | 22977180 | Arp8 and the Arp8-Arp4-actin-HSA sub-complex of INO80 strongly prefer nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting that Arp8 functions as a nucleosome recognition module. | # |
ADNP
(details) |
15766 | activity-dependent neuroprotector homeobox | 23394 | Q9H2P0 | ADNP_HUMAN | ADNP_N PF19627 3-755, Homeodomain PF00046 770-810 | Adnp | 1338758 | Q9Z103 | ADNP_MOUSE | ZFHX | Homeoboxes / ZF class | Chromatin remodeling cofactor | # | 17878164 | # | chromatin | # | # | # | Identified as a member of SWI/SNF chromatin remodeling complex. UniProt: Potential transcription factor. | # |
AEBP2
(details) |
24051 | AE binding protein 2 | 121536 | Q6ZN18 | AEBP2_HUMAN | Aebp2 | 1338038 | Q9Z248 | AEBP2_MOUSE | # | # | Histone modification write cofactor | Histone methylation | 15225548 | PRC2 | DNA | # | # | 15225548 | The HMTase activity requires a minimum of three components-EZH2, EED, and SUZ12-while AEBP2 is required for optimal enzymatic activity. Using a stable SUZ12 knockdown cell line, SUZ12 knockdown results in cell growth defects, which correlate with genome-wide alteration on H3-K27 methylation as well as upregulation of a number of Hox genes. | # | |
AICDA
(details) |
13203 | activation-induced cytidine deaminase | 57379 | Q9GZX7 | AICDA_HUMAN | APOBEC_N PF08210 9-177 | Aicda | 1342279 | Q9WVE0 | AICDA_MOUSE | APOBEC | Apolipoprotein B mRNA editing enzymes | DNA modification | DNA demethylation | 21496894 | APOB_mRNA_editosome | DNA | ssDNA, hmC | hmU | 21496894 | AICDA or AID is required for OCT4 and NANOG promoter demethylation, 5mCs are first oxidized to 5hmCs by TET proteins. 5hmCs are then deaminated by AID/APOBEC deaminases into 5hmU. Finally, 5hmU can be excised by 5hmU glycosylases and repaired by the BER pathway with unmethylated cytosines | # |
AIRE
(details) |
360 | autoimmune regulator | 326 | O43918 | AIRE_HUMAN | HSR PF03172 5-102, SAND PF01342 200-239, PHD PF00628 299-340 | Aire | 1338803 | Q9Z0E3 | AIRE_MOUSE | PHF | Zinc fingers, PHD-type | Histone modification read, TF | # | 18292755 | # | histone, DNA | H3K4, H3K4me3, DNA motif | # | 18292755 | AIRE selectively interacts with histone H3 through its first plant homeodomain (PHD) finger (AIRE–PHD1) and preferentially binds to non-methylated H3K4 (H3K4me0). Accordingly, in vivo AIRE binds to and activates promoters containing low levels of H3K4me3 in human embryonic kidney 293 cells. AIRE–PHD1 is an important member of a newly identified class of PHD fingers that specifically recognize H3K4me0, thus providing a new link between the status of histone modifications. | # |
ALKBH1
(details) |
17911 | alkB, alkylation repair homolog 1 (E. coli) | 8846 | Q13686 | ALKB1_HUMAN | 2OG-FeII_Oxy_2 PF13532 110-345 | Alkbh1 | 2384034 | P0CB42 | ALKB1_MOUSE | ALKB | Alkylation repair homologs | Histone modification | # | 22961808 | # | histone | H2A | # | # | ALKBH1 is a histone H2A dioxygenase involved in neural differentiation. | # |
ALKBH1
(details) |
17911 | Nucleic acid dioxygenase ALKBH1 (EC 1.14.11.-) (Alkylated DNA repair protein alkB homolog 1) (Alpha-ketoglutarate-dependent dioxygenase ABH1) (DNA 6mA demethylase) (DNA N6-methyl adenine demethylase ALKBH1) (EC 1.14.11.51) (DNA lyase ABH1) (EC 4.2.99.18) (DNA oxidative demethylase ALKBH1) (EC 1.14.11.33) (mRNA N(3)-methylcytidine demethylase) (EC 1.14.11.-) | 8846 | Q13686 | ALKB1_HUMAN | 2OG-FeII_Oxy_2 PF13532 110-345 | Alkbh1 | 2384034 | P0CB42 | ALKB1_MOUSE | ALKBH | Alkylation repair homologs | RNA modification, DNA modification | DNA demethylation, RNA demethylation | 18603530, 31188562, 18163532 | # | DNA, RNA | m3C, m1A of mRNA | C, A | 31188562, 30392959, 30017583 | Demethylates mRNAs containing N3-methylcytidine modification. Specifically demethylates DNA methylated on the 6th position of adenine (N6-methyladenosine) DNA. | New |
ALKBH4
(details) |
21900 | Alpha-ketoglutarate-dependent dioxygenase alkB homolog 4 (Alkylated DNA repair protein alkB homolog 4) (DNA N6-methyl adenine demethylase ALKBH4) (EC 1.14.11.51) (Lysine-specific demethylase ALKBH4) (EC 1.14.11.-) | 54784 | Q9NXW9 | ALKB4_HUMAN | Alkbh4 | 1919291 | Q9D8F1 | ALKB4_MOUSE | ALKBH | Alkylation repair homologs | DNA modification | DNA demethylation | 30982744 | # | DNA | m6A of DNA | A | 30982744 | Preserves Polycomb silencing | New | |
ALKBH5
(details) |
25996 | alkB homolog 5, RNA demethylase | 54890 | Q6P6C2 | ALKB5_HUMAN | 2OG-FeII_Oxy_2 PF13532 117-275 | Alkbh5 | 2144489 | Q3TSG4 | ALKB5_MOUSE | ALKBH | Alkylation repair homologs | RNA modification | RNA demethylation | 23177736 | # | RNA | m6A of mRNA | A | 23177736 | Regulates export and metabolism of mRNA | New |
ANKRD32
(details) |
25408 | ankyrin repeat domain 32 | 84250 | Q9BQI6 | ANR32_HUMAN | RTT107_BRCT_5 PF16770 9-90, Ank_2 PF12796 811-900 | Ankrd32 | 2145448 | Q8R3P9 | ANR32_MOUSE | ANKRD | Ankyrin repeat domain containing | Histone modification read | # | 21423274 | # | histone | H2AXS139 | # | 21423274 | Table 1 in the reference (ANKRD32=BRCT repeat) | # |
ANP32A
(details) |
13233 | acidic (leucine-rich) nuclear phosphoprotein 32 family, member A | 8125 | P39687 | AN32A_HUMAN | LRR_9 PF14580 52-146 | Anp32a | 108447 | O35381 | AN32A_MOUSE | ANP32 | ANP32 acidic nuclear phosphoproteins | Chromatin remodeling cofactor | # | 11163245 | # | chromatin | # | # | 11163245 | pp32 = ANP32A is a member of a family of leucine-rich acidic nuclear proteins ( 7 and 19). Results suggest potential roles of INHAT subunits in chromatin remodeling and transcriptional regulation; INHAT complex including pp32 inhibits the HAT activity of p300/CBP and PCAF by binding to their substrate, histones. | # |
ANP32B
(details) |
16677 | acidic (leucine-rich) nuclear phosphoprotein 32 family, member B | 10541 | Q92688 | AN32B_HUMAN | LRR_9 PF14580 21-149 | Anp32b | 1914878 | Q9EST5 | AN32B_MOUSE | ANP32 | ANP32 acidic nuclear phosphoproteins | Histone chaperone | # | 20538007 | # | histone | H3, H4 | # | 20538007 | The LRR domain of ANP32B possesses histone chaperone activity and forms a curved structure with a parallel beta-sheet on the concave side and mostly helical elements on the convex side. Analyses revealed that the interaction of ANP32B with the core histones H3-H4 occurs on its concave side | # |
ANP32E
(details) |
16673 | acidic (leucine-rich) nuclear phosphoprotein 32 family, member E | 81611 | Q9BTT0 | AN32E_HUMAN | LRR_9 PF14580 35-146 | Anp32e | 1913721 | P97822 | AN32E_MOUSE | ANP32 | ANP32 acidic nuclear phosphoproteins | Histone chaperone, Histone modification read | # | 24463511 | SWR | histone | H2A.Z | # | 24463511 | ANP32E interacts with a short region of the docking domain of H2A.Z through a new motif termed H2A.Z interacting domain (ZID). | # |
APBB1
(details) |
581 | amyloid beta (A4) precursor protein-binding, family B, member 1 (Fe65) | 322 | O00213 | APBB1_HUMAN | WW PF00397 256-283, PID PF00640 370-507 542-664 | Apbb1 | 107765 | Q9QXJ1 | APBB1_MOUSE | # | # | Histone modification | # | 21403922 | # | histone | H2AX | # | # | Chromatin acetylation, β-amyloid precursor protein and its binding partner FE65 in DNA double strand break repair. UniProt: May act by specifically recognizing and binding histone H2AX phosphorylated on 'Tyr-142' (H2AXY142ph) at double-strand breaks (DSBs), recruiting other pro-apoptosis factors such as MAPK8/JNK1. Required for histone H4 acetylation at double-strand breaks (DSBs). | # |
APEX1
(details) |
587 | APEX nuclease (multifunctional DNA repair enzyme) 1 | 328 | P27695 | APEX1_HUMAN | Exo_endo_phos PF03372 65-309 | Apex1 | 88042 | P28352 | APEX1_MOUSE | # | # | DNA modification cofactor | DNA demethylation | # | # | DNA | # | # | # | UniProt: May play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. | # |
APOBEC1
(details) |
604 | apolipoprotein B mRNA editing enzyme, catalytic polypeptide 1 | 339 | P41238 | ABEC1_HUMAN | APOBEC4_like PF18774 27-158 | Apobec1 | 103298 | P51908 | ABEC1_MOUSE | APOBEC | Apolipoprotein B mRNA editing enzymes | DNA modification, RNA modification | DNA demethylation, mRNA editing | 22001110 | APOB_mRNA_editosome | DNA, RNA | ssDNA, mRNA, mC | U | 22001110 | Fig. A2 in the reference (APOBEC1 or A1 has no known mammalian DNA substrate but it has DNA deaminase activity sufficient to induce reversion mutations when overexpressed in E. coli. In addition, A1 expressed in neurons may have a protective function against HSV (Herpers simplex virus) that involves ssDNA deamination of the viral genome). | # |
APOBEC2
(details) |
605 | apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 2 | 10930 | Q9Y235 | ABEC2_HUMAN | APOBEC2 PF18772 47-223 | Apobec2 | 1343178 | Q9WV35 | ABEC2_MOUSE | APOBEC | Apolipoprotein B mRNA editing enzymes | DNA modification, RNA modification | DNA demethylation, mRNA editing | 21496894, 22001110 | # | DNA, RNA | ssDNA, mRNA, mC | hmU | 22001110, 21496894 | Fig. A2 in the reference | # |
APOBEC3A
(details) |
17343 | apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3A | 200315 | P31941 | ABC3A_HUMAN | NAD2 PF18782 13-195 | # | # | # | # | APOBEC | Apolipoprotein B mRNA editing enzymes | DNA modification, RNA modification | DNA demethylation, mRNA editing | 22001110 | # | DNA, RNA | ssDNA, mRNA, mC | dhU | 22001110 | Fig. A2 in the reference (Targets are exogenous retroviruses ssDNA like HIV, DNA viruses or transposable elements/ endogenous retroelements e.g. LINEs, SINEs and LTR). | # |
APOBEC3B
(details) |
17352 | apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3B | 9582 | Q9UH17 | ABC3B_HUMAN | NAD2 PF18782 8-190 193-379 | Apobec3 | 1933111 | Q99J72 | ABEC3_MOUSE | APOBEC | Apolipoprotein B mRNA editing enzymes | DNA modification, RNA modification | DNA demethylation, mRNA editing | 22001110 | # | DNA, RNA | ssDNA, mRNA, mC | dhU | 22001110 | Fig. A2 in the reference (Targets are DNA viruses or transposable elements/ endogenous retroelements e.g. LINEs, SINEs and LTR). | # |
APOBEC3C
(details) |
17353 | apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3C | 27350 | Q9NRW3 | ABC3C_HUMAN | NAD2 PF18782 11-189 | # | # | # | # | APOBEC | Apolipoprotein B mRNA editing enzymes | DNA modification, RNA modification | DNA demethylation, mRNA editing | 22001110 | # | DNA, RNA | ssDNA, mRNA, mC | dhU | 22001110 | Fig. A2 in the reference (Targets are transposable elements/ endogenous retroelements e.g. LINEs, SINEs and LTR). | # |
APOBEC3D
(details) |
17354 | apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3D | 140564 | Q96AK3 | ABC3D_HUMAN | NAD2 PF18782 10-202 207-381 | # | # | # | # | APOBEC | Apolipoprotein B mRNA editing enzymes | DNA modification, RNA modification | DNA demethylation, mRNA editing | 21835787 | # | DNA, RNA | ssDNA, mRNA, mC | dhU | 22001110 | Fig. A2 in the reference (Targets are exogenous retroviruses ssDNA like HIV or transposable elements/ endogenous retroelements e.g. LINEs and SINEs). | # |
APOBEC3F
(details) |
17356 | apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3F | 200316 | Q8IUX4 | ABC3F_HUMAN | NAD2 PF18782 4-190 192-372 | # | # | # | # | APOBEC | Apolipoprotein B mRNA editing enzymes | DNA modification, RNA modification | DNA demethylation, mRNA editing | 22001110 | APOB_mRNA_editosome | DNA, RNA | ssDNA, mRNA, mC | dhU | 22001110 | Fig. A2 in the reference (Targets are exogenous retroviruses ssDNA like HIV, DNA viruses or transposable elements/ endogenous retroelements e.g. LINEs, SINEs and LTR). | # |
APOBEC3G
(details) |
17357 | apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3G | 60489 | Q9HC16 | ABC3G_HUMAN | NAD2 PF18782 8-190 200-381 | # | # | # | # | APOBEC | Apolipoprotein B mRNA editing enzymes | DNA modification, RNA modification | DNA demethylation, mRNA editing | 22001110 | APOB_mRNA_editosome | DNA, RNA | ssDNA, mRNA, mC | dhU | 22001110 | Fig. A2 in the reference (Targets are exogenous retroviruses ssDNA like HIV, DNA viruses or transposable elements/ endogenous retroelements e.g. SINEs and LTR). | # |
APOBEC3H
(details) |
24100 | apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3H | 164668 | Q6NTF7 | ABC3H_HUMAN | APOBEC3 PF18771 25-157 | # | # | # | # | APOBEC | Apolipoprotein B mRNA editing enzymes | DNA modification, RNA modification | DNA demethylation, mRNA editing | 22001110 | APOB_mRNA_editosome | DNA, RNA | ssDNA, mRNA, mC | dhU | 22001110 | Fig. A2 in the reference (Targets are exogenous retroviruses ssDNA like HIV or transposable elements/ endogenous retroelements e.g. LINEs, SINEs and LTR). | # |
ARID1A
(details) |
11110 | AT rich interactive domain 1A (SWI-like) | 8289 | O14497 | ARI1A_HUMAN | ARID PF01388 1018-1104, BAF250_C PF12031 1970-2222 | Arid1a | 1935147 | A2BH40 | ARI1A_MOUSE | ARID | # | Chromatin remodeling cofactor | # | 18448678 | BAF, nBAF, npBAF, PBAF, SWI/SNF_Brg1(I), SWI/SNF_Brg1(II), SWI/SNF_Brm, WINAC, bBAF, SWI/SNF BRM-BRG1 | DNA | DNA motif | # | 18448678 | BAF250a=ARID1A mediated chromatin remodeling plays a critical role in maintaining a particular chromatin configuration of its target genes that is essential for ES pluripotency and mesoderm formation. | # |
ARID1B
(details) |
18040 | AT rich interactive domain 1B (SWI1-like) | 57492 | Q8NFD5 | ARI1B_HUMAN | ARID PF01388 1137-1223, BAF250_C PF12031 2006-2266 | Arid1b | 1926129 | # | # | ARID | # | Histone modification write | Histone ubiquitination | 20086098 | BAF, nBAF, npBAF, PBAF, SWI/SNF-like_EPAFa, SWI/SNF-like EPAFB, SWI/SNF BRM-BRG1 | histone, DNA | H2BK120, DNA motif | # | 20086098 | The characteristic member of human SWI/SNF-A is BAF250/ARID1, of which there are two isoforms, BAF250a/ARID1a and BAF250b/ARID1b. The immunopurified BAF250b E3 ubiquitin ligase was found to target histone H2B at lysine 120 for monoubiquitination in vitro. | # |
ARID2
(details) |
18037 | AT rich interactive domain 2 (ARID, RFX-like) | 196528 | Q68CP9 | ARID2_HUMAN | ARID PF01388 17-101, RFX_DNA_binding PF02257 524-602 | Arid2 | 1924294 | # | # | ARID | # | Chromatin remodeling cofactor | # | 15640446 | PBAF | DNA | DNA motif | # | 15640446 | Extends the role of ARID-containing subunits as components of SWI/SNF-related chromatin-remodeling complexes. Analysis of ARID2 in the DNA pull-down assay (Figure 4) indicates that it binds DNA without sequence specificity, like all other known ARID-containing components of SWI/SNF-related complexes. | # |
ARID4A
(details) |
9885 | AT rich interactive domain 4A (RBP1-like) | 5926 | P29374 | ARI4A_HUMAN | RBB1NT PF08169 171-268, ARID PF01388 311-397, Tudor-knot PF11717 577-631 | Arid4a | 2444354 | # | # | ARID | # | Histone modification write cofactor | Histone acetylation | 15640446 | mSin3A | DNA | DNA motif | # | 15640446 | ARID4 subfamily DNA-binding activity is represented here by RBP1 (ARID4A). Amino acid identity within the ARID consensus is 75% between RBP1 (ARID4A) and RBP1L1 (ARID4B), the only other member of this class. Both RBP1 and RBP1L1/SAP180 have been found in association with the mSIN3-histone deacetylase complex. | # |
ARID4B
(details) |
15550 | AT rich interactive domain 4B (RBP1-like) | 51742 | Q4LE39 | ARI4B_HUMAN | RBB1NT PF08169 169-263, ARID PF01388 308-394, Tudor-knot PF11717 572-626 | Arid4b | 2137512 | A2CG63 | ARI4B_MOUSE | ARID | # | Histone modification write cofactor | Histone acetylation | 15640446 | mSin3A | DNA | DNA motif | # | 15640446 | ARID4 subfamily DNA-binding activity is represented here by RBP1 (ARID4A). Amino acid identity within the ARID consensus is 75% between RBP1 (ARID4A) and RBP1L1 (ARID4B), the only other member of this class. Both RBP1 and RBP1L1/SAP180 have been found in association with the mSIN3-histone deacetylase complex. | # |
ARNTL
(details) |
701 | aryl hydrocarbon receptor nuclear translocator-like | 406 | O00327 | BMAL1_HUMAN | HLH PF00010 74-126, PAS PF00989 149-254, PAS_11 PF14598 339-442 | Arntl | 1096381 | Q9WTL8 | BMAL1_MOUSE | bHLH | Basic helix-loop-helix proteins | Histone modification write cofactor, TF | TF activator | 14645221, 24395244 | # | histone | # | # | 14645221, 24395244 | The coincidence of a rhythm in histone H3 and histone H4 acetylation on the proximal E-box of hPer1 with transcriptional activation of per1 and per2 is consistent with the heterodimeric complexes of CLOCK, NPAS2 and BMAL1 = ARNTL recruiting a histone acetyltransferase (HAT)-containing transcriptional co-activation complex to achieve maximal target gene activation; CLOCK:BMAL1 functions like pioneer transcription factors and regulates the DNA accessibility of other transcription factors. | # |
ARRB1
(details) |
711 | arrestin, beta 1 | 408 | P49407 | ARRB1_HUMAN | Arrestin_N PF00339 19-173, Arrestin_C PF02752 193-355 | Arrb1 | 99473 | Q8BWG8 | ARRB1_MOUSE | # | # | Histone modification | # | 17618287, 16325578 | # | histone | # | # | # | Recruits acetylase p300. Regulates histone acetylation and gene transcription. UniProt: Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. | # |
ASF1A
(details) |
20995 | anti-silencing function 1A histone chaperone | 25842 | Q9Y294 | ASF1A_HUMAN | ASF1_hist_chap PF04729 1-154 | Asf1a | 1913653 | Q9CQE6 | ASF1A_MOUSE | # | # | Histone chaperone | # | 10759893 | # | histone | H3, H4 | # | 10759893 | CIA=ASF1A binds to histones H3/H4 in vitro, and the interacting region of histone H3 is located in the C-terminal helices. Human CIA, whose yeast homologue ASF1 is an anti-silencing factor, possesses histone chaperone activity | # |
ASF1B
(details) |
20996 | anti-silencing function 1B histone chaperone | 55723 | Q9NVP2 | ASF1B_HUMAN | ASF1_hist_chap PF04729 1-154 | Asf1b | 1914179 | Q9DAP7 | ASF1B_MOUSE | # | # | Histone chaperone | # | 12842904 | # | histone | H3, H4 | # | 12842904 | hCIA-II=ASF1B interacts with histone H3 in vivo and with histones H3/H4 in vitro and that it facilitates supercoiling of circular DNA when it is incubated with core histones and topoisomerase I in vitro. These data suggest that CIA-II is a histone chaperone and is implicated in the regulation of mammalian spermatogenesis. | # |
ASH1L
(details) |
19088 | ash1 (absent, small, or homeotic)-like (Drosophila) | 55870 | Q9NR48 | ASH1L_HUMAN | AWS PF17907 2105-2142, SET PF00856 2156-2261, Bromodomain PF00439 2462-2533, PHD_5 PF20826 2586-2628, BAH PF01426 2662-2798 | Ash1l | 2183158 | Q99MY8 | ASH1L_MOUSE | KMT, PHF | Chromatin-modifying enzymes / K-methyltransferases, Zinc fingers, PHD-type | Histone modification write | Histone methylation | 21239497 | # | histone | H3K36 | H3K36me | 21239497 | Human ASH1L specifically methylates histone H3 Lys-36. Implicates that there may be a regulatory mechanism of ASH1L histone methyltransferases. | # |
ASH2L
(details) |
744 | ash2 (absent, small, or homeotic)-like (Drosophila) | 9070 | Q9UBL3 | ASH2L_HUMAN | PHD_ash2p_like PF21257 105-159, ASH2L-like_WH PF21198 161-266, SPRY PF00622 421-494 | Ash2l | 1344416 | Q91X20 | ASH2L_MOUSE | PHF | Zinc fingers, PHD-type | Histone modification write cofactor | Histone methylation | 21285357 | COMPASS, Menin-associated_HMT, MLL-HCF, CHD8, MLL2/3, COMPASS-like MLL1,2, MLL4/WBP7, COMPASS-like MLL3,4 | histone | # | # | 21285357 | The oncoprotein Ash2L is a component of the mixed lineage leukemia (MLL) family members 1–4, Setd1A, and Setd1B mammalian histone H3K4 methyltransferase complexes and is essential to maintain global trimethylation of histone H3K4. | # |
ASXL1
(details) |
18318 | additional sex combs like transcriptional regulator 1 | 171023 | Q8IXJ9 | ASXL1_HUMAN | HARE-HTH PF05066 11-82, ASXH PF13919 244-363, PHD_3 PF13922 1502-1539 | Asxl1 | 2684063 | P59598 | ASXL1_MOUSE | # | # | Histone modification erase, Polycomb group (PcG) protein | Histone deubiquitination | 20436459 | PR-DUB | histone | H2AK119 | H2AK119ub1 | 20436459 | Reconstituted recombinant Drosophila and human PR-DUB=ASXL1 complexes remove monoubiquitin from H2A but not from H2B in nucleosomes. | # |
ASXL2
(details) |
23805 | additional sex combs like transcriptional regulator 2 | 55252 | Q76L83 | ASXL2_HUMAN | HARE-HTH PF05066 11-84, ASXH PF13919 266-381, PHD_3 PF13922 1376-1433 | Asxl2 | 1922552 | Q8BZ32 | ASXL2_MOUSE | # | # | Histone modification read | # | 21047783 | # | histone | H3K4, H3K9 | # | 21047783 | ASXL2 occupies the aP2 promoter together with histone-lysine N-methyltransferase MLL1 and Lys-9-acetylated and Lys-4-methylated H3 histones. Microarray analysis demonstrated that ASXL1 represses, whereas ASXL2 increases, the expression of adipogenic genes. | # |
ASXL3
(details) |
29357 | additional sex combs like transcriptional regulator 3 | 80816 | Q9C0F0 | ASXL3_HUMAN | HARE-HTH PF05066 11-82, ASXH PF13919 241-361, PHD_3 PF13922 2204-2246 | Asxl3 | 2685175 | Q8C4A5 | ASXL3_MOUSE | # | # | Scaffold protein, Polycomb group (PcG) protein | # | 23736028 | # | histone | # | # | 23736028 | ASXL family members are epigenetic scaffolding proteins that assemble epigenetic regulators and transcription factors to specific genomic loci with histone modifications, contain PHD domain. | # |
ATAD2
(details) |
30123 | ATPase family, AAA domain containing 2 | 29028 | Q6PL18 | ATAD2_HUMAN | AAA PF00004 462-597, AAA_lid_3 PF17862 624-660, Bromodomain PF00439 1002-1066 | Atad2 | 1917722 | Q8CDM1 | ATAD2_MOUSE | AATP | ATPases / AAA-type | Chromatin remodeling | # | 17998543 | # | chromatin | # | # | 17998543 | Although ANCCA=ATAD2 may not be critical for ERα recruitment to its target genes, it plays an important role in the recruitment or assembly of ERα–CBP complex at the chromatin and hence the histone modifications mediated by the complex. | # |
ATAD2B
(details) |
29230 | ATPase family, AAA domain containing 2B | 54454 | Q9ULI0 | ATD2B_HUMAN | AAA PF00004 437-571, AAA_lid_3 PF17862 598-633, Bromodomain PF00439 975-1041 | Atad2b | 2444798 | # | # | AATP | ATPases / AAA-type | Histone modification read | # | 15308210 | # | histone | H1.4, H2A, H2B, H3 and H4 | # | 15308210 | Binds acetylated lysine residues in histone H1.4, H2A, H2B, H3 and H4 (in vitro). | # |
ATF2
(details) |
784 | activating transcription factor 2 | 1386 | P15336 | ATF2_HUMAN | bZIP_1 PF00170 354-411 | Atf2 | 109349 | P16951 | ATF2_MOUSE | bZIP | Basic leucine zipper proteins | Histone modification write, TF | Histone acetylation, TF activator | 10821277 | # | histone, DNA | H2B, H4, DNA motif | # | 10821277 | ATF-2 is a histone acetyltransferase (HAT), which specifically acetylates histones H2B and H4 in vitro, exhibits histone acetyltransferase (HAT) activity. | # |
ATF7IP
(details) |
20092 | activating transcription factor 7 interacting protein | 55729 | Q6VMQ6 | MCAF1_HUMAN | ATF7IP_BD PF16788 570-783, fn3_4 PF16794 1160-1259 | Atf7ip | 1858965 | Q7TT18 | MCAF1_MOUSE | # | # | Histone modification write cofactor | Histone methylation | 14536086 | # | histone | # | # | 14536086 | Promoter H3-K9 trimethylation is the cause of transcriptional repression and that mAM/hAM facilitates conversion of H3-K9 dimethyl to trimethyl by ESET/SETDB1. | # |
ATM
(details) |
795 | ATM serine/threonine kinase | 472 | Q13315 | ATM_HUMAN | TAN PF11640 2-128, FAT PF02259 2089-2487, PI3_PI4_kinase PF00454 2713-2963, FATC PF02260 3026-3056 | Atm | 107202 | Q62388 | ATM_MOUSE | # | # | Histone modification write | Histone phosphorylation | 19261749 | # | histone | H2AXS139 | # | 19261749 | Damage-induced ATM/ATR phosphorylation on S139 of histone H2AX directly recruits MDC1 through MDC1’s BRCT domains. MDC1 itself is a substrate of ATM/ATR. | # |
ATN1
(details) |
3033 | atrophin 1 | 1822 | P54259 | ATN1_HUMAN | Atrophin-1 PF03154 1-271 407-1190 | Atn1 | 104725 | O35126 | ATN1_MOUSE | # | # | Histone modification erase cofactor | # | 10973986 | # | histone | # | # | 10973986 | When cotransfected into Neuro-2a cells, atrophin-1 and ETO/MTG8 colocalize. | # |
ATR
(details) |
882 | ATR serine/threonine kinase | 545 | Q13535 | ATR_HUMAN | UME PF08064 1125-1221, FAT PF02259 1770-2090, PI3_PI4_kinase PF00454 2322-2567, FATC PF02260 2613-2644 | Atr | 108028 | Q9JKK8 | ATR_MOUSE | # | # | Histone modification write | Histone phosphorylation | 11673449 | # | histone | H2AX | # | 11673449 | While H2AX phosphorylation requires ATR, this phosphorylation event is independent of Hus1. Thus, the phosphorylated H2AX may function upstream of Hus1 in the transduction of DNA damage. | # |
ATRX
(details) |
886 | alpha thalassemia/mental retardation syndrome X-linked | 546 | P46100 | ATRX_HUMAN | ADD_ATRX PF17981 162-213, SNF2-rel_dom PF00176 1563-1888, Helicase_C PF00271 2022-2155 | Atrx | 103067 | Q61687 | ATRX_MOUSE | # | # | Chromatin remodeling | # | 9499421 | # | histone | H3K9me2, H3K9me3, H3K4 | # | 9499421, 21666677 | The characteristics of the helicase domains make the XNP protein a new member of the SNF2/SWI DNA helicase family. XNP could regulate gene expression by direct interaction with heterochromatin-associated proteins.A yeast two-hybrid analysis using XNP and several human heterochromatin-associated proteins showed a specific interaction between the XNP and the EZH2 proteins. | # |
ATXN7
(details) |
10560 | ataxin 7 | 6314 | O15265 | ATX7_HUMAN | SCA7 PF08313 332-395 | Atxn7 | 2179277 | Q8R4I1 | ATX7_MOUSE | ATXN | Ataxins | Histone modification write cofactor | Histone acetylation | 16494529 | SAGA | histone | # | # | 16494529 | Ataxin-7 (ATXN7) is a subunit of the GCN5 histone acetyltransferase–containing coactivator complexes TFTC/STAGA. TFTC/STAGA complexes purified from SCA7 mice have normal TRRAP, GCN5, TAF12, and SPT3 levels and that their histone or nucleosomal acetylation activities are unaffected. | # |
ATXN7L3
(details) |
25416 | ataxin 7-like 3 | 56970 | Q14CW9 | AT7L3_HUMAN | Sgf11 PF08209 81-112, SCA7 PF08313 207-237 | Atxn7l3 | 3036270 | A2AWT3 | AT7L3_MOUSE | # | # | Histone modification erase cofactor | Histone deubiquitination | 18206972 | SAGA | histone | # | # | 18206972 | ATXN7L3, USP22, and ENY2 are the human orthologs of yeast Sgf11, Ubp8, and Sus1, respectively, and they are integral components of TFTC/STAGA complex. These three proteins together form a module of the TFTC/STAGA complex, which specifically removes the ubiquitin moiety from monoubiquitinated histones H2A and H2B. | # |
AURKA
(details) |
11393 | aurora kinase A | 6790 | O14965 | AURKA_HUMAN | Pkinase PF00069 133-383 | Aurka | 894678 | P97477 | AURKA_MOUSE | PPP1R | Serine/threonine phosphatases / Protein phosphatase 1, regulatory subunits | Histone modification write | Histone phosphorylation | 12576638 | # | histone | H3 | H3S10ph | 12576638 | Xenopus Aurora-A = AURKA, pEg2, phosphorylate specifically H3 at Serine10 in vitro. | # |
AURKB
(details) |
11390 | aurora kinase B | 9212 | Q96GD4 | AURKB_HUMAN | Pkinase PF00069 77-327 | Aurkb | 107168 | O70126 | AURKB_MOUSE | PPP1R | Serine/threonine phosphatases / Protein phosphatase 1, regulatory subunits | Histone modification write | Histone phosphorylation | 11856369 | # | histone | H3S10, H3S28 | # | 11856369 | Aurora-B=AURKB directly phosphorylated H3, not only at Ser10 but also at Ser28. | # |
AURKC
(details) |
11391 | aurora kinase C | 6795 | Q9UQB9 | AURKC_HUMAN | Pkinase PF00069 43-293 | Aurkc | 1321119 | O88445 | AURKC_MOUSE | # | # | Histone modification write | Histone phosphorylation | 15499654 | # | histone | H3S10, H3S28 | # | 15499654 | Aurora-C=AURKC, like Aurora-B kinase, is a chromosomal passenger protein localizing first to centromeres and then to the midzone of mitotic cells. Aurora-C transcript is expressed at a moderate level albeit about an order of magnitude lower than Aurora-B transcript in diploid human fibroblasts. | # |
BABAM1
(details) |
25008 | BRISC and BRCA1 A complex member 1 | 29086 | Q9NWV8 | BABA1_HUMAN | Babam1 | 1915501 | Q3UI43 | BABA1_MOUSE | # | # | Histone modification erase cofactor | Histone deubiquitination | 19261746 | BRISC, BRCA1-A | histone | # | # | 19261746 | MERIT40 (Mediator of Rap80 Interactions and Targeting 40 kD)/(C19orf62) is a Rap80-associated protein. MERIT40 is required for Rap80-associated lysine63–ubiquitin DUB activity, a critical component of BRCA1–Rap80 G2 checkpoint and viability responses to ionizing radiation. Thus, MERIT40 represents a novel factor that links BRCA1–Rap80 complex integrity, DSB recognition, and ubiquitin chain hydrolytic activities to the DNA damage response. | # | |
BAHD1
(details) |
29153 | bromo adjacent homology domain containing 1 | 22893 | Q8TBE0 | BAHD1_HUMAN | BAH PF01426 624-777 | Bahd1 | 2139371 | Q497V6 | BAHD1_MOUSE | # | # | Chromatin remodeling | # | 19666599 | # | histone | H3K27me3 | # | 19666599 | Two-hybrid screen suggest that BAHD1 could link chromatin condensation activities to DNA-binding transcription factors. The BAH domain does not bind H3K27me3 in vitro but is required for BAHD1 colocalization with H3K27me3 in vivo. | # |
BANP
(details) |
13450 | BTG3 associated nuclear protein | 54971 | Q8N9N5 | BANP_HUMAN | BEN PF10523 251-319 | Banp | 1889023 | Q8VBU8 | BANP_MOUSE | BEND | BEN domain containing | Histone modification write | Histone acetylation | 16166625 | # | histone | H3K9, H4K8 | # | 16166625 | SMAR1 (=BANP) directs the histone modifications at a distance. Overexpression of SMAR1 deacetylates the histones in the probe II and III region and depletion of SMAR1 increases acetylation in this region. Possibly SMAR1 controls the histone acetylation status at a distance. | # |
BAP1
(details) |
950 | BRCA1 associated protein-1 (ubiquitin carboxy-terminal hydrolase) | 8314 | Q92560 | BAP1_HUMAN | Peptidase_C12 PF01088 5-214, UCH_C PF18031 643-688 | Bap1 | 1206586 | Q99PU7 | BAP1_MOUSE | # | # | Histone modification erase, Polycomb group (PcG) protein | Histone deubiquitination | 20436459 | PR-DUB | histone | H2AK119ub1 | H2AK119 | 19815555, 19188440, 20436459 | The Polycomb group proteins BAP1 and ASX form a conserved complex in vivo and in vitro. | # |
BARD1
(details) |
952 | BRCA1 associated RING domain 1 | 580 | Q99728 | BARD1_HUMAN | zf-RING_6 PF14835 42-107, Ank_2 PF12796 428-523, BRCT PF00533 569-643 | Bard1 | 1328361 | O70445 | BARD1_MOUSE | ANKRD | Ankyrin repeat domain containing | Histone modification write | Histone ubiquitination | 19916563 | BRCC, BRCA1-A | histone | H2AX, H2A, H2B, H3, H4 | H2AXub, H2Aub, H2Bub, H3ub, H4ub | 19916563, 12485996 | BARD1, like CstF-50, also interacts with RNA polymerase II. BARD1-mediated inhibition of polyadenylation may prevent inappropriate RNA processing during transcription, | # |
BAZ1A
(details) |
960 | bromodomain adjacent to zinc finger domain, 1A | 11177 | Q9NRL2 | BAZ1A_HUMAN | WAC_Acf1_DNA_bd PF10537 24-123, DDT PF02791 423-486, WHIM1 PF15612 592-633, WSD PF15613 802-926, PHD PF00628 1151-1195, Bromodomain PF00439 1439-1517 | Baz1a | 1309478 | O88379 | BAZ1A_MOUSE | PHF | Zinc fingers, PHD-type | Histone chaperone | # | 14759371 | ACF, CHRAC | histone | # | # | 14759371 | ACF1-ISWI complex (ATP-dependent chromatin assembly and remodeling factor [ACF]) associates with histone-fold proteins (CHRAC-15 and CHRAC-17 in the human chromatin accessibility complex [CHRAC]). These histone-fold proteins facilitate ATP-dependent nucleosome sliding by ACF. Direct interaction of the CHRAC-15/17 complex with the ACF1 subunit is essential for this process. | # |
BAZ1B
(details) |
961 | bromodomain adjacent to zinc finger domain, 1B | 9031 | Q9UIG0 | BAZ1B_HUMAN | WAC_Acf1_DNA_bd PF10537 22-121, WHIM1 PF15612 726-762, WSD PF15613 899-1026, PHD PF00628 1187-1231, Bromodomain PF00439 1348-1427 | Baz1b | 1353499 | Q9Z277 | BAZ1B_MOUSE | PHF | Zinc fingers, PHD-type | Histone modification write | Histone phosphorylation | 19092802 | B-WICH, WINAC | histone | H2AXT142, H3 | H2AXY142ph | 19092802 | WSTF=BAZ1B phosphorylates Tyr 142 of H2A.X, and WSTF activity has an important role in regulating several events that are critical for the DNA damage response. | # |
BAZ2A
(details) |
962 | bromodomain adjacent to zinc finger domain, 2A | 11176 | Q9UIF9 | BAZ2A_HUMAN | MBD PF01429 550-619, DDT PF02791 850-911, WHIM1 PF15612 951-993, WSD PF15613 1111-1788, PHD PF00628 1679-1723, Bromodomain PF00439 1803-1882 | Baz2a | 2151152 | Q91YE5 | BAZ2A_MOUSE | PHF | Zinc fingers, PHD-type | Chromatin remodeling, Histone modification erase | Histone deacetylation | 11532953 | NoRC | histone, DNA | H4K16ac, DNA motif | H4K5, H4K8, H4K12 | 11532953 | TIP5=BAZ2A is a member of a family of chromatin remodeling factors. Fig. 1 in the reference. | # |
BAZ2B
(details) |
963 | bromodomain adjacent to zinc finger domain, 2B | 29994 | Q9UIF8 | BAZ2B_HUMAN | MBD PF01429 743-811, DDT PF02791 1088-1150, domain PF15612 1193-1227, WSD PF15613 1374-1410, PHD PF00628 1934-1978, Bromodomain PF00439 2069-2151 | Baz2b | 2442782 | # | # | PHF | Zinc fingers, PHD-type | Histone modification read | # | 22464331 | # | histone, DNA | H1.4ac, H2Aac, H2Bac, H3ac, H4Kac | # | 22464331 | Fig. 5 in the reference. | # |
BCOR
(details) |
20893 | BCL6 corepressor | 54880 | Q6W2J9 | BCOR_HUMAN | BCOR PF15808 1183-1395, Ank_2 PF12796 1467-1559, PUFD PF16553 1634-1745 | Bcor | 1918708 | Q8CGN4 | BCOR_MOUSE | ANKRD | Ankyrin repeat domain containing | Polycomb group (PcG) protein | # | 16943429 | BCOR | # | # | # | 16943429 | The recruitment of BCOR complex PcG proteins to target genes by BCL6=BCOR in B cells suggests that BCL6 functions as a PcG-targeting factor. | # |
BCORL1
(details) |
25657 | BCL6 corepressor-like 1 | 63035 | Q5H9F3 | BCORL_HUMAN | Ank_2 PF12796 1500-1591, PUFD PF16553 1668-1782 | Bcorl1 | 2443910 | A2AQH4 | BCORL_MOUSE | ANKRD | Ankyrin repeat domain containing | Histone modification erase cofactor | Histone deacetylation | 23523425, 17379597 | BCOR | histone | H3K36me2 | # | 23523425 | Homologous to BCOR; which is a component of a complex (dRAF-like complex) in companion with KDM2B, a H3K36me2 demethylase. | # |
BMI1
(details) |
1066 | BMI1 proto-oncogene, polycomb ring finger | 648 | P35226 | BMI1_HUMAN | zf-C3HC4_2 PF13923 18-56, RAWUL PF16207 162-226 | Bmi1 | 88174 | P25916 | BMI1_MOUSE | RNF, PCGF | RING-type (C3HC4) zinc fingers, Polycomb group ring fingers | Polycomb group (PcG) protein | # | 15386022 | PRC1 | # | # | # | 15386022 | The complex, termed hPRC1L (human Polycomb repressive complex 1-like), is composed of several Polycomb-group proteins including Ring1, Ring2, Bmi1 and HPH2. | # |
BPTF
(details) |
3581 | bromodomain PHD finger transcription factor | 2186 | Q12830 | BPTF_HUMAN | DDT PF02791 241-299, PHD PF00628 393-434 2870-2915, WSD PF15613 457-524, Bromodomain PF00439 2939-3018 | Bptf | 2444008 | # | # | PHF | Zinc fingers, PHD-type | Chromatin remodeling | # | 18974875 | NuRF | chromatin | # | # | 18974875 | Chromatin remodeling protein Bptf (Bromodomain PHD-finger Transcription Factor), the largest subunit of NURF (Nucleosome Remodeling Factor) in a mammal. | # |
BRCA1
(details) |
1100 | breast cancer 1, early onset | 672 | P38398 | BRCA1_HUMAN | zf-C3HC4 PF00097 24-64, BRCT_assoc PF12820 361-492, BRCT PF00533 1649-1724 1758-1845 | Brca1 | 104537 | P48754 | BRCA1_MOUSE | RNF, PPP1R | RING-type (C3HC4) zinc fingers, Serine/threonine phosphatases / Protein phosphatase 1, regulatory subunits | Histone modification write cofactor, TF | Histone acetylation, Histone methylation, Histone ubiquitination, TF activator, TF repressor | 20820192 | BRCC, BRCA1-A | DNA | DNA motif | # | 20820192 | BRCA1 acts as a transcription factor, which regulates expression of many genes involved in many biological processes. DNMT1, the methylation maintenance enzyme, is a transcriptional target of BRCA1. Impaired function of BRCA1 leads to global DNA hypomethylation, loss of genomic imprinting, and an open chromatin configuration in several types of tissues examined in a BRCA1 mutant mouse model at premaligant stages. BRCA1 deficiency is also associated with significantly increased expression levels of several protooncogenes. | # |
BRCA2
(details) |
1101 | breast cancer 2, early onset | 675 | P51587 | BRCA2_HUMAN | BRCA2 PF00634 1002-1036 1216-1244 1424-1452 1521-1548 1665-1847 1842-1867 1974-2003 2054-2083, BRCA-2_helical PF09169 2476-2667, BRCA-2_OB1 PF09103 2669-2798, BRCA2DBD_OB2 PF21318 2804-2863 2969-3034, Tower PF09121 2831-2868, BRCA-2_OB3 PF09104 3053-3189, domain PF22687 3270-3382 | Brca2 | 109337 | P97929 | BRCA2_MOUSE | FANC | Fanconi anemia, complementation groups | Histone modification write | Histone acetylation | 9619837 | BRCC | histone, DNA | H3, H4, ssDNA | # | 9619837 | BRCA2 proteins acetylate primarily H3 and H4 of free histones. This suggests that HAT activity of BRCA2 may play an important role in the regulation of transcription and tumor suppressor function. | # |
BRCC3
(details) |
24185 | BRCA1/BRCA2-containing complex, subunit 3 | 79184 | P46736 | BRCC3_HUMAN | JAB PF01398 8-147, BRCC36_C PF18110 226-308 | Brcc3 | 2389572 | P46737 | BRCC3_MOUSE | # | # | Histone modification erase | Histone deubiquitination | 19202061 | BRISC, BRCA1-A | histone | H2AK63, H2AXK63 | H2A, H2AX | 19202061 | Involved in DNA damage response and reverses RNF8 ubiquitination activity. Rap80-BRCC36 DUB Activity and γH2AX hydrolysis Ubiquitination. Rap80 is required for BRCA1 and BRCC36 localization to DSBs. | # |
BRD1
(details) |
1102 | bromodomain containing 1 | 23774 | O95696 | BRD1_HUMAN | EPL1 PF10513 47-195, PHD_2 PF13831 229-261, zf-HC5HC2H_2 PF13832 270-389, Bromodomain PF00439 572-653, PWWP PF00855 929-1039 | Brd1 | 1924161 | # | # | # | # | Histone modification read | # | 21720545 | MOZ/MORF | histone | H3K36me3, H3 | # | 21720545 | The PWWP domains in BRPF1, BRPF2=BRD1, HDGF2, MUM1 and the N-terminal PWWP domains of WHSC1 and WHSC1L1 show weak binding affinity to histones with H3K36, K3K79 or H4K20 methylation. | # |
BRD2
(details) |
1103 | bromodomain containing 2 | 6046 | P25440 | BRD2_HUMAN | Bromodomain PF00439 85-167 354-440, BET PF17035 640-704 | Brd2 | 99495 | Q7JJ13 | BRD2_MOUSE | # | # | Histone modification read | # | 18406326, 20495584 | # | histone | H3K9me2, H3K14me2, H4K5ac, H4K12ac, H3K27ac | # | 18406326, 20495584 | Brd2- and Brd3-associated chromatin is significantly enriched in H4K5, H4K12, and H3K14 acetylation and contains relatively little dimethylated H3K9. Both Brd2 and Brd3 allowed RNA polymerase II to transcribe through nucleosomes in a defined transcription system. Such activity depended on specific histone H4 modifications known to be recognized by the Brd proteins.. BRD2 is involved in recognizing acetylated lysines, including H3K27ac, and its involvement in transcriptional regulation. | # |
BRD3
(details) |
1104 | bromodomain containing 3 | 8019 | Q15059 | BRD3_HUMAN | Bromodomain PF00439 46-127 315-402, BET PF17035 571-634 | Brd3 | 1914632 | Q8K2F0 | BRD3_MOUSE | # | # | Histone modification read | # | 18406326 | # | histone | H3K9me2, H3K14me2, H4K5ac, H4K12ac | # | 18406326 | Brd2- and Brd3-associated chromatin is significantly enriched in H4K5, H4K12, and H3K14 acetylation and contains relatively little dimethylated H3K9. Both Brd2 and Brd3 allowed RNA polymerase II to transcribe through nucleosomes in a defined transcription system. Such activity depended on specific histone H4 modifications known to be recognized by the Brd proteins. | # |
BRD4
(details) |
13575 | bromodomain containing 4 | 23476 | O60885 | BRD4_HUMAN | Bromodomain PF00439 70-151 358-444, BET PF17035 610-672, BRD4_CDT PF17105 1324-1362 | Brd4 | 1888520 | Q9ESU6 | BRD4_MOUSE | # | # | Histone modification read | # | 12840145 | # | histone | H3K9, H3K14, H4K5, H4K12 | # | 12840145 | Brd4 avidly binds to di- and tetraacetylated histone H4 and diacetylated H3, but weakly or not at all to mono- and unacetylated H3 and H4. | # |
BRD7
(details) |
14310 | bromodomain containing 7 | 29117 | Q9NPI1 | BRD7_HUMAN | Bromodomain PF00439 142-223, DUF3512 PF12024 298-483 | Brd7 | 1349766 | O88665 | BRD7_MOUSE | # | # | Histone modification read | # | 17498659 | SWI/SNF BRM-BRG1 | histone | H3K9ac, H3K14ac, H3K8ac | # | 17498659 | BRD7 bromodomain contains the typical left-handed four-helix bundle topology, and can bind with weak affinity to lysine-acetylated peptides derived from histone H3 with K9 or K14 acetylated and from histone H4 with K8, K12 or K16 acetylated. | # |
BRD8
(details) |
19874 | bromodomain containing 8 | 10902 | Q9H0E9 | BRD8_HUMAN | Bromodomain PF00439 723-797 1115-1193 | Brd8 | 1925906 | Q8R3B7 | BRD8_MOUSE | # | # | Histone modification read | # | 14966270 | SWR, NuA4, NuA4-related complex | histone | # | # | 14966270 | Part of the NuA4 histone acetyltransferase complex. | # |
BRD9
(details) |
25818 | bromodomain containing 9 | 65980 | Q9H8M2 | BRD9_HUMAN | Bromodomain PF00439 146-227, DUF3512 PF12024 288-462 | Brd9 | 2145317 | Q3UQU0 | BRD9_MOUSE | # | # | Histone modification read | # | 22464331 | SWI/SNF BRM-BRG1 | histone | H3 | # | 22464331 | Fig. 5 in the reference. | # |
BRDT
(details) |
1105 | bromodomain, testis-specific | 676 | Q58F21 | BRDT_HUMAN | Bromodomain PF00439 39-120 277-363, BET PF17035 509-572, BRD4_CDT PF17105 901-947 | Brdt | 1891374 | Q91Y44 | BRDT_MOUSE | # | # | Histone modification read | # | 22901802 | # | histone | H4K5ac, H4K8ac | # | 22901802 | Biochemical and crystallographic studies confirm that occupancy of the BRDT acetyl-lysine binding pocket by JQ1 prevents recognition of acetylated histone H4. | # |
BRE
(details) |
1106 | brain and reproductive organ-expressed (TNFRSF1A modulator) | 9577 | Q9NXR7 | BRE_HUMAN | BRE PF06113 9-334 | Bre | 1333875 | Q8K3W0 | BRE_MOUSE | # | # | Histone modification write cofactor | Histone ubiquitination | 14636569 | BRISC, BRCC, BRCA1-A | histone | # | # | 14636569 | BRCC36 and BRCC45 are novel components of the complex with sequence homology to a subunit of the signalosome and proteasome complexes. Reconstitution of a recombinant four-subunit complex containing BRCA1/BARD1/BRCC45/BRCC36 revealed an enhanced E3 ligase activity compared to that of BRCA1/BARD1 heterodimer. Furthermore, a recent report describes the ability of BRCA1-BARD1 heterodimer to autoubiquitinate BRCA1 and BARD1 and transubiquitinate the histone H2A(X). | # |
BRMS1
(details) |
17262 | breast cancer metastasis suppressor 1 | 25855 | Q9HCU9 | BRMS1_HUMAN | Sds3 PF08598 60-183 | Brms1 | 2388804 | Q99N20 | BRMS1_MOUSE | # | # | Chromatin remodeling | # | 17000776 | mSin3A | chromatin | # | # | 17000776 | As a corepressor, BRMS1 can function as a more global regulator of chromatin structure, as evidenced by its ability to decrease promoter occupancy of Ac-H3 and Ac-H4 on both the cIAP2 and the Bfl-1/A1 promoters. | # |
BRMS1L
(details) |
20512 | breast cancer metastasis-suppressor 1-like | 84312 | Q5PSV4 | BRM1L_HUMAN | Sds3 PF08598 62-184 | Brms1l | 1196337 | Q3U1T3 | BRM1L_MOUSE | # | # | Histone modification erase | Histone deacetylation | 15451426 | mSin3A | histone | # | # | 15451426 | p40-associated Sin3A/HDAC1 complex can deacetylate histone peptides in vitro. p40 can also repress transcription when tethered to the Gal-regulated promoter by the Gal-DNA binding domain. | # |
BRPF1
(details) |
14255 | bromodomain and PHD finger containing, 1 | 7862 | P55201 | BRPF1_HUMAN | EPL1 PF10513 105-255, PHD_2 PF13831 288-320, zf-HC5HC2H_2 PF13832 329-448, Bromodomain PF00439 639-718, PWWP PF00855 1085-1196 | Brpf1 | 1926033 | # | # | # | # | Histone modification read | # | 20400950 | MOZ/MORF | histone | H3K36me3 | # | 20400950 | Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1. | # |
BRPF3
(details) |
14256 | bromodomain and PHD finger containing, 3 | 27154 | Q9ULD4 | BRPF3_HUMAN | EPL1 PF10513 48-194, PHD_2 PF13831 227-259, zf-HC5HC2H_2 PF13832 268-386, Bromodomain PF00439 599-680, PWWP PF00855 1076-1187 | Brpf3 | 2146836 | # | # | # | # | Histone modification write cofactor | Histone acetylation | 18794358 | MOZ/MORF | histone | # | # | 18794358 | Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. BRPF proteins bridge the association of MOZ and MORF with ING5 and EAF6. | # |
BRWD1
(details) |
12760 | bromodomain and WD repeat domain containing 1 | 54014 | Q9NSI6 | BRWD1_HUMAN | WD40 PF00400 182-214 217-255 262-302 360-396 457-497, Bromodomain PF00439 1166-1251 1325-1402 | Brwd1 | 1890651 | Q921C3 | BRWD1_MOUSE | WDR | WD repeat domain containing | Histone modification read | # | 22464331 | # | histone | H3 | # | 22464331 | Fig. 5 in the reference. | # |
BRWD3
(details) |
17342 | bromodomain and WD repeat domain containing 3 | 254065 | Q6RI45 | BRWD3_HUMAN | WD40 PF00400 176-208 211-249 256-296 318-345 355-392 455-494 511-536, Bromodomain PF00439 1153-1231 1355-1414 | Brwd3 | 3029414 | A2AHJ4 | BRWD3_MOUSE | WDR | WD repeat domain containing | Histone modification read | # | 22464331 | # | histone | H3 | # | 22464331 | Fig. 5 in the reference. | # |
BUB1
(details) |
1148 | BUB1 mitotic checkpoint serine/threonine kinase | 699 | O43683 | BUB1_HUMAN | Mad3_BUB1_I PF08311 8-125, Pkinase PF00069 789-1007 | Bub1 | 1100510 | O08901 | BUB1_MOUSE | # | # | Histone modification write | Histone phosphorylation | 20929775 | # | histone | H2AS121 | H2AS121ph | 20929775 | Bub1 mediates histone 2A-serine 121 (H2A-S121) phosphorylation. | # |
C11orf30
(details) |
18071 | chromosome 11 open reading frame 30 | 56946 | Q7Z589 | EMSY_HUMAN | ENT PF03735 16-84 | 2210018M11Rik | 1924203 | Q8BMB0 | EMSY_MOUSE | # | # | Histone modification write cofactor | Histone methylation | 19131338 | # | histone | # | # | # | Part of a complex with histone methyltranferase activity. UniProt: Regulator which is able to repress transcription, possibly via its interaction with a multiprotein chromatin remodeling complex that modifies the chromatin. | # |
C14orf169
(details) |
20968 | # | # | Q9H6W3 | NO66_HUMAN | JmjC_2 PF08007 298-427, RIOX1_C_WH PF21233 511-637 | - | - | Q9JJF3 | NO66_MOUSE | # | # | Histone modification erase | Histone methylation | 23160351 | # | histone | H3K4me3, H3K4me1, H3K36me2 | H3K4me2, H3K4, H3K36me1 | 23160351 | H3K4me3 demethylase Rbp2 (Kdm5a). In addition to NO66=C14orf169, at least four other H3K36me3 demethylases are known. | # |
C17orf49
(details) |
28737 | chromosome 17 open reading frame 49 | 124944 | Q8IXM2 | BAP18_HUMAN | 0610010K14Rik | 1915609 | Q9DCT6 | BAP18_MOUSE | # | # | Histone modification read | # | 20850016 | CHD8, MLL2/3, MLL4/WBP7 | histone | H3K4me3 | # | 20850016 | H3K4me3 readers Sgf29, TRRAP, PHF8, GATAD1, and BAP18=C17orf49, are associated mainly with promoters (Figures S3A and S3B) and coincide with H3K4me3 marking. | # | |
CARM1
(details) |
23393 | coactivator-associated arginine methyltransferase 1 | 10498 | Q86X55 | CARM1_HUMAN | CARM1 PF11531 27-139, PrmA PF06325 184-257, domain PF22528 291-453 | Carm1 | 1913208 | Q9WVG6 | CARM1_MOUSE | PRMT | Protein arginine methyltransferases | Histone modification write | Histone methylation | 12237300 | # | histone | H3R17 | H3R17me, H3R17me2a | 16497732, 19405910 | Methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activate transcription via chromatin remodeling. CARM1-directed arginine methylation of histone H3 in the promoters of steroid hormone-responsive genes is induced by steroid hormone treatment of cells. | # |
CBLL1
(details) |
21225 | E3 ubiquitin-protein ligase Hakai (EC 2.3.2.27) (Casitas B-lineage lymphoma-transforming sequence-like protein 1) (c-Cbl-like protein 1) (RING finger protein 188) (RING-type E3 ubiquitin transferase Hakai) | 79872 | Q75N03 | HAKAI_HUMAN | zf_Hakai PF18408 161-191 | Cbll1 | 2144842 | Q9JIY2 | HAKAI_MOUSE | RNF | Ring finger proteins | RNA modification | RNA methylation | 29507755 | WMM | RNA | A of mRNA | m6A | 29507755 | # | New |
CBX1
(details) |
1551 | chromobox homolog 1 | 10951 | P83916 | CBX1_HUMAN | Chromo PF00385 21-69, Chromo_shadow PF01393 118-170 | Cbx1 | 105369 | P83917 | CBX1_MOUSE | # | # | Histone modification read | # | 21047797 | # | histone | H3K9me3, H3K27me3 | # | 21047797 | Binding data indicate that Cbx1, -3, and -5 bind with greater affinity to H3K9me3. | # |
CBX2
(details) |
1552 | chromobox homolog 2 | 84733 | Q14781 | CBX2_HUMAN | Chromo PF00385 12-60, CBX7_C PF17218 492-523 | Cbx2 | 88289 | P30658 | CBX2_MOUSE | # | # | Histone modification read | # | 21047797 | PRC1 | histone | H3K9me3, H3K27me3 | # | 21047797 | Cbx2 and Cbx7 recognized both H3K9me3 and H3K27me3, whereas Cbx4 preferred H3K9me3. | # |
CBX3
(details) |
1553 | chromobox homolog 3 | 11335 | Q13185 | CBX3_HUMAN | Chromo PF00385 30-78, Chromo_shadow PF01393 123-174 | Cbx3 | 108515 | P23198 | CBX3_MOUSE | # | # | Histone modification read | # | 21047797 | RING2-L3MBTL2, L3MBTL1 | histone | H3K9me3 | # | 21047797 | Cbx3 chromodomain binds to H3K9me3 but not to H3K27me3. | # |
CBX4
(details) |
1554 | chromobox homolog 4 | 8535 | O00257 | CBX4_HUMAN | Chromo PF00385 11-60, CBX7_C PF17218 533-559 | Cbx4 | 1195985 | O55187 | CBX4_MOUSE | # | # | Histone modification read | # | 21047797 | PRC1 | histone | H3K9me3 | # | 21047797 | Cbx2 and Cbx7 recognizes both H3K9me3 and H3K27me3, whereas Cbx4 prefers H3K9me3. | # |
CBX5
(details) |
1555 | chromobox homolog 5 | 23468 | P45973 | CBX5_HUMAN | Chromo PF00385 20-69, Chromo_shadow PF01393 123-174 | Cbx5 | 109372 | Q61686 | CBX5_MOUSE | # | # | Histone modification read | # | 21047797 | # | histone | H3K9me, H3K27me3 | # | 21047797 | Excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph). | # |
CBX6
(details) |
1556 | chromobox homolog 6 | 23466 | O95503 | CBX6_HUMAN | Chromo PF00385 11-60, CBX7_C PF17218 358-386 | Cbx6 | 3512628 | Q9DBY5 | CBX6_MOUSE | # | # | Histone modification read | # | 21047797 | PRC1 | histone | H3K9me3, H3K27me3 | # | 21047797 | Cbx6 and Cbx8 have functional aromatic cages and hydrophobic fingers very similar to those of Cbx2, -4, and -7, but the former bind to H3K9me3 and H3K27me3 peptides with much lower affinity. | # |
CBX7
(details) |
1557 | chromobox homolog 7 | 23492 | O95931 | CBX7_HUMAN | Chromo PF00385 11-60, CBX7_C PF17218 212-239 | Cbx7 | 1196439 | Q8VDS3 | CBX7_MOUSE | # | # | Histone modification read | # | 21047797 | PRC1 | histone | H3K9me3, H3K27me3 | # | 21047797 | Cbx2 and Cbx7 recognize both H3K9me3 and H3K27me3, whereas Cbx4 prefers H3K9me3. | # |
CBX8
(details) |
15962 | chromobox homolog 8 | 57332 | Q9HC52 | CBX8_HUMAN | Chromo PF00385 11-60, CBX7_C PF17218 348-381 | Cbx8 | 1353589 | Q9QXV1 | CBX8_MOUSE | # | # | Histone modification read | # | 21047797 | PRC1 | histone | H3K9me3, H3K27me3 | # | 21047797 | Cbx6 and Cbx8 have functional aromatic cages and hydrophobic fingers very similar to those of Cbx2, -4, and -7, but the former bind to H3K9me3 and H3K27me3 peptides with much lower affinity. | # |
CCDC101
(details) |
25156 | coiled-coil domain containing 101 | 112869 | Q96ES7 | SGF29_HUMAN | SGF29_Tudor PF07039 159-288 | Ccdc101 | 1922815 | Q9DA08 | SGF29_MOUSE | # | # | Histone modification read | # | 21685874 | ATAC | histone | H3K4me, H3K4me3 | # | 21685874 | The crystal structures of the tandem Tudor domains of Saccharomyces cerevisiae and human Sgf29=CCDC101 and their complexes with H3K4me2 and H3K4me3 peptides, respectively, shows that Sgf29 selectively binds H3K4me2/3 marks. | # |
CDC6
(details) |
1744 | cell division cycle 6 | 990 | Q99741 | CDC6_HUMAN | domain PF13191 173-315, domain PF22606 346-403, Cdc6_C PF09079 455-542 | Cdc6 | 1345150 | O89033 | CDC6_MOUSE | # | # | Chromatin remodeling | # | 22358331 | # | chromatin | # | # | # | CDC6 interacts with the HP1 chromoshadow domain. | # |
CDC73
(details) |
16783 | cell division cycle 73 | 79577 | Q6P1J9 | CDC73_HUMAN | CDC73_N PF16050 1-296, CDC73_C PF05179 358-520 | Cdc73 | 2384876 | Q8JZM7 | CDC73_MOUSE | # | # | Histone modification write cofactor | Histone methylation | # | # | histone | # | # | # | UniProt: PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). | # |
CDK1
(details) |
1722 | cyclin-dependent kinase 1 | 983 | P06493 | CDK1_HUMAN | Pkinase PF00069 4-287 | Cdk1 | 88351 | P11440 | CDK1_MOUSE | CDK | Cyclin-dependent kinases | Histone modification write | Histone phosphorylation | 22509284 | # | histone | H1 | H1ph | 22509284 | Histone H1, a known CDKs target protein, was strongly phosphorylated by CDK1/cyclin B, illustrating the normal activity of CDK1/cyclin B. | # |
CDK17
(details) |
8750 | cyclin-dependent kinase 17 | 5128 | Q00537 | CDK17_HUMAN | Pkinase PF00069 192-473 | Cdk17 | 97517 | Q8K0D0 | CDK17_MOUSE | CDK | Cyclin-dependent kinases | Histone modification write | Histone phosphorylation | # | # | histone | H1 | # | # | Has a Ser/Thr-phosphorylating activity for histone H1. (Annotated by similarity.) | # |
CDK2
(details) |
1771 | cyclin-dependent kinase 2 | 1017 | P24941 | CDK2_HUMAN | Pkinase PF00069 4-286 | Cdk2 | 104772 | P97377 | CDK2_MOUSE | CDK | Cyclin-dependent kinases | Histone modification write | Histone phosphorylation | 15753125 | # | histone | H1S, H1T | H1Sph, H1Tph | 15753125 | Cdk2 is one of the enzymes recruited to replication foci (by Cdc45 or other fork proteins), followed by H1 phosphorylation and chromatin unfolding. | # |
CDK3
(details) |
1772 | cyclin-dependent kinase 3 | 1018 | Q00526 | CDK3_HUMAN | Pkinase PF00069 4-286 | Cdk3-ps | 1916931 | Q80YP0 | CDK3_MOUSE | CDK | Cyclin-dependent kinases | Histone modification write | Histone phosphorylation | # | # | histone | H1 | # | # | Cdk3 is supposed to phosphorylate histone H1, but have found no good reference to document it. | # |
CDK5
(details) |
1774 | cyclin-dependent kinase 5 | 1020 | Q00535 | CDK5_HUMAN | Pkinase PF00069 4-286 | Cdk5 | 101765 | P49615 | CDK5_MOUSE | CDK | Cyclin-dependent kinases | Histone modification write | Histone phosphorylation | 19729834 | # | histone | H1 | # | 19729834 | Reciprocal coimmunoprecipitation studies with antibodies to either myc or Cdk5 revealed that cyclin I bound to and activated endogenous Cdk5, as analyzed by histone H1 phosphorylation. | # |
CDK7
(details) |
1778 | cyclin-dependent kinase 7 | 1022 | P50613 | CDK7_HUMAN | Pkinase PF00069 12-295 | Cdk7 | 102956 | Q03147 | CDK7_MOUSE | CDK, TFIIH | Cyclin-dependent kinases, General transcription factor IIH complex subunits | Histone modification write | Histone phosphorylation | 10722743 | # | histone | H1 | # | 10722743 | Cdk7, is able to phosphorylate histone H1, and the basal activity is increased 2-fold in the presence of recombinant human cyclin H (the activating partner of Cdk7). | # |
CDK9
(details) |
1780 | cyclin-dependent kinase 9 | 1025 | P50750 | CDK9_HUMAN | Pkinase PF00069 19-315 | Cdk9 | 1328368 | Q99J95 | CDK9_MOUSE | CDK | Cyclin-dependent kinases | Histone modification cofactor | # | 19844166 | # | histone | # | # | # | CDK9 functions to guide a complex network of chromatin modifications including histone H2B monoubiquitination (H2Bub1), H3 lysine 4 trimethylation (H3K4me3) and H3K36me3. UniProt: Protein kinase involved in the regulation of transcription. Part of the complex P-TEFb involved in cotranscriptional histone modification. | # |
CDY1
(details) |
1809 | chromodomain protein, Y-linked, 1 | 9085 | Q9Y6F8 | CDY1_HUMAN | Chromo PF00385 6-57, ECH_1 PF00378 303-535 | # | # | # | # | # | # | Histone modification write | Histone acetylation | 12072557 | # | histone | H4 | # | 12072557 | Human CDY and mouse CDYL=CDY1 proteins exhibit histone acetyltransferase activity in vitro, with a strong preference for histone H4. | # |
CDY1B
(details) |
23920 | chromodomain protein, Y-linked, 1B | 253175 | Q9Y6F8 | CDY1_HUMAN | Chromo PF00385 6-57, ECH_1 PF00378 303-535 | # | # | # | # | # | # | Histone modification write | Histone acetylation | 12072557 | # | histone | H4 | # | 12072557 | Human CDY and mouse CDYL=CDY1B proteins exhibit histone acetyltransferase activity in vitro, with a strong preference for histone H4. | # |
CDY2A
(details) |
1810 | chromodomain protein, Y-linked, 2A | 9426 | Q9Y6F7 | CDY2_HUMAN | Chromo PF00385 6-57, ECH_1 PF00378 304-537 | # | # | # | # | # | # | Histone modification write | Histone acetylation | # | # | histone | # | # | # | May have histone acetyltransferase activity. (Annotated by similarity.) | # |
CDY2B
(details) |
23921 | chromodomain protein, Y-linked, 2B | 203611 | Q9Y6F7 | CDY2_HUMAN | Chromo PF00385 6-57, ECH_1 PF00378 304-537 | # | # | # | # | # | # | Histone modification write | Histone acetylation | 22498752 | # | histone | # | # | # | CDY2B annotated as histone acetyltransferase in UniProt. | # |
CDYL
(details) |
1811 | chromodomain protein, Y-like | 9425 | Q9Y232 | CDYL1_HUMAN | Chromo PF00385 61-112, ECH_1 PF00378 363-594 | Cdyl | 1339956 | Q9WTK2 | CDYL_MOUSE | # | # | Histone modification write | Histone acetylation | 12072557 | # | histone | H4 | # | 12072557 | Human CDY and mouse CDYL proteins exhibit histone acetyltransferase activity in vitro, with a strong preference for histone H4. | # |
CDYL2
(details) |
23030 | chromodomain protein, Y-like 2 | 124359 | Q8N8U2 | CDYL2_HUMAN | Chromo PF00385 7-57, ECH_1 PF00378 271-500 | Cdyl2 | 1923046 | Q9D5D8 | CDYL2_MOUSE | # | # | Histone modification read | # | 23455924 | # | histone | H3K9me3 | # | 21774827 | Many mouse chromodomain proteins are reported to bind H3K9me3 in vitro, including CDYL, CDYL2, CBX2, CBX4, CBX7 and M-phase phosphoprotein 8 (MPP8). | # |
CECR2
(details) |
1840 | cat eye syndrome chromosome region, candidate 2 | 27443 | Q9BXF3 | CECR2_HUMAN | Bromodomain PF00439 446-524 | Cecr2 | 1923799 | # | # | # | # | Histone modification read | # | 22464331 | CERF, CERF | histone | H2A, H3 | # | 22464331 | Fig. 5 in the reference. | # |
CELF1
(details) |
2549 | CUGBP Elav-like family member 1 (CELF-1) (50 kDa nuclear polyadenylated RNA-binding protein) (Bruno-like protein 2) (CUG triplet repeat RNA-binding protein 1) (CUG-BP1) (CUG-BP- and ETR-3-like factor 1) (Deadenylation factor CUG-BP) (Embryo deadenylation element-binding protein homolog) (EDEN-BP homolog) (RNA-binding protein BRUNOL-2) | 10658 | Q92879 | CELF1_HUMAN | RRM_1 PF00076 19-85 110-174 403-473 | Celf1 | 1342295 | P28659 | CELF1_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 11158314, 12649496 | # | RNA | mRNA | # | 11158314, 12649496 | Regulates MSE-dependent alternative splicing of cTNT during development in vertebrates. | New |
CELF2
(details) |
2550 | CUGBP Elav-like family member 2 (CELF-2) (Bruno-like protein 3) (CUG triplet repeat RNA-binding protein 2) (CUG-BP2) (CUG-BP- and ETR-3-like factor 2) (ELAV-type RNA-binding protein 3) (ETR-3) (Neuroblastoma apoptosis-related RNA-binding protein) (hNAPOR) (RNA-binding protein BRUNOL-3) | 10659 | O95319 | CELF2_HUMAN | RRM_1 PF00076 43-110 134-198 425-495 | Celf2 | 1338822 | Q9Z0H4 | CELF2_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 11158314, 12649496 | # | RNA | mRNA | # | 11158314, 12649496 | Regulates MSE-dependent alternative splicing of cTNT during development in vertebrates. | New |
CELF3
(details) |
11967 | CUGBP Elav-like family member 3 (CELF-3) (Bruno-like protein 1) (CAG repeat protein 4) (CUG-BP- and ETR-3-like factor 3) (ELAV-type RNA-binding protein 1) (ETR-1) (Expanded repeat domain protein CAG/CTG 4) (RNA-binding protein BRUNOL-1) (Trinucleotide repeat-containing gene 4 protein) | 11189 | Q5SZQ8 | CELF3_HUMAN | RRM_1 PF00076 9-75 97-161 382-452 | Celf3 | 1926034 | Q8CIN6 | CELF3_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 11158314, 12649496 | # | RNA | mRNA | # | 11158314, 12649496 | Regulates MSE-dependent alternative splicing of cTNT during development in vertebrates. | New |
CELF4
(details) |
14015 | CUGBP Elav-like family member 4 (CELF-4) (Bruno-like protein 4) (CUG-BP- and ETR-3-like factor 4) (RNA-binding protein BRUNOL-4) | 56853 | Q9BZC1 | CELF4_HUMAN | RRM_1 PF00076 56-121 154-216 442-473 | Celf4 | 1932407 | Q7TSY6 | CELF4_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 11158314, 12649496 | # | RNA | mRNA | # | 11158314, 12649496 | Regulates MSE-dependent alternative splicing of cTNT during development in vertebrates. | New |
CELF5
(details) |
14058 | CUGBP Elav-like family member 5 (CELF-5) (Bruno-like protein 5) (CUG-BP- and ETR-3-like factor 5) (RNA-binding protein BRUNOL-5) | 60680 | Q8N6W0 | CELF5_HUMAN | RRM_1 PF00076 47-112 136-198 402-472 | Celf5 | 2442333 | D3Z4T1 | D3Z4T1_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 11158314, 12649496 | # | RNA | mRNA | # | 11158314, 12649496 | Regulates MSE-dependent alternative splicing of cTNT during development in vertebrates. | New |
CELF6
(details) |
14059 | CUGBP Elav-like family member 6 (CELF-6) (Bruno-like protein 6) (CUG-BP- and ETR-3-like factor 6) (RNA-binding protein BRUNOL-6) | 60677 | Q96J87 | CELF6_HUMAN | RRM_1 PF00076 48-113 136-199 398-468 | Celf6 | 1923433 | Q7TN33 | CELF6_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 11158314, 12649496 | # | RNA | mRNA | # | 11158314, 12649496 | Regulates MSE-dependent alternative splicing of cTNT during development in vertebrates. | New |
CENPC
(details) |
1854 | centromere protein C | 1060 | Q03188 | CENPC_HUMAN | CENP_C_N PF15622 1-320, CENP-C_mid PF15620 324-596, CENP-C_C PF11699 857-940 | Cenpc1 | 99700 | P49452 | CENPC_MOUSE | # | # | DNA modification | DNA methylation | 19482874 | # | DNA | C | 5mC | 19482874 | CENPC recruits DNA methylation and DNMT3B to both centromeric and pericentromeric satellite repeats and regulates the histone code in these regions. | # |
CHAF1A
(details) |
1910 | chromatin assembly factor 1, subunit A (p150) | 10036 | Q13111 | CAF1A_HUMAN | CAF1-p150_N PF15557 18-224, CAF-1_p150 PF11600 324-482, CAF1A PF12253 560-633, CAF1-p150_C2 PF15539 666-932 | Chaf1a | 1351331 | Q9QWF0 | CAF1A_MOUSE | # | # | Chromatin remodeling | # | 7600578 | CAF-1 | histone | H3, H4 | # | 7600578 | p150=CHAF1A and p60 directly interact and are both required for DNA replication-dependent assembly of nucleosomes. Deletion of the p60-binding domain from the p150 protein prevents chromatin assembly. p150 and p60 form complexes with newly synthesized histones H3 and acetylated H4 in human cell extracts, suggesting that such complexes are intermediates between histone synthesis and assembly onto replicating DNA. | # |
CHAF1B
(details) |
1911 | chromatin assembly factor 1, subunit B (p60) | 8208 | Q13112 | CAF1B_HUMAN | WD40 PF00400 60-94 121-157 162-199 345-372, CAF-1_p60_C PF15512 384-540 | Chaf1b | 1314881 | Q9D0N7 | CAF1B_MOUSE | WDR | WD repeat domain containing | Chromatin remodeling | # | 7600578 | WINAC, CAF-1 | histone | H3, H4 | # | 7600578 | p150 and p60==CHAF1B directly interact and are both required for DNA replication-dependent assembly of nucleosomes. Deletion of the p60-binding domain from the p150 protein prevents chromatin assembly. p150 and p60 form complexes with newly synthesized histones H3 and acetylated H4 in human cell extracts, suggesting that such complexes are intermediates between histone synthesis and assembly onto replicating DNA. | # |
CHD1
(details) |
1915 | chromodomain helicase DNA binding protein 1 | 1105 | O14646 | CHD1_HUMAN | Chromo PF00385 313-351 389-443, SNF2-rel_dom PF00176 482-764, Helicase_C PF00271 789-902, CDH1_2_SANT_HL1 PF18375 1124-1211, CHD1-like_C PF13907 1409-1500 | Chd1 | 88393 | P40201 | CHD1_MOUSE | # | # | Chromatin remodeling | # | 12592387 | # | DNA | # | # | 12592387 | These proteins have a DNA-binding domain as well as a chromodomain motif that can directly effect chromatin structure and gene transcription. There are currently four known members of this gene family in humans (CHD1–CHD4). | # |
CHD1L
(details) |
1916 | chromodomain helicase DNA binding protein 1-like | 9557 | Q86WJ1 | CHD1L_HUMAN | SNF2-rel_dom PF00176 49-327, Helicase_C PF00271 348-459 | Chd1l | 1915308 | Q9CXF7 | CHD1L_MOUSE | # | # | Chromatin remodeling | # | 19661379 | # | DNA | # | # | 19661379 | A chromatin-remodeling enzyme, ALC1 (Amplified in Liver Cancer 1, also known as CHD1L), that interacts with poly(ADP-ribose) and catalyzes PARP1-stimulated nucleosome sliding. | # |
CHD2
(details) |
1917 | chromodomain helicase DNA binding protein 2 | 1106 | O14647 | CHD2_HUMAN | Chromo PF00385 300-338 378-447, SNF2-rel_dom PF00176 487-767, Helicase_C PF00271 792-905, CDH1_2_SANT_HL1 PF18375 1129-1219, CHD1-like_C PF13907 1465-1553 | Chd2 | 2448567 | E9PZM4 | CHD2_MOUSE | # | # | Chromatin remodeling | # | 12592387 | # | DNA | # | # | 12592387 | These proteins have a DNA-binding domain as well as a chromodomain motif that can directly effect chromatin structure and gene transcription. There are currently four known members of this gene family in humans (CHD1–CHD4). | # |
CHD3
(details) |
1918 | chromodomain helicase DNA binding protein 3 | 1107 | Q12873 | CHD3_HUMAN | CHDNT PF08073 155-201, PHD PF00628 382-423 458-500, Chromo PF00385 630-682, SNF2-rel_dom PF00176 738-1034, Helicase_C PF00271 1061-1174, DUF1087 PF06465 1294-1350, CHDII_SANT-like PF06461 1376-1517, CHDCT2 PF08074 1737-1884 | Chd3 | 1344395 | # | # | PHF | Zinc fingers, PHD-type | Chromatin remodeling | # | 12592387 | NuRD | DNA | # | # | 12592387 | These proteins have a DNA-binding domain as well as a chromodomain motif that can directly effect chromatin structure and gene transcription. There are currently four known members of this gene family in humans (CHD1–CHD4). | # |
CHD4
(details) |
1919 | chromodomain helicase DNA binding protein 4 | 1108 | Q14839 | CHD4_HUMAN | CHDNT PF08073 165-217, PHD PF00628 373-414 452-493, Chromo PF00385 621-673, SNF2-rel_dom PF00176 728-1024, Helicase_C PF00271 1052-1164, DUF1087 PF06465 1291-1350, CHDII_SANT-like PF06461 1379-1520, CHDCT2 PF08074 1726-1872 | Chd4 | 1344380 | Q6PDQ2 | CHD4_MOUSE | PHF | Zinc fingers, PHD-type | Chromatin remodeling | # | 12592387 | NuRD | DNA | # | # | 12592387 | These proteins have a DNA-binding domain as well as a chromodomain motif that can directly effect chromatin structure and gene transcription. There are currently four known members of this gene family in humans (CHD1–CHD4). | # |
CHD5
(details) |
16816 | chromodomain helicase DNA binding protein 5 | 26038 | Q8TDI0 | CHD5_HUMAN | CHDNT PF08073 149-200, PHD PF00628 346-387 418-460, Chromo PF00385 590-643, SNF2-rel_dom PF00176 701-998, Helicase_C PF00271 1025-1138, DUF1087 PF06465 1299-1354, CHDII_SANT-like PF06461 1383-1527, CHDCT2 PF08074 1733-1879 | Chd5 | 3036258 | A2A8L1 | CHD5_MOUSE | PHF | Zinc fingers, PHD-type | Chromatin remodeling | # | 12592387 | # | histone | H3K27me3, H3K4 | # | 12592387, 23948251 | A novel gene encoding a protein with chromatin remodeling, helicase and DNA-binding motifs. This gene (CHD5) is the fifth member of the CHD gene family identified in humans. | # |
CHD6
(details) |
19057 | chromodomain helicase DNA binding protein 6 | # | Q8TD26 | CHD6_HUMAN | Chromo PF00385 292-354 375-428, SNF2-rel_dom PF00176 464-750, Helicase_C PF00271 784-897 | Chd6 | 1918639 | A3KFM7 | CHD6_MOUSE | # | # | Chromatin remodeling | # | 12592387 | # | chromatin | # | # | 12592387 | A novel gene encoding a protein with chromatin remodeling, helicase and DNA-binding motifs. This gene (CHD5=CHD6) is the fifth member of the CHD gene family identified in humans. | # |
CHD7
(details) |
20626 | chromodomain helicase DNA binding protein 7 | 55636 | Q9P2D1 | CHD7_HUMAN | Chromo PF00385 801-861 881-935, SNF2-rel_dom PF00176 968-1257, Helicase_C PF00271 1291-1404, BRK PF07533 2563-2609 2644-2687 | Chd7 | 2444748 | A2AJK6 | CHD7_MOUSE | # | # | Chromatin remodeling | # | 5201778 | # | chromatin | # | # | 5201778 | CHD7 protein counts several functional domains: two chromo (chromatin organization modifier), one SNF2/SWI, one helicase and two BRK domains (Figure 4). Chromo domains are implicated in the recognition of lysine-methylated histone tails and of DNA (and RNA) targets. | # |
CHD8
(details) |
20153 | chromodomain helicase DNA binding protein 8 | 57680 | Q9HCK8 | CHD8_HUMAN | Chromo PF00385 642-703 724-778, SNF2-rel_dom PF00176 813-1100, Helicase_C PF00271 1135-1247, BRK PF07533 2310-2351 | Chd8 | 1915022 | Q09XV5 | CHD8_MOUSE | # | # | Chromatin remodeling | # | 18378692 | CHD8, MLL2/3, MLL4/WBP7 | chromatin | H1 | # | 19151705, 18378692 | CHD8 is an ATP-dependent chromatin remodeling factor that regulates beta-catenin target genes. | # |
CHD9
(details) |
25701 | chromodomain helicase DNA binding protein 9 | 80205 | Q3L8U1 | CHD9_HUMAN | Chromo PF00385 690-751 773-827, SNF2-rel_dom PF00176 863-1149, Helicase_C PF00271 1183-1296, BRK PF07533 2484-2528 2555-2603 | Chd9 | 1924001 | Q8BYH8 | CHD9_MOUSE | # | # | Chromatin remodeling | # | 16554032 | # | DNA | # | # | 16554032 | PRIC320=CHD9 is similar to a recently described chromodomain helicase DNA-binding protein [27]. The recognition of this chromatin remodeling function and nuclear receptor coactivator function is suggestive of the multiple roles played by these nuclear receptor cofactors. | # |
CHEK1
(details) |
1925 | checkpoint kinase 1 | 1111 | O14757 | CHK1_HUMAN | Pkinase PF00069 10-264 | Chek1 | 1202065 | O35280 | CHK1_MOUSE | # | # | Histone modification write | Histone phosphorylation | # | # | histone | H3.1 | H3.1ph | # | UniProt: May regulate the transcription of genes that regulate cell-cycle progression through the phosphorylation of histones. Phosphorylates histone H3.1 (to form H3T11ph), which leads to epigenetic inhibition of a subset of genes. | # |
CHRAC1
(details) |
13544 | chromatin accessibility complex 1 | 54108 | Q9NRG0 | CHRC1_HUMAN | CBFD_NFYB_HMF PF00808 18-79 | Chrac1 | 2135796 | Q9JKP8 | CHRC1_MOUSE | # | # | Histone chaperone | # | 10880450 | CHRAC | DNA | # | # | 10880450 | Human homologues of two novel putative histone-fold proteins in Drosophila CHRAC are present in HuCHRAC. The two human histone-fold proteins form a stable complex that binds naked DNA but not nucleosomes. | # |
CHTOP
(details) |
24511 | chromatin target of PRMT1 | 26097 | Q9Y3Y2 | CHTOP_HUMAN | FoP_duplication PF13865 167-243 | Chtop | 1913761 | Q9CY57 | CHTOP_MOUSE | # | # | # | # | 25284789 | # | DNA | # | # | # | 5-Hydroxymethylcytosine plays a critical role in glioblastomagenesis by recruiting the CHTOP-methylosome complex. | # |
CHUK
(details) |
1974 | conserved helix-loop-helix ubiquitous kinase | 1147 | O15111 | IKKA_HUMAN | Pkinase PF00069 16-290, IKBKB_SDD PF18397 387-658, IKKbetaNEMObind PF12179 708-744 | Chuk | 99484 | Q60680 | IKKA_MOUSE | # | # | Histone modification write | Histone phosphorylation | 17434128 | # | histone | H3 | # | 17434128 | In the nucleus, IKKα=CHUK is recruited to the promoter region of the NF-κB-regulated genes by interacting with CBP, and contributes to NF-κB-mediated gene expressions through phosphorylation of histone H3. | # |
CIR1
(details) |
24217 | corepressor interacting with RBPJ, 1 | 9541 | Q86X95 | CIR1_HUMAN | Cir_N PF10197 13-49 | Cir1 | 1914185 | Q9DA19 | CIR1_MOUSE | # | # | Histone modification read | # | 9874765 | # | histone | # | # | 9874765 | CIR binds to histone deacetylase and to SAP30 and serves as a linker between CBF1 and the histone deacetylase complex. | # |
CIT
(details) |
1985 | citron rho-interacting serine/threonine kinase | 11113 | O14578 | CTRO_HUMAN | Pkinase PF00069 97-360, Pkinase_C PF00433 376-422, PH PF00169 1445-1563, CNH PF00780 1602-1855 | Cit | 105313 | P49025 | CTRO_MOUSE | # | # | Histone modification write cofactor, Histone modification write cofactor | Histone methylation, Histone phosphorylation | 18245345 | # | histone | H3K9 | H3K9me | 18245345 | Drosophila sticky/citron kinase (=CIT) is a regulator of cell-cycle progression, genetically interacts with Argonaute 1 and modulates epigenetic gene silencing. | # |
CLNS1A
(details) |
2080 | chloride channel, nucleotide-sensitive, 1A | 1207 | P54105 | ICLN_HUMAN | Voldacs PF03517 35-159 | Clns1a | 109638 | Q61189 | ICLN_MOUSE | # | # | Histone modification write cofactor | Histone methylation | # | methylosome | # | # | # | # | Part of the methylosome complex | # |
CLOCK
(details) |
2082 | clock circadian regulator | 9575 | O15516 | CLOCK_HUMAN | HLH PF00010 34-83, PAS PF00989 109-177, PAS_11 PF14598 274-377 | Clock | 99698 | O08785 | CLOCK_MOUSE | KAT, bHLH | Chromatin-modifying enzymes / K-acetyltransferases, Basic helix-loop-helix proteins | Histone modification write | Histone acetylation | # | # | histone | H3, H4 | # | # | Acetylates primarily histones H3 and H4. (Annotated by similarity.) | # |
CRB2
(details) |
18688 | crumbs family member 2 | 286204 | Q5IJ48 | CRUM2_HUMAN | EGF PF00008 110-144 149-179 188-259 321-356 361-384 609-639 811-841 1060-1092 1176-1209, Laminin_G_2 PF02210 503-587 668-775 898-1020, hEGF PF12661 1098-1128 1137-1171 | Crb2 | 2679260 | Q80YA8 | CRUM2_MOUSE | # | # | Histone modification read | # | 21423274 | # | histone | H4K20 | # | 21423274 | Table 1 in the reference. | # |
CREBBP
(details) |
2348 | CREB binding protein | 1387 | Q92793 | CBP_HUMAN | zf-TAZ PF02135 351-431 1772-1843, KIX PF02172 590-669, Bromodomain PF00439 1103-1176, RING_CBP-p300 PF06001 1192-1230, HAT_KAT11 PF08214 1340-1645, ZZ PF00569 1702-1743, Creb_binding PF09030 2035-2111 | Crebbp | 1098280 | P45481 | CBP_MOUSE | KAT | Chromatin-modifying enzymes / K-acetyltransferases | Histone modification write | Histone acetylation | 8945521 | # | histone | # | # | 8945521 | The transcriptional coactivators p300 and CBP=CREBBP are histone acetyltransferases. | # |
CSNK2A1
(details) |
2457 | casein kinase 2, alpha 1 polypeptide | 1457 | P68400 | CSK21_HUMAN | Pkinase PF00069 39-324 | Csnk2a1 | 88543 | Q60737 | CSK21_MOUSE | # | # | Histone modification | # | 24217316, 22325352 | RING2-FBRS | histone | # | # | 24217316, 22325352 | Part of a RING2 complex. | # |
CSRP2BP
(details) |
15904 | CSRP2 binding protein | 57325 | Q9H8E8 | CSR2B_HUMAN | Acetyltransf_1 PF00583 669-751 | Csrp2bp | 1917264 | Q8CID0 | CSR2B_MOUSE | # | # | Histone modification write | Histone acetylation | 19103755 | ATAC | histone | H4 | # | 19103755 | The SANT domains in ADA2a and ZZZ3/ATAC1 might enable the complex to associate with nucleosome tails in order to potentiate the catalytic activities of GCN5 and ATAC2, similar to what has been shown for the SANT domains in yeast Ada2 and Swi3. | # |
CTBP1
(details) |
2494 | C-terminal binding protein 1 | 1487 | Q13363 | CTBP1_HUMAN | 2-Hacid_dh_C PF02826 135-317 | Ctbp1 | 1201685 | O88712 | CTBP1_MOUSE | # | # | Chromatin remodeling | # | 21102443 | LSD-CoREST | chromatin | # | # | 21102443 | CtBP is a homodimer or heterodimer of CtBP1 and CtBP2 that assembles with a diverse array of factors that regulate chromatin structure. | # |
CTBP2
(details) |
2495 | C-terminal binding protein 2 | 1488 | P56545 | CTBP2_HUMAN | 2-Hacid_dh_C PF02826 141-323 | Ctbp2 | 1201686 | P56546 | CTBP2_MOUSE | # | # | Histone modification write cofactor | Histone methylation | 16702210 | # | histone | H3K9 | H3K9me, H3K9me2 | 16702210 | It is possible that CtBPs or CtBP-interacting molecules have various impacts on the G9a/GLP-mediated (a SET-domain mammalian histone methyltransferase responsible for mono- and dimethylation of lysine 9 in histone H3 (H3K9)) functions through Wiz interaction. | # |
CTCF
(details) |
13723 | CCCTC-binding factor (zinc finger protein) | 10664 | P49711 | CTCF_HUMAN | zf-C2H2 PF00096 266-288 294-316 322-345 351-373 379-401 437-460 555-575 | Ctcf | 109447 | Q61164 | CTCF_MOUSE | ZNF | Zinc fingers, C2H2-type | Chromatin remodeling, TF | TF activator | 16949368 | # | DNA | DNA motif | # | 16949368 | A CTCF-CHD8 complex is involved in both enhancer blocking and epigenetic remodeling at chromatin boundary in vivo. | # |
CTCFL
(details) |
16234 | CCCTC-binding factor (zinc finger protein)-like | 140690 | Q8NI51 | CTCFL_HUMAN | zf-C2H2 PF00096 313-336 342-364 398-421 428-451 546-566 | Ctcfl | 3652571 | A2APF3 | CTCFL_MOUSE | ZNF | Zinc fingers, C2H2-type | Chromatin remodeling | # | 18765639 | # | DNA | # | # | 18765639 | BORIS=CTCFL acts as a scaffold upon which BAT3 and SET1A assemble and through which BAT3 and SET1A exert their effects upon chromatin structure and gene expression. In contrast to CTCF, BORIS appears to be a methylation-independent DNA-binding protein (28b) that activates, rather than inhibits, gene expression. | # |
CTR9
(details) |
16850 | CTR9, Paf1/RNA polymerase II complex component | 9646 | Q6PD62 | CTR9_HUMAN | TPR_19 PF14559 170-231 508-564 715-750, TPR_8 PF13181 312-373 681-714, TPR_10 PF13374 451-484, domain PF13432 567-680 | Ctr9 | 109345 | Q62018 | CTR9_MOUSE | TTC | Tetratricopeptide (TTC) repeat domain containing | Histone modification cofactor | # | 24036311 | # | histone | H3K36 | # | # | CTR9/PAF1c regulates molecular lineage identity, histone H3K36 trimethylation and genomic imprinting during preimplantation development. | # |
CUL1
(details) |
2551 | cullin 1 | 8454 | Q13616 | CUL1_HUMAN | Cullin PF00888 20-662, Cullin_Nedd8 PF10557 706-766 | Cul1 | 1349658 | Q9WTX6 | CUL1_MOUSE | # | # | Chromatin remodeling cofactor | # | 9663463 | # | histone | H3K9me3, H3K36me3, H1.4K26me3 | H3K9, H3K36, H1.4K26 | 21757720 | The SKP1-Cul1-F-box and leucine-rich repeat protein 4 (SCF-FbxL4) ubiquitin ligase regulates lysine demethylase 4A (KDM4A)/Jumonji domain-containing 2A (JMJD2A) protein. The JMJD2/KDM43 histone demethylase family removes trimethylated H3K9, H3K36, and H1.4K26 . | # |
CUL2
(details) |
2552 | cullin 2 | 8453 | Q13617 | CUL2_HUMAN | Cullin PF00888 13-644, Cullin_Nedd8 PF10557 675-736 | Cul2 | 1918995 | Q9D4H8 | CUL2_MOUSE | # | # | Chromatin remodeling cofactor | # | # | # | chromatin | HP1 (Heterochromatin protein 1) | # | 9122164 | The VHL-HP1 (heterochromatin protein 1) interaction recruits VHL to chromatin. VHL interacts with elongin B, elongin C, and cullin 2 through its α domain and these proteins form an E3 ubiquitin ligase complex. | # |
CUL3
(details) |
2553 | cullin 3 | 8452 | Q13618 | CUL3_HUMAN | Cullin PF00888 34-665, Cullin_Nedd8 PF10557 698-760 | Cul3 | 1347360 | Q9JLV5 | CUL3_MOUSE | # | # | Histone modification write | Histone ubiquitination | 15897469 | # | histone | MACROH2A | # | 15897469 | E3 ubiquitin ligase consisting of SPOP and CULLIN3=CUL3 is able to ubiquitinate the Polycomb group protein BMI1 and the variant histone MACROH2A. | # |
CUL4A
(details) |
2554 | cullin 4A | 8451 | Q13619 | CUL4A_HUMAN | Cullin PF00888 63-661, Cullin_Nedd8 PF10557 691-751 | Cul4a | 1914487 | Q3TCH7 | CUL4A_MOUSE | # | # | Histone modification write | Histone ubiquitination | 16678110 | # | histone | H3, H4 | # | 16678110 | Results shown in Figure 4A demonstrate that knockdown of CUL4A or CUL4B significantly reduces H3 and H4 ubiquitylation levels, indicating that both CUL4A and CUL4B contribute to histone H3 and H4 ubiquitylation in vivo. | # |
CUL4B
(details) |
2555 | cullin 4B | 8450 | Q13620 | CUL4B_HUMAN | Cullin PF00888 214-814, Cullin_Nedd8 PF10557 844-905 | Cul4b | 1919834 | A2A432 | CUL4B_MOUSE | # | # | Histone modification write | Histone ubiquitination | 16678110 | # | histone | H3, H4 | # | 16678110 | Results shown in Figure 4A demonstrate that knockdown of CUL4A or CUL4B significantly reduces H3 and H4 ubiquitylation levels, indicating that both CUL4A and CUL4B contribute to histone H3 and H4 ubiquitylation in vivo. | # |
CUL5
(details) |
2556 | cullin 5 | 8065 | Q93034 | CUL5_HUMAN | Cullin PF00888 18-671, Cullin_Nedd8 PF10557 711-772 | Cul5 | 1922967 | Q9D5V5 | CUL5_MOUSE | # | # | DNA modification cofactor | DNA methylation | 20847044 | # | DNA | # | # | 20847044 | In cancer cells, many promoters become aberrantly methylated through the activity of the de novo DNA methyltransferases DNMT3a and DNMT3b and acquire repressive chromatin marks, and, indeed, DNMT3b interacted with CUL1, CUL2, CUL3, CUL4A, and CUL5. | # |
CXXC1
(details) |
24343 | CXXC finger protein 1 | 30827 | Q9P0U4 | CXXC1_HUMAN | PHD PF00628 29-73, zf-CXXC PF02008 163-208, CpG_bind_C PF12269 400-636 | Cxxc1 | 1921572 | Q9CWW7 | CXXC1_MOUSE | PHF | Zinc fingers, PHD-type | Chromatin remodeling, TF | # | 21407193 | COMPASS | DNA | CG, DNA motif | # | 21407193 | CFP1=CXXC1 is a CXXC domain-containing protein. CXXC domain proteins direct different chromatin-modifying activities to various chromatin regions. | # |
DAPK3
(details) |
2676 | death-associated protein kinase 3 | 1613 | O43293 | DAPK3_HUMAN | Pkinase PF00069 13-275 | Dapk3 | 1203520 | O54784 | DAPK3_MOUSE | # | # | Histone modification write | Histone phosphorylation | 12560483 | # | histone | H3T11 | # | 12560483 | Dlk/ZIP=DAPK3 kinase phosphorylates histone H3 at a novel site, Thr11, rather than Ser10, which is characteristic of mitotic chromosomes. | # |
DAXX
(details) |
2681 | death-domain associated protein | 1616 | Q9UER7 | DAXX_HUMAN | Daxx PF03344 56-145, DAXX_hist_bd PF20920 301-381 | Daxx | 1197015 | O35613 | DAXX_MOUSE | # | # | # | # | 23075851 | # | histone | H3.3 | # | # | DAXX envelops a histone H3.3-H4 dimer for H3.3-specific recognition. | # |
DDB1
(details) |
2717 | damage-specific DNA binding protein 1, 127kDa | 1642 | Q16531 | DDB1_HUMAN | MMS1_N PF10433 75-542, CPSF_A PF03178 788-1100 | Ddb1 | 1202384 | Q3U1J4 | DDB1_MOUSE | # | # | Histone modification write | Histone ubiquitination | 16678110 | # | histone | H2A | # | 16678110 | DDB1-CUL4ADDB2 E3 in vivo targets histone H2A for ubiquitination at UV-damage DNA sites, where DDB2 serves as the substrate receptor. | # |
DDB2
(details) |
2718 | damage-specific DNA binding protein 2, 48kDa | 1643 | Q92466 | DDB2_HUMAN | WD40 PF00400 234-271 284-316 | Ddb2 | 1355314 | Q99J79 | DDB2_MOUSE | WDR | WD repeat domain containing | Histone modification write cofactor | Histone ubiquitination | 16678110 | # | histone | # | # | 16678110 | DDB1-CUL4ADDB2 E3 in vivo targets histone H2A for ubiquitination at UV-damage DNA sites, where DDB2 serves as the substrate receptor. | # |
DDX17
(details) |
2740 | Probable ATP-dependent RNA helicase DDX17 (EC 3.6.4.13) (DEAD box protein 17) (DEAD box protein p72) (DEAD box protein p82) (RNA-dependent helicase p72) | 10521 | Q92841 | DDX17_HUMAN | DEAD PF00270 195-365, Helicase_C PF00271 405-512 | Ddx17 | 1914290 | Q501J6 | DDX17_MOUSE | DDX | DEAD-box helicases | RNA modification | Alternative splicing | 24910439 | # | RNA | mRNA | # | 24910439 | Coregulator of master transcriptional regulators of differentiation | New |
DDX21
(details) |
2744 | DEAD (Asp-Glu-Ala-Asp) box helicase 21 | 9188 | Q9NR30 | DDX21_HUMAN | DEAD PF00270 211-383, Helicase_C PF00271 434-532, GUCT PF08152 620-708 | Ddx21 | 1860494 | Q9JIK5 | DDX21_MOUSE | DDX | DEAD-boxes | RNA modification | # | 11237763 | B-WICH | RNA | # | # | 11237763 | Human RNA helicase II/Gu (hRH II/Gu) protein unwinds double-stranded RNA, folds single-stranded RNA, and may play important roles in ribosomal RNA biogenesis, RNA editing, RNA transport, and general transcription. | # |
DDX5
(details) |
2746 | Probable ATP-dependent RNA helicase DDX5 (EC 3.6.4.13) (DEAD box protein 5) (RNA helicase p68) | 1655 | P17844 | DDX5_HUMAN | DEAD PF00270 118-288, Helicase_C PF00271 328-435, P68HR PF08061 500-532 551-583 | Ddx5 | 105037 | Q61656 | DDX5_MOUSE | DDX | DEAD-box helicases | RNA modification | Alternative splicing | 24910439 | # | RNA | RNA | # | 24910439 | Coregulator of master transcriptional regulators of differentiation | New |
DDX50
(details) |
17906 | DEAD (Asp-Glu-Ala-Asp) box polypeptide 50 | 79009 | Q9BQ39 | DDX50_HUMAN | DEAD PF00270 162-334, Helicase_C PF00271 385-483, GUCT PF08152 574-662 | Ddx50 | 2182303 | Q99MJ9 | DDX50_MOUSE | DDX | DEAD-boxes | RNA modification | # | 11823437 | # | RNA | # | # | 11823437 | In addition to the proposed role of DEAD-box RNA helicases in transcription, some of these enzymes promote mRNA translation. | # |
DEK
(details) |
2768 | DEK proto-oncogene | 7913 | P35659 | DEK_HUMAN | DEK_C PF08766 320-374 | Dek | 1926209 | Q7TNV0 | DEK_MOUSE | # | # | Chromatin remodeling | # | 17524367 | B-WICH | histone | H4 | # | 17524367 | It has been suggested that DEK functions as an “architectural” protein in chromatin. This is because DEK changes the structure of the DNA to which it is bound and could therefore influence gene activity. | # |
DHX9
(details) |
2750 | ATP-dependent RNA helicase A (EC 3.6.4.13) (DEAH box protein 9) (DExH-box helicase 9) (Leukophysin) (LKP) (Nuclear DNA helicase II) (NDH II) (RNA helicase A) | 1660 | Q08211 | DHX9_HUMAN | dsrm PF00035 4-70 180-251, DEAD PF00270 395-547, Helicase_C PF00271 639-768, HA2_N PF04408 832-860, HA2_C PF21010 861-919, OB_NTP_bind PF07717 991-1073 | Dhx9 | 108177 | O70133 | DHX9_MOUSE | DHX | DEAH-box helicases | RNA modification | Alternative splicing | 28221134 | # | RNA | mRNA | # | 28221134 | Regulates alternative splicing of E1A | New |
DMAP1
(details) |
18291 | DNA methyltransferase 1 associated protein 1 | 55929 | Q9NPF5 | DMAP1_HUMAN | SANT_DAMP1_like PF16282 124-202, DMAP1 PF05499 242-400 | Dmap1 | 1913483 | Q9JI44 | DMAP1_MOUSE | # | # | Chromatin remodeling | # | 14966270 | NuA4, NuA4-related complex, SRCAP | chromatin | # | # | 14966270 | SANT-domain protein DMAP1 links NuA4 to DNA replication and is also present in distinct proteins | # |
DNAJC1
(details) |
20090 | DnaJ (Hsp40) homolog, subfamily C, member 1 | 64215 | Q96KC8 | DNJC1_HUMAN | DnaJ PF00226 65-126, Myb_DNA-binding PF00249 496-541 | Dnajc1 | 103268 | Q61712 | DNJC1_MOUSE | DNAJ | Heat shock proteins / DNAJ (HSP40) | Histone modification write cofactor, Histone modification erase cofactor | Histone acetylation, Histone deacetylation | 16271702 | # | histone | # | # | 16271702 | HTJ1=DNAJC1 consists of two SANT domains separated by a spacer region. SANT domains can also mediate protein–protein interaction, particularly with histone deacetylases and histone acetyl transferases. | # |
DNAJC2
(details) |
13192 | DnaJ (Hsp40) homolog, subfamily C, member 2 | 27000 | Q99543 | DNJC2_HUMAN | DnaJ PF00226 88-157, domain PF21884 178-283, RAC_head PF16717 340-426, Myb_DNA-binding PF00249 553-599 | Dnajc2 | 99470 | P54103 | DNJC2_MOUSE | DNAJ | Heat shock proteins / DNAJ (HSP40) | Histone modification read | # | 21179169 | # | histone | H2A | # | 21179169 | The ubiquitin mark at histone H2A may be a docking site for ZRF1. | # |
DND1
(details) |
23799 | DND microRNA-mediated repression inhibitor 1 | 373863 | Q8IYX4 | DND1_HUMAN | RRM_1 PF00076 60-122, DND1_DSRM PF14709 256-331 | Dnd1 | 2447763 | Q6VY05 | DND1_MOUSE | RBM | RNA binding motif (RRM) containing | RNA modification | # | 23890083 | # | RNA | # | # | 23890083 | The RNA binding protein DEAD-END (DND1) is one of the few proteins known to regulate microRNA (miRNA) activity at the level of miRNA-mRNA interaction. APOBEC3G may bind mRNAs (maybe together with DND1) and subsequently interact with components of the miRISC to activate translation repression or interact with translation initiation factors to inhibit them. APOBEC3G may bind to DND1 and sequester it away from mRNAs and miRNAs, the cytidine deaminase activity of APOBEC3 may allow it to edit the 3′-UTR sequences of P27, LATS2 and CX43 to inhibit DND1 binding. | # |
DNMT1
(details) |
2976 | DNA (cytosine-5-)-methyltransferase 1 | 1786 | P26358 | DNMT1_HUMAN | DMAP_binding PF06464 19-101, DNMT1-RFD PF12047 394-535, zf-CXXC PF02008 646-691, BAH PF01426 755-878 931-1100, DNA_methylase PF00145 1140-1592 | Dnmt1 | 94912 | P13864 | DNMT1_MOUSE | # | # | DNA modification | DNA methylation | 18754681 | # | DNA | dhC | dhU | 18754681 | The CXXC region (C is cysteine; X is any amino acid) of DNMT1 binds specifically to unmethylated CpG dinucleotides. Thus, the CXXC domain encompassing the amino terminus region of DNMT1 cooperates with the catalytic domain for DNA methyltransferase activity. | # |
DNMT3A
(details) |
2978 | DNA (cytosine-5-)-methyltransferase 3 alpha | 1788 | Q9Y6K1 | DNM3A_HUMAN | domain PF22855 1-283, PWWP PF00855 293-374, ADD_DNMT3 PF17980 476-530, ADDz_Dnmt3b PF21255 537-586, DNA_methylase PF00145 634-766 | Dnmt3a | 1261827 | O88508 | DNM3A_MOUSE | # | # | DNA modification | DNA methylation | 12138111 | # | DNA | dhC | dhU | 12138111 | One form of Dnmt3a has been identified and shown to be capable of methylating DNA bothin vitro and in vivo. | # |
DNMT3B
(details) |
2979 | DNA (cytosine-5-)-methyltransferase 3 beta | 1789 | Q9UBC3 | DNM3B_HUMAN | PWWP PF00855 226-309, ADD_DNMT3 PF17980 423-471, ADDz_Dnmt3b PF21255 478-527, DNA_methylase PF00145 575-707 | Dnmt3b | 1261819 | O88509 | DNM3B_MOUSE | # | # | DNA modification | DNA methylation | 10325416 | # | DNA | dhC | dhU | 10325416 | DNA methyltransferases (Dnmt3a and Dnmt3b) in mouse methylate hemimethylated and unmethylated templates with equal efficiencies and are candidates for de novo methyltransferases. | # |
DNMT3L
(details) |
2980 | DNA (cytosine-5-)-methyltransferase 3-like | 29947 | Q9UJW3 | DNM3L_HUMAN | ADD_DNMT3 PF17980 37-87, ADDz_Dnmt3b PF21255 96-146 | Dnmt3l | 1859287 | Q9CWR8 | DNM3L_MOUSE | # | # | Histone modification read | # | 17687327 | # | histone | H3K4 | # | 17687327 | DNMT3L specifically interacts with the extreme amino terminus of histone H3, this interaction is strongly inhibited by methylation at lysine 4 of histone H3. | # |
DNTTIP2
(details) |
24013 | deoxynucleotidyltransferase, terminal, interacting protein 2 | 30836 | Q5QJE6 | TDIF2_HUMAN | Fcf2 PF08698 640-732 | Dnttip2 | 1923173 | Q8R2M2 | TDIF2_MOUSE | # | # | Chromatin remodeling | # | 12786946 | # | histone | H2A, H2B | # | 12786946 | TdIF2 would function as a chromatin remodeling protein at the N region synthesis. | # |
DOT1L
(details) |
24948 | DOT1-like histone H3K79 methyltransferase | 84444 | Q8TEK3 | DOT1L_HUMAN | DOT1 PF08123 117-317 | Dot1l | 2143886 | - | - | KMT | Chromatin-modifying enzymes / K-methyltransferases | Histone modification write | Histone methylation | 12123582 | # | histone | H3K79 | # | 12123582 | Human DOT1-like (DOT1L) protein possesses intrinsic H3-K79-specific histone methyltransferase (HMTase) activity in vitro and in vivo. | # |
DPF1
(details) |
20225 | D4, zinc and double PHD fingers family 1 | # | Q92782 | DPF1_HUMAN | DPF1-3_N PF14051 14-83, PHD PF00628 274-325 327-372 | Dpf1 | 1352748 | Q9QX66 | DPF1_MOUSE | PHF | Zinc fingers, PHD-type | Chromatin remodeling cofactor | # | 21931736 | nBAF, SWI/SNF BRM-BRG1 | chromatin | # | # | 21931736 | Belongs to the neuron-specific chromatin remodeling complex (nBAF complex). Baf45b=DPF1 and Baf53b are both brain specific components of the SWI/SNF complex varaint nBAF. | # |
DPF2
(details) |
9964 | D4, zinc and double PHD fingers family 2 | 5977 | Q92785 | REQU_HUMAN | DPF1-3_N PF14051 14-81, PHD PF00628 273-327 330-374 | Dpf2 | 109529 | Q61103 | REQU_MOUSE | PHF | Zinc fingers, PHD-type | Chromatin remodeling | # | 21888896 | SWI/SNF BRM-BRG1 | histone, DNA | # | # | 21888896 | The different domains of DPF2 may function in a cooperative manner in some intracellular processes, which could bind histone and DNA via tandem PHD domain and C2H2 ZF domain, respectively in the context of nucleosome. | # |
DPF3
(details) |
17427 | D4, zinc and double PHD fingers, family 3 | 8110 | Q92784 | DPF3_HUMAN | DPF1-3_N PF14051 14-84, PHD PF00628 261-316 319-363 | Dpf3 | 1917377 | P58269 | DPF3_MOUSE | PHF | Zinc fingers, PHD-type | Chromatin remodeling | # | 21423274 | BAF, nBAF, SWI/SNF BRM-BRG1 | histone | H3, H4 | # | 21423274 | Table 1 in the reference. DPF3 is associated with the BAF chromatin remodeling complex and binds methylated and acetylated lysine residues of histone 3 and 4. | # |
DPPA3
(details) |
19199 | developmental pluripotency associated 3 | 359787 | Q6W0C5 | DPPA3_HUMAN | PGC7_Stella PF15549 4-143 | Dppa3 | 1920958 | Q8QZY3 | DPPA3_MOUSE | # | # | Histone modification read | # | # | # | histone | H3K9me2 | # | # | Specifically recognizes and binds histone H3 dimethylated at 'Lys-9' (H3K9me2) on maternal genome, | # |
DPY30
(details) |
24590 | dpy-30 homolog (C. elegans) | 84661 | Q9C005 | DPY30_HUMAN | Dpy-30 PF05186 52-92 | Dpy30 | 1913560 | Q99LT0 | DPY30_MOUSE | # | # | Histone modification write cofactor | Histone methylation | 19556245 | COMPASS, Menin-associated_HMT, MLL-HCF, CHD8, MLL2/3, COMPASS-like MLL1,2, MLL4/WBP7, COMPASS-like MLL3,4 | histone | # | # | 19556245 | The isolated MLL1 SET domain is an H3K4 monomethyltransferase. When the MLL1 SET domain fragment is assembled with a complex containing WDR5, RbBP5, Ash2L, and DPY-30, the rate of lysine methylation is dramatically increased, but only to the dimethyl form of H3K4, suggesting that the MLL1 core complex is predominantly a dimethyltransferase. | # |
DR1
(details) |
3017 | down-regulator of transcription 1, TBP-binding (negative cofactor 2) | 1810 | Q01658 | NC2B_HUMAN | CBFD_NFYB_HMF PF00808 12-75 | Dr1 | 1100515 | Q91WV0 | NC2B_MOUSE | # | # | Histone chaperone | # | 18838386 | ATAC | histone | # | # | 18838386 | YEATS2-NC2beta=DR1 histone fold module that interacts with the TATA-binding protein (TBP) and negatively regulates transcription when recruited to a promoter. | # |
DTX3L
(details) |
30323 | deltex 3 like, E3 ubiquitin ligase | 151636 | Q8TDB6 | DTX3L_HUMAN | DTX3L_a-b PF21717 134-194, DTX3L_KH-like PF21718 235-357 373-508, zf-C3HC4_2 PF13923 561-599, DTC PF18102 608-739 | Dtx3l | 2656973 | Q3UIR3 | DTX3L_MOUSE | RNF | RING-type (C3HC4) zinc fingers | Histone modification write | Histone ubiquitination | 19818714 | # | histone | H4K91 | # | 19818714 | BBAP=DTX3L selectively monoubiquitylates histone H4 lysine 91 and protects cells exposed to DNA-damaging agents. | # |
DZIP3
(details) |
30938 | DAZ interacting zinc finger protein 3 | 9666 | Q86Y13 | DZIP3_HUMAN | TTC3_DZIP3_dom PF19179 229-330, HEPN_DZIP3 PF18738 421-546, zf-RING_2 PF13639 1148-1188 | Dzip3 | 1917433 | Q7TPV2 | DZIP3_MOUSE | RNF, PPP1R | RING-type (C3HC4) zinc fingers, Serine/threonine phosphatases / Protein phosphatase 1, regulatory subunits | Histone modification write | Histone ubiquitination | 18206970 | # | histone, RNA | H2AK119 | H2AK119ub | 18206970 | The N-CoR/HDAC1/3 complex specifically recruits a previously-unidentified specific histone H2A ubiquitin ligase, 2A-HUB/hRUL138 = DZIP3, to a subset of regulated gene promoters. | # |
E2F6
(details) |
3120 | E2F transcription factor 6 | 1876 | O75461 | E2F6_HUMAN | E2F_TDP PF02319 65-128, E2F_CC-MB PF16421 143-237 | E2f6 | 1354159 | O54917 | E2F6_MOUSE | # | # | TF | TF repressor | # | RING2-L3MBTL2, CHD8, MLL2/3, MLL4/WBP7 | DNA | DNA motif | # | # | Epigenetic complex (MLL) partner. | # |
EED
(details) |
3188 | embryonic ectoderm development | 8726 | O75530 | EED_HUMAN | WD40 PF00400 181-219 233-264 400-437 | Eed | 95286 | Q921E6 | EED_MOUSE | WDR | WD repeat domain containing | Polycomb group (PcG) protein | # | 9584199 | PRC2 | # | # | # | 9584199 | Enx1/EZH2 and EED are members of a class of PcG proteins that is distinct from previously described human PcG proteins. | # |
EEF1AKMT3
(details) |
24936 | EEF1A lysine methyltransferase 3 | 25895 | Q96AZ1 | EFMT3_HUMAN | Methyltransf_16 PF10294 38-195 | Eef1akmt3 | 3645330 | D3YWP0 | EFMT3_MOUSE | METTL | Methyltransferase like | Protein modification | Protein methylation | 28108655 | # | protein | Lys165 of eEF1A | K165m | 28108655 | Modulates mRNA translation | New |
EEF1AKMT4
(details) |
53611 | EEF1A lysine methyltransferase 4 | 110599564 | P0DPD7 | EFMT4_HUMAN | Methyltransf_11 PF08241 63-172 | Eef1akmt4 | 5903914 | P0DPE0 | EFMT4_MOUSE | # | # | Protein modification | Protein methylation | 28520920 | # | protein | eEF1A (elongation factor alpha) | methylation K36 | 28520920 | Regulates interaction between eEF1A and aminoacyl-t-RNA and gene expression. | New |
EEF1AKNMT
(details) |
24248 | eEF1A lysine and N-terminal methyltransferase | 51603 | Q8N6R0 | EFNMT_HUMAN | domain PF13649 53-157, Spermine_synth PF01564 493-616 | Eef1aknmt | 1918699 | Q91YR5 | EFNMT_MOUSE | METTL | Methyltransferase like | Protein modification | Protein methylation | 30143613 | # | protein | Lys55 of eEF1A | K55m | 30143613 | Modulates mRNA translation | New |
EHMT1
(details) |
24650 | euchromatic histone-lysine N-methyltransferase 1 | 79813 | Q9H9B1 | EHMT1_HUMAN | EHMT1-2_CRR PF21533 539-633, Ank_4 PF13637 772-836, Ank_2 PF12796 838-904 907-990, Pre-SET PF05033 1015-1118, SET PF00856 1137-1243 | Ehmt1 | 1924933 | Q5DW34 | EHMT1_MOUSE | KMT, ANKRD | Chromatin-modifying enzymes / K-methyltransferases, Ankyrin repeat domain containing | Histone modification write | Histone methylation | 18264113 | # | histone | H3K9 | H3K9me1, H3K9me2 | 18264113 | G9a and G9a-like protein (GLP)=EHMT1 are euchromatin-associated methyltransferases that repress transcription by mono- and dimethylating histone H3 at Lys9 (H3K9). | # |
EHMT2
(details) |
14129 | euchromatic histone-lysine N-methyltransferase 2 | 10919 | Q96KQ7 | EHMT2_HUMAN | EHMT1-2_CRR PF21533 447-540, Ank_2 PF12796 655-746 750-816, Ank PF00023 850-882, Pre-SET PF05033 927-1030, SET PF00856 1049-1155 | Ehmt2 | 2148922 | Q9Z148 | EHMT2_MOUSE | KMT, ANKRD | Chromatin-modifying enzymes / K-methyltransferases, Ankyrin repeat domain containing | Histone modification write | Histone methylation | 18264113 | # | histone | H3K9 | H3K9me1, H3K9me2 | 18264113 | G9a=EHMT2 and G9a-like protein (GLP) are euchromatin-associated methyltransferases that repress transcription by mono- and dimethylating histone H3 at Lys9 (H3K9). | # |
EID1
(details) |
1191 | EP300 interacting inhibitor of differentiation 1 | 23741 | Q9Y6B2 | EID1_HUMAN | Eid1 | 1889651 | Q9DCR4 | EID1_MOUSE | # | # | Histone modification write cofactor | Histone acetylation | 11073990 | # | histone | # | # | 11073990 | Inhibition of MyoD may be explained by EID-1's ability to bind and inhibit p300's histone acetylase activity, an essential MyoD coactivator. Thus, EID-1 binds both Rb and p300 and is a novel repressor of MyoD function. | # | |
EID2
(details) |
28292 | EP300 interacting inhibitor of differentiation 2 | 163126 | Q8N6I1 | EID2_HUMAN | Eid2 | 2681174 | Q6X7S9 | EID2_MOUSE | # | # | Histone modification write cofactor | Histone acetylation | 14585496 | # | histone | # | # | 14585496 | Overexpression of EID-2 inhibits muscle-specific gene expression through inhibition of MyoD-dependent transcription. This inhibitory effect on gene expression can be explained by EID-2's ability to associate with and inhibit the acetyltransferase activity of p300. These data suggest that EID-1 and -2 represent a novel family of proteins that negatively regulate differentiation through a p300-dependent mechanism. | # | |
EID2B
(details) |
26796 | EP300 interacting inhibitor of differentiation 2B | 126272 | Q96D98 | EID2B_HUMAN | Eid2b | 1924095 | # | # | # | # | Histone modification erase cofactor | Histone acetylation | 15970276 | # | histone | # | # | 15970276 | The transrepressional function of EID-2 depends on recruitment of class I histone deacetylases (HDACs). HDACs participate in the dynamic process of chromatin remodeling, forming corepressor complexes that repress transcription by deacetylating histones and transcription factors. | # | |
EIF4A3
(details) |
18683 | Eukaryotic initiation factor 4A-III (eIF-4A-III) (eIF4A-III) (EC 3.6.4.13) (ATP-dependent RNA helicase DDX48) (ATP-dependent RNA helicase eIF4A-3) (DEAD box protein 48) (Eukaryotic initiation factor 4A-like NUK-34) (Eukaryotic translation initiation factor 4A isoform 3) (Nuclear matrix protein 265) (NMP 265) (hNMP 265) [Cleaved into: Eukaryotic initiation factor 4A-III, N-terminally processed] | 9775 | P38919 | IF4A3_HUMAN | DEAD PF00270 63-225, Helicase_C PF00271 264-372 | EIf4A3 | 1923731 | Q91VC3 | IF4A3_MOUSE | DDX | DEAD-box helicases | RNA modification | Alternative splicing | 22203037 | # | RNA | mRNA | # | 22203037 | Production of the proapoptotic Bcl-x(S) splice variant. | New |
ELP2
(details) |
18248 | elongator acetyltransferase complex subunit 2 | 55250 | Q6IA86 | ELP2_HUMAN | WD40 PF00400 51-91 103-143 200-237 275-320 381-415 606-641 665-696 | Elp2 | 1889642 | Q91WG4 | ELP2_MOUSE | ELP, WDR | Elongator acetyltransferase complex subunits, WD repeat domain containing | Histone modification write cofactor | Histone acetylation | 11818576 | Pol2 elongator | histone | # | # | 11818576 | Acts as subunit of the RNA polymerase II elongator complex, which is a histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. | # |
ELP3
(details) |
20696 | elongator acetyltransferase complex subunit 3 | 55140 | Q9H9T3 | ELP3_HUMAN | Radical_SAM PF04055 107-295, Radical_SAM_C PF16199 312-392 | Elp3 | 1921445 | Q9CZX0 | ELP3_MOUSE | KAT, ELP | Chromatin-modifying enzymes / K-acetyltransferases, Elongator acetyltransferase complex subunits | Histone modification write | Histone acetylation | 11818576 | Pol2 elongator | histone | H3, H4? | # | 11818576 | Elp3 contains domains characteristic of proteins with acetyltransferase activity, and its complex was found to acetylate histones, with specificity to H3 and to a much lesser extent H4. | # |
ELP4
(details) |
1171 | elongator acetyltransferase complex subunit 4 | 26610 | Q96EB1 | ELP4_HUMAN | PAXNEB PF05625 48-400 | Elp4 | 1925016 | Q9ER73 | ELP4_MOUSE | ELP | Elongator acetyltransferase complex subunits | Histone modification write cofactor | Histone acetylation | 11714725 | Pol2 elongator | histone | # | # | 11714725 | The three small holo-Elongator subunits, hELP4, p38, and p30, are required to activate the HAT activity of hELP3, or one of these proteins may have intrinsic HAT activity. | # |
ELP5
(details) |
30617 | elongator acetyltransferase complex subunit 5 | 23587 | Q8TE02 | ELP5_HUMAN | Elong_Iki1 PF10483 11-181 222-281 | Elp5 | 1859017 | Q99L85 | ELP5_MOUSE | ELP | Elongator acetyltransferase complex subunits | Histone modification write cofactor | Histone acetylation | 11904415 | Pol2 elongator | histone | H3K14, H4K8 | # | 11904415 | The elongating, hyperphosphorylated form of RNA polymerase II is associated with the Elongator complex, which has the histone acetyltransferase (HAT) Elp3 as a subunit. The three smallest Elongator subunits--Elp4, Elp5, and Elp6--are required for HAT activity, and Elongator binds to both naked and nucleosomal DNA. Elongator may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4. | # |
ELP6
(details) |
25976 | elongator acetyltransferase complex subunit 6 | 54859 | Q0PNE2 | ELP6_HUMAN | ELP6 PF09807 4-251 | Elp6 | 1919349 | Q8BK75 | ELP6_MOUSE | ELP | Elongator acetyltransferase complex subunits | Histone modification write cofactor | Histone acetylation | 22854966 | Pol2 elongator | histone | # | # | 22854966 | The Elongator complex is composed of 6 subunits (Elp1-Elp6) and promotes RNAPII transcript elongation through histone acetylation in the nucleus as well as tRNA modification in the cytoplasm. DERP6/ELP5 and C3ORF75/ELP6 are key players for migration, invasion and tumorigenicity of melanoma cells, as integral subunits of Elongator. | # |
ENY2
(details) |
24449 | enhancer of yellow 2 homolog (Drosophila) | 56943 | Q9NPA8 | ENY2_HUMAN | EnY2 PF10163 13-95 | Eny2 | 1919286 | Q9JIX0 | ENY2_MOUSE | # | # | Histone modification erase cofactor | Histone ubiquitination | 18206972 | SAGA | histone | # | # | 18206972 | ATXN7L3, USP22, and ENY2 are required as cofactors for the full transcriptional activity by nuclear receptors. Thus, the deubiquitinase activity of the TFTC/STAGA HAT complex is necessary to counteract heterochromatin silencing and acts as a positive cofactor for activation by nuclear receptors in vivo. | # |
EP300
(details) |
3373 | E1A binding protein p300 | 2033 | Q09472 | EP300_HUMAN | zf-TAZ PF02135 335-415 1734-1806, KIX PF02172 567-648, Bromodomain PF00439 1067-1141, RING_CBP-p300 PF06001 1156-1194, HAT_KAT11 PF08214 1306-1611, ZZ PF00569 1665-1706, Creb_binding PF09030 2015-2097 | Ep300 | 1276116 | B2RWS6 | EP300_MOUSE | KAT | Chromatin-modifying enzymes / K-acetyltransferases | Histone modification write | Histone acetylation | 17065153 | # | histone | H2A, H2B, H3, H4 | # | 17065153 | Acetylation of proteins by p300=EP300 histone acetyltransferase plays a critical role in the regulation of gene expression. | # |
EP400
(details) |
11958 | E1A binding protein p400 | 57634 | Q96L91 | EP400_HUMAN | EP400_N PF15790 30-489, HSA PF07529 803-869 2178-2241, SNF2-rel_dom PF00176 1094-1372, Helicase_C PF00271 1899-2012 | Ep400 | 1276124 | Q8CHI8 | EP400_MOUSE | # | # | Chromatin remodeling, Histone modification write | Histone acetylation | 20876283 | SWR, NuA4, NuA4-related complex | histone | # | # | 20876283 | p400 is a novel DNA damage response protein and p400-mediated alterations in nucleosome and chromatin structure promote both chromatin ubiquitination and the accumulation of brca1 and 53BP1 at sites of DNA damage. | # |
EPC1
(details) |
19876 | enhancer of polycomb homolog 1 (Drosophila) | 80314 | Q9H2F5 | EPC1_HUMAN | EPL1 PF10513 6-148, E_Pc_C PF06752 581-836 | Epc1 | 1278322 | Q8C9X6 | EPC1_MOUSE | # | # | Polycomb group (PcG) protein | # | 14966270 | NuA4, Piccolo_NuA4, NuA4-related complex | histone | # | # | 14966270 | The Enhancer of Polycomb homology domain of human EPC1, like Epl1 in yeast (7), is a conserved functional key for histone acetylation since it bridges the MYST HAT with the ING protein to enable potent nucleosome histone acetyltransferase activity. | # |
EPC2
(details) |
24543 | enhancer of polycomb homolog 2 (Drosophila) | 26122 | Q52LR7 | EPC2_HUMAN | EPL1 PF10513 4-148, E_Pc_C PF06752 575-807 | Epc2 | 1278321 | Q8C0I4 | EPC2_MOUSE | # | # | Chromatin remodeling | # | 19898529 | # | chromatin | # | # | # | NuA4 and SWR1-C: two chromatin-modifying complexes with overlapping functions and components | # |
ERBB4
(details) |
3432 | v-erb-b2 avian erythroblastic leukemia viral oncogene homolog 4 | 2066 | Q15303 | ERBB4_HUMAN | Recep_L_domain PF01030 55-166 358-477, Furin-like PF00757 184-335, GF_recep_IV PF14843 502-633, TM_ErbB1 PF21314 653-687, PK_Tyr_Ser-Thr PF07714 718-974 | Erbb4 | 104771 | Q61527 | ERBB4_MOUSE | # | # | Histone modification cofactor | # | 23230144 | # | histone | H3K9me3 | # | 23230144 | ErbB4 intracellular domain (4ICD) that translocates into the nucleus to control gene expression through inhibiting an increase of H3K9me3. | # |
ERCC6
(details) |
3438 | excision repair cross-complementation group 6 | 2074 | Q03468 | ERCC6_HUMAN | SNF2-rel_dom PF00176 509-810, Helicase_C PF00271 843-952 | Ercc6 | 1100494 | # | # | # | # | Chromatin remodeling | # | 15226310 | B-WICH | chromatin | # | # | 15226310 | CSB=ERCC6 is a DNA-dependent ATPase and is able to remodel chromatin at the expense of ATP. | # |
EXOSC1
(details) |
17286 | exosome component 1 | 51013 | Q9Y3B2 | EXOS1_HUMAN | ECR1_N PF14382 8-43, EXOSC1 PF10447 95-135 | Exosc1 | 1913833 | Q9DAA6 | EXOS1_MOUSE | # | # | Scaffold protein, RNA modification | RNA degradation | 17174896 | RNA exosome | RNA | # | # | 17174896 | RNA abundance is regulated by balancing transcription and RNA degradation, processes that control the temporal and spatial distribution of cellular RNA. After decapping, 5′ to 3′ RNA degradation is accomplished by Xrn1, a 5′ to 3′ exoribonuclease. In the 3′ to 5′ pathway, RNA degradation is catalyzed by a multisubunit 3′ to 5′ exoribonuclease complex termed the RNA exosome. Three additional exosome subunits, Csl4=EXOSC1, Rrp4=EXOSC2, and Rrp40=EXOSC3, include S1 or KH domains, which are postulated to bind RNA. | # |
EXOSC2
(details) |
17097 | exosome component 2 | 23404 | Q13868 | EXOS2_HUMAN | ECR1_N PF14382 26-64, RRP4_S1 PF21266 75-146, KH_6 PF15985 169-210 | Exosc2 | 2385133 | Q8VBV3 | EXOS2_MOUSE | # | # | Scaffold protein, RNA modification | RNA degradation | 17174896 | RNA exosome | RNA | # | # | 17174896 | RNA abundance is regulated by balancing transcription and RNA degradation, processes that control the temporal and spatial distribution of cellular RNA. After decapping, 5′ to 3′ RNA degradation is accomplished by Xrn1, a 5′ to 3′ exoribonuclease. In the 3′ to 5′ pathway, RNA degradation is catalyzed by a multisubunit 3′ to 5′ exoribonuclease complex termed the RNA exosome. Three additional exosome subunits, Csl4=EXOSC1, Rrp4=EXOSC2, and Rrp40=EXOSC3, include S1 or KH domains, which are postulated to bind RNA. | # |
EXOSC3
(details) |
17944 | exosome component 3 | 51010 | Q9NQT5 | EXOS3_HUMAN | RRP40_N_mamm PF21261 26-106, RRP40_S1 PF21262 108-191, KH_6 PF15985 197-244 | Exosc3 | 1913612 | Q7TQK4 | EXOS3_MOUSE | # | # | Scaffold protein, RNA modification | RNA degradation | 17174896 | RNA exosome | RNA | # | # | 17174896 | RNA abundance is regulated by balancing transcription and RNA degradation, processes that control the temporal and spatial distribution of cellular RNA. After decapping, 5′ to 3′ RNA degradation is accomplished by Xrn1, a 5′ to 3′ exoribonuclease. In the 3′ to 5′ pathway, RNA degradation is catalyzed by a multisubunit 3′ to 5′ exoribonuclease complex termed the RNA exosome. Three additional exosome subunits, Csl4=EXOSC1, Rrp4=EXOSC2, and Rrp40=EXOSC3, include S1 or KH domains, which are postulated to bind RNA. | # |
EXOSC4
(details) |
18189 | exosome component 4 | 54512 | Q9NPD3 | EXOS4_HUMAN | RNase_PH PF01138 21-152, RNase_PH_C PF03725 155-219 | Exosc4 | 1923576 | Q921I9 | EXOS4_MOUSE | # | # | Scaffold protein, RNA modification | RNA degradation | 17174896 | RNA exosome | RNA | # | # | 17174896 | RNA abundance is regulated by balancing transcription and RNA degradation, processes that control the temporal and spatial distribution of cellular RNA. After decapping, 5′ to 3′ RNA degradation is accomplished by Xrn1, a 5′ to 3′ exoribonuclease. In the 3′ to 5′ pathway, RNA degradation is catalyzed by a multisubunit 3′ to 5′ exoribonuclease complex termed the RNA exosome. Three additional exosome subunits, Csl4=EXOSC1, Rrp4=EXOSC2, and Rrp40=EXOSC3, include S1 or KH domains, which are postulated to bind RNA. | # |
EXOSC5
(details) |
24662 | exosome component 5 | 56915 | Q9NQT4 | EXOS5_HUMAN | RNase_PH PF01138 28-147, RNase_PH_C PF03725 151-215 | Exosc5 | 107889 | Q9CRA8 | EXOS5_MOUSE | # | # | Scaffold protein, RNA modification | RNA degradation | 17174896 | RNA exosome | RNA | # | # | 17174896 | RNA abundance is regulated by balancing transcription and RNA degradation, processes that control the temporal and spatial distribution of cellular RNA. After decapping, 5′ to 3′ RNA degradation is accomplished by Xrn1, a 5′ to 3′ exoribonuclease. In the 3′ to 5′ pathway, RNA degradation is catalyzed by a multisubunit 3′ to 5′ exoribonuclease complex termed the RNA exosome. Three additional exosome subunits, Csl4=EXOSC1, Rrp4=EXOSC2, and Rrp40=EXOSC3, include S1 or KH domains, which are postulated to bind RNA. | # |
EXOSC6
(details) |
19055 | exosome component 6 | 118460 | Q5RKV6 | EXOS6_HUMAN | RNase_PH PF01138 37-175 | Exosc6 | 1919794 | Q8BTW3 | EXOS6_MOUSE | # | # | Scaffold protein, RNA modification | RNA degradation | 17174896 | RNA exosome | RNA | # | # | 17174896 | RNA abundance is regulated by balancing transcription and RNA degradation, processes that control the temporal and spatial distribution of cellular RNA. After decapping, 5′ to 3′ RNA degradation is accomplished by Xrn1, a 5′ to 3′ exoribonuclease. In the 3′ to 5′ pathway, RNA degradation is catalyzed by a multisubunit 3′ to 5′ exoribonuclease complex termed the RNA exosome. Three additional exosome subunits, Csl4=EXOSC1, Rrp4=EXOSC2, and Rrp40=EXOSC3, include S1 or KH domains, which are postulated to bind RNA. | # |
EXOSC7
(details) |
28112 | exosome component 7 | 23016 | Q15024 | EXOS7_HUMAN | RNase_PH PF01138 32-166, RNase_PH_C PF03725 196-261 | Exosc7 | 1913696 | Q9D0M0 | EXOS7_MOUSE | # | # | Scaffold protein, RNA modification | RNA degradation | 17174896 | RNA exosome | RNA | # | # | 17174896 | RNA abundance is regulated by balancing transcription and RNA degradation, processes that control the temporal and spatial distribution of cellular RNA. After decapping, 5′ to 3′ RNA degradation is accomplished by Xrn1, a 5′ to 3′ exoribonuclease. In the 3′ to 5′ pathway, RNA degradation is catalyzed by a multisubunit 3′ to 5′ exoribonuclease complex termed the RNA exosome. Three additional exosome subunits, Csl4=EXOSC1, Rrp4=EXOSC2, and Rrp40=EXOSC3, include S1 or KH domains, which are postulated to bind RNA. | # |
EXOSC8
(details) |
17035 | exosome component 8 | 11340 | Q96B26 | EXOS8_HUMAN | RNase_PH PF01138 31-166, RNase_PH_C PF03725 192-257 | Exosc8 | 1916889 | Q9D753 | EXOS8_MOUSE | # | # | Scaffold protein, RNA modification | RNA degradation | 17174896 | RNA exosome | RNA | # | # | 17174896 | RNA abundance is regulated by balancing transcription and RNA degradation, processes that control the temporal and spatial distribution of cellular RNA. After decapping, 5′ to 3′ RNA degradation is accomplished by Xrn1, a 5′ to 3′ exoribonuclease. In the 3′ to 5′ pathway, RNA degradation is catalyzed by a multisubunit 3′ to 5′ exoribonuclease complex termed the RNA exosome. Three additional exosome subunits, Csl4=EXOSC1, Rrp4=EXOSC2, and Rrp40=EXOSC3, include S1 or KH domains, which are postulated to bind RNA. | # |
EXOSC9
(details) |
9137 | exosome component 9 | 5393 | Q06265 | EXOS9_HUMAN | RNase_PH PF01138 32-163, RNase_PH_C PF03725 189-254 | Exosc9 | 1355319 | Q9JHI7 | EXOS9_MOUSE | # | # | Scaffold protein, RNA modification | RNA degradation | 17174896 | RNA exosome | RNA | # | # | 17174896 | RNA abundance is regulated by balancing transcription and RNA degradation, processes that control the temporal and spatial distribution of cellular RNA. After decapping, 5′ to 3′ RNA degradation is accomplished by Xrn1, a 5′ to 3′ exoribonuclease. In the 3′ to 5′ pathway, RNA degradation is catalyzed by a multisubunit 3′ to 5′ exoribonuclease complex termed the RNA exosome. Three additional exosome subunits, Csl4=EXOSC1, Rrp4=EXOSC2, and Rrp40=EXOSC3, include S1 or KH domains, which are postulated to bind RNA. | # |
EYA1
(details) |
3519 | EYA transcriptional coactivator and phosphatase 1 | 2138 | Q99502 | EYA1_HUMAN | Hydrolase PF00702 323-566 | Eya1 | 109344 | P97767 | EYA1_MOUSE | PTPE | Protein tyrosine phosphatases / Asp-based PTPs | Histone modification erase | Histone phosphorylation | 19234442 | # | histone | H2AXT142 | # | 19234442 | Eya effectively removes the phosphotyrosine mark from H2AX, while the phosphatase-inactive mutant Eya proteins (Eya1 D323A or Eya3 D246A) have little or no effect. | # |
EYA2
(details) |
3520 | EYA transcriptional coactivator and phosphatase 2 | 2139 | O00167 | EYA2_HUMAN | Hydrolase PF00702 269-512 | Eya2 | 109341 | O08575 | EYA2_MOUSE | PTPE | Protein tyrosine phosphatases / Asp-based PTPs | Histone modification erase | Histone phosphorylation | 19351884 | # | histone | H2AXT142 | # | 19351884 | EYA2 and EYA3 display specificity (dephosphorylation) for Tyr-142 of H2A.X in assays in vitro. | # |
EYA3
(details) |
3521 | EYA transcriptional coactivator and phosphatase 3 | 2140 | Q99504 | EYA3_HUMAN | Hydrolase PF00702 304-548 | Eya3 | 109339 | P97480 | EYA3_MOUSE | PTPE | Protein tyrosine phosphatases / Asp-based PTPs | Histone modification erase | Histone phosphorylation | 19351884 | # | histone | H2AXT142 | # | 19351884 | EYA2 and EYA3 display specificity (dephosphorylation) for Tyr-142 of H2A.X in assays in vitro. | # |
EYA4
(details) |
3522 | EYA transcriptional coactivator and phosphatase 4 | 2070 | O95677 | EYA4_HUMAN | Hydrolase PF00702 370-614 | Eya4 | 1337104 | Q9Z191 | EYA4_MOUSE | PTPE | Protein tyrosine phosphatases / Asp-based PTPs | Histone modification erase | Histone phosphorylation | # | # | histone | H2AXY142ph | H2AXY142 | 24096489 | In response to double-stranded breaks, EYA4 dephosphorylates the Tyr-142 residue of H2AX facilitating phosphorylation of Ser-139 of H2AX (forming γH2AX), leading to the recruitment of DNA repair complex components to sites of double-stranded break. | # |
EZH1
(details) |
3526 | enhancer of zeste 1 polycomb repressive complex 2 subunit | 2145 | Q92800 | EZH1_HUMAN | EZH2_WD-Binding PF11616 39-68, PRC2_HTH_1 PF18118 160-262, Ezh2_MCSS PF21358 267-322, preSET_CXC PF18264 560-591, SET PF00856 624-727 | Ezh1 | 1097695 | P70351 | EZH1_MOUSE | KMT | Chromatin-modifying enzymes / K-methyltransferases | Histone modification write, Polycomb group (PcG) protein | Histone methylation | 19026781 | PRC2 | histone | H3K27 | H3K27me1, H3K27me2, H3K27me3 | 19026781 | Polycomb group proteins are critical to maintaining gene repression established during Drosophila development. Part of this group forms the PRC2 complex containing Ez that catalyzes di- and trimethylation of histone H3 lysine 27 (H3K37me2/3), marks repressive to transcription. The mammalian homologs Ezh1 and Ezh2 form similar PRC2 complexes but exhibit contrasting repressive roles. While PRC2-Ezh2 catalyzes H3K27me2/3 and its knockdown affects global H3K27me2/3 levels, PRC2-Ezh1 performs this function weakly. | # |
EZH2
(details) |
3527 | enhancer of zeste 2 polycomb repressive complex 2 subunit | 2146 | Q15910 | EZH2_HUMAN | EZH2_WD-Binding PF11616 39-68, PRC2_HTH_1 PF18118 159-249, Ezh2_MCSS PF21358 259-309, preSET_CXC PF18264 559-590, SET PF00856 623-726 | Ezh2 | 107940 | Q61188 | EZH2_MOUSE | KMT | Chromatin-modifying enzymes / K-methyltransferases | Histone modification write, Polycomb group (PcG) protein | Histone methylation | 19026781 | PRC2 | histone | H3K27 | H3K27me1, H3K27me2, H3K27me3 | 19026781 | Polycomb group proteins are critical to maintaining gene repression established during Drosophila development. Part of this group forms the PRC2 complex containing Ez that catalyzes di- and trimethylation of histone H3 lysine 27 (H3K37me2/3), marks repressive to transcription. The mammalian homologs Ezh1 and Ezh2 form similar PRC2 complexes, but exhibit contrasting repressive roles. While PRC2-Ezh2 catalyzes H3K27me2/3 and its knockdown affects global H3K27me2/3 levels, PRC2-Ezh1 performs this function weakly. | # |
FAM175A
(details) |
25829 | family with sequence similarity 175, member A | 84142 | Q6UWZ7 | F175A_HUMAN | MPN_2A_DUB_like PF21125 9-172 | Fam175a | 1917931 | Q8BPZ8 | F175A_MOUSE | # | # | Scaffold protein | # | 19261749 | BRCA1-A | TF | # | # | 19261749 | Abra1=FAM175A protein, which appears to act as a scaffold for the A complex. Abra1 is known to mediate the interaction of Rap80 with BRCA1. | # |
FAM175B
(details) |
28975 | family with sequence similarity 175, member B | 23172 | Q15018 | F175B_HUMAN | MPN_2A_DUB_like PF21125 3-167 | Fam175b | 1926116 | Q3TCJ1 | F175B_MOUSE | # | # | Histone modification erase cofactor | Histone ubiquitination | 20656690 | BRISC | histone | H2AK63 | H2AK63ub | 20656690 | # | # |
FBL
(details) |
3599 | fibrillarin | 2091 | P22087 | FBRL_HUMAN | Fibrillarin PF01269 88-314 | Fbl | 95486 | P35550 | FBRL_MOUSE | # | # | Histone modification write | Histone methylation | 24352239 | # | histone | H2AQ104 | H2AQ104me | 24352239 | Nop1 is a methyltransferase in yeast, and fibrillarin is the orthologue enzyme in human cells. The modification is exclusively enriched over the 35S ribosomal DNA transcriptional unit. Glutamine methylation of H2A is the first histone epigenetic mark dedicated to a specific RNA polymerase and define its function as a regulator of FACT interaction with nucleosomes. | # |
FBRS
(details) |
20442 | fibrosin | 64319 | Q9HAH7 | FBRS_HUMAN | Auts2 PF15336 82-273 | Fbrs | 104648 | Q8R089 | FBRS_MOUSE | # | # | Histone modification | # | 24217316, 22325352 | RING2-FBRS | histone | # | # | 24217316, 22325352 | Part of a RING2 complex. | # |
FBRSL1
(details) |
29308 | fibrosin-like 1 | 57666 | Q9HCM7 | FBSL_HUMAN | Auts2 PF15336 587-788 | Fbrsl1 | 1920907 | # | # | # | # | Histone modification | # | 24217316, 22325352 | RING2-FBRS | histone | # | # | 24217316, 22325352 | Part of a RING2 complex. | # |
FOXA1
(details) |
5021 | forkhead box A1 | 3169 | P55317 | FOXA1_HUMAN | Forkhead_N PF08430 16-169, Forkhead PF00250 170-255, HNF_C PF09354 396-455 | Foxa1 | 1347472 | P35582 | FOXA1_MOUSE | FOX | Forkhead boxes | Chromatin remodeling, TF | # | 22406422 | # | chromatin, DNA | DNA motif | # | # | FOXA1 functions in organizing nucleosome positioning. | # |
FOXO1
(details) |
3819 | forkhead box O1 | 2308 | Q12778 | FOXO1_HUMAN | Forkhead PF00250 160-244, FOXO_KIX_bdg PF16675 430-506, FOXO-TAD PF16676 597-635 | Foxo1 | 1890077 | Q9R1E0 | FOXO1_MOUSE | FOX | Forkhead boxes | TF | # | 22406422 | # | histone, DNA | DNA motif, H3, H4 | # | # | FOXO1 interacts with core histones H3 and H4. | # |
FOXP1
(details) |
3823 | forkhead box P1 | 27086 | Q9H334 | FOXP1_HUMAN | FOXP-CC PF16159 302-370, Forkhead PF00250 465-541 | Foxp1 | 1914004 | P58462 | FOXP1_MOUSE | FOX | Forkhead boxes | TF | # | 22406422 | # | histone, DNA | DNA motif | # | # | Recruitment of specific chromatin-modifying complexes with HDAC activity. | # |
FOXP2
(details) |
13875 | forkhead box P2 | 93986 | O15409 | FOXP2_HUMAN | FOXP-CC PF16159 342-410, Forkhead PF00250 504-581 | Foxp2 | 2148705 | P58463 | FOXP2_MOUSE | FOX | Forkhead boxes | TF | # | 22406422 | # | histone, DNA | DNA motif | # | # | Recruitment of specific chromatin-modifying complexes with HDAC activity. | # |
FOXP3
(details) |
6106 | forkhead box P3 | 50943 | Q9BZS1 | FOXP3_HUMAN | FOXP-CC PF16159 193-263, Forkhead PF00250 337-414 | Foxp3 | 1891436 | Q99JB6 | FOXP3_MOUSE | FOX | Forkhead boxes | TF | # | 22406422 | # | histone, DNA | DNA motif | # | # | Recruitment of specific chromatin-modifying complexes with HDAC activity. | # |
FOXP4
(details) |
20842 | forkhead box P4 | 116113 | Q8IVH2 | FOXP4_HUMAN | FOXP-CC PF16159 305-371, Forkhead PF00250 467-544 | Foxp4 | 1921373 | Q9DBY0 | FOXP4_MOUSE | FOX | Forkhead boxes | TF | # | 22406422 | # | histone, DNA | DNA motif | # | # | Recruitment of specific chromatin-modifying complexes with HDAC activity. | # |
FTO
(details) |
24678 | FTO alpha-ketoglutarate dependent dioxygenase | 79068 | Q9C0B1 | FTO_HUMAN | FTO_NTD PF12933 37-325, FTO_CTD PF12934 329-496 | Fto | 1347093 | Q8BGW1 | FTO_MOUSE | ALKBH | Alkylation repair homologs | RNA modification | RNA demethylation | 23653210 | # | RNA | m6A of mRNA | hm6A, f6A, A | 3218240 | # | New |
GADD45A
(details) |
4095 | growth arrest and DNA-damage-inducible, alpha | 1647 | P24522 | GA45A_HUMAN | Ribosomal_L7Ae PF01248 21-114 | Gadd45a | 107799 | P48316 | GA45A_MOUSE | # | # | Chromatin remodeling | # | 21986581 | # | histone | H2A, H2B, H3, H4 | # | 21986581 | Active DNA demethylation is partially attributed to the ability of Gadd45(A, B, C) proteins to bind histones and modify accessibility of DNA on damaged chromatin. | # |
GADD45B
(details) |
4096 | growth arrest and DNA-damage-inducible, beta | 4616 | O75293 | GA45B_HUMAN | Ribosomal_L7Ae PF01248 22-116 | Gadd45b | 107776 | P22339 | GA45B_MOUSE | # | # | Chromatin remodeling | # | 21986581 | # | histone | H2A, H2B, H3, H4 | # | 21986581 | Active DNA demethylation is partially attributed to the ability of Gadd45(A, B, C) proteins to bind histones and modify accessibility of DNA on damaged chromatin. | # |
GADD45G
(details) |
4097 | growth arrest and DNA-damage-inducible, gamma | 10912 | O95257 | GA45G_HUMAN | Ribosomal_L7Ae PF01248 25-106 | Gadd45g | 1346325 | Q9Z111 | GA45G_MOUSE | # | # | Chromatin remodeling | # | 21986581 | # | histone | H2A, H2B, H3, H4 | # | 21986581 | Active DNA demethylation is partially attributed to the ability of Gadd45(A, B, C) proteins to bind histones and modify accessibility of DNA on damaged chromatin. | # |
GATAD1
(details) |
29941 | GATA zinc finger domain containing 1 | 57798 | Q8WUU5 | GATD1_HUMAN | Gatad1 | 1914460 | Q920S3 | GATD1_MOUSE | GATAD | GATA zinc finger domain containing | Histone modification read | # | 20850016 | # | histone | H3K4me3 | # | # | GATA zinc finger domain containing 1 (GATAD1) has been identified as a H3K4me3 interactor. | # | |
GATAD2A
(details) |
29989 | GATA zinc finger domain containing 2A | 54815 | Q86YP4 | P66A_HUMAN | P66_CC PF16563 137-179, GATA PF00320 417-451 | Gatad2a | 2384585 | Q8CHY6 | P66A_MOUSE | GATAD | GATA zinc finger domain containing | Histone modification read | # | 16415179 | NuRD | histone | H2A, H2B, H3, H4 | # | 16415179 | In vitro translated p66α=GATAD2A and p66β showed a strong affinity for all histone tails tested. | # |
GATAD2B
(details) |
30778 | GATA zinc finger domain containing 2B | 57459 | Q8WXI9 | P66B_HUMAN | P66_CC PF16563 158-199, GATA PF00320 420-454 | Gatad2b | 2443225 | Q8VHR5 | P66B_MOUSE | GATAD | GATA zinc finger domain containing | Histone modification read | # | 16415179 | NuRD | histone | H2A, H2B, H3, H4 | # | 16415179 | In vitro translated p66α and p66β=GATAD2B showed a strong affinity for all histone tails tested. | # |
GFI1
(details) |
4237 | growth factor independent 1 transcription repressor | 2672 | Q99684 | GFI1_HUMAN | zf-C2H2 PF00096 255-278 284-306 312-334 340-362 368-390 396-419 | Gfi1 | 103170 | P70338 | GFI1_MOUSE | ZNF | Zinc fingers, C2H2-type | Chromatin remodeling | # | 16287849 | # | # | # | # | # | Gfi1 coordinates epigenetic repression of p21Cip/WAF1 by recruitment of histone lysine methyltransferase G9a and histone deacetylase 1. | # |
GFI1B
(details) |
4238 | growth factor independent 1B transcription repressor | 8328 | Q5VTD9 | GFI1B_HUMAN | zf-C2H2 PF00096 163-186 192-214 220-242 248-270 276-298 304-327 | Gfi1b | 1276578 | O70237 | GFI1B_MOUSE | ZNF | Zinc fingers, C2H2-type | Histone modification cofactor | # | 24395799 | # | # | # | # | # | The principal hematopoietic regulator T-cell acute lymphocytic leukemia-1 (TAL1) is involved in regulating H3K27me3 variations in collaboration with the transcription factor growth factor independent 1B (GFI1B). | # |
GLYR1
(details) |
24434 | glyoxylate reductase 1 homolog (Arabidopsis) | 84656 | Q49A26 | GLYR1_HUMAN | PWWP PF00855 8-89, NAD_binding_2 PF03446 269-425, NAD_binding_11 PF14833 431-551 | Glyr1 | 1921272 | Q922P9 | GLYR1_MOUSE | # | # | Histone modification read | # | 20850016 | # | histone | H3K4me3 | # | 20850016 | N-PAC=GLYR1, MSH-6, and NSD1 as well as NSD2 were identified as H3K36me3 interactors (Figure 1C; Table S2). Interestingly, these four proteins share a PWWP domain which is part of the Tudor domain “Royal Family” and includes the Tudor, chromo and MBT domains that can interact with methylated lysine residues. | # |
GSE1
(details) |
28979 | Gse1 coiled-coil protein | 23199 | Q14687 | GSE1_HUMAN | DUF3736 PF12540 718-861 | Gse1 | 1098275 | Q3U3C9 | GSE1_MOUSE | # | # | Histone modification erase | Histone acetylation | 8724849 | BHC, LSD-CoREST | RNA | # | # | 8724849 | A novel repeat composed of alternating Arg and Glu (RE repeat) was observed in KIAA0182. Alternating Arg-Asp tracts have been found in many RNA-binding proteins as a characteristic sequence. The presence of the RE repeat with structural similarity to the RD repeat strongly suggests that KIAA0182=GSE1 exhibits an RNA-binding activity. | # |
GSG2
(details) |
19682 | germ cell associated 2 (haspin) | 83903 | Q8TF76 | HASP_HUMAN | Haspin_kinase PF12330 420-783 | Gsg2 | 1194498 | Q9Z0R0 | HASP_MOUSE | # | # | Histone modification write | Histone phosphorylation | 20705812 | # | histone | H3T3 | H3T3ph | 20705812 | Phosphorylation of histone H3 threonine 3 (H3T3ph) by Haspin=GSG2 is necessary for CPC accumulation at centromeres and that CPC subunit Survivin binds directly to H3T3ph. | # |
GTF2I
(details) |
4659 | general transcription factor IIi | 2969 | P78347 | GTF2I_HUMAN | GTF2I PF02946 112-188 360-436 465-541 569-647 733-809 868-942 | Gtf2i | 1202722 | Q9ESZ8 | GTF2I_MOUSE | # | # | TF | # | 9334314 | BHC | DNA | DNA motif | # | # | Added because it is a complex partner. | # |
GTF3C4
(details) |
4667 | general transcription factor IIIC, polypeptide 4, 90kDa | 9329 | Q9UKN8 | TF3C4_HUMAN | TFIIIC_delta PF12657 61-517, DUF5921 PF19336 516-592, zf-TFIIIC PF12660 741-789 | Gtf3c4 | 2138937 | Q8BMQ2 | TF3C4_MOUSE | KAT, GTF | Chromatin-modifying enzymes / K-acetyltransferases, General transcription factors | Histone modification write | Histone acetylation | 10523658 | # | histone | H3 | # | 10523658 | hTFIIIC90=GTF3C4 has an intrinsic histone acetyltransferase activity with a substrate specificity for histone H3. | # |
HAT1
(details) |
4821 | histone acetyltransferase 1 | 8520 | O14929 | HAT1_HUMAN | Hat1_N PF10394 26-187, HAT1_C PF21183 287-337 | Hat1 | 96013 | Q8BY71 | HAT1_MOUSE | KAT | Chromatin-modifying enzymes / K-acetyltransferases | Histone modification write | Histone acetylation | 9427644 | # | histone | H4, H2A | # | 9427644 | The human holoenzyme consists of two subunits: a catalytic subunit, Hat1, and a subunit that binds core histones, p46, which greatly stimulates the acetyltransferase activity of Hat1. On the other hand, given that the Hat1 holoenzyme bound weakly to H2A and also acetylated the H2A | # |
HCFC1
(details) |
4839 | host cell factor C1 | 3054 | P51610 | HCFC1_HUMAN | Kelch_1 PF01344 32-69, Kelch_5 PF13854 78-114 319-361, Kelch_3 PF13415 216-263 | Hcfc1 | 105942 | Q61191 | HCFC1_MOUSE | # | # | Chromatin remodeling | # | 12670868 | NSL, COMPASS, MLL-HCF, CHD8, MLL2/3, COMPASS-like MLL1,2, MLL4/WBP7 | chromatin | # | # | 12670868 | A series of molecular activities are associated with the N-terminal subunit of HCF-1 in HSV uninfected cells. Two of these activities are associated with opposing roles in the regulation of transcription through the modulation of chromatin structure: Sin3 HDAC and a novel human Set1/Ash2 HMT. | # |
HCFC2
(details) |
24972 | host cell factor C2 | 29915 | Q9Y5Z7 | HCFC2_HUMAN | Kelch_1 PF01344 22-60, Kelch_5 PF13854 69-104 312-354, Kelch_3 PF13415 207-253 | Hcfc2 | 1915183 | Q9D968 | HCFC2_MOUSE | # | # | Histone modification write cofactor, Histone modification write cofactor | Histone methylation, Histone acetylation | 15199122 | MLL-HCF, CHD8, MLL2/3, MLL4/WBP7 | histone | H3 | # | 15199122 | HCF-2 (HCFC2), which specifically interact with a conserved binding motif in the MLL(N) (p300) subunit of MLL (histone methyltransferase ) and provide a potential mechanism for regulating its antagonistic transcriptional properties. | # |
HDAC1
(details) |
4852 | histone deacetylase 1 | 3065 | Q13547 | HDAC1_HUMAN | Hist_deacetyl PF00850 28-318 | Hdac1 | 108086 | O09106 | HDAC1_MOUSE | # | # | Histone modification erase | Histone acetylation | 10220385 | SWI/SNF_Brm, NuRD, BHC, MeCP1, mSin3A, core HDAC, mSin3A-like complex, RING2-L3MBTL2, CREST-BRG1, LSD-CoREST | histone | H3, H4 | # | 10220385 | HDAC1, HDAC4, HDAC5, and HDAC6 deacetylate all four core histones equally well, though deacetylation by HDAC4 and HDAC5 is incomplete. | # |
HDAC10
(details) |
18128 | histone deacetylase 10 | 83933 | Q969S8 | HDA10_HUMAN | Hist_deacetyl PF00850 24-321 | Hdac10 | 2158340 | Q6P3E7 | HDA10_MOUSE | # | # | Histone modification erase | Histone acetylation | 11861901 | # | histone | H2AKac, H2BKac, H3Kac, H4Kac | H2AK, H2BK, H3K, H4K | 11861901 | HDAC10 can deacetylate histones. | # |
HDAC11
(details) |
19086 | histone deacetylase 11 | 79885 | Q96DB2 | HDA11_HUMAN | Hist_deacetyl PF00850 35-318 | Hdac11 | 2385252 | Q91WA3 | HDA11_MOUSE | # | # | Histone modification erase | Histone acetylation | 9346952 | # | histone | H2AKac, H2BKac, H3Kac, H4Kac | H2AK, H2BK, H3K, H4K | 9346952 | HDAC11 is a bona fide histone deacetylase. | # |
HDAC2
(details) |
4853 | histone deacetylase 2 | 3066 | Q92769 | HDAC2_HUMAN | Hist_deacetyl PF00850 29-319 | Hdac2 | 1097691 | P70288 | HDAC2_MOUSE | # | # | Histone modification erase | Histone acetylation | 9346952 | SWI/SNF_Brg1(I), SWI/SNF_Brg1(II), SWI/SNF_Brm, NuRD, BHC, MeCP1, mSin3A, core HDAC, mSin3A-like complex, RING2-L3MBTL2, LSD-CoREST | histone | H2AKac, H2BKac, H3Kac, H4Kac | H2AK, H2BK, H3K, H4K | 9346952 | HDAC1, HDAC2, and HDAC3 constitute a human HDAC family. All three proteins possess histone deacetylase activity, and repress transcription when bound to a promoter. | # |
HDAC3
(details) |
4854 | histone deacetylase 3 | 8841 | O15379 | HDAC3_HUMAN | Hist_deacetyl PF00850 22-313 | Hdac3 | 1343091 | O88895 | HDAC3_MOUSE | # | # | Histone modification erase | Histone acetylation | 10655483 | # | histone | H2AKac, H2BKac, H3Kac, H4Kac | H2AK, H2BK, H3K, H4K | 10655483 | HDAC1, HDAC2, and HDAC3 constitute a human HDAC family. All three proteins possess histone deacetylase activity, and repress transcription when bound to a promoter. | # |
HDAC4
(details) |
14063 | histone deacetylase 4 | 9759 | P56524 | HDAC4_HUMAN | HDAC4_Gln PF12203 63-153, Hist_deacetyl PF00850 675-992 | Hdac4 | 3036234 | Q6NZM9 | HDAC4_MOUSE | # | # | Histone modification erase | Histone acetylation | 10220385 | # | histone | H2AKac, H2BKac, H3Kac, H4Kac | H2AK, H2BK, H3K, H4K | 10220385 | HDAC1, HDAC4, HDAC5, and HDAC6 deacetylate all four core histones equally well, though deacetylation by HDAC4 and HDAC5 is incomplete. | # |
HDAC5
(details) |
14068 | histone deacetylase 5 | 10014 | Q9UQL6 | HDAC5_HUMAN | HDAC4_Gln PF12203 67-162, Hist_deacetyl PF00850 704-1022 | Hdac5 | 1333784 | Q9Z2V6 | HDAC5_MOUSE | # | # | Histone modification erase | Histone acetylation | 10220385 | # | histone | H2AKac, H2BKac, H3Kac, H4Kac | H2AK, H2BK, H3K, H4K | 10220385 | HDAC1, HDAC4, HDAC5, and HDAC6 deacetylate all four core histones equally well, though deacetylation by HDAC4 and HDAC5 is incomplete. | # |
HDAC6
(details) |
14064 | histone deacetylase 6 | 10013 | Q9UBN7 | HDAC6_HUMAN | Hist_deacetyl PF00850 106-402 499-798, zf-UBP PF02148 1132-1193 | Hdac6 | 1333752 | Q9Z2V5 | HDAC6_MOUSE | # | # | Histone modification erase | Histone acetylation | 10220385 | # | histone | H2AKac, H2BKac, H3Kac, H4Kac | H2AK, H2BK, H3K, H4K | 10220385 | HDAC1, HDAC4, HDAC5, and HDAC6 deacetylate all four core histones equally well, though deacetylation by HDAC4 and HDAC5 is incomplete. (HDAC6 is possibly not involved in epigenetic signalling, but it deacetylates microtubules and heat shock protein 90; PMID:22498752) | # |
HDAC7
(details) |
14067 | histone deacetylase 7 | 51564 | Q8WUI4 | HDAC7_HUMAN | Hist_deacetyl PF00850 541-858 | Hdac7 | 1891835 | Q8C2B3 | HDAC7_MOUSE | # | # | Histone modification erase | Histone acetylation | 18285338 | # | histone | H2AKac, H2BKac, H3Kac, H4Kac | H2AK, H2BK, H3K, H4K | 18285338 | The isolated and purified catalytic domain of the human class IIa HDAC, cdHDAC7, has an intrinsic low level of deacetylase activity in the absence of any complex partner which can be inhibited by known HDAC inhibitors such as the hydroxamic acid TSA. It has been showen that the isolated catalytic domain of class IIa HDACs have weak but measurable intrinsic catalytic activity on chemically acetylated core histones. | # |
HDAC8
(details) |
13315 | histone deacetylase 8 | 55869 | Q9BY41 | HDAC8_HUMAN | Hist_deacetyl PF00850 33-320 | Hdac8 | 1917565 | Q8VH37 | HDAC8_MOUSE | # | # | Histone modification erase | Histone acetylation | 10748112 | # | histone | H2AKac, H2BKac, H3Kac, H4Kac | H2AK, H2BK, H3K, H4K | 10748112 | HDAC8 exhibited deacetylase activity toward acetylated histone, indicating that this protein is a bona fide histone deacetylase. | # |
HDAC9
(details) |
14065 | histone deacetylase 9 | 9734 | Q9UKV0 | HDAC9_HUMAN | HDAC4_Gln PF12203 37-119, Hist_deacetyl PF00850 654-972 | Hdac9 | 1931221 | Q99N13 | HDAC9_MOUSE | # | # | Histone modification erase | Histone acetylation | 12590135 | # | histone | H3Kac, H4Kac | H3K, H4K | 12590135 | A new member of the Class II HDAC family, HDAC9. The enzyme contains a conserved deacetylase domain, represses reporter activity when recruited to a promoter, and utilizes histones H3 and H4 as substrates in vitro and in vivo. | # |
HDGF
(details) |
4856 | hepatoma-derived growth factor | 3068 | P51858 | HDGF_HUMAN | PWWP PF00855 13-93 | Hdgf | 1194494 | P51859 | HDGF_MOUSE | # | # | Chromatin remodeling, TF | TF repressor | 18331345, 17974029 | # | DNA | DNA motif | # | 18331345 | SUMOylated HDGF is not bound to chromatin. | # |
HDGFL2
(details) |
14680 | HDGF like 2 | 84717 | Q7Z4V5 | HDGR2_HUMAN | PWWP PF00855 7-86, LEDGF PF11467 472-568 | Hdgfrp2 | 1194492 | Q3UMU9 | HDGR2_MOUSE | # | # | Histone modification read | # | 217205545 | # | histone | H3K79me3, H4K20me3, H3K36me3 | # | 217205545 | The crystal structures of the PWWP domains from seven different human proteins and three PWWP domain complex structures with histone peptides, i.e., BRPF1-H3K36me3, HDGF2-H3K79me3 and HDGF2-H4K20me3 shows that the PWWP domain can not only bind DNA but also histones. | # |
HELLS
(details) |
4861 | helicase, lymphoid-specific | 3070 | Q9NRZ9 | HELLS_HUMAN | SNF2-rel_dom PF00176 226-576, Helicase_C PF00271 600-712 | Hells | 106209 | Q60848 | HELLS_MOUSE | # | # | Chromatin remodeling | # | 14612388 | # | chromatin | # | # | 14517253, 14612388 | Lymphoid-specific helicase (Lsh=HELLS) is another member of the SNF2 family of chromatin remodeling proteins. | # |
HIF1AN
(details) |
17113 | hypoxia inducible factor 1, alpha subunit inhibitor | 55662 | Q9NWT6 | HIF1N_HUMAN | Cupin_8 PF13621 51-299 | Hif1an | 2442345 | Q8BLR9 | HIF1N_MOUSE | # | # | Histone modification erase cofactor | Histone acetylation | 11641274 | # | histone | # | # | 11641274 | VHL and FIH-1=HIF1AN interact with histone deacetylases in vitro. | # |
HINFP
(details) |
17850 | histone H4 transcription factor | 25988 | Q9BQA5 | HINFP_HUMAN | zf-C2H2_4 PF13894 229-251, zf-C2H2 PF00096 255-278 345-368 | Hinfp | 2429620 | Q8K1K9 | HINFP_MOUSE | ZNF | Zinc fingers, C2H2-type | Histone modification read, TF | TF activator, TF repressor | 14585971 | # | histone, DNA | H4, DNA motif | # | 14585971 | HiNF-P interacts with conserved H4 cell cycle regulatory sequences in vivo. | # |
HIRA
(details) |
4916 | histone cell cycle regulator | 7290 | P54198 | HIRA_HUMAN | WD40 PF00400 9-44 64-97 122-159 166-201, Hira PF07569 764-962 | Hira | 99430 | Q61666 | HIRA_MOUSE | WDR | WD repeat domain containing | Histone modification read | # | 9710638 | # | histone | H2B, H4 | # | 9710638 | HIRA interacts with core histone H4. H2B- and H4-binding domains are overlapping but distinguishable in the carboxy-terminal region of HIRA, and the region for HIRA interaction has been mapped to the amino-terminal tail of H2B and the second alpha helix of H4. | # |
HIRIP3
(details) |
4917 | HIRA interacting protein 3 | 8479 | Q9BW71 | HIRP3_HUMAN | CHZ PF09649 486-556 | Hirip3 | 2142364 | Q8BLH7 | HIRP3_MOUSE | # | # | Histone modification read | # | 9710638 | # | histone | H2A, H3 | # | 9710638 | In vitro, HIRIP3 directly interacted with HIRA but also with core histones H2B and H3, suggesting that a HIRA-HIRIP3-containing complex could function in some aspects of chromatin and histone metabolism. | # |
HJURP
(details) |
25444 | Holliday junction recognition protein | 55355 | Q8NCD3 | HJURP_HUMAN | Scm3 PF10384 11-71, HJURP_mid PF12346 123-391, HJURP_C PF12347 416-466 560-620 | Hjurp | 2685821 | Q6PG16 | HJURP_MOUSE | # | # | Histone chaperone | # | 21478274 | # | histone | H4 | # | 21478274 | Deposition of CENP-A to the centromere requires histone chaperone HJURP (Holliday junction recognition protein). The crystal structure of an HJURP–CENP-A–histone H4 complex shows that HJURP binds a CENP-A–H4 heterodimer. | # |
HLCS
(details) |
4976 | holocarboxylase synthetase (biotin-(proprionyl-CoA-carboxylase (ATP-hydrolysing)) ligase) | 3141 | P50747 | BPL1_HUMAN | BPL_LplA_LipB PF03099 472-603, BPL_C PF02237 669-716 | Hlcs | 894646 | Q920N2 | BPL1_MOUSE | # | # | Histone modification write | # | 14613969 | # | histone | H1, H2A, H2B, H4 | # | 14613969 | Nuclear HCS =HLCS retains its biotinylating activity and has been shown to biotinylate purified histones in vitro. | # |
HLTF
(details) |
11099 | helicase-like transcription factor | 6596 | Q14527 | HLTF_HUMAN | HIRAN PF08797 61-154, SNF2-rel_dom PF00176 242-720, zf-C3HC4_2 PF13923 760-800, Helicase_C PF00271 834-950 | Hltf | 1196437 | Q6PCN7 | HLTF_MOUSE | RNF | RING-type (C3HC4) zinc fingers | Chromatin remodeling cofactor | # | 18719106 | # | chromatin | # | # | 18719106 | Acts as a ubiquitin ligase for 'Lys-63'-linked polyubiquitination of chromatin-bound PCNA. | # |
HMG20A
(details) |
5001 | high mobility group 20A | 10363 | Q9NP66 | HM20A_HUMAN | HMG_box PF00505 103-170 | Hmg20a | 1914117 | Q9DC33 | HM20A_MOUSE | HMGX | High mobility group / Non-canonical | Chromatin remodeling cofactor | # | 24227653 | LSD-CoREST | histone | H3K4 | # | 24227653 | Involved in the recruitment of the histone methyltransferase KMT2A/MLL1 and consequent increased methylation of histone H3 lysine 4. | # |
HMG20B
(details) |
5002 | high mobility group 20B | 10362 | Q9P0W2 | HM20B_HUMAN | HMG_box PF00505 70-138 | Hmg20b | 1341190 | Q9Z104 | HM20B_MOUSE | HMGX | High mobility group / Non-canonical | Chromatin remodeling | # | 11997092 | BHC, LSD-CoREST | DNA | # | # | 11997092 | The high-mobility-group (HMG) proteins are chromatin-associated proteins that are common to all higher organisms. They bind DNA in a sequence-specific or non-sequence-specific way to induce DNA bending, and regulate chromatin function and gene expression. | # |
HMGB1
(details) |
4983 | high mobility group box 1 | 3146 | P09429 | HMGB1_HUMAN | HMG_box_2 PF09011 6-79, HMG_box PF00505 95-163 | Hmgb1 | 96113 | P63158 | HMGB1_MOUSE | HMG | High-mobility group / Canonical | Chromatin remodeling | # | 19158276 | # | chromatin | # | # | # | Chromatin-specific remodeling by HMGB1 and linker histone H1 silences proinflammatory genes during endotoxin tolerance. | # |
HMGN1
(details) |
4984 | high mobility group nucleosome binding domain 1 | 3150 | P05114 | HMGN1_HUMAN | HMG14_17 PF01101 2-96 | Hmgn1 | 96120 | P18608 | HMGN1_MOUSE | HMG | High-mobility group / Canonical | Chromatin remodeling | # | 22395460, 20123071 | # | histone | H1 | # | # | HMGB1-4 proteins are believed to dock to the H1 linker. | # |
HMGN2
(details) |
4986 | high mobility group nucleosomal binding domain 2 | 3151 | P05204 | HMGN2_HUMAN | HMG14_17 PF01101 2-89 | Hmgn2 | 96136 | P09602 | HMGN2_MOUSE | HMG | High-mobility group / Canonical | Chromatin remodeling | # | 22395460, 20123071 | # | histone | H1 | # | # | HMGB1-4 proteins are believed to dock to the H1 linker. | # |
HMGN3
(details) |
12312 | high mobility group nucleosomal binding domain 3 | 9324 | Q15651 | HMGN3_HUMAN | HMG14_17 PF01101 2-95 | Hmgn3 | 2138069 | Q9DCB1 | HMGN3_MOUSE | HMG | High-mobility group / Canonical | Chromatin remodeling | # | 22395460, 20123071 | # | histone | H1 | # | # | HMGB1-4 proteins are believed to dock to the H1 linker. | # |
HMGN4
(details) |
4989 | high mobility group nucleosomal binding domain 4 | 10473 | O00479 | HMGN4_HUMAN | HMG14_17 PF01101 2-89 | # | # | # | # | HMG | High-mobility group / Canonical | Chromatin remodeling | # | 22395460, 20123071 | # | histone | H1 | # | # | HMGB1-4 proteins are believed to dock to the H1 linker. | # |
HMGN5
(details) |
8013 | high mobility group nucleosome binding domain 5 | 79366 | P82970 | HMGN5_HUMAN | HMG14_17 PF01101 1-112 | Hmgn5 | 1355295 | Q9JL35 | HMGN5_MOUSE | HMG | High-mobility group / Canonical | Chromatin remodeling | # | 22395460, 20123071 | # | histone | H1 | # | # | HMGB1-4 proteins are believed to dock to the H1 linker. | # |
HNRNPU
(details) |
5048 | Heterogeneous nuclear ribonucleoprotein U (hnRNP U) (GRIP120) (Nuclear p120 ribonucleoprotein) (Scaffold-attachment factor A) (SAF-A) (p120) (pp120) | 3192 | Q00839 | HNRPU_HUMAN | SAP PF02037 8-42, SPRY PF00622 355-462, AAA_33 PF13671 499-643 | Hnrpu | 1858195 | Q8VEK3 | HNRPU_MOUSE | HNRNP | Heterogeneous nuclear ribonucleoproteins | RNA modification | Alternative splicing | 22325991 | # | RNA | mRNA | # | 22325991 | Regulates SMN2 alternative splicing | New |
HNRPL
(details) |
5045 | Heterogeneous nuclear ribonucleoprotein L (hnRNP L) | 3191 | P14866 | HNRPL_HUMAN | RRM_1 PF00076 106-155, RRM_8 PF11835 191-269, RRM_5 PF13893 361-480, domain PF22976 492-587 | Hnrpl | 104816 | Q8R081 | HNRPL_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 25623890 | # | RNA | mRNA | # | 25623890 | Regulates exon inclusion of CD44 | New |
HNRPM
(details) |
5046 | Heterogeneous nuclear ribonucleoprotein M (hnRNP M) | 4670 | P52272 | HNRPM_HUMAN | HnRNP_M_NLS PF11532 41-70, RRM_1 PF00076 74-143 206-274 655-722 | Hnrpm | 1926465 | Q9D0E1 | HNRPM_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 19874820 | # | RNA | mRNA | # | 19874820 | Regulates alternative splicing FGFR2. | New |
HP1BP3
(details) |
24973 | heterochromatin protein 1, binding protein 3 | 50809 | Q5SSJ5 | HP1B3_HUMAN | Linker_histone PF00538 159-229 262-328 342-411 | Hp1bp3 | 109369 | Q3TEA8 | HP1B3_MOUSE | # | # | Chromatin remodeling | # | 25100860 | # | chromatin | # | # | # | Chromatin organizer protein HP1BP3 is mediating chromatin condensation during hypoxia. | # |
HR
(details) |
5172 | hair growth associated | 55806 | O43593 | HAIR_HUMAN | JmjC PF02373 1051-1139 | Hr | 96223 | Q61645 | HAIR_MOUSE | # | # | Histone modification erase | Histone methylation | 24334705 | # | histone | H3K9me1, H3K9me2 | H3K9 | 24334705 | HR can demethylate monomethylated or dimethylated histone H3 lysine 9 (H3K9me1 or me2). | # |
HSFX3
(details) |
52395 | heat shock transcription factor family, X-linked member 3 | 101928917 | A0A1B0GWH4 | HSFX3_HUMAN | HSF_DNA-bind PF00447 83-181 | # | # | # | # | # | # | # | # | # | # | # | # | # | # | # | New |
HSPA1A
(details) |
5232 | heat shock 70kDa protein 1A | 3303 | P08107 | HSP71_HUMAN | Hspa1a | 96244 | Q61696 | HS71A_MOUSE | HSP70 | Heat shock proteins / HSP70 | Histone modification write cofactor, Histone modification write cofactor | Histone methylation, Histone acetylation | 22123078 | CHD8, MLL2/3, MLL4/WBP7 | histone | # | # | 22123078 | # | # | |
HSPA1A
(details) |
5232 | heat shock protein family A (Hsp70) member 1B | 3303 | P0DMV8 | HS71A_HUMAN | HSP70 PF00012 6-611 | Hspa1a | 96244 | Q61696 | HS71A_MOUSE | HSPA | Heat shock 70kDa proteins | Histone modification write cofactor | Histone acetylation, Histone methylation, Histone ubiquitination | 16809764, 2123078 | # | Protein | HDAC | # | 16809764, 2123078, 24613385 | Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling. | New |
HSPA1B
(details) |
5233 | heat shock 70kDa protein 1B | 3304 | P08107 | HSP71_HUMAN | Hspa1a | 96244 | Q61696 | HS71A_MOUSE | HSP70 | Heat shock proteins / HSP70 | Histone modification write cofactor, Histone modification write cofactor | Histone methylation, Histone acetylation | 22123078 | CHD8, MLL2/3, MLL4/WBP7 | histone | # | # | 22123078 | # | # | |
HSPA1B
(details) |
5233 | heat shock protein family A (Hsp70) member 1B | 3304 | P0DMV9 | HS71B_HUMAN | HSP70 PF00012 6-611 | Hspa1b | 99517 | P17879 | HS71B_MOUSE | HSPA | Heat shock 70kDa proteins | Histone modification write cofactor | Histone acetylation, Histone methylation, Histone ubiquitination | 16809764, 2123078 | # | Protein | HDAC | # | 16809764, 2123078, 24613385 | Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling. | New |
HUWE1
(details) |
30892 | HECT, UBA and WWE domain containing 1, E3 ubiquitin protein ligase | 10075 | Q7Z6Z7 | HUWE1_HUMAN | DUF908 PF06012 25-338, DUF913 PF06025 404-820, domain PF22562 1317-1355, WWE PF02825 1617-1679, UBM PF14377 2962-2994 3055-3081, HECT PF00632 4067-4373 | Huwe1 | 1926884 | Q7TMY8 | HUWE1_MOUSE | # | # | Histone modification write | Histone ubiquitination | 15767685 | # | histone | H3K9 | # | 15767685 | A HECT=HUWE1 domain-containing E3 that ubiquitinates histones. | # |
IKBKAP
(details) |
5959 | inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase complex-associated protein | 8518 | O95163 | ELP1_HUMAN | IKI3 PF04762 2-955 | Ikbkap | 1914544 | Q7TT37 | ELP1_MOUSE | ELP | Elongator acetyltransferase complex subunits | Scaffold protein | # | 11818576, 11714725 | Pol2 elongator | # | RNA | # | 11818576, 11714725 | The human Elongator facilitates transcription by RNA polymerase II in a chromatin- and acetyl-CoA-dependent manner. Several human homologues of the yeast Elongator subunits have been identified as subunits of the human Elongator complex, including StIP1 (STAT-interacting protein 1) and IKAP (IKK complex-associated protein) =IKBKAP. | # |
IKZF1
(details) |
13176 | IKAROS family zinc finger 1 (Ikaros) | 10320 | Q13422 | IKZF1_HUMAN | zf-C2H2 PF00096 145-167 173-195 201-224 | Ikzf1 | 1342540 | Q03267 | IKZF1_MOUSE | ZNF, IKZF | Zinc fingers, C2H2-type, IKAROS zinc fingers | Chromatin remodeling, TF | # | 19141594 | # | DNA | DNA motif | # | 19141594 | Ikaros=IKZF1 forms dimers and multimers efficiently, and it has been proposed that Ikaros induces heterochromatization or chromatin remodeling of mouse DNA, resulting in repression or activation of target genes. The results provide insight into possible structural and functional roles of pericentromeric regions in mouse and human chromosomes. | # |
IKZF3
(details) |
13178 | IKAROS family zinc finger 3 (Aiolos) | 22806 | Q9UKT9 | IKZF3_HUMAN | zf-C2H2 PF00096 146-168 202-222 | Ikzf3 | 1342542 | O08900 | IKZF3_MOUSE | ZNF, IKZF | Zinc fingers, C2H2-type, "IKAROS zinc fingers" | TF | # | # | # | DNA | DNA motif | # | # | Associates with histone deacetylase complexes containing HDAC1, MTA2 and SIN3A. (UniProt) | # |
ING1
(details) |
6062 | inhibitor of growth family, member 1 | 3621 | Q9UK53 | ING1_HUMAN | ING PF12998 186-254 | Ing1 | 1349481 | Q9QXV3 | ING1_MOUSE | PHF | Zinc fingers, PHD-type | Histone modification read | # | 18533182 | # | histone | H3K4me3 | # | 18533182 | Both DNA repair and apoptotic activities of ING1 require the interaction of the C-terminal plant homeodomain (PHD) finger with histone H3 trimethylated at Lys4 (H3K4me3). The ING1 PHD finger recognizes methylated H3K4 but not other histone modifications as revealed by peptide microarrays. | # |
ING2
(details) |
6063 | inhibitor of growth family, member 2 | 3622 | Q9H160 | ING2_HUMAN | ING PF12998 27-122 | Ing2 | 1916510 | Q9ESK4 | ING2_MOUSE | PHF | Zinc fingers, PHD-type | Histone modification read | # | 16728974 | mSin3A-like complex | histone | H3K4me3 | # | 16728974 | ING2, a native subunit of a repressive mSin3a-HDAC1 histone deacetylase complex, binds with high affinity to the trimethylated species. In response to DNA damage, recognition of H3K4me3 by the ING2 PHD domain stabilizes the mSin3a-HDAC1 complex at the promoters of proliferation genes. | # |
ING3
(details) |
14587 | inhibitor of growth family, member 3 | 54556 | Q9NXR8 | ING3_HUMAN | ING PF12998 3-104 | Ing3 | 1919027 | Q8VEK6 | ING3_MOUSE | PHF | Zinc fingers, PHD-type | Chromatin remodeling, Histone modification write cofactor | Histone acetylation | 12545155 | SWR, NuA4, Piccolo_NuA4 | histone | H2A, H4 | # | 12545155 | p47ING3 has a PHD-finger motif at its C-terminal region similar to p33ING1 and p33ING2. Although the precise function of the PHD-finger motif is not fully clarified, it is found in proteins involved in chromatin remodeling. | # |
ING4
(details) |
19423 | inhibitor of growth family, member 4 | 51147 | Q9UNL4 | ING4_HUMAN | ING PF12998 6-107 | Ing4 | 107307 | Q8C0D7 | ING4_MOUSE | PHF | Zinc fingers, PHD-type | Histone modification read | # | 18381289 | HBO1 | histone | H3K4me3 | # | 18381289 | Crystal structure of ING4-PHD bound to H3K4me3. | # |
ING5
(details) |
19421 | inhibitor of growth family, member 5 | 84289 | Q8WYH8 | ING5_HUMAN | ING PF12998 6-107 | Ing5 | 1922816 | Q9D8Y8 | ING5_MOUSE | PHF | Zinc fingers, PHD-type | Histone modification read | # | 18623064 | HBO1, MOZ/MORF | histone | H3K4me3, H3K4me2 | # | 18623064 | Crystal structure of the ING5 PHD finger in complex with its histone target (H3K4me3). Binding affinities for unmodified, mono-, di-, and tri-methylated histone peptides showed that both full-length ING5 and methylated H3K4 are essential for the acetyltransferase activity of the MOZ/MORF and HBO1 complexes. | # |
INO80
(details) |
26956 | INO80 complex subunit | 54617 | Q9ULG1 | INO80_HUMAN | DBINO PF13892 277-405, SNF2-rel_dom PF00176 521-821, Helicase_C PF00271 1102-1214 | Ino80 | 1915392 | Q6ZPV2 | INO80_MOUSE | INO80 | INO80 complex subunits | Chromatin remodeling | # | 16298340 | Ino80 | DNA | # | # | 16298340 | The proteins belonging to SWI2/SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. Functional activity of the domains from hINO80 gene both in terms of the DNA dependent ATPase as well as DNA binding activity. | # |
INO80B
(details) |
13324 | INO80 complex subunit B | 83444 | Q9C086 | IN80B_HUMAN | PAPA-1 PF04795 187-284, zf-HIT PF04438 308-336 | Ino80b | 1917270 | Q99PT3 | IN80B_MOUSE | ZNHIT, INO80 | Zinc fingers, HIT-type, INO80 complex subunits | Chromatin remodeling cofactor | # | 21303910 | Ino80 | chromatin | # | # | 21303910 | Composed of the hIno80 Snf2 ATPase domain, the Ies2=INO80B and Ies6 proteins, the AAA+ ATPases Tip49a and Tip49b, and the actin-related protein Arp5. | # |
INO80C
(details) |
26994 | INO80 complex subunit C | 125476 | Q6PI98 | IN80C_HUMAN | YL1_C PF08265 142-170 | Ino80c | 2443014 | Q8BHA0 | IN80C_MOUSE | INO80 | INO80 complex subunits | Chromatin remodeling cofactor | # | 16230350 | Ino80, CHD8, MLL2/3, MLL4/WBP7 | chromatin | # | # | 16230350 | FLAG-tagged PAPA-1, C18orf37, Amida, FLJ20309, and FLJ90652 each copurified with the hINO80 helicase and the Tip49a, Tip49b, PAPA-1, C18orf37, Arp4, Arp5, Arp8, Amida, NFRKB, MCRS1, FLJ90652, and FLJ20309 proteins, which argues that they are all components of a multiprotein hINO80-containing complex. | # |
INO80D
(details) |
25997 | INO80 complex subunit D | 54891 | Q53TQ3 | IN80D_HUMAN | zf-C3Hc3H PF13891 18-79 453-511 | Ino80d | 3027003 | Q66JY2 | IN80D_MOUSE | INO80 | INO80 complex subunits | Chromatin remodeling cofactor | # | 21303910 | Ino80 | chromatin | # | # | 21303910 | Component of the chromatin remodeling INO80 complex. | # |
INO80E
(details) |
26905 | INO80 complex subunit E | 283899 | Q8NBZ0 | IN80E_HUMAN | Ino80e | 2141881 | # | # | INO80 | INO80 complex subunits | Chromatin remodeling cofactor | # | 21303910 | # | chromatin | # | # | 21303910 | Component of the chromatin remodeling INO80 complex. | # | |
JADE1
(details) |
30027 | jade family PHD finger 1 | 79960 | Q6IE81 | JADE1_HUMAN | EPL1 PF10513 17-181, PHD_2 PF13831 218-251, zf-HC5HC2H_2 PF13832 256-369 | Jade1 | 1925835 | Q6ZPI0 | JADE1_MOUSE | PHF | Zinc fingers, PHD-type | Histone modification write | Histone acetylation | 16387653 | HBO1 | histone | H3, H4 | H3ac, H4ac | 16387653 | HBO1-JADE(1,2,3=PHF15,PHF16,PHF17)-ING-hEAF6 tetramer complexes are likely responsible for the majority of histone H4 acetylation higher eukaryotes. | # |
JADE2
(details) |
22984 | jade family PHD finger 2 | 23338 | Q9NQC1 | JADE2_HUMAN | EPL1 PF10513 16-177, PHD_2 PF13831 214-247, zf-HC5HC2H_2 PF13832 253-364 | Jade2 | 1924151 | Q6ZQF7 | JADE2_MOUSE | PHF | Zinc fingers, PHD-type | Histone modification write | Histone acetylation | 16387653 | HBO1 | histone | H3, H4 | H3ac, H4ac | 16387653 | HBO1-JADE(1,2,3=PHF15,PHF16,PHF17)-ING-hEAF6 tetramer complexes are likely responsible for the majority of histone H4 acetylation higher eukaryotes. | # |
JADE3
(details) |
22982 | jade family PHD finger 3 | 9767 | Q92613 | JADE3_HUMAN | EPL1 PF10513 47-177, PHD_2 PF13831 215-248, zf-HC5HC2H_2 PF13832 254-366 | Jade3 | 2148019 | Q6IE82 | JADE3_MOUSE | PHF | Zinc fingers, PHD-type | Histone modification write | Histone acetylation | 14612400 | HBO1 | histone | H3, H4 | H3ac, H4ac | 14612400 | Function in the activation and/or repression of Hox complex genes via modulation of chromatin structure. | # |
JAK2
(details) |
6192 | Janus kinase 2 | 3717 | O60674 | JAK2_HUMAN | FERM_F1 PF18379 39-133, FERM_F2 PF18377 144-261, Jak1_Phl PF17887 306-381, domain PF21990 398-502, PK_Tyr_Ser-Thr PF07714 545-805 849-1122 | Jak2 | 96629 | Q62120 | JAK2_MOUSE | SH2D | SH2 domain containing | Histone modification write | Histone phosphorylation | 19783980 | # | histone | H3T41 | H3T41ph | 19783980 | Human JAK2 is present in the nucleus of haematopoietic cells and directly phosphorylates Tyr 41 (Y41) on histone H3. | # |
JARID2
(details) |
6196 | jumonji, AT rich interactive domain 2 | 3720 | Q92833 | JARD2_HUMAN | JmjN PF02375 558-591, ARID PF01388 624-709, JmjC PF02373 916-1031, zf-C5HC2 PF02928 1139-1191 | Jarid2 | 104813 | Q62315 | JARD2_MOUSE | # | # | Histone modification write cofactor | Histone methylation | 20075857 | PRC2 | histone | H3K27, H3K9 | # | 20075857 | JARID2 is sufficient to recruit PcG proteins to a heterologous promoter, and inhibition of JARID2 expression leads to a major loss of PcG binding and to a reduction of H3K27me3 levels on target genes. | # |
JDP2
(details) |
17546 | Jun dimerization protein 2 | 122953 | Q8WYK2 | JDP2_HUMAN | bZIP_1 PF00170 70-128 | Jdp2 | 1932093 | P97875 | JDP2_MOUSE | bZIP | basic leucine zipper proteins | Chromatin remodeling, Histone modification erase cofactor | Histone acetylation | 16518400 | # | DNA | # | # | 16518400 | JDP2 has histone-chaperone activity in vitro. The sequence-specific DNA-binding protein JDP2 may control transcription via direct regulation of the modification of histones and the assembly of chromatin. | # |
JMJD1C
(details) |
12313 | jumonji domain containing 1C | 221037 | Q15652 | JHD2C_HUMAN | domain PF22989 11-86, domain PF22988 108-181, domain PF22987 179-254, JmjC PF02373 2379-2481 | Jmjd1c | 1918614 | Q69ZK6 | JHD2C_MOUSE | # | # | Histone modification erase | Histone methylation | 17549425 | # | histone | H3K9me | H3K9 | 17549425 | JMJD1A (TSGA), JMJD1B (5qNCA) and JMJD1C with the common domain architecture are histone H3K9 demethylases implicated in the nuclear hormone receptor-based transcriptional regulation. | # |
JMJD6
(details) |
19355 | jumonji domain containing 6 | 23210 | Q6NYC1 | JMJD6_HUMAN | JmjC PF02373 174-288 | Jmjd6 | 1858910 | Q9ERI5 | JMJD6_MOUSE | # | # | Histone modification erase | Histone methylation | 17947579 | # | histone | H3R2me, H4R3me | H3R2, H4R3 | 17947579 | The Jumonji domain-containing 6 protein (JMJD6) is a JmjC-containing iron- and 2-oxoglutarate-dependent dioxygenase that demethylates histone H3 at arginine 2 (H3R2) and histone H4 at arginine 3 (H4R3) in both biochemical and cell-based assays. | # |
KANSL1
(details) |
24565 | KAT8 regulatory NSL complex subunit 1 | 284058 | Q7Z3B3 | KANL1_HUMAN | PEHE PF15275 887-1020 | Kansl1 | 1923969 | Q80TG1 | KANL1_MOUSE | # | # | Histone modification write cofactor, Histone modification write cofactor | Histone methylation, Histone acetylation | 20018852 | NSL, CHD8, MLL2/3, MLL4/WBP7 | histone | H4 | H4ac | 20018852 | As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription. | # |
KANSL2
(details) |
26024 | KAT8 regulatory NSL complex subunit 2 | 54934 | Q9H9L4 | KANL2_HUMAN | zf-C3Hc3H PF13891 28-92 308-365 | Kansl2 | 1916862 | Q8BQR4 | KANL2_MOUSE | # | # | Histone modification write cofactor | Histone acetylation | 20018852 | NSL | histone | H5 | H4ac | 20018852 | As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription. | # |
KANSL3
(details) |
25473 | KAT8 regulatory NSL complex subunit 3 | 55683 | Q9P2N6 | KANL3_HUMAN | Abhydrolase_11 PF20408 329-449 | Kansl3 | 1918055 | A2RSY1 | KANL3_MOUSE | # | # | Histone modification write cofactor | Histone acetylation | 20018852 | NSL | histone | H6 | H4ac | 20018852 | As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription. | # |
KAT2A
(details) |
4201 | K(lysine) acetyltransferase 2A | 2648 | Q92830 | KAT2A_HUMAN | PCAF_N PF06466 92-335, Acetyltransf_1 PF00583 536-627, Bromodomain PF00439 738-819 | Kat2a | 1343101 | Q9JHD2 | KAT2A_MOUSE | KAT | Chromatin-modifying enzymes / K-acetyltransferases | Histone modification write | Histone acetylation | 10611234 | TFTC-HAT, SAGA, ATAC, STAGA | histone | # | # | 10611234 | Current models of HAT protein activity suggest that one hypothesis for the role of hGCN5=KAT2A in c-Myc's activities might be due to the relaxing of chromatin packaging at target genes following histone acetylation by hGCN5. | # |
KAT2B
(details) |
8638 | K(lysine) acetyltransferase 2B | 8850 | Q92831 | KAT2B_HUMAN | PCAF_N PF06466 77-323, Acetyltransf_1 PF00583 531-622, Bromodomain PF00439 733-814 | Kat2b | 1343094 | Q9JHD1 | KAT2B_MOUSE | KAT | Chromatin-modifying enzymes / K-acetyltransferases | Histone modification write | Histone acetylation | 8945521 | # | histone | # | # | 8945521 | The cellular p300/CBP associated factor (PCAF=KAT2B) possesses intrinsic histone acetyltransferase activity. | # |
KAT5
(details) |
5275 | K(lysine) acetyltransferase 5 | 10524 | Q92993 | KAT5_HUMAN | Tudor-knot PF11717 7-65, zf-MYST PF17772 229-283, MOZ_SAS PF01853 288-470 | Kat5 | 1932051 | Q8CHK4 | KAT5_MOUSE | KAT, ZC2HC | Chromatin-modifying enzymes / K-acetyltransferases, Zinc fingers, C2HC-type containing | Histone modification write | Histone acetylation | 10096020 | SWR, NuA4, Piccolo_NuA4 | histone | H2AK5, H3K14, H4K5,H4K8, H4K12, H4K16 | H2AK5ac, H3K14ac, H4K5ac, H4K8ac, H4K12ac, H4K16ac | 10096020 | Tip60=KAT5 significantly acetylates amino-terminal tail peptides of histones H2A, H3 and H4, but not H2B, consistent with substrate preference on intact histones. Preferred acetylation sites for Tip60 are the Lys-5 of histone H2A, the Lys-14 of histone H3, and the Lys-5, -8, -12, -16 of histone H4. | # |
KAT6A
(details) |
13013 | K(lysine) acetyltransferase 6A | 7994 | Q92794 | KAT6A_HUMAN | SAMD1_WH PF21524 10-73, PHD PF00628 208-263 264-310, zf-MYST PF17772 507-560, MOZ_SAS PF01853 564-741 | Kat6a | 2442415 | Q8BZ21 | KAT6A_MOUSE | KAT, ZC2HC, PHF | Chromatin-modifying enzymes / K-acetyltransferases, Zinc fingers, C2HC-type containing, Zinc fingers, PHD-type | Histone modification write | Histone acetylation | 11313971 | MOZ/MORF | histone | H3, H4 | H3ac, H4ac | 11313971 | The monocytic leukemia zinc finger protein MOZ=KAT6A is a histone acetyltransferase. | # |
KAT6B
(details) |
17582 | K(lysine) acetyltransferase 6B | 23522 | Q8WYB5 | KAT6B_HUMAN | SAMD1_WH PF21524 9-73, PHD PF00628 271-317, zf-MYST PF17772 718-771, MOZ_SAS PF01853 776-979 | Kat6b | 1858746 | Q8BRB7 | KAT6B_MOUSE | KAT, ZC2HC, PHF | Chromatin-modifying enzymes / K-acetyltransferases, Zinc fingers, C2HC-type containing, Zinc fingers, PHD-type | Histone modification write | Histone acetylation | 10497217 | MOZ/MORF | histone | H3 | H3ac | 10497217 | A novel human histone acetyltransferase, termed MORF=KAT6B (monocytic leukemia zinc finger protein-related factor). | # |
KAT7
(details) |
17016 | K(lysine) acetyltransferase 7 | 11143 | O95251 | KAT7_HUMAN | zf-C2HC PF01530 184-212, zf-MYST PF17772 337-388, MOZ_SAS PF01853 393-570 | Kat7 | 2182799 | Q5SVQ0 | KAT7_MOUSE | KAT, ZC2HC | Chromatin-modifying enzymes / K-acetyltransferases, Zinc fingers, C2HC-type containing | Histone modification write | Histone acetylation | 10438470 | HBO1 | histone | H4 | H4ac | 10438470 | A novel protein, HBO1=KAT7 (histone acetyltransferase binding to ORC), that interacts with human ORC1 protein. | # |
KAT8
(details) |
17933 | K(lysine) acetyltransferase 8 | 84148 | Q9H7Z6 | KAT8_HUMAN | Tudor-knot PF11717 54-110, zf-MYST PF17772 176-230, MOZ_SAS PF01853 235-412 | Kat8 | 1915023 | Q9D1P2 | KAT8_MOUSE | KAT, ZC2HC | Chromatin-modifying enzymes / K-acetyltransferases, Zinc fingers, C2HC-type containing | Histone modification write | Histone acetylation | 10786633 | NSL, CHD8, MLL2/3, COMPASS-like MLL1,2, MLL4/WBP7 | histone | H2A, H3, H4 | H2Aac, H3ac, H4ac | 10786633 | A recombinant C-terminal portion of hMOF=KAT8 has histone acetyltransferase activity directed toward histones H3, H2A and H4, a specificity characteristic of other MYST family histone acetyltransferases. | # |
KDM1A
(details) |
29079 | lysine (K)-specific demethylase 1A | 23028 | O60341 | KDM1A_HUMAN | SWIRM PF04433 183-264, Amino_oxidase PF01593 288-826 | Kdm1a | 1196256 | Q6ZQ88 | KDM1A_MOUSE | KDM | Chromatin-modifying enzymes / K-demethylases | Histone modification erase | Histone methylation | 16223729 | NuRD, BHC, SCL | histone | H3K4me1, H3K4me2, H3K9me | H3K4, H3K9 | 16223729 | Human histone demethylase LSD1=KDM1A is a flavin-dependent amine oxidase that catalyzes the specific removal of methyl groups from mono- and dimethylated Lys4 of histone H3. | # |
KDM1B
(details) |
21577 | lysine (K)-specific demethylase 1B | 221656 | Q8NB78 | KDM1B_HUMAN | zf-CW PF07496 137-189, SWIRM PF04433 292-364, Amino_oxidase PF01593 392-819 | Kdm1b | 2145261 | Q8CIG3 | KDM1B_MOUSE | KDM | Chromatin-modifying enzymes / K-demethylases | Histone modification erase | Histone methylation | 19727073 | # | histone | H3K4me1, H3K4me2 | H3K4 | 19727073 | KDM1B is a histone H3K4 demethylase required to establish maternal genomic imprints. | # |
KDM2A
(details) |
13606 | lysine (K)-specific demethylase 2A | 22992 | Q9Y2K7 | KDM2A_HUMAN | JHD PF17811 304-343, zf-CXXC PF02008 565-609, PHD_4 PF16866 615-676, F-box-like PF12937 896-935 | Kdm2a | 1354736 | P59997 | KDM2A_MOUSE | FBXL, KDM | F-boxes / Leucine-rich repeats, Chromatin-modifying enzymes / K-demethylases | Histone modification erase | Histone methylation | 20417597 | # | histone | H3K36me2 | H3K36 | 20417597 | CpG islands directly recruit the H3K36-specific lysine demethylase enzyme KDM2A. Nucleation of KDM2A at these elements results in removal of H3K36 methylation, creating CpG island chromatin that is uniquely depleted of this modification. | # |
KDM2B
(details) |
13610 | lysine (K)-specific demethylase 2B | 84678 | Q8NHM5 | KDM2B_HUMAN | Cupin_8 PF13621 150-331, JHD PF17811 334-375, zf-CXXC PF02008 607-651, PHD_4 PF16866 657-723, F-box-like PF12937 1068-1107 | Kdm2b | 1354737 | Q6P1G2 | KDM2B_MOUSE | FBXL, KDM | F-boxes / Leucine-rich repeats, Chromatin-modifying enzymes / K-demethylases | Histone modification erase | Histone methylation | 17994099 | BCOR | histone | H3K4me3, H3K36me2 | H3K4, H3K36 | 17994099 | JHDM1B =KDM2B is a histone demethylase that catalyses the demethylation of H3K4me3. | # |
KDM3A
(details) |
20815 | lysine (K)-specific demethylase 3A | 55818 | Q9Y4C1 | KDM3A_HUMAN | domain PF22989 8-82, domain PF22988 92-182, domain PF22987 184-249, JmjC PF02373 1158-1264 | Kdm3a | 98847 | Q6PCM1 | KDM3A_MOUSE | KDM | Chromatin-modifying enzymes / K-demethylases | Histone modification erase | Histone methylation | 16603237 | # | histone | H3K9me1, H3K9me2 | H3K9 | 16603237 | JHDM2A =KDM3A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor. | # |
KDM3B
(details) |
1337 | lysine (K)-specific demethylase 3B | 51780 | Q7LBC6 | KDM3B_HUMAN | domain PF22989 10-83, domain PF22988 91-188, domain PF22987 189-254, JmjC PF02373 1599-1704 | Kdm3b | 1923356 | Q6ZPY7 | KDM3B_MOUSE | KDM | Chromatin-modifying enzymes / K-demethylases | Histone modification erase | Histone methylation | 16603237 | # | histone | H3K9me1, H3K9me2 | H3K9 | 16603237 | A JmjC domain-containing protein (KDM3B=JmjC domain-containing histone demethylation protein 2B), JHDM2A, which specifically demethylates mono- and dimethyl-H3K9. | # |
KDM4A
(details) |
22978 | lysine (K)-specific demethylase 4A | 9682 | O75164 | KDM4A_HUMAN | JmjN PF02375 14-49, JmjC PF02373 175-291, PHD_2 PF13831 732-767, zf-HC5HC2H_2 PF13832 774-884, Tudor_2 PF18104 902-936 959-994 | Kdm4a | 2446210 | Q8BW72 | KDM4A_MOUSE | KDM, TDRD | Chromatin-modifying enzymes / K-demethylases, Tudor domain containing | Histone modification erase | Histone methylation | 16603238 | # | histone | H3K4me3, H3K36me3 | H3K4me2, H3K36me2 | 16603238 | The JmjC domain-containing protein JMJD2A =KDM4A reverses trimethylated H3-K9/K36 to di- but not mono- or unmethylated products. Overexpression of JMJD2A (but not a catalytically inactive mutant) reduces H3-K9/K36 trimethylation levels in cultured cells. | # |
KDM4B
(details) |
29136 | lysine (K)-specific demethylase 4B | 23030 | O94953 | KDM4B_HUMAN | JmjN PF02375 16-50, JmjC PF02373 176-292, PHD_2 PF13831 754-789, zf-HC5HC2H_2 PF13832 796-907, Tudor_2 PF18104 922-956 978-1014 | Kdm4b | 2442355 | Q91VY5 | KDM4B_MOUSE | KDM, TDRD | Chromatin-modifying enzymes / K-demethylases, Tudor domain containing | Histone modification erase | Histone methylation | 16603238 | # | histone | H3K9me3 | H3K9me1, H3K9me2 | 16603238 | Human JMJD2(B, C, D) =KDM4(B, C, D) subfamily members function as trimethylation-specific demethylases, converting H3-K9Me3 to H3-K9Me2 and H3-K9Me1, respectively. | # |
KDM4C
(details) |
17071 | lysine (K)-specific demethylase 4C | 23081 | Q9H3R0 | KDM4C_HUMAN | JmjN PF02375 17-51, JmjC PF02373 177-293, PHD_2 PF13831 712-747, zf-HC5HC2H_2 PF13832 754-864, Tudor_2 PF18104 881-916 939-974 | Kdm4c | 1924054 | Q8VCD7 | KDM4C_MOUSE | KDM, TDRD | Chromatin-modifying enzymes / K-demethylases, Tudor domain containing | Histone modification erase | Histone methylation | 16603238 | # | histone | H3K9me3, H3K36me3 | H3K9me1, H3K9me2 | 16603238 | Human JMJD2(B, C, D) =KDM4(B, C, D) subfamily members function as trimethylation-specific demethylases, converting H3-K9Me3 to H3-K9Me2 and H3-K9Me1, respectively. | # |
KDM4D
(details) |
25498 | lysine (K)-specific demethylase 4D | 55693 | Q6B0I6 | KDM4D_HUMAN | JmjN PF02375 19-53, JmjC PF02373 179-295 | Kdm4d | 3606484 | Q3U2K5 | KDM4D_MOUSE | KDM | Chromatin-modifying enzymes / K-demethylases | Histone modification erase | Histone methylation | 16603238 | # | histone | H3K9me3 | H3K9me1, H3K9me2 | 16603238 | Human JMJD2(B, C, D) =KDM4(B, C, D) subfamily members function as trimethylation-specific demethylases, converting H3-K9Me3 to H3-K9Me2 and H3-K9Me1, respectively. | # |
KDM4E
(details) |
37098 | lysine (K)-specific demethylase 4E | 390245 | B2RXH2 | KDM4E_HUMAN | JmjN PF02375 16-50, JmjC PF02373 176-292 | # | # | # | # | KDM | Chromatin-modifying enzymes / K-demethylases | Histone modification erase | Histone methylation | 21914792 | # | histone | H3K9me2, H3K9me3 | H3K9 | 21914792 | KDM4D and KDM4E (which is catalytically active) catalyze demethylation of H3K9me3/me2. | # |
KDM5A
(details) |
9886 | lysine (K)-specific demethylase 5A | 5927 | P29375 | KDM5A_HUMAN | JmjN PF02375 20-53, ARID PF01388 86-170, PHD PF00628 296-340 1164-1215, JmjC PF02373 470-586, KDM5_C-hel PF21323 590-644, zf-C5HC2 PF02928 676-728, PLU-1 PF08429 741-1070 | Kdm5a | 2136980 | Q3UXZ9 | KDM5A_MOUSE | KDM, PHF | Chromatin-modifying enzymes / K-demethylases, Zinc fingers, PHD-type | Histone modification erase | Histone methylation | 17320163 | # | histone | H3K4me3 | H3K4 | 17320163 | The retinoblastoma binding protein RBP2 =KDM5A is an H3K4 demethylase. | # |
KDM5B
(details) |
18039 | lysine (K)-specific demethylase 5B | 10765 | Q9UGL1 | KDM5B_HUMAN | JmjN PF02375 33-66, ARID PF01388 99-183, PHD PF00628 312-356 1178-1221 1487-1535, JmjC PF02373 486-602, KDM5_C-hel PF21323 606-660, zf-C5HC2 PF02928 692-744, PLU-1 PF08429 758-1088 | Kdm5b | 1922855 | Q80Y84 | KDM5B_MOUSE | KDM, PHF | Chromatin-modifying enzymes / K-demethylases, Zinc fingers, PHD-type | Histone modification erase | Histone methylation | 17363312 | # | histone | H3K4me3 | H3K4 | 17363312 | PLU-1 =KDM5B, a transcriptional repressor implicated in breast cancer, is a histone demethylase enzyme that has the ability to reverse the trimethyl H3K4 modification state. | # |
KDM5C
(details) |
11114 | lysine (K)-specific demethylase 5C | 8242 | P41229 | KDM5C_HUMAN | JmjN PF02375 15-48, ARID PF01388 80-165, PHD PF00628 327-371, JmjC PF02373 501-617, KDM5_C-hel PF21323 621-675, zf-C5HC2 PF02928 707-759, PLU-1 PF08429 771-1098 | Kdm5c | 99781 | P41230 | KDM5C_MOUSE | KDM, PHF | Chromatin-modifying enzymes / K-demethylases, Zinc fingers, PHD-type | Histone modification erase | Histone methylation | 17320160 | # | histone | H3K4me3 | H3K4me2, H3K4me1 | 17320160 | The X-linked mental retardation (XLMR) gene SMCX (JARID1C)=KDM5C, which encodes a JmjC-domain protein, reverses H3K4me3 to di- and mono- but not unmethylated products. | # |
KDM5D
(details) |
11115 | lysine (K)-specific demethylase 5D | 8284 | Q9BY66 | KDM5D_HUMAN | JmjN PF02375 15-48, ARID PF01388 81-165, PHD PF00628 317-361, JmjC PF02373 491-607, KDM5_C-hel PF21323 611-665, zf-C5HC2 PF02928 697-749, PLU-1 PF08429 763-1085 | Kdm5d | 99780 | Q62240 | KDM5D_MOUSE | KDM, PHF | Chromatin-modifying enzymes / K-demethylases, Zinc fingers, PHD-type | Histone modification erase | Histone methylation | 17320160 | # | histone | H3K4me3, H3K4me2 | H3K4 | 17320160 | SMCX family members, including SMCY=KDM5D, RBP2, and PLU-1, demethylate H3K4me3. | # |
KDM6A
(details) |
12637 | lysine (K)-specific demethylase 6A | 7403 | O15550 | KDM6A_HUMAN | TPR_8 PF13181 205-237, JmjC PF02373 1133-1241, KDM6_C-hel PF21322 1248-1303, KDM6_GATAL PF21326 1320-1380 | Kdm6a | 1095419 | O70546 | KDM6A_MOUSE | KDM, TTC | Chromatin-modifying enzymes / K-demethylases, Tetratricopeptide (TTC) repeat domain containing | Histone modification erase | Histone methylation | 17851529 | CHD8, MLL2/3, MLL4/WBP7, COMPASS-like MLL3,4 | histone | H3K27me2. H3K27me3 | H3K27 | 17851529 | The JmjC-domain-containing proteins UTX=KDM6A and JMJD3 catalyse demethylation of H3K27me3/2. | # |
KDM6B
(details) |
29012 | lysine (K)-specific demethylase 6B | 23135 | O15054 | KDM6B_HUMAN | JmjC PF02373 1377-1485, KDM6_C-hel PF21322 1492-1547, KDM6_GATAL PF21326 1560-1623 | Kdm6b | 2448492 | Q5NCY0 | KDM6B_MOUSE | KDM | Chromatin-modifying enzymes / K-demethylases | Histone modification erase | Histone methylation | 17851529 | # | histone | H3K27me2. H3K27me4 | H3K28 | 17851529 | The JmjC-domain-containing proteins UTX=KDM6A and JMJD3=KDM6B catalyse demethylation of H3K27me3/2. | # |
KDM7A
(details) |
22224 | lysine (K)-specific demethylase 7A | 80853 | Q6ZMT4 | KDM7A_HUMAN | PHD PF00628 40-85, JmjC PF02373 269-369, JHD PF17811 373-480 | Kdm7a | 2443388 | Q3UWM4 | KDM7A_MOUSE | KDM, PHF | Chromatin-modifying enzymes / K-demethylases, Zinc fingers, PHD-type | Histone modification erase | Histone methylation | 20194436 | # | histone | H3K9me2, H3K27me2, H4K20me1 | H3K9, H3K27, H4K20 | 20194436 | KDM7 (also known as JHDM1D) is a dual demethylase for H3K9 and H3K27 that functions as an eraser of silencing marks on chromatin during brain development. Specifically binds trimethylated 'Lys-4' of histone H3 (H3K4me3), affecting histone demethylase specificity: in presence of H3K4me3, it has no demethylase activity toward H3K9me2, while it has high activity toward H3K27me2. Demethylates H3K9me2 in absence of H3K4me3. Has activity toward H4K20Me1 only when nucleosome is used as a substrate and when not histone octamer is used as substrate. | # |
KDM8
(details) |
25840 | lysine (K)-specific demethylase 8 | 79831 | Q8N371 | KDM8_HUMAN | Cupin_8 PF13621 194-416 | Kdm8 | 1924285 | Q9CXT6 | KDM8_MOUSE | KDM | Chromatin-modifying enzymes / K-demethylases | Histone modification erase | Histone methylation | 20457893 | # | histone | H3K36me2 | H3K36 | 20457893 | JMJD5 (now renamed KDM8), a JmjC family member, demethylates H3K36me2 and is required for cell cycle progression. | # |
KEAP1
(details) |
23177 | kelch-like ECH-associated protein 1 | 9817 | Q14145 | KEAP1_HUMAN | BTB PF00651 67-178, BACK PF07707 184-285, Kelch_1 PF01344 327-359 361-410 412-457 459-504 507-551 553-598 | Keap1 | 1858732 | Q9Z2X8 | KEAP1_MOUSE | KLHL, BTBD | Kelch-like, "BTB/POZ domain containing" | Chromatin remodeling | # | 21920360 | # | chromatin | # | # | # | Interacts with the NURF Nucleosome Remodeling Factor complex. | # |
KHDRBS1
(details) |
18116 | KH domain-containing, RNA-binding, signal transduction-associated protein 1 (GAP-associated tyrosine phosphoprotein p62) (Src-associated in mitosis 68 kDa protein) (Sam68) (p21 Ras GTPase-activating protein-associated p62) (p68) | 10657 | Q07666 | KHDR1_HUMAN | Qua1 PF16274 102-153, KH_1 PF00013 159-209, Sam68-YY PF16568 368-420 | Khdrbs1 | 893579 | Q60749 | KHDR1_MOUSE | KHDRBS | Signal transduction and activation of RNA metabolism family | RNA modification | Alternative splicing | 24514149 | # | RNA | mRNA | # | 24514149 | Regulates BCL-X and VEGF alternative splicing | New |
KLF18
(details) |
51793 | Kruppel like factor 18 | 105378952 | A0A0U1RQI7 | KLF18_HUMAN | zf-C2H2 PF00096 994-1018 1024-1046 | Zfp352 | 2387418 | A2AML7 | A2AML7_MOUSE | KLF | Kruppel like factors | TF | # | 24244731 | # | DNA | DNA | # | 24244731 | # | New |
KMT2A
(details) |
7132 | lysine (K)-specific methyltransferase 2A | 4297 | Q03164 | KMT2A_HUMAN | zf-CXXC PF02008 1149-1194, PHD PF00628 1481-1530 1569-1624, zf-HC5HC2H PF13771 1897-1978, FYRN PF05964 2016-2077, FYRC PF05965 3666-3747, SET PF00856 3840-3945 | Kmt2a | 96995 | P55200 | KMT2A_MOUSE | KMT, PHF | Chromatin-modifying enzymes / K-methyltransferases, Zinc fingers, PHD-type | Histone modification write | Histone methylation | 19187761 | MLL-HCF, CHD8, COMPASS-like MLL1,2 | histone | H3K4 | H3K4me | 19187761 | MLL1 SET domain can incorporate methyl groups into unmodified or H3K4me1 substrates, signifying both mono- and dimethylation activity. | # |
KMT2B
(details) |
15840 | lysine (K)-specific methyltransferase 2B | 9757 | Q9UMN6 | KMT2B_HUMAN | zf-CXXC PF02008 959-1005, PHD PF00628 1203-1250 1251-1300 1337-1393, zf-HC5HC2H PF13771 1605-1685, FYRN PF05964 1731-1784, FYRC PF05965 2415-2494, SET PF00856 2580-2691 | Kmt2b | 109565 | O08550 | KMT2B_MOUSE | KMT | Chromatin-modifying enzymes / K-methyltransferases | Histone modification write | Histone methylation | 17707229 | Menin-associated_HMT, MLL2/3, COMPASS-like MLL3,4 | histone | H3K4 | H3K4me3 | 17707229 | MLL (=KMT2B)-containing complexes methylate histone H3 at lysine 4 (H3K4) and have been implicated in the regulation of transcription. | # |
KMT2C
(details) |
13726 | lysine (K)-specific methyltransferase 2C | 58508 | Q8NEZ4 | KMT2C_HUMAN | zf-HC5HC2H PF13771 248-331, PHD PF00628 343-389 390-436 466-519 958-1008, zf-HC5HC2H_2 PF13832 4401-4506, FYRN PF05964 4546-4604, FYRC PF05965 4608-4692, SET PF00856 4781-4887 | Kmt2c | 2444959 | Q8BRH4 | KMT2C_MOUSE | KMT, PHF | Chromatin-modifying enzymes / K-methyltransferases, Zinc fingers, PHD-type | Histone modification write | Histone methylation | 20937768 | MLL2/3, COMPASS-like MLL3,4 | histone | H3K4 | H3K4me | 20937768 | In humans, multiple Set1-like HMT complexes with H3K4 HMT activities have been identified. Each of these complexes contains the SET domain-containing homologs of yeast Set1, including human Set1 (hSet1), MLL1 (mixed lineage leukemia 1, also known as MLL, HRX, ALL1, or KMT2A), MLL2 (mixed-lineage leukemia 2, also known as HRX2 or KMT2B), MLL3 (mixed-lineage leukemia 3, also known as HALR or KMT2C), and MLL4 (mixed-lineage leukemia 4, also known as ALR or KMT2D), which carry the enzymatic activity for the associated complexes. | # |
KMT2D
(details) |
7133 | lysine (K)-specific methyltransferase 2D | 8085 | O14686 | KMT2D_HUMAN | zf-HC5HC2H PF13771 139-218, PHD PF00628 228-274 276-321 1379-1428 1429-1474, zf-HC5HC2H_2 PF13832 5031-5136, FYRN PF05964 5176-5233, FYRC PF05965 5236-5322, SET PF00856 5408-5513 | Kmt2d | 2682319 | Q6PDK2 | KMT2D_MOUSE | KMT, PHF | Chromatin-modifying enzymes / K-methyltransferases, Zinc fingers, PHD-type | Histone modification write | Histone methylation | 20937768 | COMPASS-like MLL1,2, MLL4/WBP7, COMPASS-like MLL3,4 | histone | H3K4 | H3K4me | 20937768 | In humans, multiple Set1-like HMT complexes with H3K4 HMT activities have been identified. Each of these complexes contains the SET domain-containing homologs of yeast Set1, including human Set1 (hSet1), MLL1 (mixed lineage leukemia 1, also known as MLL, HRX, ALL1, or KMT2A), MLL2 (mixed-lineage leukemia 2, also known as HRX2 or KMT2B), MLL3 (mixed-lineage leukemia 3, also known as HALR or KMT2C), and MLL4 (mixed-lineage leukemia 4, also known as ALR or KMT2D), which carry the enzymatic activity for the associated complexes. | # |
KMT2E
(details) |
18541 | lysine (K)-specific methyltransferase 2E | 55904 | Q8IZD2 | KMT2E_HUMAN | PHD_5 PF20826 118-164, SET PF00856 343-447 | Kmt2e | 1924825 | Q3UG20 | KMT2E_MOUSE | KMT, PHF | Chromatin-modifying enzymes / K-methyltransferases, Zinc fingers, PHD-type | Histone modification write | Histone methylation | 19377461 | # | histone | H3K4 | H3K4me1, H3K4me2 | 19377461 | Nuclear GlcNAcylation of the histone lysine methyltransferase (HKMT), MLL5, by O-GlcNAc transferase facilitates retinoic-acid-induced granulopoiesis in human HL60 promyelocytes through methylation of H3K4. | # |
L3MBTL1
(details) |
15905 | l(3)mbt-like 1 (Drosophila) | 26013 | Q9Y468 | LMBL1_HUMAN | MBT PF02820 310-377 417-484 521-586, zf-C2HC PF01530 622-650 | L3mbtl1 | 2676663 | A2A5N8 | LMBL1_MOUSE | ZC2HC, SAMD | Zinc fingers, C2HC-type containing, Sterile alpha motif (SAM) domain containing | Histone modification read | # | 18026117 | L3MBTL1 | histone | H1BK26, H4K20 | # | 18026117 | Crystal structures of the L3MBTL1 MBT repeats in complex with histone H4 peptides dimethylated on Lys20 (H4K20me2). Only the second of the three MBT repeats can bind mono- and dimethylated histone peptides. Its binding pocket has similarities to that of 53BP1 and is able to recognize the degree of histone lysine methylation. | # |
L3MBTL2
(details) |
18594 | l(3)mbt-like 2 (Drosophila) | 83746 | Q969R5 | LMBL2_HUMAN | zf-FCS_1 PF21319 87-118, MBT PF02820 214-286 327-390 432-503 540-604 | L3mbtl2 | 2443584 | P59178 | LMBL2_MOUSE | # | # | Histone modification read | # | 19233876 | RING2-L3MBTL2 | histone | H3K4, H3K9, H3K27, H4K20 | # | 19233876 | Methylation-state-specific recognition of histones by the MBT repeat protein L3MBTL2. | # |
L3MBTL3
(details) |
23035 | l(3)mbt-like 3 (Drosophila) | 84456 | Q96JM7 | LMBL3_HUMAN | MBT PF02820 268-335 375-441 479-544, SAM_1 PF00536 707-770 | L3mbtl3 | 2143628 | Q8BLB7 | LMBL3_MOUSE | SAMD | Sterile alpha motif (SAM) domain containing | Histone modification read | # | 23292653 | # | histone | H4K20me | # | 23292653 | Binds L3MBTL3 with a similar affinity to H4K20me histone | # |
L3MBTL4
(details) |
26677 | l(3)mbt-like 4 (Drosophila) | 91133 | Q8NA19 | LMBL4_HUMAN | MBT PF02820 88-155 196-263 300-366, zf-C2HC PF01530 379-407, SAM_1 PF00536 543-605 | L3mbtl4 | 2444889 | B1B1A0 | LMBL4_MOUSE | SAMD | Sterile alpha motif (SAM) domain containing | Histone modification read | # | 20698951 | # | histone | HKme | # | 20698951 | The L3MBTL4 protein contains three "malignant brain tumor" (MBT) domains. The MBT domain binds methylated histone residues. | # |
LAS1L
(details) |
25726 | LAS1-like (S. cerevisiae) | 81887 | Q9Y4W2 | LAS1L_HUMAN | Las1 PF04031 43-187 | Las1l | 1923380 | A2BE28 | LAS1L_MOUSE | # | # | Histone modification write cofactor, Histone modification write cofactor | Histone methylation, Histone acetylation | 20442285 | CHD8, MLL2/3, MLL4/WBP7 | histone | H3K4, H3,H4,H2A | H3K4me, H3K4me2, H3Ac, H4Ac, H2AAc | 15960975 | Facultative member of the MLL1/MLL complex. | # |
LBR
(details) |
6518 | lamin B receptor | 3930 | Q14739 | LBR_HUMAN | LBR_tudor PF09465 2-56, ERG4_ERG24 PF01222 199-615 | Lbr | 2138281 | Q3U9G9 | LBR_MOUSE | TDRD | Tudor domain containing | # | # | 22498752 | # | chromatin | # | # | # | Anchors the lamina and the heterochromatin to the inner nuclear membrane. | # |
LEO1
(details) |
30401 | Leo1, Paf1/RNA polymerase II complex component, homolog (S. cerevisiae) | 123169 | Q8WVC0 | LEO1_HUMAN | Leo1 PF04004 374-538 | Leo1 | 2685031 | Q5XJE5 | LEO1_MOUSE | # | # | Histone modification write cofactor | Histone ubiquitination | 24038468 | # | histone | # | # | # | Part of the PAF1 complex, which may be involved in recruitment of ubiquitination complexes. Important for PAF1 binding to H3. | # |
LRWD1
(details) |
21769 | leucine-rich repeats and WD repeat domain containing 1 | 222229 | Q9UFC0 | LRWD1_HUMAN | domain PF12799 48-104, WD40 PF00400 384-421 | Lrwd1 | 1918985 | Q8BUI3 | LRWD1_MOUSE | WDR | WD repeat domain containing | Chromatin remodeling | # | 20932478 | # | histone, DNA | H3K9me3, H3K27me3 | # | 20932478 | A highly conserved, leucine-rich repeats and WD40 repeat domain-containing protein 1 (LRWD1) or ORC-associated (ORCA) in human cells that interacts with ORC and modulates chromatin association of ORC. ORCA colocalizes with ORC and shows similar cell-cycle dynamics. ORCA efficiently recruits ORC to chromatin. | # |
MAGOH
(details) |
6815 | Protein mago nashi homolog | 4116 | P61326 | MGN_HUMAN | Mago_nashi PF02792 5-146 | Magoh | 1330312 | P61327 | MGN_MOUSE | # | # | RNA modification | Alternative splicing | 22203037 | # | RNA | mRNA | # | 22203037 | Regulates alternative splicing of apoptotic regulators | New |
MAP3K7
(details) |
6859 | mitogen-activated protein kinase kinase kinase 7 | 6885 | O43318 | M3K7_HUMAN | PK_Tyr_Ser-Thr PF07714 36-284 | Map3k7 | 1346877 | Q62073 | M3K7_MOUSE | MAP3K | Mitogen-activated protein kinase cascade / Kinase kinase kinases | Histone modification write | # | 18838386 | # | histone | # | # | # | A member of the ATAC complex. | # |
MAPKAPK3
(details) |
6888 | mitogen-activated protein kinase-activated protein kinase 3 | 7867 | Q16644 | MAPK3_HUMAN | Pkinase PF00069 47-304 | Mapkapk3 | 2143163 | Q3UMW7 | MAPK3_MOUSE | # | # | Chromatin remodeling | # | 15563468 | # | chromatin | # | # | 15563468 | MAPKAP kinase 3pK phosphorylates and regulates chromatin association of the polycomb group protein Bmi1. | # |
MASTL
(details) |
19042 | microtubule associated serine/threonine kinase-like | 84930 | Q96GX5 | GWL_HUMAN | Pkinase PF00069 36-188 736-835 | Mastl | 1914371 | Q8C0P0 | GWL_MOUSE | # | # | Histone modification write | Histone phosphorylation | 20818157 | # | histone | H1, H3 | H1p, H3p | 20818157 | Phosphorylates histone protein in vitro; however such activity is unsure in vivo (UniProt). | # |
MAX
(details) |
6913 | MYC associated factor X | 4149 | P61244 | MAX_HUMAN | HLH PF00010 24-74 | Max | 96921 | P28574 | MAX_MOUSE | bHLH | Basic helix-loop-helix proteins | Histone modification write cofactor, TF | Histone methylation, Histone acetylation, TF activator, TF repressor | 18271930, 12004135 | CHD8, MLL2/3, MLL4/WBP7 | DNA | DNA motif | # | 18271930, 12004135 | Part of a multimeric protein complex that contains E2F6, Mga and Max. The complex contains chromatin modifiers such as a novel histone methyltransferase that modifies lysine 9 of histone H3, HP1gamma, and Polycomb group (PcG) proteins. | # |
MAZ
(details) |
6914 | MYC-associated zinc finger protein (purine-binding transcription factor) | 4150 | P56270 | MAZ_HUMAN | zf-C2H2 PF00096 279-301 337-360 366-388, zf-C2H2_4 PF13894 307-329 | Maz | 1338823 | P56671 | MAZ_MOUSE | ZNF | Zinc fingers, C2H2-type | Chromatin remodeling | # | 21920360 | # | chromatin | # | # | # | Interacts with the NURF Nucleosome Remodeling Factor complex. | # |
MBD1
(details) |
6916 | methyl-CpG binding domain protein 1 | 4152 | Q9UIS9 | MBD1_HUMAN | MBD PF01429 2-70, zf-CXXC PF02008 169-215 219-262 331-377 | Mbd1 | 1333811 | Q9Z2E2 | MBD1_MOUSE | # | # | Histone modification write cofactor, TF | Histone methylation, TF repressor | 15327775 | # | DNA | mCG, DNA motif | # | 15327775 | MBD1 recruits SETDB1 to the large subunit of chromatin assembly factor CAF-1 to form an S phase-specific CAF-1/MBD1/SETDB1 complex that facilitates methylation of H3-K9 during replication-coupled chromatin assembly. In the absence of MBD1, H3-K9 methylation is lost at multiple genomic loci and results in activation of p53BP2 gene, normally repressed by MBD1 in HeLa cells. Data suggest a model in which H3-K9 methylation by SETDB1 is dependent on MBD1 and is heritably maintained through DNA replication to support the formation of stable heterochromatin at methylated DNA. | # |
MBD2
(details) |
6917 | methyl-CpG binding domain protein 2 | 8932 | Q9UBB5 | MBD2_HUMAN | MBD PF01429 150-213, MBDa PF16564 221-294, MBD_C PF14048 296-385 | Mbd2 | 1333813 | Q9Z2E1 | MBD2_MOUSE | # | # | Histone modification write cofactor, Histone modification erase cofactor, TF | Histone methylation, Histone acetylation, TF repressor | 16415179 | NuRD, MeCP1 | DNA | mCG, DNA motif | # | 16415179 | Wild-type subnuclear distribution of p66alpha and p66beta depends on the presence of MBD2. Both proteins interact with the tails of all octamer histones in vitro, and acetylation of histone tails interferes with p66 binding. | # |
MBD3
(details) |
6918 | methyl-CpG binding domain protein 3 | 53615 | O95983 | MBD3_HUMAN | MBD PF01429 2-69, MBDa PF16564 79-149, MBD_C PF14048 152-241 | Mbd3 | 1333812 | Q9Z2D8 | MBD3_MOUSE | # | # | Histone modification erase cofactor | Histone acetylation | 12124384 | NuRD | histone | # | # | 12124384 | MBD3 has been identified as a component of the NuRD/Mi2 complex that shows chromatin remodeling and histone deacetylase activities. MBD3 MBD is necessary and sufficient for binding to HDAC1 and MTA2, two components of the NuRD/Mi2 complex. It has been suggested that mCpG-binding-defective MBD3 has evolutionarily conserved its MBD because of the secondary role played by the MBD in protein-protein interactions. | # |
MBD4
(details) |
6919 | methyl-CpG binding domain protein 4 | 8930 | O95243 | MBD4_HUMAN | MBD PF01429 81-149, domain PF00730 463-560 | Mbd4 | 1333850 | Q9Z2D7 | MBD4_MOUSE | # | # | DNA modification | # | 10930409 | # | DNA | G:T, G:U | # | 10930409 | MED1 functions as a mismatch-specific DNA repair enzyme. MED1 lacks uracil glycosylase activity on single-strand DNA and abasic site lyase activity. The glycosylase activity of MED1 prefers substrates containing a G:T mismatch within methylated or unmethylated CpG sites; since G:T mismatches can originate via deamination of 5-methylcytosine to thymine, MED1 may act as a caretaker of genomic fidelity at CpG sites. | # |
MBD5
(details) |
20444 | methyl-CpG binding domain protein 5 | 55777 | Q9P267 | MBD5_HUMAN | Mbd5 | 2138934 | B1AYB6 | MBD5_MOUSE | # | # | Chromatin remodeling | # | 20700456 | # | chromatin | # | # | 20700456 | MBD5 and MBD6 may contribute to the unique epigenetic machinery of neurons or to the global reorganization of chromatin during spermatogenesis. | # | |
MBD6
(details) |
20445 | methyl-CpG binding domain protein 6 | 114785 | Q96DN6 | MBD6_HUMAN | Mbd6 | 106378 | Q3TY92 | MBD6_MOUSE | # | # | Chromatin remodeling | # | 20700456 | # | chromatin | # | # | 20700456 | MBD5 and MBD6 may contribute to the unique epigenetic machinery of neurons or to the global reorganization of chromatin during spermatogenesis. | # | |
MBIP
(details) |
20427 | MAP3K12 binding inhibitory protein 1 | 51562 | Q9NS73 | MBIP1_HUMAN | Mbip | 1918320 | Q99LQ1 | MBIP1_MOUSE | # | # | Histone modification write cofactor | Histone acetylation | 19103755 | ATAC | histone | # | # | 19103755 | Novel proteins identified as STAGA/ TFTC subunits, such as ATAC2, DR1, MBIP, WDR5, YEATS2, and ZZZ3/ATAC1. | # | |
MBNL1
(details) |
6923 | Muscleblind-like protein 1 (Triplet-expansion RNA-binding protein) | 4154 | Q9NR56 | MBNL1_HUMAN | zf-CCCH_2 PF14608 19-39, domain PF22628 48-86 216-253, zf-CCCH PF00642 183-205 | Mbnl1 | 1928482 | Q9JKP5 | MBNL1_MOUSE | ZC3H | Zinc fingers CCCH-type | RNA modification | Alternative splicing | 16946708, 19470458, 15257297 | # | RNA | mRNA | # | 16946708, 19470458, 15257297 | Regulates the TNNT2 exon 5 skipping through competition with U2AF2. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion but induces insulin receptor (IR) pre-mRNA exon inclusion but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle. Antagonistic regulator with CELF proteins. | New |
MBNL3
(details) |
20564 | Muscleblind-like protein 3 (Cys3His CCG1-required protein) (Muscleblind-like X-linked protein) (Protein HCHCR) | 55796 | Q9NUK0 | MBNL3_HUMAN | zf-CCCH_2 PF14608 20-40, domain PF22628 49-87 211-248, zf-CCCH_4 PF18044 179-200 | Mbnl3 | 2444912 | Q8R003 | MBNL3_MOUSE | ZC3H | Zinc fingers CCCH-type | RNA modification | Alternative splicing | 15257297 | # | RNA | mRNA | # | 15257297 | Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle. Antagonistic regulator with CELF proteins. | New |
MBTD1
(details) |
19866 | mbt domain containing 1 | 54799 | Q05BQ5 | MBTD1_HUMAN | zf-FCS_1 PF21319 52-82, MBT PF02820 189-248 289-352 388-459 496-560 | Mbtd1 | 2143977 | Q6P5G3 | MBTD1_MOUSE | # | # | Polycomb group (PcG) protein | # | 19841675 | # | histone | H4K20me1, H4K20me2 | # | 19841675 | MBTD1, Malignant Brain Tumor domain-containing protein 1, is a PcG protein. | # |
MCRS1
(details) |
6960 | microspherule protein 1 | 10445 | Q96EZ8 | MCRS1_HUMAN | MCRS_N PF13325 134-331, FHA PF00498 363-435 | Mcrs1 | 1858420 | Q99L90 | MCRS1_MOUSE | INO80 | INO80 complex subunits | Histone modification write | Histone acetylation | 20018852 | Ino80, NSL, CHD8, MLL2/3, MLL4/WBP7 | histone | H4K5, H4K8, H4K16 | H4K5ac, H4K8ac, H4K16ac | 20018852 | Human MOF (MYST1), a member of the MYST (Moz-Ybf2/Sas3-Sas2-Tip60) family of histone acetyltransferases (HATs), is the human ortholog of the Drosophila males absent on the first (MOF) protein. | # |
MDC1
(details) |
21163 | mediator of DNA-damage checkpoint 1 | 9656 | Q14676 | MDC1_HUMAN | FHA PF00498 54-122, RTT107_BRCT_5 PF16770 1888-1970, BRCT_2 PF16589 1994-2074 | Mdc1 | 3525201 | Q5PSV9 | MDC1_MOUSE | # | # | Histone modification read | # | 16377563 | # | histone | H2AX | # | 16377563 | Mammalian MDC1/NFBD1 directly binds to phospho-H2AX (gammaH2AX) by specifically interacting with the phosphoepitope at the gammaH2AX carboxyl terminus. | # |
MEAF6
(details) |
25674 | MYST/Esa1-associated factor 6 | 64769 | Q9HAF1 | EAF6_HUMAN | NuA4 PF09340 18-95 | Meaf6 | 1917338 | Q2VPQ9 | EAF6_MOUSE | # | # | Histone modification write cofactor | Histone acetylation | 18794358 | HBO1, NuA4, MOZ/MORF | histone | H2A, H3K14, H4K5, H4K8, H4K12 | H2Aac, H3K14ac, H4K5ac, H4K8ac, H4K12ac | 18794358 | BRPF proteins bridge the association of MOZ and MORF with ING5 and EAF6=MEAF6. An N-terminal region of BRPF1 interacts with the acetyltransferases; the enhancer of polycomb (EPc) homology domain in the middle part binds to ING5 and EAF6. The association of BRPF1 with EAF6 is weak, but ING5 increases the affinity. These three proteins form a trimeric core that is conserved from Drosophila melanogaster to humans, although authentic orthologs of MOZ and MORF are absent in invertebrates. Deletion mapping studies revealed that the acetyltransferase domain of MOZ/MORF is sufficient for BRPF1 interaction. At the functional level, complex formation with BRPF1 and ING5 drastically stimulates the activity of the acetyltransferase domain in acetylation of nucleosomal histone H3 and free histones H3 and H4. | # |
MECP2
(details) |
6990 | methyl CpG binding protein 2 | 4204 | P51608 | MECP2_HUMAN | MBD PF01429 97-159 | Mecp2 | 99918 | Q9Z2D6 | MECP2_MOUSE | # | # | Histone modification write cofactor, Histone modification write cofactor, TF | Histone methylation, Histone acetylation, TF repressor | 10773092 | # | DNA | mCG, DNA motif | # | 10773092 | Methyl-CpG-binding protein 2 (MeCP2) contains a transcriptional repression domain (TRD), which can act by recruitment of a large transcriptional co-repressor complex containing histone deacetylases HDAC1 and 2. | # |
MEN1
(details) |
7010 | multiple endocrine neoplasia I | # | O00255 | MEN1_HUMAN | Menin PF05053 4-499 550-610 | Men1 | 1316736 | O88559 | MEN1_MOUSE | # | # | Histone modification write cofactor | Histone methylation | 14992727 | Menin-associated_HMT, MLL-HCF, CHD8, MLL2/3, COMPASS-like MLL1,2, MLL4/WBP7 | histone | H3K4 | H3K4me | 14992727, 15199122 | Essential component of a MLL/SET1 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3 (H3K4) (UniProt). | # |
METTL11B
(details) |
31932 | methyltransferase like 11B | 149281 | Q5VVY1 | NTM1B_HUMAN | Methyltransf_PK PF05891 65-278 | Mettl11b | 2685053 | B2RXM4 | NTM1B_MOUSE | METTL | Methyltransferase like | Histone modification writer | Histone methylation | 26543159 | # | protein | CENP-A | K55m | 26543159 | Regulates centromere function and mitosis | New |
METTL14
(details) |
29330 | methyltransferase like 14 | 57721 | Q9HCE5 | MET14_HUMAN | MT-A70 PF05063 186-363 | Mettl14 | 2442926 | Q3UIK4 | MET14_MOUSE | METTL | Methyltransferase like | RNA modification | RNA methylation | 24316715 | WMM | RNA | A of mRNA | m(6)A | 24316715 | Regulates mRNA stability, processing miRNA, DNA-reparation | New |
METTL16
(details) |
28484 | methyltransferase like 16 | 79066 | Q86W50 | MET16_HUMAN | Methyltransf_10 PF05971 1-291 | Mettl16 | 1914743 | Q9CQG2 | MET16_MOUSE | METTL | Methyltransferase like | RNA modification | RNA methylation | 29051200 | # | RNA | U6 snRNA (A43) | m6A43 | 32266935 | Tunes snRNA–pre‐mRNA interactions, controls alternative splicing | New |
METTL21A
(details) |
30476 | methyltransferase like 21A | 151194 | Q8WXB1 | MT21A_HUMAN | Methyltransf_16 PF10294 26-189 | Mettl21a | 1914349 | Q9CQL0 | MT21A_MOUSE | METTL | Methyltransferase like | Protein modification | Protein methylation | # | # | protein | Hsp70 | Km3 | 23921388 | Modulates the affinity of Hsp70 for targets | New |
METTL3
(details) |
17563 | methyltransferase like 3 | 56339 | Q86U44 | MTA70_HUMAN | MT-A70 PF05063 389-550 | Mettl3 | 1927165 | Q8C3P7 | MTA70_MOUSE | METTL | Methyltransferase like | RNA modification | RNA methylation | 24316715 | WMM | RNA | A of mRNA | m(6)A | 24316715 | Regulates mRNA stability, processing miRNA, DNA-reparation | New |
METTL4
(details) |
24726 | methyltransferase like 4 | 64863 | Q8N3J2 | METL4_HUMAN | MT-A70 PF05063 281-454 | Mettl4 | 1924031 | Q3U034 | METL4_MOUSE | METTL | Methyltransferase like | RNA modification, DNA modification | RNA methylation, DNA methylation | 30982744 | # | DNA, RNA | A of DNA, U2 snRNA | m(6)A | 31913360 | Regulates transcriptional silencing, Polycomb silencing, splicing regulation | New |
MGA
(details) |
14010 | MGA, MAX dimerization protein | 23269 | Q8IWI9 | MGAP_HUMAN | T-box PF00907 77-259, MGA_dom PF16059 1043-1085, HLH PF00010 2425-2474 | Mga | 1352483 | A2AWL7 | MGAP_MOUSE | # | # | Histone modification write cofactor, TF | Histone methylation, Histone acetylation, TF activator, TF repressor | # | RING2-L3MBTL2, CHD8, MLL2/3, MLL4/WBP7 | DNA | DNA motif | # | # | Added because it is a complex partner | # |
MGEA5
(details) |
7056 | meningioma expressed antigen 5 (hyaluronidase) | 10724 | O60502 | NCOAT_HUMAN | NAGidase PF07555 61-341 | Mgea5 | 1932139 | Q9EQQ9 | NCOAT_MOUSE | # | # | Histone modification write | Histone acetylation | 15485860 | # | histone | H3K14, H4K8 | H3K14ac, H4K8ac | 15485860 | The HAT domain of NCOAT=MGEA5 has the ability to acetylate all four core histones when either free or bound by DNA in the context of oligonucleosome arrays. | # |
MINA
(details) |
19441 | MYC induced nuclear antigen | 84864 | Q8IUF8 | MINA_HUMAN | JmjC_2 PF08007 137-261, ROXA-like_wH PF20514 331-431 | Mina | 1914264 | Q8CD15 | MINA_MOUSE | # | # | Histone modification erase | Histone methylation | 19502796 | # | histone | H3K9me3 | H3K9 | 19502796 | mdig=MINA is involved in demethylation of tri-methyl lysine 9 on histone H3. | # |
MIS18A
(details) |
1286 | MIS18 kinetochore protein A | 54069 | Q9NYP9 | MS18A_HUMAN | Yippee-Mis18 PF03226 81-186 | Mis18a | 1913828 | Q9CZJ6 | MIS18A_MOUSE | # | # | Chromatin remodeling | # | 17199038 | Mis18 | histone | CENPA | # | 17199038 | Recruits CENPA to centromeres. Regulates normal chromosome segregation during mitosis. | New |
MIS18BP1
(details) |
20190 | MIS18 binding protein 1 | 55320 | Q6P0N0 | M18BP_HUMAN | SANTA PF09133 376-470 | Mis18bp1 | 2145099 | Q80WQ8 | M18BP_MOUSE | Myb/SANT domain containing | Myb/SANT domain containing | Chromatin remodeling | # | 17199038 | Mis18 | histone | CENPA | # | 17199038 | Recruits CENPA to centromeres. Regulates normal chromosome segregation during mitosis. | New |
MLLT1
(details) |
7134 | myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 1 | 4298 | Q03111 | ENL_HUMAN | YEATS PF03366 27-107, AHD PF17793 496-555 | Mllt1 | 1927238 | # | # | # | # | Chromatin remodeling cofactor | # | 23623499 | SWI/SNF-like_EPAFa, SWI/SNF-like EPAFB | chromatin | # | # | 23623499 | MLL-ENL (=MLLT1) inhibits polycomb repressive complex 1. | # |
MLLT10
(details) |
16063 | myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 10 | 8028 | P55197 | AF10_HUMAN | PHD_2 PF13831 37-72, zf-HC5HC2H_2 PF13832 80-197 | Mllt10 | 1329038 | O54826 | AF10_MOUSE | PHF | Zinc fingers, PHD-type | Histone modification write cofactor | Histone methylation | 20203130 | # | histone | H3K79 | H3K79me3 | 20203130 | MLLT10 =AF10 plays an important role in Dot1’s HMTase activity through either DotCom stability, catalytic activity, or the recruitment of the complex to chromatin. | # |
MLLT6
(details) |
7138 | myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 6 | 4302 | P55198 | AF17_HUMAN | PHD_2 PF13831 20-55, zf-HC5HC2H_2 PF13832 63-180 | Mllt6 | 1935145 | # | # | PHF | Zinc fingers, PHD-type | Histone modification write cofactor | Histone methylation | 20203130 | # | histone | H3K79 | H3K79me3 | 20203130 | MLLT6 =AF17, nucleosomes containing monoubiquitinated H2B are a better substrate for DotCom in the generation of trimethylated H3K79. DotCom requires monoubiquitination of H2B for H3K79 trimethylation. | # |
MORF4L1
(details) |
16989 | mortality factor 4 like 1 | 10933 | Q9UBU8 | MO4L1_HUMAN | Tudor-knot PF11717 11-52, MRG PF05712 175-351 | Morf4l1 | 1096551 | P60762 | MO4L1_MOUSE | # | # | Histone modification read | # | 21423274 | NuA4 | histone | H4 | # | 21423274 | Table 1 in reference (MRG15 =MORF4L1). | # |
MORF4L2
(details) |
16849 | mortality factor 4 like 2 | 9643 | Q15014 | MO4L2_HUMAN | MRG PF05712 101-280 | Morf4l2 | 1927167 | Q9R0Q4 | MO4L2_MOUSE | # | # | Histone modification erase cofactor | Histone acetylation | 12963728 | NuA4 | histone | # | # | 12963728 | The FLJ10914 protein is associated with components of the TRRAP/TIP60 histone acetyltransferase complex and binds directly to the MORF4-related MRG15 and MRGX proteins. | # |
MOV10
(details) |
7200 | Mov10 RISC complex RNA helicase | 4343 | Q9HCE1 | MOV10_HUMAN | MOV-10_N PF21632 15-85, MOV-10_Ig-like PF21633 119-240, Mov-10_helical PF21635 291-358, MOV-10_beta-barrel PF21634 358-448, AAA_11 PF13086 499-572 610-690, AAA_12 PF13087 699-921 | Mov10 | 97054 | P23249 | MOV10_MOUSE | # | # | # | # | 20543829 | # | histone | # | # | # | MOV10 may be directly involved in transcriptional silencing by PcG complexes. | # |
MPHOSPH8
(details) |
29810 | M-phase phosphoprotein 8 | 54737 | Q99549 | MPP8_HUMAN | Chromo PF00385 59-108, Ank_2 PF12796 571-665, Ank PF00023 666-695 | Mphosph8 | 1922589 | Q3TYA6 | MPP8_MOUSE | ANKRD | Ankyrin repeat domain containing | Histone modification read | # | 21419134 | # | histone | H3K9me3, H3K9me2 | # | 21419134 | M-phase phosphoprotein 8 (MPP8=MPHOSPH8) harbors an N-terminal chromodomain and a C-terminal ankyrin repeat domain. MPP8, via its chromodomain, binds histone H3 peptide tri- or di-methylated at lysine 9 (H3K9me3/H3K9me2) in submicromolar affinity. | # |
MPND
(details) |
25934 | MPN domain-containing | 84954 | Q8N594 | MPND_HUMAN | RAMA PF18755 66-169, JAB PF01398 271-369 | Mpnd | 1915297 | Q3TV65 | MPND_MOUSE | # | # | Histone modification erase | Histone ubiquitination | 30982744 | # | histone | H2A-Ub (K119) | H2A | 30982744 | Polycomb repressing deubiquitinase | New |
MRGBP
(details) |
15866 | MRG/MORF4L binding protein | 55257 | Q9NV56 | MRGBP_HUMAN | Eaf7 PF07904 36-96 | Mrgbp | 1920497 | Q9DAT2 | MRGBP_MOUSE | # | # | Histone modification write cofactor | Histone acetylation | 12963728 | NuA4 | histone | # | # | 12963728 | TRCp120, DMAP1, and MRGBP are components of the mammalian TRRAP/TIP60 histone acetyltransferase complex. | # |
MSH6
(details) |
7329 | mutS homolog 6 | 2956 | P52701 | MSH6_HUMAN | PWWP PF00855 92-182, MutS_I PF01624 408-524, MutS_II PF05188 538-693, MutS_III PF05192 738-1064, MutS_IV PF05190 932-1024, MutS_V PF00488 1130-1324 | Msh6 | 1343961 | P54276 | MSH6_MOUSE | # | # | Histone modification read | # | 21423274 | # | histone | H3K36me3 | # | 21423274, 23622243 | Table 1 in the reference. Via its PWWP domain it specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair reaction. | # |
MSL1
(details) |
27905 | male-specific lethal 1 homolog (Drosophila) | 339287 | Q68DK7 | MSL1_HUMAN | MSL1_dimer PF16801 216-250, PEHE PF15275 478-591 | Msl1 | 1921276 | Q6PDM1 | MSL1_MOUSE | # | # | Histone modification write | Histone ubiquitination | 21726816 | # | histone | H2BK34 | H2BK34ub | 21726816 | MSL1/2 ubiquitylates nucleosomal H2B on K34 in vitro. | # |
MSL2
(details) |
25544 | male-specific lethal 2 homolog (Drosophila) | 55167 | Q9HCI7 | MSL2_HUMAN | zf-RING_10 PF16685 39-110, MSL2-CXC PF16682 455-506 | Msl2 | 1925103 | Q69ZF8 | MSL2_MOUSE | RNF | RING-type (C3HC4) zinc fingers | Histone modification write | Histone ubiquitination | 21726816 | # | histone | H2BK34 | H2BK34ub | 21726816 | RING finger protein MSL2 in the MOF-MSL complex is a histone ubiquitin E3 ligase. MSL2, together with MSL1, has robust histone ubiquitylation activity that mainly targets nucleosomal H2B on lysine 34 (H2B K34ub), a site within a conserved basic patch on H2B tail. | # |
MSL3
(details) |
7370 | male-specific lethal 3 homolog (Drosophila) | 10943 | Q8N5Y2 | MS3L1_HUMAN | domain PF22732 11-87, MRG PF05712 161-505 | Msl3 | 1341851 | Q9WVG9 | MS3L1_MOUSE | # | # | Histone modification read | # | 20943666 | # | histone | H4K20me1 | # | 20943666 | MSL3 plays an important role in targeting the male specific lethal complex to chromatin in both humans and flies by binding to H4K20Me. | # |
MST1
(details) |
7380 | macrophage stimulating 1 (hepatocyte growth factor-like) | 4485 | P26927 | HGFL_HUMAN | PAN_1 PF00024 26-104, Kringle PF00051 109-186 190-268 283-361 370-448, Trypsin PF00089 485-704 | Mst1 | 96080 | P26928 | HGFL_MOUSE | # | # | Histone modification | # | 17320507 | # | histone | # | # | # | Classified as histone-modifying enzymes in paper. | # |
MTA1
(details) |
7410 | metastasis associated 1 | 9112 | Q13330 | MTA1_HUMAN | BAH PF01426 5-162, ELM2 PF01448 167-219, Myb_DNA-binding PF00249 287-331, GATA PF00320 393-429, MTA_R1 PF17226 464-543 | Mta1 | 2150037 | Q8K4B0 | MTA1_MOUSE | GATAD | GATA zinc finger domain containing | Chromatin remodeling cofactor | # | 9885572 | NuRD | chromatin | # | # | 9885572 | One subunit of NURD was identified as MTA1, a metastasis-associated protein with a region similar to the nuclear receptor corepressor, N-CoR; and antibodies against NURD partially relieve transcriptional repression by thyroid hormone receptor. These results suggest that ATP-dependent chromatin remodeling can participate in transcriptional repression by assisting repressors in gaining access to chromatin. | # |
MTA2
(details) |
7411 | metastasis associated 1 family, member 2 | 9219 | O94776 | MTA2_HUMAN | BAH PF01426 4-142, ELM2 PF01448 147-199, Myb_DNA-binding PF00249 266-311, GATA PF00320 367-403, MTA_R1 PF17226 450-525 | Mta2 | 1346340 | Q9R190 | MTA2_MOUSE | GATAD | GATA zinc finger domain containing | Histone modification erase cofactor | Histone acetylation | 10444591 | NuRD | histone | # | # | 10444591 | MTA2 directs the assembly of an active histone deacetylase complex, and the association of MTA2 with the core HDAC/RbAp complex requires MBD3. | # |
MTA3
(details) |
23784 | metastasis associated 1 family, member 3 | 57504 | Q9BTC8 | MTA3_HUMAN | BAH PF01426 4-145, ELM2 PF01448 150-202, Myb_DNA-binding PF00249 269-314, GATA PF00320 379-415, MTA_R1 PF17226 462-537 | Mta3 | 2151172 | Q924K8 | MTA3_MOUSE | GATAD | GATA zinc finger domain containing | Chromatin remodeling cofactor | # | 12705869 | NuRD | chromatin | # | # | 12705869 | The product of human MTA3 is an estrogen-dependent component of the Mi-2/NuRD transcriptional corepressor in breast epithelial cells. MTA3 constitutes a key component of an estrogen-dependent pathway regulating growth and differentiation. | # |
MTF2
(details) |
29535 | metal response element binding transcription factor 2 | 22823 | Q9Y483 | MTF2_HUMAN | Tudor_2 PF18104 49-84, PHD PF00628 105-154, Mtf2_C PF14061 544-590 | Mtf2 | 105050 | Q02395 | MTF2_MOUSE | TDRD, PHF | Tudor domain containing, "Zinc fingers, PHD-type" | Polycomb group (PcG) protein | # | 21881606 | PRC2 | histone | H3K36me3 | # | 21881606 | Polycomb group (PcG) that binds histone H3 trimethylated at Lys-36. | # |
MUM1
(details) |
29641 | melanoma associated antigen (mutated) 1 | 84939 | Q2TAK8 | MUM1_HUMAN | PWP3A-B_N PF20887 1-105, MUM1-like_PWWP PF20884 411-484, PWP3A-B_C PF20886 561-707 | Mum1 | 1915364 | Q6DID5 | MUM1_MOUSE | # | # | Histone modification read | # | 217205545 | # | histone | H3K36me, K3K79me, H4K20me | # | 217205545 | The PWWP domains in BRPF1, BRPF2, HDGF2, MUM1 and the N-terminal PWWP domains of WHSC1 and WHSC1L1 show weak binding affinity to histones with H3K36, K3K79 or H4K20 | # |
MYBBP1A
(details) |
7546 | MYB binding protein (P160) 1a | 10514 | Q9BQG0 | MBB1A_HUMAN | DNA_pol_phi PF04931 38-834 | Mybbp1a | 106181 | Q7TPV4 | MBB1A_MOUSE | # | # | Chromatin remodeling cofactor | # | 16603771 | B-WICH | chromatin | # | # | 16603771 | The WSTF (Williams syndrome transcription factor) protein is involved in vitamin D-mediated transcription and replication as a component of two distinct ATP-dependent chromatin remodeling complexes, WINAC and WICH, respectively. The WICH complex (WSTF-SNF2h) interacts with several nuclear proteins as follows: Sf3b155/SAP155, RNA helicase II/Guα, Myb-binding protein 1a, CSB. | # |
MYO1C
(details) |
7597 | myosin IC | 4641 | O00159 | MYO1C_HUMAN | Myosin_head PF00063 49-718, IQ PF00612 737-755 758-778, Myosin_TH1 PF06017 887-1058 | Myo1c | 106612 | Q9WTI7 | MYO1C_MOUSE | MYOI | Myosins / Myosin superfamily : Class I | Chromatin remodeling cofactor | # | 16603771 | B-WICH | chromatin | # | # | 16603771 | The WSTF (Williams syndrome transcription factor) protein is involved in vitamin D-mediated transcription and replication as a component of two distinct ATP-dependent chromatin remodeling complexes, WINAC and WICH, respectively. The WICH complex (WSTF-SNF2h) interacts with several nuclear proteins as follows: Sf3b155/SAP155, RNA helicase II/Gualpha, Myb-binding protein 1a, CSB, the proto-oncogene Dek, and nuclear myosin 1 in a large 3-MDa assembly, B-WICH, during active transcription. | # |
MYSM1
(details) |
29401 | Myb-like, SWIRM and MPN domains 1 | 114803 | Q5VVJ2 | MYSM1_HUMAN | Myb_DNA-binding PF00249 120-163, SWIRM PF04433 382-461, JAB PF01398 576-679 | Mysm1 | 2444584 | Q69Z66 | MYSM1_MOUSE | # | # | Histone modification erase | Histone ubiquitination | 17707232 | # | histone | H2Aub | H2A | 17707232 | JAMM/MPN(+) domain-containing histone H2A deubiquitinase (2A-DUB, or KIAA1915/MYSM1) is specific for monoubiquitinated H2A (uH2A) that has permitted delineation of a strategy for specific regulatory pathways of gene activation. | # |
NAA60
(details) |
25875 | N(alpha)-acetyltransferase 60, NatF catalytic subunit | 79903 | Q9H7X0 | NAA60_HUMAN | Acetyltransf_1 PF00583 27-155 | Naa60 | 1922013 | Q9DBU2 | NAA60_MOUSE | NAA | N(alpha)-acetyltransferase subunits | Histone modification write | Histone acetylation | 21981917 | # | histone | H4K20, H4K79, H4K91 | H4K20ac, H4K79ac, H4K91ac | 21981917 | HAT4 =NAA60 is localized in the Golgi apparatus and displays a substrate preference for lysine residues of free histone H4, including H4K79 and H4K91, that reside in the globular domain of H4. | # |
NAP1L1
(details) |
7637 | nucleosome assembly protein 1-like 1 | 4673 | P55209 | NP1L1_HUMAN | NAP PF00956 77-344 | Nap1l1 | 1855693 | P28656 | NP1L1_MOUSE | # | # | Histone chaperone | # | 18226242 | # | histone | # | # | 18226242 | Human Nucleosome Assembly Protein-1 (hNAP-1) =NAP1L1 is known to act as a histone chaperone that shuttles histones H2A/H2B into the nucleus, assembles nucleosomes and promotes chromatin fluidity, thereby affecting transcription of several cellular genes. | # |
NAP1L2
(details) |
7638 | nucleosome assembly protein 1-like 2 | 4674 | Q9ULW6 | NP1L2_HUMAN | NAP PF00956 111-408 | Nap1l2 | 106654 | P51860 | NP1L2_MOUSE | # | # | Histone modification cofactor | # | 21333655, 17591696 | # | histone | H3, H4 | # | # | Interacts with H3 and H4 and may be involved in regulation of acetylation. | # |
NAP1L4
(details) |
7640 | nucleosome assembly protein 1-like 4 | 4676 | Q99733 | NP1L4_HUMAN | NAP PF00956 65-338 | Nap1l4 | 1316687 | Q78ZA7 | NP1L4_MOUSE | # | # | Histone modification cofactor | # | 21333655 | # | histone | H3, H4 | # | # | Interacts with H3 and H4 and may be involved in regulation of acetylation. | # |
NASP
(details) |
7644 | nuclear autoantigenic sperm protein (histone-binding) | 4678 | P49321 | NASP_HUMAN | SHNi-TPR PF10516 542-575, TPR_8 PF13181 584-615 | Nasp | 1355328 | Q99MD9 | NASP_MOUSE | TTC | Tetratricopeptide (TTC) repeat domain containing | Chromatin remodeling | # | 8724350 | # | histone | H1 | # | 8724350 | Binds to linker H1 histones, but not to core histones. | # |
NAT10
(details) |
29830 | N-acetyltransferase 10 (GCN5-related) | 55226 | Q9H0A0 | NAT10_HUMAN | TmcA_N PF08351 9-201, Helicase_RecD PF05127 282-486, GNAT_acetyltr_2 PF13718 529-753, tRNA_bind_2 PF13725 763-974 | Nat10 | 2138939 | Q8K224 | NAT10_MOUSE | # | # | Histone modification write | Histone acetylation | 14592445 | # | histone | # | # | 14592445 | hALP =NAT10 can specifically acetylate free histones in vitro. hALP may influence the activity of histone acetylation and possibly up-regulate telomerase activity through transactivation of hTERT promoter. | # |
NAT10
(details) |
29830 | N-acetyltransferase 10 | 55226 | Q9H0A0 | NAT10_HUMAN | TmcA_N PF08351 9-201, Helicase_RecD PF05127 282-486, GNAT_acetyltr_2 PF13718 529-753, tRNA_bind_2 PF13725 763-974 | Nat10 | 2138939 | Q8K224 | NAT10_MOUSE | GNAT | GCN5 related N-acetyltransferase | RNA modification | RNA acetylation | 30449621 | # | RNA | C of mRNA | ac4C | 30449621 | Regulates mRNA stabiility and therefore translation efficiency | New |
NBN
(details) |
7652 | nibrin | 4683 | O60934 | NBN_HUMAN | FHA PF00498 24-100, BRCT PF00533 114-181, NIBRIN_BRCT_II PF16508 217-323, Nbs1_C PF08599 685-749 | Nbn | 1351625 | Q9R207 | NBN_MOUSE | # | # | Chromatin remodeling | # | 19338747 | # | histone | H2AX | # | # | Interacts with H2AX. UniProt: It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. | # |
NCL
(details) |
7667 | nucleolin | 4691 | P19338 | NUCL_HUMAN | RRM_1 PF00076 309-377 395-459 488-554 574-641 | Ncl | 97286 | P09405 | NUCL_MOUSE | RBM | RNA binding motif (RRM) containing | Histone chaperone | # | 16601700 | # | histone, DNA, RNA | DNA motif, RNA motif | # | 16601700, 15371412 | The nuclear protein nucleolin =NCL possesses a histone chaperone activity and this factor greatly enhances the activity of the chromatin remodeling machineries SWI/SNF and ACF. | # |
NCOA1
(details) |
7668 | nuclear receptor coactivator 1 | 8648 | Q15788 | NCOA1_HUMAN | PAS PF00989 116-176, PAS_11 PF14598 259-368, NCOA_u2 PF16665 437-682, SRC-1 PF08832 630-699, Nuc_rec_co-act PF08815 921-974, DUF1518 PF07469 1142-1189 1208-1268 | Ncoa1 | 1276523 | P70365 | NCOA1_MOUSE | KAT, bHLH | Chromatin-modifying enzymes / K-acetyltransferases, Basic helix-loop-helix proteins | Histone modification write | Histone acetylation | 9296499 | # | histone | H3, H4 | # | 9296499 | The HAT activity of SRC-1=NCOA1 maps to its carboxy-terminal region and is primarily specific for histones H3 and H4. Acetylation by SRC-1 and PCAF of histones bound at specific promoters may result from ligand binding to steroid receptors and could be a mechanism by which the activation functions of steroid receptors and associated coactivators enhance formation of a stable preinitiation complex, thereby increasing transcription of specific genes from transcriptionally repressed chromatin templates. | # |
NCOA2
(details) |
7669 | nuclear receptor coactivator 2 | 10499 | Q15596 | NCOA2_HUMAN | PAS PF00989 119-182, PAS_11 PF14598 268-375, NCOA_u2 PF16665 463-581, SRC-1 PF08832 635-709, DUF4927 PF16279 730-821, Nuc_rec_co-act PF08815 1072-1115, DUF1518 PF07469 1274-1340 | Ncoa2 | 1276533 | Q61026 | NCOA2_MOUSE | KAT, bHLH | Chromatin-modifying enzymes / K-acetyltransferases, Basic helix-loop-helix proteins | Chromatin remodeling cofactor | # | 9590696 | # | chromatin | # | # | 9590696 | GR, SRC-1/NcoA1 and GRIP-1/TIF-2/NcoA2 are known to bind to distinct regions. The chromatin remodeling complexes and coactivators may contribute to the transcriptional activation of organized chromatin templates. | # |
NCOA3
(details) |
7670 | nuclear receptor coactivator 3 | 8202 | Q9Y6Q9 | NCOA3_HUMAN | PAS PF00989 117-179, PAS_11 PF14598 265-372, NCOA_u2 PF16665 490-572, SRC-1 PF08832 588-707, DUF4927 PF16279 722-817, Nuc_rec_co-act PF08815 1045-1092, DUF1518 PF07469 1273-1348 | Ncoa3 | 1276535 | O09000 | NCOA3_MOUSE | KAT, bHLH | Chromatin-modifying enzymes / K-acetyltransferases, Basic helix-loop-helix proteins | Histone modification write | Histone acetylation | 9267036 | # | histone | # | # | 9267036 | ACTR =NCOA3 is a potent histone acetyltransferase and appears to define a distinct evolutionary branch. | # |
NCOA6
(details) |
15936 | nuclear receptor coactivator 6 | 23054 | Q14686 | NCOA6_HUMAN | NCOA6_TRADD-N PF13820 47-182 | Ncoa6 | 1929915 | Q9JL19 | NCOA6_MOUSE | # | # | Histone modification write cofactor | Histone methylation | 17500065 | CHD8, MLL2/3, COMPASS-like MLL3,4 | histone | # | # | 17500065 | Ectopically expressed PTIP is capable of interacting with DNA damage response proteins including 53BP1, while endogenous PTIP, and a novel protein PA1 are both components of a Set1-like histone methyltransferase (HMT) complex that also contains ASH2L, RBBP5, WDR5, hDPY-30, NCOA6, SET domain-containing HMTs MLL3 and MLL4, and substoichiometric amount of JmjC domain-containing putative histone demethylase UTX. | # |
NCOR1
(details) |
7672 | nuclear receptor corepressor 1 | 9611 | O75376 | NCOR1_HUMAN | GPS2_interact PF15784 151-235, Myb_DNA-binding PF00249 626-670 | Ncor1 | 1349717 | Q60974 | NCOR1_MOUSE | # | # | Histone modification erase cofactor | Histone acetylation | 14527417 | # | histone | # | # | # | UniProt: Part of a complex which promotes histone deacetylation and the formation of repressive chromatin structures which may impede the access of basal transcription factors. | # |
NCOR2
(details) |
7673 | nuclear receptor corepressor 2 | 9612 | Q9Y618 | NCOR2_HUMAN | GPS2_interact PF15784 150-228, Myb_DNA-binding PF00249 431-474 613-657 | Ncor2 | 1337080 | Q9WU42 | NCOR2_MOUSE | # | # | Histone modification erase cofactor | Histone acetylation | 14527417, 25006126 | # | # | # | # | # | Ncor2 knockdown upregulates fos transcription by modulating the acetylation level in the fos promoter region. | # |
NEK6
(details) |
7749 | NIMA-related kinase 6 | 10783 | Q9HC98 | NEK6_HUMAN | Pkinase PF00069 45-296 | Nek6 | 1891638 | Q9ES70 | NEK6_MOUSE | # | # | Histone modification write | Histone phosphorylation | 12054534 | # | histone | H1, H3 | H1ph, H3ph | 12054534 | Recombinant hNek6 protein produced in insect cells effectively phosphorylates histones H1 and H3, but not casein. Thus Nek6 is a mitotic histone kinase which regulates chromatin condensation in mammalian cells. | # |
NEK9
(details) |
18591 | NIMA-related kinase 9 | 91754 | Q8TD19 | NEK9_HUMAN | Pkinase PF00069 54-308, RCC1 PF00415 399-441 445-496 499-547, RCC1_2 PF13540 655-683 | Nek9 | 2387995 | Q8K1R7 | NEK9_MOUSE | # | # | Histone modification write | Histone phosphorylation | 14660563 | # | histone | H1 | H1ph | 14660563 | Endogenous, immunoprecipitated Nek9 kinase can become activated (i.e. phosphorylation on histone H1). | # |
NFRKB
(details) |
7802 | nuclear factor related to kappaB binding protein | 4798 | Q6P4R8 | NFRKB_HUMAN | NFRKB_winged PF14465 375-480 | Nfrkb | 2442410 | Q6PIJ4 | NFRKB_MOUSE | INO80 | INO80 complex subunits | Chromatin remodeling cofactor, TF | # | 16230350 | Ino80 | DNA | DNA motif | # | 16230350 | Five proteins appear to be unique to the human INO80 complex. NFRKB is a large (more than 1300 amino acids) protein. The C-terminal half of NFRKB contains low complexity, mucin-like repeats. | # |
NFYB
(details) |
7805 | nuclear transcription factor Y, beta | 4801 | P25208 | NFYB_HUMAN | CBFD_NFYB_HMF PF00808 58-122 | Nfyb | 97317 | P63139 | NFYB_MOUSE | # | # | Chromatin remodeling, TF | TF activator | 15243141, 23332751 | # | DNA | DNA motif | # | 23332751 | NF-Y is a sequence-specific transcription factor with nucleosome-like properties of nonspecific DNA binding and helps establish permissive chromatin modifications at CCAAT promoters. | # |
NFYC
(details) |
7806 | nuclear transcription factor Y, gamma | 4802 | Q13952 | NFYC_HUMAN | Histone PF00125 24-105 | Nfyc | 107901 | P70353 | NFYC_MOUSE | # | # | Histone modification | # | 21445285 | # | histone | # | # | # | NF-Y recruits Ash2L to impart H3K4 trimethylation on CCAAT promoters | # |
NIPBL
(details) |
28862 | Nipped-B homolog (Drosophila) | 25836 | Q6KC79 | NIPBL_HUMAN | Cohesin_HEAT PF12765 1794-1835, Nipped-B_C PF12830 2276-2449 | Nipbl | 1918425 | Q6KCD5 | NIPBL_MOUSE | # | # | Histone modification erase cofactor | Histone acetylation | 25255084, 18854353 | # | # | # | # | # | Probably involved in cohesin loading and promoter-enhancer interaction. Attracts histone deacetylases. | # |
NOC2L
(details) |
24517 | nucleolar complex associated 2 homolog (S. cerevisiae) | 26155 | Q9Y3T9 | NOC2L_HUMAN | Noc2 PF03715 331-624 | Noc2l | 1931051 | Q9WV70 | NOC2L_MOUSE | # | # | Chromatin remodeling, TF | TF repressor | 15100215 | # | histone | H3 | # | 15100215 | INHAT =NOC2L (inhibitor of acetyltransferases) is a specific histone H3 N-terminal tail-binding complex. | # |
NPAS2
(details) |
7895 | neuronal PAS domain protein 2 | 4862 | Q99743 | NPAS2_HUMAN | HLH PF00010 11-58, PAS PF00989 84-151, PAS_11 PF14598 250-353 | Npas2 | 109232 | P97460 | NPAS2_MOUSE | bHLH | Basic helix-loop-helix proteins | Chromatin remodeling, TF | TF activator | 14645221, 24196956 | # | DNA | DNA motif | # | 14645221 | There is a time-dependent recruitment of chromatin remodeling machinery by NPAS2 in vivo. | # |
NPM1
(details) |
7910 | nucleophosmin (nucleolar phosphoprotein B23, numatrin) | 4869 | P06748 | NPM_HUMAN | Nucleoplasmin PF03066 17-117, NPM1-C PF16276 244-293 | Npm1 | 106184 | Q61937 | NPM_MOUSE | # | # | Histone chaperone | # | 25349213 | # | histone | H3, H2B, H4 | # | # | Co-immunoprecipitation shows that NPM1 is associated with HP1γ, core and linker histones. Uniprot: Acts as a chaperonin for the core histones H3, H2B and H4. | # |
NPM2
(details) |
7930 | nucleophosmin/nucleoplasmin 2 | 10361 | Q86SE8 | NPM2_HUMAN | Nucleoplasmin PF03066 19-119 | Npm2 | 1890811 | Q80W85 | NPM2_MOUSE | # | # | Histone chaperone | # | 21863821 | # | histone | H2A, H2B | # | # | Core histone chaperon. In the absence of histone tetramers, these chaperones bind H2A-H2B dimers. | # |
NSD1
(details) |
14234 | nuclear receptor binding SET domain protein 1 | 64324 | Q96L73 | NSD1_HUMAN | PWWP PF00855 318-408 1756-1846, domain PF23011 1542-1587, domain PF22908 1591-1639, domain PF23004 1640-1692, PHD PF00628 1710-1748, AWS PF17907 1900-1940, SET PF00856 1953-2059, C5HCH PF17982 2162-2210 | Nsd1 | 1276545 | O88491 | NSD1_MOUSE | KMT, PHF | Chromatin-modifying enzymes / K-methyltransferases, Zinc fingers, PHD-type | Histone modification write | Histone methylation | 21196496 | # | histone | H3K36, H4K20 | H3K36me, H4K20me | 21196496 | NSD1 is a SET domain histone methyltransferase that primarily dimethylates nucleosomal histone H3 lysine 36 (H3K36). | # |
NSL1
(details) |
24548 | NSL1, MIS12 kinetochore complex component | 25936 | Q96IY1 | NSL1_HUMAN | Mis14 PF08641 80-190 | Nsl1 | 2685830 | Q8K305 | NSL1_MOUSE | # | # | Histone modification write cofactor | Histone acetylation | 20018852 | # | histone | H4K16 | H4K16ac | 20018852 | Binding of NSL1 to MOF enhances MOF acetylation of histone H4 on lysine 16 and of the DNA binding transcription factor p53. | # |
NSRP1
(details) |
25305 | Nuclear speckle splicing regulatory protein 1 (Coiled-coil domain-containing protein 55) (Nuclear speckle-related protein 70) (NSrp70) | 84081 | Q9H0G5 | NSRP1_HUMAN | NSRP1_N PF09745 59-174, NRP1_C PF20427 310-489 | Nsrp1 | 2144305 | Q5NCR9 | NSRP1_MOUSE | MicroRNA protein coding host genes | MicroRNA protein coding host genes | RNA modification | Alternative splicing | 21296756 | # | RNA | mRNA | # | 21296756 | Regultes alternative splicing site selection | New |
NSUN2
(details) |
25994 | NOP2/Sun RNA methyltransferase 2 | 54888 | Q08J23 | NSUN2_HUMAN | Methyltr_RsmB-F PF01189 170-341 | Nsun2 | 107252 | Q1HFZ0 | NSUN2_MOUSE | NSUN | NOP2/Sun RNA methyltransferase family | RNA modification | RNA methylation | 27444144 | # | RNA | C of mRNA | m5C | 33622495 | Regulates cell proliferation by methylation of 5`-UTR or 3`-UTR of CDK1 and p27 mRNA | New |
NSUN6
(details) |
23529 | NOP2/Sun RNA methyltransferase 6 | 221078 | Q8TEA1 | NSUN6_HUMAN | Methyltr_RsmB-F PF01189 229-399 | Nsun6 | 1921705 | Q7TS68 | NSUN6_MOUSE | NSUN | NOP2/Sun RNA methyltransferase family | RNA modification | RNA methylation | 33330931 | # | RNA | C of mRNA | m5C | 33330931 | Marks translation termination by methylation of cytosine within the CTCCA motif | New |
NTMT1
(details) |
23373 | N-terminal Xaa-Pro-Lys N-methyltransferase 1 | 28989 | Q9BV86 | NTM1A_HUMAN | Methyltransf_PK PF05891 8-222 | Ntmt1 | 1913867 | Q8R2U4 | NTM1A_MOUSE | METTL | Methyltransferase like | Histone modification writer | Histone methylation | 26543159 | # | protein | CENP-A, CENP-B, RCC1 | Km1/m2/m3, Rm, Pm | 26543159 | Regulates centromere function and mitosis | New |
NUP98
(details) |
8068 | Nuclear pore complex protein Nup98-Nup96 (EC 3.4.21.-) [Cleaved into: Nuclear pore complex protein Nup98 (98 kDa nucleoporin) (Nucleoporin Nup98) (Nup98); Nuclear pore complex protein Nup96 (96 kDa nucleoporin) (Nucleoporin Nup96) (Nup96)] | 4928 | P52948 | NUP98_HUMAN | Nup98_GLEBS PF21240 169-209, Nucleoporin2 PF04096 738-884, Nup96 PF12110 1331-1629 | Nup98 | 109404 | Q6PFD9 | NUP98_MOUSE | NUP | Nucleoporins | RNA modification | Alternative splicing | 28221134 | # | RNA | mRNA | # | 28221134 | Regulates alternative splicing of E1A | New |
OGT
(details) |
8127 | O-linked N-acetylglucosamine (GlcNAc) transferase | 8473 | O15294 | OGT1_HUMAN | TPR_11 PF13414 90-144 363-410 429-471, TPR_8 PF13181 157-190 225-258, TPR_1 PF00515 191-224 259-292, TPR_12 PF13424 293-360, Glyco_transf_41 PF13844 477-1016 | Ogt | 1339639 | Q8CGY8 | OGT1_MOUSE | TTC | Tetratricopeptide (TTC) repeat domain containing | Histone modification write | Histone GlcNAcylation | 22121020 | NSL | histone | H2BS112 | H2BS112GlcNa | 22121020 | Histone H2B is GlcNAcylated at residue S112 by OGT in vitro and in living cells. Histone GlcNAcylation fluctuated in response to extracellular glucose through the hexosamine biosynthesis pathway (HBP). | # |
OIP5
(details) |
20300 | Opa interacting protein 5 | 11339 | O43482 | MS18B_HUMAN | Yippee-Mis18 PF03226 76-182 | Oip5 | 1917895 | A2AQ14 | MS18B_MOUSE | # | # | Chromatin remodeling | # | 17199038 | Mis18 | histone | CENPA | # | 17199038 | Recruits CENPA to centromeres. Regulates normal chromosome segregation during mitosis. | New |
PADI1
(details) |
18367 | peptidyl arginine deiminase, type I | 29943 | Q9ULC6 | PADI1_HUMAN | PAD_N PF08526 2-114, PAD_M PF08527 115-277, PAD PF03068 285-662 | Padi1 | 1338893 | Q9Z185 | PADI1_MOUSE | PADI | Peptidyl arginine deiminases | Histone modification | Histone citrullination | 15087120 | # | histone | H2AR, H3R, H4R | H2ARci, H3Rci, H4Rci | 15087120 | Peptidylarginine deiminases (PADs) convert arginine residues in proteins into citrullines. They are suspected to be involved in multiple sclerosis and rheumatoid arthritis pathophysiology, and they play a role in epidermis homeostasis and possibly in regulation of gene expression through histone modification | # |
PADI2
(details) |
18341 | peptidyl arginine deiminase, type II | 11240 | Q9Y2J8 | PADI2_HUMAN | PAD_N PF08526 2-114, PAD_M PF08527 115-274, PAD PF03068 286-664 | Padi2 | 1338892 | Q08642 | PADI2_MOUSE | PADI | Peptidyl arginine deiminases | Histone modification | Histone citrullination | 15087120 | # | histone | H2AR, H3R, H4R | H2ARci, H3Rci, H4Rci | 15087120 | Peptidylarginine deiminases (PADs) convert arginine residues in proteins into citrullines. They are suspected to be involved in multiple sclerosis and rheumatoid arthritis pathophysiology, and they play a role in epidermis homeostasis and possibly in regulation of gene expression through histone modification | # |
PADI3
(details) |
18337 | peptidyl arginine deiminase, type III | 51702 | Q9ULW8 | PADI3_HUMAN | PAD_N PF08526 1-113, PAD_M PF08527 115-281, PAD PF03068 290-661 | Padi3 | 1338891 | Q9Z184 | PADI3_MOUSE | PADI | Peptidyl arginine deiminases | Histone modification | Histone citrullination | 15087120 | # | histone | H2AR, H3R, H4R | H2ARci, H3Rci, H4Rci | 15087120 | Peptidylarginine deiminases (PADs) convert arginine residues in proteins into citrullines. They are suspected to be involved in multiple sclerosis and rheumatoid arthritis pathophysiology, and they play a role in epidermis homeostasis and possibly in regulation of gene expression through histone modification | # |
PADI4
(details) |
18368 | peptidyl arginine deiminase, type IV | 23569 | Q9UM07 | PADI4_HUMAN | PAD_N PF08526 1-113, PAD_M PF08527 113-275, PAD PF03068 286-661 | Padi4 | 1338898 | Q9Z183 | PADI4_MOUSE | PADI | Peptidyl arginine deiminases | Histone modification | Histone citrullination | 15339660 | # | histone | H2AR, H3R2, H3R8, H3R17, H3R26, H4R | H2ARci, H3R2ci, H3R8ci, H3R17ci, H3R26ci, H4Rci | 15339660 | Deimination converts histone arginine to citrulline and antagonizes arginine methylation. Peptidyl arginine deiminase 4 (PADI4) specifically deiminates, arginine residues R2, R8, R17, and R26 in the H3 tail. Deimination by PADI4 prevents arginine methylation by CARM1. | # |
PAF1
(details) |
25459 | Paf1, RNA polymerase II associated factor, homolog (S. cerevisiae) | 54623 | Q8N7H5 | PAF1_HUMAN | Paf1 PF03985 31-420 | Paf1 | 1923988 | Q8K2T8 | PAF1_MOUSE | # | # | Histone modification write cofactor | Histone ubiquitination | 16307923 | # | histone | H2, H3 | # | # | Involved in H2 and H3 ubiquitination. Involved in H2 and H3 ubiquitination. UniProt: PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). | # |
PAGR1
(details) |
28707 | PAXIP1 associated glutamate-rich protein 1 | 79447 | Q9BTK6 | PAGR1_HUMAN | PAXIP1_C PF15364 88-226 | 2900092E17Rik | 1914528 | Q99L02 | PAGR1_MOUSE | # | # | Histone modification write cofactor, Histone modification write cofactor | Histone methylation, Histone acetylation | 17500065 | CHD8, MLL2/3, MLL4/WBP7, COMPASS-like MLL3,4 | histone | # | # | 17500065 | Component of the MLL2/MLL3 complex (UniProt). | # |
PAK2
(details) |
8591 | p21 protein (Cdc42/Rac)-activated kinase 2 | 5062 | Q13177 | PAK2_HUMAN | PBD PF00786 73-130, Pkinase PF00069 249-500 | Pak2 | 1339984 | Q8CIN4 | PAK2_MOUSE | # | # | Histone modification write | Histone phosphorylation | 21724829 | # | histone | H4S47 | H4S47ph | 21724829 | Phosphorylation of histone H4 Ser 47 (H4S47ph), catalyzed by the PAK2 kinase, promotes nucleosome assembly of H3.3-H4 and inhibits nucleosome assembly of H3.1-H4 by increasing the binding affinity of HIRA to H3.3-H4 and reducing association of CAF-1 with H3.1-H4. | # |
PARG
(details) |
8605 | poly (ADP-ribose) glycohydrolase | 8505 | Q86W56 | PARG_HUMAN | PARG_cat_N PF20811 582-699, PARG_cat_C PF05028 705-909 | Parg | 1347094 | O88622 | PARG_MOUSE | # | # | Chromatin remodeling | # | 23102699, 21398629 | # | histone | H3K9 | # | 23102699, 21398629 | Reverses PARP activity. Both PAR and PARP-1 have an influence on PARG recruitment. Also recruitment through a PBD-mediated interaction of PARG with PCNA. | # |
PARP1
(details) |
270 | poly (ADP-ribose) polymerase 1 | 142 | P09874 | PARP1_HUMAN | zf-PARP PF00645 11-88 115-198, PADR1_N PF21728 232-290, PADR1_Zn_ribbon PF08063 291-332, BRCT PF00533 387-463, WGR PF05406 554-632, PARP_reg PF02877 662-794, PARP PF00644 808-1007 | Parp1 | 1340806 | P11103 | PARP1_MOUSE | PARP | Poly (ADP-ribose) polymerases | Chromatin remodeling | # | 20926656, 17177976, 17396150 | # | histone | H1 | # | 20926656 | Histone H1 poly[ADP]-ribosylation = PARP1, and its loss at specific loci, may be an epigenetic mechanism involved in the reprogramming of neuronal gene expression required for memory consolidation. | # |
PARP2
(details) |
272 | poly (ADP-ribose) polymerase 2 | 10038 | Q9UGN5 | PARP2_HUMAN | WGR PF05406 116-194, PARP_reg PF02877 231-363, PARP PF00644 376-577 | Parp2 | 1341112 | O88554 | PARP2_MOUSE | PARP | Poly (ADP-ribose) polymerases | Chromatin remodeling cofactor | # | 20092359 | # | # | # | # | 20092359 | PARP activity is involved in processes such as chromatin remodeling. Component of a base excision repair (BER) complex, containing at least XRCC1, PARP1, POLB and LRIG3. Homo- and heterodimer with PARP1. | # |
PARP3
(details) |
273 | poly (ADP-ribose) polymerase family, member 3 | 10039 | Q9Y6F1 | PARP3_HUMAN | WGR PF05406 66-144, PARP_reg PF02877 181-320, PARP PF00644 334-532 | Parp3 | 1891258 | # | # | PARP | Poly (ADP-ribose) polymerases | Polycomb group (PcG) protein | # | 16924674 | # | # | # | # | 16924674 | PARP-3 is part of Polycomb group protein complexes. | # |
PAXIP1
(details) |
8624 | PAX interacting (with transcription-activation domain) protein 1 | 22976 | Q6ZW49 | PAXI1_HUMAN | PTCB-BRCT PF12738 102-165 710-771, BRCT PF00533 604-684, RTT107_BRCT_5 PF16770 860-947, BRCT_2 PF16589 973-1062 | Paxip1 | 1890430 | Q6NZQ4 | PAXI1_MOUSE | # | # | Histone modification write cofactor | Histone methylation | 17178841 | CHD8, MLL2/3, MLL4/WBP7, COMPASS-like MLL3,4 | histone | H3K4 | H3K4me3 | 17178841 | ALR (MLL2) is a member of the human MLL family, which belongs to a larger SET1 family of histone methyltransferases. ALR is present within a stable multiprotein complex containing a cohort of proteins shared with other SET1 family complexes and several unique components, such as PTIP and the jumonji family member UTX. | # |
PBK
(details) |
18282 | PDZ binding kinase | 55872 | Q96KB5 | TOPK_HUMAN | Pkinase PF00069 35-317 | Pbk | 1289156 | Q9JJ78 | TOPK_MOUSE | # | # | Histone modification write | Histone phosphorylation | 16982762 | # | histone | H3S10 | H3S10ph | # | PBK/TOPK can phosphorylate histone H3 at Ser10 in vitro and in vivo, and mediate its growth-promoting effect through histone H3 modification. Can phosphorylate histone H3 at Ser10 in vitro and in vivo. | # |
PBRM1
(details) |
30064 | polybromo 1 | 55193 | Q86U86 | PB1_HUMAN | Bromodomain PF00439 64-136 200-272 400-470 541-608 677-746 790-865, BAH PF01426 957-1074 1156-1272, HMG_box PF00505 1379-1441 | Pbrm1 | 1923998 | Q8BSQ9 | PB1_MOUSE | # | # | Histone modification read | # | 22464331 | PBAF, SWI/SNF BRM-BRG1 | histone | H3 | # | 22464331 | Fig. 5 in the reference (PBRM1 =PB1). | # |
PCGF1
(details) |
17615 | polycomb group ring finger 1 | 84759 | Q9BSM1 | PCGF1_HUMAN | zf-C3HC4_2 PF13923 47-85, RAWUL PF16207 190-253 | Pcgf1 | 1917087 | Q8R023 | PCGF1_MOUSE | RNF, PCGF | RING-type (C3HC4) zinc fingers, Polycomb group ring fingers | Polycomb group (PcG) protein | # | 15620699 | PRC1, BCOR | # | # | # | 15620699 | Nervous system polycomb 1 (NSPc1=PCGF1) shares high homology with vertebrate PcG proteins Mel-18 and Bmi-1. | # |
PCGF2
(details) |
12929 | polycomb group ring finger 2 | 7703 | P35227 | PCGF2_HUMAN | zf-C3HC4_2 PF13923 18-56, RAWUL PF16207 164-228 | Pcgf2 | 99161 | P23798 | PCGF2_MOUSE | RNF, PCGF | RING-type (C3HC4) zinc fingers, Polycomb group ring fingers | Polycomb group (PcG) protein | # | 21282530 | PRC1 | # | # | # | 21282530 | CBX7 and CBX8, two Polycomb (Pc) homologs that repress INK4a, both participate in PRC1-like complexes with at least two Posterior sex combs (Psc) proteins, MEL18 =PCGF2 and BMI1. | # |
PCGF3
(details) |
10066 | polycomb group ring finger 3 | 10336 | Q3KNV8 | PCGF3_HUMAN | zf-C3HC4_2 PF13923 17-55, RAWUL PF16207 172-236 | Pcgf3 | 1916837 | Q8BTQ0 | PCGF3_MOUSE | RNF, PCGF | RING-type (C3HC4) zinc fingers, Polycomb group ring fingers | Polycomb group (PcG) protein | # | 21282530 | PRC1, RING2-FBRS | # | # | # | 21282530 | There are multiple orthologs of the archetypal PRC1 proteins; five Pc proteins (CBX2, CBX4, CBX6, CBX7 and CBX8), six Psc proteins (BMI1, MEL18, MBLR, NSPC1, RNF159 and RNF3=PCGF3). | # |
PCGF5
(details) |
28264 | polycomb group ring finger 5 | 84333 | Q86SE9 | PCGF5_HUMAN | zf-C3HC4_2 PF13923 18-56, RAWUL PF16207 163-216 | Pcgf5 | 1923505 | Q3UK78 | PCGF5_MOUSE | RNF, PCGF | RING-type (C3HC4) zinc fingers, Polycomb group ring fingers | Polycomb group (PcG) protein | # | 21282530 | PRC1, RING2-FBRS | # | # | # | 21282530 | There are multiple orthologs of the archetypal PRC1 proteins; five Pc proteins (CBX2, CBX4, CBX6, CBX7 and CBX8), six Psc proteins (BMI1, MEL18, MBLR, NSPC1, RNF159==PCGF5 and RNF3). | # |
PCGF6
(details) |
21156 | polycomb group ring finger 6 | 84108 | Q9BYE7 | PCGF6_HUMAN | zf-C3HC4_2 PF13923 134-172, RAWUL PF16207 275-323 | Pcgf6 | 1918291 | Q99NA9 | PCGF6_MOUSE | RNF, PCGF | RING-type (C3HC4) zinc fingers, Polycomb group ring fingers | Polycomb group (PcG) protein | # | 21282530 | PRC1, RING2-L3MBTL2 | # | # | # | 21282530 | There are multiple orthologs of the archetypal PRC1 proteins; five Pc proteins (CBX2, CBX4, CBX6, CBX7 and CBX8), six Psc proteins (BMI1, MEL18, MBLR=PCGF6, NSPC1, RNF159 and RNF3). | # |
PCNA
(details) |
8729 | proliferating cell nuclear antigen | 5111 | P12004 | PCNA_HUMAN | PCNA_N PF00705 1-124, PCNA_C PF02747 127-254 | Pcna | 97503 | P17918 | PCNA_MOUSE | # | # | Chromatin remodeling | # | 12786946 | # | histone | H2A, H2B | # | 12786946 | PCNA forms a ternary complex with DNTTIP2 and core histone. | # |
PDP1
(details) |
9279 | pyruvate dehyrogenase phosphatase catalytic subunit 1 | 54704 | Q9P0J1 | PDP1_HUMAN | PP2C PF00481 202-439 | Pdp1 | 2685870 | Q3UV70 | PDP1_MOUSE | PPM | Serine/threonine phosphatases / Protein phosphatases, Mg2+/Mn2+ dependent | Histone modification read | # | 22150589 | # | histone, DNA | H4K20me3 | # | 22150589 | The PWWP domain of Pdp1 binds not only to H4K20me3 (trimethylated Lys(20) of histone H4), but also to dsDNA (double-stranded DNA) via an aromatic cage and a positively charged area respectively. Pdp1 is a PWWP (proline-tryptophan-tryptophan-proline) domain-containing protein, which associates with Set9 to regulate its chromatin localization and methyltransferase activity towards H4K20. | # |
PELP1
(details) |
30134 | proline, glutamate and leucine rich protein 1 | 27043 | Q8IZL8 | PELP1_HUMAN | RIX1 PF08167 75-231, PELP1_HEAT PF08166 425-473 558-635 | Pelp1 | 1922523 | Q9DBD5 | PELP1_MOUSE | # | # | Histone modification read, Histone modification write cofactor | Histone methylation, Histone acetylation | 15456770, 11481323 | CHD8, MLL2/3, MLL4/WBP7 | histone | H1, H3, H4 | # | 15456770, 15374949 | C-terminal glutamic acid-abundant region bound to the hypoacetylated histones H3 and H4 and prevents them from becoming substrates of histone acetyltransferase. Thus PELP1 promotes and maintains the hypoacetylated state of histones at the target genomic site, and ER binding reverses its role to hyperacetylate histones through an as yet unidentified mechanism. | # |
PHC1
(details) |
3182 | polyhomeotic homolog 1 (Drosophila) | 1911 | P78364 | PHC1_HUMAN | zf-FCS_1 PF21319 798-827, PHC2_SAM_assoc PF16616 829-936, SAM_1 PF00536 939-1002 | Phc1 | 103248 | Q64028 | PHC1_MOUSE | SAMD | Sterile alpha motif (SAM) domain containing | Polycomb group (PcG) protein | # | 16024804 | PRC1 | # | # | # | 16024804 | Phc1 plays a pivotal role in mediating the PcG-dependent bridging of distant chromatin templates. | # |
PHC2
(details) |
3183 | polyhomeotic homolog 2 (Drosophila) | 1912 | Q8IXK0 | PHC2_HUMAN | zf-FCS_1 PF21319 640-669, PHC2_SAM_assoc PF16616 670-789, SAM_1 PF00536 791-856 | Phc2 | 1860454 | Q9QWH1 | PHC2_MOUSE | SAMD | Sterile alpha motif (SAM) domain containing | Polycomb group (PcG) protein | # | 16024804 | PRC1 | # | # | # | 16024804 | Phc2 is involved in the anterior-posterior (A-P) specification of the vertebral column through the regulation of Hox gene expression, as well as other PcG proteins. | # |
PHC3
(details) |
15682 | polyhomeotic homolog 3 (Drosophila) | 80012 | Q8NDX5 | PHC3_HUMAN | zf-FCS_1 PF21319 783-812, SAM_1 PF00536 919-981 | Phc3 | 2181434 | Q8CHP6 | PHC3_MOUSE | SAMD | Sterile alpha motif (SAM) domain containing | Polycomb group (PcG) protein | # | 16024804 | PRC1 | # | # | # | 16024804 | All known components of the PRC1 protein complex are found stably associated with CBX proteins. In particular, all the human Psc orthologs (BMI1, PCGF1, PCGF2, PCGF3, PCGF5, and PCGF6), the Ph orthologs (PHC1, PHC2, and PHC3). | # |
PHF1
(details) |
8919 | PHD finger protein 1 | 5252 | O43189 | PHF1_HUMAN | Tudor_2 PF18104 34-69, PHD PF00628 90-139, Mtf2_C PF14061 534-564 | Phf1 | 98647 | Q9Z1B8 | PHF1_MOUSE | TDRD, PHF | Tudor domain containing, Zinc fingers, PHD-type | Polycomb group (PcG) protein | # | 18086877 | PRC2 | # | # | # | 18086877 | The EED-EZH2 complex, containing the core subunits EZH2, EED, SUZ12, and RbAp48, functions as a histone H3K27-specific methyltransferase. The related EED-EZH2 protein complex is distinguished from the previous complex by the presence of another PcG protein, hPHF1. | # |
PHF10
(details) |
18250 | PHD finger protein 10 | 55274 | Q8WUB8 | PHF10_HUMAN | PHD PF00628 380-433 436-478 | Phf10 | 1919307 | Q9D8M7 | PHF10_MOUSE | PHF | Zinc fingers, PHD-type | Chromatin remodeling | # | 20068294 | npBAF, SWI/SNF BRM-BRG1 | chromatin | # | # | 20068294 | PHF10 belongs to a family of plant homeodomain (PHD) containing proteins which play a role in transcription regulation via chromatin remodeling. | # |
PHF12
(details) |
20816 | PHD finger protein 12 | 57649 | Q96QT6 | PHF12_HUMAN | PHD PF00628 59-102 273-318, PHF12_MRG_bd PF16737 201-236 | Phf12 | 1924057 | Q5SPL2 | PHF12_MOUSE | PHF | Zinc fingers, PHD-type | Histone modification erase cofactor | Histone acetylation | 11390640 | # | histone | # | # | 11390640 | Pf1 =PHF12 is a novel PHD zinc finger protein that links the TLE corepressor to the mSin3A-histone deacetylase complex. | # |
PHF13
(details) |
22983 | PHD finger protein 13 | 148479 | Q86YI8 | PHF13_HUMAN | PHD_5 PF20826 226-279 | Phf13 | 2446217 | Q8K2W6 | PHF13_MOUSE | PHF | Zinc fingers, PHD-type | Histone modification read | # | 19638409 | # | histone | H3K4me3 | # | 19638409 | Interacts with histone H3 that is trimethylated at 'Lys-4' (H3K4me3). | # |
PHF14
(details) |
22203 | PHD finger protein 14 | 9678 | O94880 | PHF14_HUMAN | PHD_2 PF13831 334-359, zf-HC5HC2H_2 PF13832 384-498, PHD PF00628 728-776 871-918 | Phf14 | 1923539 | Q9D4H9 | PHF14_MOUSE | PHF | Zinc fingers, PHD-type | Histone modification read | # | 23688586 | # | histone | H2A, H2B, H3 | H2Aac, H2Bac, H3ac | 23688586 | PHF14α is bound to histones. Histone H3, H2A, and H2B can be co-immunoprecipitated with GFP-PHF14α, but not with GFP alone, from total cell lysate. Histones H3, H2A, and H2B can be pulled down together with non-tagged exogenous PHF14α using an anti-PHF14 antibody. | # |
PHF19
(details) |
24566 | PHD finger protein 19 | 26147 | Q5T6S3 | PHF19_HUMAN | Tudor_2 PF18104 43-78, PHD PF00628 99-148, Mtf2_C PF14061 531-578 | Phf19 | 1921266 | Q9CXG9 | PHF19_MOUSE | TDRD, PHF | Tudor domain containing, Zinc fingers, PHD-type | Chromatin remodeling, Histone modification write cofactor | Histone acetylation | 15563832 | PRC2 | histone | # | # | 15563832 | Based on motifs identified within the hPCL3 =PHF19 open reading frames, hPCL3 proteins are likely to be nuclear proteins that regulate transcription and/or chromatin structure. | # |
PHF2
(details) |
8920 | PHD finger protein 2 | 5253 | O75151 | PHF2_HUMAN | PHD PF00628 8-53, JmjC PF02373 237-336, JHD PF17811 340-443 | Phf2 | 1338034 | Q9WTU0 | PHF2_MOUSE | KDM, PHF | Chromatin-modifying enzymes / K-demethylases, Zinc fingers, PHD-type | Histone modification erase | Histone methylation | 21532585 | # | histone | H3K9me2 | H3K9 | 21532585 | The protein kinase A (PKA)-dependent histone lysine demethylase complex, PHF2-ARID5B. PHF2, a jmjC demethylase, is enzymatically inactive by itself, but becomes an active H3K9Me2 demethylase through PKA-mediated phosphorylation. | # |
PHF20
(details) |
16098 | PHD finger protein 20 | 51230 | Q9BVI0 | PHF20_HUMAN | Tudor_3 PF18115 89-136, PHF20_AT-hook PF12618 147-282, PHD_5 PF20826 647-699 | Phf20 | 2444148 | Q8BLG0 | PHF20_MOUSE | TDRD, PHF | Tudor domain containing, Zinc fingers, PHD-type | Histone modification write | Histone acetylation | 22449972 | NSL, CHD8, MLL2/3, MLL4/WBP7 | histone | H4 | H4ac | 22449972 | The second Tudor domain of PHF20 displays preference for dimethylated histones substrates. | # |
PHF20L1
(details) |
24280 | PHD finger protein 20-like 1 | 51105 | A8MW92 | P20L1_HUMAN | Tudor_2 PF18104 90-124, PHD20L1_u1 PF16660 309-439, PHD_5 PF20826 675-729 | Phf20l1 | 2444412 | Q8CCJ9 | P20L1_MOUSE | TDRD, PHF | Tudor domain containing, Zinc fingers, PHD-type | Histone modification read | # | 21423274 | # | histone | H3K4me | # | 21423274 | Table 1 in the reference. Via its PWWP domain it specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair rea | # |
PHF21A
(details) |
24156 | PHD finger protein 21A | 51317 | Q96BD5 | PF21A_HUMAN | PHD PF00628 491-532 | Phf21a | 2384756 | Q6ZPK0 | PF21A_MOUSE | PHF | Zinc fingers, PHD-type | Histone modification erase cofactor | Histone methylation | 16140033 | BHC, LSD-CoREST | histone | # | # | 16140033 | LSD1 is a recently identified human lysine (K)-specific histone demethylase. LSD1 is associated with HDAC1/2; CoREST, a SANT domain-containing corepressor; and BHC80=PHF21A, a PHD domain-containing protein, among others. | # |
PHF8
(details) |
20672 | PHD finger protein 8 | 23133 | Q9UPP1 | PHF8_HUMAN | PHD PF00628 44-89, JmjC PF02373 270-370, JHD PF17811 374-481 | Phf8 | 2444341 | Q80TJ7 | PHF8_MOUSE | KDM, PHF | Chromatin-modifying enzymes / K-demethylases, Zinc fingers, PHD-type | Histone modification erase | Histone methylation | 21423274 | # | histone | H3K9me1, H3K9me2, H3K27me2, H4K20me1, H3K36me2, H3K36me3, H3K4me3 | H3K9, H3K27, H4K20, H3K36, H3K4 | 21423274 | Table 1 in the reference. Via its PWWP domain it specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair rea | # |
PHIP
(details) |
15673 | pleckstrin homology domain interacting protein | 55023 | Q8WWQ0 | PHIP_HUMAN | WD40 PF00400 179-211 214-252 259-298 357-393 456-495, Bromodomain PF00439 1166-1250 1327-1404 | Phip | 1932404 | Q8VDD9 | PHIP_MOUSE | WDR, DCAF | WD repeat domain containing, DDB1 and CUL4 associated factors | Histone modification read | # | 22464331 | # | histone | H3 | # | 22464331 | Fig. 5 in the reference. | # |
PIWIL4
(details) |
18444 | piwi-like RNA-mediated gene silencing 4 | 143689 | Q7Z3Z4 | PIWL4_HUMAN | PAZ PF02170 272-405, Piwi PF02171 546-837 | Piwil4 | 3041167 | Q8CGT6 | PIWL4_MOUSE | AGO | Argonaute/PIWI family | Chromatin remodeling, Histone modification erase cofactor | Histone methylation | 17544373 | # | histone | H3K9 | # | 17544373 | Induced histone H3 lysine 9 methylation at the p16(Ink4a) (CDKN2A) locus. Suggests that PIWIL4 plays important roles in the chromatin-modifying pathway in human somatic cells. | # |
PKM
(details) |
9021 | pyruvate kinase, muscle | 5315 | P14618 | KPYM_HUMAN | PK PF00224 43-375, PK_C PF02887 411-528 | Pkm | 97591 | P52480 | KPYM_MOUSE | # | # | Histone modification write cofactor | Histone phosphorylation | 24706538 | # | histone | H3S10, H3S28, H2BS32 | H3S10ph, H3S28ph, H2BS32ph, H3T11ph | 24706538 | Transcriptional activation by epidermal growth factor (EGF) is mediated via phosphorylation of H3S10, H3S28, and H2BS32 by Rsk-2 and PKM2. | # |
PKN1
(details) |
9405 | protein kinase N1 | 5585 | Q16512 | PKN1_HUMAN | HR1 PF02185 38-98 127-194 214-278, Pkinase PF00069 616-874, Pkinase_C PF00433 895-937 | Pkn1 | 108022 | P70268 | PKN1_MOUSE | # | # | Histone modification write | Histone phosphorylation | 18066052 | # | histone | H3T11 | H3T11ph | 18066052 | Protein-kinase-C-related kinase 1 (PRK1=PKN1) phosphorylates histone H3 at threonine 11 (H3T11) upon ligand-dependent recruitment to androgen receptor target genes. | # |
POGZ
(details) |
18801 | pogo transposable element with ZNF domain | 23126 | Q7Z3K3 | POGZ_HUMAN | HTH_Tnp_Tc5 PF03221 1025-1082, DDE_1 PF03184 1157-1287 | Pogz | 2442117 | Q8BZH4 | POGZ_MOUSE | # | # | Histone modification read | Histone methylation | 20562864, 20850016 | # | histone | H3K9me3 | # | # | Part of a H3K9me3 reader complex; modulates dissociation of HP1alpha. | # |
POLE3
(details) |
13546 | polymerase (DNA directed), epsilon 3, accessory subunit | 54107 | Q9NRF9 | DPOE3_HUMAN | CBFD_NFYB_HMF PF00808 9-73 | Pole3 | 1933378 | Q9JKP7 | DPOE3_MOUSE | POL | DNA polymerases | Histone chaperone | # | 10880450 | CHRAC | histone | # | # | 10880450 | The human homologues of two novel putative histone-fold proteins in Drosophila CHRAC are present in HuCHRAC. The two human histone-fold proteins form a stable complex that binds naked DNA but not nucleosomes. | # |
PPARGC1A
(details) |
9237 | peroxisome proliferator-activated receptor gamma, coactivator 1 alpha | 10891 | Q9UBK2 | PRGC1_HUMAN | RRM_1 PF00076 679-739 | Ppargc1a | 1342774 | O70343 | PRGC1_MOUSE | RBM | RNA binding motif (RRM) containing | Histone modification cofactor | # | 10558993 | # | histone | # | # | # | PPARgamma coactivator-1 (PGC-1) promotes transcription through the assembly of a complex that includes the histone acetyltransferases steroid receptor coactivator-1 (SRC-1). Promotes transcription through the assembly of a complex that includes HAT p300. | # |
PPM1G
(details) |
9278 | protein phosphatase, Mg2+/Mn2+ dependent, 1G | 5496 | O15355 | PPM1G_HUMAN | PP2C PF00481 26-108 303-489 | Ppm1g | 106065 | Q61074 | PPM1G_MOUSE | PPM | Serine/threonine phosphatases / Protein phosphatases, Mg2+/Mn2+ dependent | Chromatin remodeling | # | 23723158 | # | chromatin | # | # | 23723158 | Together with CHRAC1, ACF1 and ISWI/SNF2H proteins, it forms the ISWI chromatin-remodeling complex, CHRAC (UniProt). | # |
PPP2CA
(details) |
9299 | protein phosphatase 2, catalytic subunit, alpha isozyme | 5515 | P67775 | PP2AA_HUMAN | Metallophos PF00149 51-244 | Ppp2ca | 1321159 | P63330 | PP2AA_MOUSE | PPP | Serine/threonine phosphatases / Protein phosphatase, catalytic subunits | Histone modification write | Histone phosphorylation | 18758438 | # | histone | H2AX | H2AXph | 18758438 | PP2A =PPP2CA (rather than PP4) has been implicated as a mammalian γH2AX phosphatase. | # |
PPP4C
(details) |
9319 | protein phosphatase 4, catalytic subunit | 5531 | P60510 | PP4C_HUMAN | Metallophos PF00149 48-241 | Ppp4c | 1891763 | P97470 | PP4C_MOUSE | PPP | Serine/threonine phosphatases / Protein phosphatase, catalytic subunits | Histone modification erase | Histone phosphorylation | 18758438 | PPP4C-PPP4R2-PPP4R3A | histone | H2AXS139ph | H2AXS139 | 18758438 | PP4 and PP2A counteract phosphorylation of H2AX. | # |
PPP4R2
(details) |
18296 | protein phosphatase 4, regulatory subunit 2 | 151987 | Q9NY27 | PP4R2_HUMAN | PPP4R2 PF09184 5-309 | Ppp4r2 | 3027896 | Q0VGB7 | PP4R2_MOUSE | PPP4R | Serine/threonine phosphatases / Protein phosphatase 4, regulatory subunits | Histone modification cofactor | # | 18614045 | PPP4C-PPP4R2-PPP4R3A | histone | # | # | # | Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4) complex. PPARgamma coactivator-1 (PGC-1) promotes transcription through the assembly of a complex that includes the histone acetyltransferases steroid receptor coactivator-1 | # |
PQBP1
(details) |
9330 | Polyglutamine-binding protein 1 (PQBP-1) (38 kDa nuclear protein containing a WW domain) (Npw38) (Polyglutamine tract-binding protein 1) | 10084 | O60828 | PQBP1_HUMAN | Pqbp1 | 1859638 | Q91VJ5 | PQBP1_MOUSE | # | # | RNA modification | Alternative splicing | 23512658 | # | RNA | mRNA | # | 23512658 | Regulates alternative splcing of BCL-X and another apoptotic factors. | New | |
PRDM1
(details) |
9346 | PR domain containing 1, with ZNF domain | 639 | O75626 | PRDM1_HUMAN | PRDM2_PR PF21549 95-209, zf-C2H2 PF00096 575-597 603-625 631-653 659-681 | Prdm1 | 99655 | Q60636 | PRDM1_MOUSE | ZNF | Zinc fingers, C2H2-type | Histone modification write cofactor | Histone methylation | 23856557 | # | histone | H3K9 | H3K9me | 23856557 | The Prdm family may possess HKMTase properties. Some Prdms show intrinsic HKMTase activity (Prdm2, Prdm3, Prdm8, Prdm9, and Prdm16). In addition, Prdm1, Prdm5, and Prdm6 lack intrinsic HKMTase activity, but instead recruit G9a/Ehmt2/KMT1C, a strong mammalian histone H3 lysine 9 (H3K9) methyltransferase, to mediate HKMTase activity (see Fog et al., 2012 for a review). Another structural feature is that the Prdm family has multiple kruppel-type zinc finger (ZF) domains in the C-terminus involved in sequence-specific DNA binding and protein-protein interactions. | # |
PRDM11
(details) |
13996 | PR domain containing 11 | 56981 | Q9NQV5 | PRD11_HUMAN | PRDM2_PR PF21549 152-268 | Prdm11 | 2685553 | A2AGX3 | PRD11_MOUSE | # | # | Histone modification write | Histone methylation | 23508829 | # | histone | # | # | 23508829 | The PR (PRDI-BF1 and RIZ) domain is 20–30% identical to the SET module, which is directly responsible for the catalytic activity of several histone lysine-methyltransferases . | # |
PRDM12
(details) |
13997 | PR domain containing 12 | 59335 | Q9H4Q4 | PRD12_HUMAN | PRDM2_PR PF21549 89-213, zf-C2H2 PF00096 244-265 271-293 | Prdm12 | 2685844 | A2AJ77 | PRD12_MOUSE | ZNF | Zinc fingers, C2H2-type | Histone modification write cofactor | Histone methylation | 23856557 | # | histone | H3K9 | H3K9me | 23856557 | Prdm12 recruits G9a to methylate histone H3 on lysine 9 through its zinc finger domains. | # |
PRDM13
(details) |
13998 | PR domain containing 13 | 59336 | Q9H4Q3 | PRD13_HUMAN | PRDM2_PR PF21549 11-120, zf-C2H2 PF00096 137-159 574-595 601-623 630-653 | Prdm13 | 2448528 | E9PZZ1 | PRD13_MOUSE | # | # | Histone modification write | Histone methylation | 24370451 | # | histone | # | # | # | PRDM13 identified as a histone methyltransferase. | # |
PRDM14
(details) |
14001 | PR domain containing 14 | 63978 | Q9GZV8 | PRD14_HUMAN | PRDM2_PR PF21549 262-377, zf-C2H2 PF00096 461-483 489-511 546-568 | Prdm14 | 3588194 | E9Q3T6 | PRD14_MOUSE | ZNF | Zinc fingers, C2H2-type | DNA modification | DNA demethylation | 24335252 | # | DNA | mC | # | 24335252 | PRDM14 promotes active DNA demethylation. | # |
PRDM16
(details) |
14000 | PR domain containing 16 | 63976 | Q9HAZ2 | PRD16_HUMAN | PRDM2_PR PF21549 84-212, zf-C2H2_6 PF13912 230-250, zf-C2H2 PF00096 281-303 309-331 337-360 366-388 394-416 424-443 951-973 979-1002 1008-1030 | Prdm16 | 1917923 | A2A935 | PRD16_MOUSE | ZNF | Zinc fingers, C2H2-type | Histone modification write cofactor, TF | Histone methylation, TF repressor | 12816872, 23856557 | # | histone, DNA | H3K9, DNA motif | H3K9me | 23856557 | The Prdm family may possess HKMTase properties. Some Prdms show intrinsic HKMTase activity (Prdm2, Prdm3, Prdm8, Prdm9, and Prdm16). In addition, Prdm1, Prdm5, and Prdm6 lack intrinsic HKMTase activity, but instead recruit G9a/Ehmt2/KMT1C, a strong mammalian histone H3 lysine 9 (H3K9) methyltransferase, to mediate HKMTase activity (see Fog et al., 2012 for a review). Another structural feature is that the Prdm family has multiple kruppel-type zinc finger (ZF) domains in the C-terminus involved in sequence-specific DNA binding and protein-protein interactions. | # |
PRDM2
(details) |
9347 | PR domain containing 2, with ZNF domain | 7799 | Q13029 | PRDM2_HUMAN | PRDM2_PR PF21549 30-144, zf-C2H2 PF00096 360-382 390-412, zf-C2H2_6 PF13912 483-506 1455-1475 | Prdm2 | 107628 | # | # | KMT | Chromatin-modifying enzymes / K-methyltransferases | Histone modification write | Histone methylation | 20084102 | # | histone | H3K9 | H3K9me | 20084102 | The structures of the catalytic domains of GLP, G9a, Suv39H2 and PRDM2, four of the eight known human H3K9 methyltransferases in their apo conformation or in complex with the methyl donating cofactor, and peptide substrates. | # |
PRDM4
(details) |
9348 | PR domain containing 4 | 11108 | Q9UKN5 | PRDM4_HUMAN | zf_PR_Knuckle PF18445 366-404, PRDM2_PR PF21549 414-537, zf-C2H2 PF00096 618-640 646-668 674-696 | Prdm4 | 1920093 | Q80V63 | PRDM4_MOUSE | ZNF | Zinc fingers, C2H2-type | Histone modification write | Histone methylation | 23048031 | # | histone | H4R3 | H4R3me2s | 23048031 | Transcription factor positive regulatory domain 4 (PRDM4) recruits protein arginine methyltransferase 5 (PRMT5) to mediate histone arginine methylation and control neural stem cell proliferation and differentiation. | # |
PRDM5
(details) |
9349 | PR domain containing 5 | 11107 | Q9NQX1 | PRDM5_HUMAN | PRDM2_PR PF21549 8-127, zf-C2H2 PF00096 199-219 262-287 295-317 320-342 376-398 404-426 432-455 489-511 517-539 545-567 573-595 602-625, zf-met PF12874 234-254, zf-C2H2_6 PF13912 348-370 461-483 | Prdm5 | 1918029 | Q9CXE0 | PRDM5_MOUSE | ZNF | Zinc fingers, C2H2-type | Histone modification write | Histone methylation | 23856557 | # | histone | H3K9 | H3K9me | 23856557 | Some Prdms show intrinsic HKMTase activity (Prdm2, Prdm3, Prdm8, Prdm9, and Prdm16). In addition, Prdm1, Prdm5, and Prdm6 lack intrinsic HKMTase activity, but instead recruit G9a/Ehmt2/KMT1C, a strong mammalian histone H3 lysine 9 (H3K9) methyltransferase, to mediate HKMTase activity (see Fog et al., 2012 for a review). Another structural feature is that the Prdm family has multiple kruppel-type zinc finger (ZF) domains in the C-terminus involved in sequence-specific DNA binding and protein-protein interactions. | # |
PRDM6
(details) |
9350 | PR domain containing 6 | 93166 | Q9NQX0 | PRDM6_HUMAN | PRDM2_PR PF21549 255-374, zf-C2H2 PF00096 501-523 529-551 557-577 | Prdm6 | 2684938 | Q3UZD5 | PRDM6_MOUSE | ZNF | Zinc fingers, C2H2-type | Histone modification write | Histone methylation | 17898714, 16537907 | # | histone | H3R2, H4K20 | H3R2me1, H3R2me2, H4K20me1 | 17898714, 18057026 | The arginine methyltransferase PRMT6 catalyses H3R2 di-methylation in vitro and controls global levels of H3R2me2a in vivo. H3R2 methylation by PRMT6 was prevented by the presence of H3K4me3 on the H3 tail. PRISM =PRDM6 acts as a transcriptional repressor by interacting with class I histone deacetylases and the G9a histone methyltransferase, thereby identifying PRISM as a novel SMC-restricted epigenetic regulator. | # |
PRDM7
(details) |
9351 | PR domain containing 7 | 11105 | Q9NQW5 | PRDM7_HUMAN | KRAB PF01352 28-65, SSXRD PF09514 169-204, PRDM2_PR PF21549 245-365 | # | # | # | # | ZNF, ZKRAB | Zinc fingers, C2H2-type | Histone modification write | Histone methylation | # | # | histone | # | # | # | Probable histone methyltransferase (by similarity). | # |
PRDM8
(details) |
13993 | PR domain containing 8 | 56978 | Q9NQV8 | PRDM8_HUMAN | PRDM2_PR PF21549 26-138, zf-C2H2_4 PF13894 667-688 | Prdm8 | 1924880 | Q8BZ97 | PRDM8_MOUSE | # | # | Histone modification write | Histone methylation | 23856557 | # | histone | # | # | 23856557 | Some Prdms show intrinsic HKMTase activity (Prdm2, Prdm3, Prdm8, Prdm9, and Prdm16). In addition, Prdm1, Prdm5, and Prdm6 lack intrinsic HKMTase activity, but instead recruit G9a/Ehmt2/KMT1C, a strong mammalian histone H3 lysine 9 (H3K9) methyltransferase, to mediate HKMTase activity (see Fog et al., 2012 for a review). Another structural feature is that the Prdm family has multiple kruppel-type zinc finger (ZF) domains in the C-terminus involved in sequence-specific DNA binding and protein-protein interactions. | # |
PRDM9
(details) |
13994 | PR domain containing 9 | 56979 | Q9NQV7 | PRDM9_HUMAN | KRAB PF01352 32-62, SSXRD PF09514 89-97, PRDM2_PR PF21549 246-366, zf-C2H2_5 PF21225 390-411, zf-C2H2 PF00096 552-574 580-602 608-630 636-658 670-714 720-742 748-770 776-798 804-826 832-854 860-882 | Prdm9 | 2384854 | Q96EQ9 | PRDM9_MOUSE | ZKRAB, ZNF | Zinc fingers, C2H2-type | Histone modification write | Histone methylation | 17916234 | # | histone | H3K4 | H3K4me3 | 17916234 | Meisetz, the mouse ortholog of the long PRDM9 isoform, is able to activate the progression into meiosis through the trimethylation of the lysine 4 on histone H3. | # |
PRKAA1
(details) |
9376 | protein kinase, AMP-activated, alpha 1 catalytic subunit | 5562 | Q13131 | AAPK1_HUMAN | Pkinase PF00069 27-279, AMPK_alpha_AID PF21147 299-343, AdenylateSensor PF16579 406-479 | Prkaa1 | 2145955 | Q5EG47 | AAPK1_MOUSE | # | # | Histone modification write | Histone phosphorylation | 20647423 | # | histone | H2BS36 | H2BS36ph | # | In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Part of AMPK. | # |
PRKAA2
(details) |
9377 | protein kinase, AMP-activated, alpha 2 catalytic subunit | 5563 | P54646 | AAPK2_HUMAN | Pkinase PF00069 16-268, AMPK_alpha_AID PF21147 288-333, AdenylateSensor PF16579 401-477 | Prkaa2 | 1336173 | Q8BRK8 | AAPK2_MOUSE | # | # | Histone modification write | Histone phosphorylation | 20647423 | # | histone | H2BS36 | H2BS36ph | # | In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph) as a part of AMPK. | # |
PRKAB1
(details) |
9378 | protein kinase, AMP-activated, beta 1 non-catalytic subunit | 5564 | Q9Y478 | AAKB1_HUMAN | AMPK1_CBM PF16561 79-160, AMPKBI PF04739 200-269 | Prkab1 | 1336167 | Q9R078 | AAKB1_MOUSE | # | # | Histone modification write cofactor | Histone phosphorylation | 20647423 | # | histone | # | # | # | Non-catalytic subunit of AMP-activated protein kinase (AMPK). | # |
PRKAB2
(details) |
9379 | protein kinase, AMP-activated, beta 2 non-catalytic subunit | 5565 | O43741 | AAKB2_HUMAN | AMPK1_CBM PF16561 78-160, AMPKBI PF04739 202-271 | Prkab2 | 1336185 | Q6PAM0 | AAKB2_MOUSE | # | # | Histone modification write cofactor | Histone phosphorylation | 20647423 | # | histone | # | # | # | Non-catalytic subunit of AMP-activated protein kinase (AMPK). | # |
PRKAG1
(details) |
9385 | protein kinase, AMP-activated, gamma 1 non-catalytic subunit | 5571 | P54619 | AAKG1_HUMAN | CBS PF00571 45-96 127-176 203-249 276-323 | Prkag1 | 108411 | O54950 | AAKG1_MOUSE | # | # | Histone modification write cofactor | Histone phosphorylation | 20647423 | # | histone | # | # | # | AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK). | # |
PRKAG2
(details) |
9386 | protein kinase, AMP-activated, gamma 2 non-catalytic subunit | 51422 | Q9UGJ0 | AAKG2_HUMAN | CBS PF00571 277-328 359-409 435-481 510-555 | Prkag2 | 1336153 | Q91WG5 | AAKG2_MOUSE | # | # | Histone modification write cofactor | Histone phosphorylation | 20647423 | # | histone | # | # | # | AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK). | # |
PRKAG3
(details) |
9387 | protein kinase, AMP-activated, gamma 3 non-catalytic subunit | 53632 | Q9UGI9 | AAKG3_HUMAN | CBS PF00571 283-332 358-404 430-478 | Prkag3 | 1891343 | Q8BGM7 | AAKG3_MOUSE | # | # | Histone modification write cofactor | Histone phosphorylation | 20647423 | # | histone | # | # | # | AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK). | # |
PRKCA
(details) |
9393 | protein kinase C, alpha | 5578 | P17252 | KPCA_HUMAN | C1_1 PF00130 37-86 102-152, C2 PF00168 172-276, Pkinase PF00069 341-584, Pkinase_C PF00433 624-658 | Prkca | 97595 | P20444 | KPCA_MOUSE | # | # | Histone modification write cofactor | Histone phosphorylation | 22796964 | # | histone | H3 | # | # | Modifies H3, but may be a quite general kinase. | # |
PRKCB
(details) |
9395 | protein kinase C, beta | 5579 | P05771 | KPCB_HUMAN | C1_1 PF00130 37-86 102-153, C2 PF00168 172-277, Pkinase PF00069 344-596, Pkinase_C PF00433 621-662 | Prkcb | 97596 | P68404 | KPCB_MOUSE | # | # | Histone modification write | Histone methylation | 20228790 | # | histone | H3T6 | H3T6ph | 20228790 | Phosphorylation of histone H3 at threonine 6 (H3T6) by protein kinase C beta I (PKCbeta(I), also known as PRKCbeta) is the key event that prevents LSD1 from demethylating H3K4 during AR-dependent gene activation. | # |
PRKCD
(details) |
9399 | protein kinase C, delta | 5580 | Q05655 | KPCD_HUMAN | PKC_C2 PF21494 3-112, C1_1 PF00130 159-209 231-281, Pkinase PF00069 350-603, Pkinase_C PF00433 624-665 | Prkcd | 97598 | P28867 | KPCD_MOUSE | # | # | Histone modification | # | 17984964 | # | histone | # | # | # | Cross-regulation of histone modifications | # |
PRKDC
(details) |
9413 | protein kinase, DNA-activated, catalytic polypeptide | 5591 | P78527 | PRKDC_HUMAN | DNA-PKcs_N PF20500 15-874, DNAPKcs_CC1-2 PF20502 1001-1796, DNAPKcs_CC3 PF08163 1596-1947 1825-2207, DNAPKcs_CC5 PF19704 2131-2890, FAT PF02259 2943-3468, PI3_PI4_kinase PF00454 3749-4013, FATC PF02260 4098-4128 | Prkdc | 104779 | P97313 | PRKDC_MOUSE | # | # | Histone modification write | Histone phosphorylation | 14627815 | # | histone | H2AXS139, H2AFXS139 | H2AXS139ph, H2AFXS139ph | 14627815 | Acetylation largely enhances the phosphorylation of H2AX by DNA-PK=PRKDC, and this acetylation effect is observed when H2AX exists in the context of nucleosomes but not in a free form. | # |
PRMT1
(details) |
5187 | protein arginine methyltransferase 1 | 3276 | Q99873 | ANM1_HUMAN | Methyltransf_25 PF13649 92-189, domain PF22528 194-358 | Prmt1 | 107846 | Q9JIF0 | ANM1_MOUSE | PRMT | Protein arginine methyltransferases | Histone modification write | Histone methylation | 11387442 | # | histone | H4R3 | H4R3me1, H4R3me2a | 11387442 | PRMT1 specifically methylates arginine 3 (Arg 3) of H4 in vitro and in vivo. Methylation of Arg 3 by PRMT1 facilitates subsequent acetylation of H4 tails by p300. | # |
PRMT2
(details) |
5186 | protein arginine methyltransferase 2 | 3275 | P55345 | ANM2_HUMAN | SH3_1 PF00018 36-82, MTS PF05175 131-210, domain PF22528 244-415 | Prmt2 | 1316652 | Q9R144 | ANM2_MOUSE | PRMT | Protein arginine methyltransferases | Histone modification write | Histone methylation | 19405910 | # | histone | H4 | H4me | 19405910 | PRMT2 activity is substantially lower than PRMT1 in vitro, but both enzymes selectively methylate histone H4 and PRMT2, like PRMT1, may act as a transcription co-activator through this modification. | # |
PRMT5
(details) |
10894 | protein arginine methyltransferase 5 | 10419 | O14744 | ANM5_HUMAN | PRMT5_TIM PF17285 36-290, PRMT5 PF05185 299-464, PRMT5_C PF17286 467-635 | Prmt5 | 1351645 | Q8CIG8 | ANM5_MOUSE | PRMT | Protein arginine methyltransferases | Histone modification write | Histone methylation | 18404153 | methylosome | histone | H3R8, H4R3 | H3R8me, H4R3me | 18404153 | PRMT5 regulates gene transcription by methylating histones H3 (R8) and H4. | # |
PRMT6
(details) |
18241 | protein arginine methyltransferase 6 | 55170 | Q96LA8 | ANM6_HUMAN | Methyltransf_25 PF13649 85-182, domain PF22528 188-362 | Prmt6 | 2139971 | Q6NZB1 | ANM6_MOUSE | PRMT | Protein arginine methyltransferases | Histone modification write | Histone methylation | 18079182 | # | histone | H2AR3, H3R2, H4R4 | H2AR3me, H4R3me, H3R2me2a | 18079182 | PRMT6 methylates histone H3 at R2 and histones H4/H2A at R3 in vitro. Overexpression and knockdown analysis identify PRMT6 as the major H3 R2 methyltransferase in vivo. | # |
PRMT7
(details) |
25557 | protein arginine methyltransferase 7 | 54496 | Q9NVM4 | ANM7_HUMAN | PrmA PF06325 64-124, domain PF22528 177-348 515-686 | Prmt7 | 2384879 | Q922X9 | ANM7_MOUSE | PRMT | Protein arginine methyltransferases | Histone modification write | Histone methylation | 15494416 | # | histone | H2A, H4R3 | H2A, H4R3me2 | 15494416 | PRMT7 contains methyltransferase activity, the methylated (labeled) histones are H2A and H4. | # |
PRMT8
(details) |
5188 | protein arginine methyltransferase 8 | 56341 | Q9NR22 | ANM8_HUMAN | PrmA PF06325 111-184, domain PF22528 217-380 | Prmt8 | 3043083 | Q6PAK3 | ANM8_MOUSE | PRMT | Protein arginine methyltransferases | Histone modification write | Histone methylation | 16051612 | # | histone | H4R | H4Rme | 16051612 | PRMT8 preferentially methylates histone H4 and the recombinant forms of GAR and Npl3, thus displaying PRMT1-like substrate specificity. | # |
PRMT9
(details) |
25099 | protein arginine methyltransferase 9 | 90826 | Q6P2P2 | ANM9_HUMAN | PrmA PF06325 175-235, domain PF22528 366-461 750-837 | Prmt10 | 2142651 | Q3U3W5 | ANM9_MOUSE | PRMT | Protein arginine methyltransferases | Histone modification write | Histone methylation | 18007657 | # | histone | H4R3 | H4R3me2 | 18007657 | Arabidopsis thaliana protein arginine methyltransferase 10 (AtPRMT10)--the Arabidopsis homologue of PHRMT10 (=PRMT9)--has been shown to be a type I PRMT, which preferentially asymmetrically methylated histone H4R3 in vitro. Belongs to SAM-binding ethyltransferase superfamily. | # |
PRPF31
(details) |
15446 | pre-mRNA processing factor 31 | 26121 | Q8WWY3 | PRP31_HUMAN | Nop PF01798 100-332, Prp31_C PF09785 341-465 | Prpf31 | 1916238 | Q8CCF0 | PRP31_MOUSE | # | # | Histone modification write cofactor, Histone modification write cofactor | Histone methylation, Histone acetylation | # | CHD8, MLL2/3, MLL4/WBP7 | histone | # | # | # | Added because it is a complex partner | # |
PRR14
(details) |
28458 | proline rich 14 | 78994 | Q9BWN1 | PRR14_HUMAN | Tantalus PF15386 463-519 | Prr14 | 2384565 | Q7TPN9 | PRR14_MOUSE | # | # | Histone modification write | Histone phosphorylation | 24209742 | # | histone | H3K9me2, H3K9me3 | # | # | Binds to H3K9me2/3 through interaction with HP1, and not by direct interaction. PRR14 is incorporated rapidly into chromatin through HP1 binding, tethering heterochromatin to nuclear lamina. | # |
PSIP1
(details) |
9527 | PC4 and SFRS1 interacting protein 1 | 11168 | O75475 | PSIP1_HUMAN | PWWP PF00855 8-88, LEDGF PF11467 350-446 | Psip1 | 2142116 | Q99JF8 | PSIP1_MOUSE | # | # | Chromatin remodeling | # | 217205545 | # | chromatin | # | # | 217205545 | The PWWP domain in PSIP1 displays affinity for DNA and chromatin and its chromatin binding ability is crucial for the HIV-1 integration. PSIP1 has been found to promote association of the MLL complex with transcriptionally active chromatin through its PWWP domain. | # |
PTBP1
(details) |
9583 | Polypyrimidine tract-binding protein 1 (PTB) (57 kDa RNA-binding protein PPTB-1) (Heterogeneous nuclear ribonucleoprotein I) (hnRNP I) | 5725 | P26599 | PTBP1_HUMAN | RRM_5 PF13893 59-144 340-460, RRM_8 PF11835 178-258, RRM_1 PF00076 484-544 | Ptbp1 | 97791 | P17225 | PTBP1_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 21518792, 16260624 | # | RNA | mRNA | # | 21518792, 16260624 | Regulates exon selection in alpha-tropomyosin mRNA | New |
PTBP1
(details) |
9583 | Polypyrimidine tract-binding protein 1 (PTB) (57 kDa RNA-binding protein PPTB-1) (Heterogeneous nuclear ribonucleoprotein I) (hnRNP I) | 5725 | P26599 | PTBP1_HUMAN | RRM_5 PF13893 59-144 340-460, RRM_8 PF11835 178-258, RRM_1 PF00076 484-544 | Ptbp1 | 97791 | P17225 | PTBP1_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 16260624, 21518792 | # | RNA | mRNA | # | 16260624, 21518792 | Modulates alternative 5'-splice site and muscle-cell specific exon selection. | New |
PUF60
(details) |
17042 | Poly(U)-binding-splicing factor PUF60 (60 kDa poly(U)-binding-splicing factor) (FUSE-binding protein-interacting repressor) (FBP-interacting repressor) (Ro-binding protein 1) (RoBP1) (Siah-binding protein 1) (Siah-BP1) | 22827 | Q9UHX1 | PUF60_HUMAN | RRM_1 PF00076 131-201 228-297 | Puf60 | 1915209 | Q3UEB3 | PUF60_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 17579712, 16452196 | # | RNA | mRNA | # | 17579712, 16452196 | Regulates alternative splcing of FIR | New |
RAD51
(details) |
9817 | RAD51 recombinase | 5888 | Q06609 | RAD51_HUMAN | HHH_5 PF14520 32-79, Rad51 PF08423 95-336 | Rad51 | 97890 | Q08297 | RAD51_MOUSE | # | # | Histone modification erase | Histone ubiquitination | 15665856 | BRCC | # | histone | # | 15665856 | # | # |
RAD54B
(details) |
17228 | RAD54 homolog B (S. cerevisiae) | 25788 | Q9Y620 | RA54B_HUMAN | SNF2-rel_dom PF00176 299-595, Helicase_C PF00271 643-758 | Rad54b | 3605986 | Q6PFE3 | RA54B_MOUSE | # | # | Chromatin remodeling | # | 21357745 | # | chromatin | # | # | 21357745 | Rad54’s ATPase =RAD54B affects the chromatin association of the protein and Rad54 ATPase activity specifically influences its dissociation from foci. | # |
RAD54L
(details) |
9826 | RAD54-like (S. cerevisiae) | 8438 | Q92698 | RAD54_HUMAN | SNF2-rel_dom PF00176 156-462, Helicase_C PF00271 499-611 | Rad54l | 894697 | P70270 | RAD54_MOUSE | # | # | Chromatin remodeling | # | 8805304 | # | chromatin | # | # | 8805304 | V(D)J recombination does not involve homologous recombination, but mHR54 =RAD54L could mediate a substrate preparation step that V(D)J and meiotic recombination have in common, such as changing the chromatin structure of the loci that will be rearranged. | # |
RAD54L2
(details) |
29123 | RAD54-like 2 (S. cerevisiae) | 23132 | Q9Y4B4 | ARIP4_HUMAN | SNF2-rel_dom PF00176 274-598, Helicase_C PF00271 725-854 | Rad54l2 | 1933196 | Q99NG0 | ARIP4_MOUSE | # | # | Chromatin remodeling | # | 19692572 | # | chromatin | # | # | 19692572 | ARIP4 =RAD54L2 contains SNF2 domain that functions as a motor protein in chromatin remodeling complexes. | # |
RAG1
(details) |
9831 | recombination activating gene 1 | 5896 | P15918 | RAG1_HUMAN | RAG1_imp_bd PF12560 1-291, zf-C3HC4 PF00097 293-331, zf-RAG1 PF10426 354-383, RAG1 PF12940 387-1022 | Rag1 | 97848 | P15919 | RAG1_MOUSE | RNF | RING-type (C3HC4) zinc fingers | Histone modification write | Histone ubiquitination | 21256161 | # | histone, DNA | H3.3K, DNA motif | H3.3Kub | 21256161 | It has been suggested that RAG1 targets H3.3, the H3 variant known to be associated with recombining loci, and thus most likely to be encountered by RAG1 during V(D)J recombination. This reaction is absolutely dependent on an intact RAG1 RING domain, and requires regions of the far N-terminus of RAG1 where the H3.3 binding sight is likely to reside and regions within the H3 amino-terminal tail. Several H3.3 lysines are subject to ubiquitylation. | # |
RAG2
(details) |
9832 | recombination activating gene 2 | 5897 | P55895 | RAG2_HUMAN | RAG2 PF03089 52-390, RAG2_PHD PF13341 414-490 | Rag2 | 97849 | P21784 | RAG2_MOUSE | # | # | Histone modification read | # | 21423274 | # | histone | H3K4me3 | # | 21423274 | Recombination-activating protein, RAG2, binds to H3K4me3 at transcribed genes while RAG1 recognizes the recombination signal sequence. | # |
RAI1
(details) |
9834 | retinoic acid induced 1 | 10743 | Q7Z5J4 | RAI1_HUMAN | zf-HC5HC2H PF13771 1825-1903 | Rai1 | 103291 | Q61818 | RAI1_MOUSE | # | # | Chromatin remodeling | # | 22498752 | # | chromatin | # | # | # | RAI1 regulates transcription through chromatin remodeling, according to UniProt. | # |
RARA
(details) |
9864 | retinoic acid receptor, alpha | 5914 | P10276 | RARA_HUMAN | zf-C4 PF00105 87-155, Hormone_recep PF00104 227-399 | Rara | 97856 | P11416 | RARA_MOUSE | NR | Nuclear hormone receptors | Histone modification write cofactor, TF | Histone methylation, TF activator, TF repressor | 19377461 | # | histone | H3K4 | H3K4me, H3K4me2 | 19377461 | MLL5 is biochemically identified in a GlcNAcylation-dependent multi-subunit complex associating with nuclear retinoic acid receptor RARalpha (also known as RARA), serving as a mono- and di-methyl transferase to H3K4. | # |
RB1
(details) |
9884 | retinoblastoma 1 | 5925 | P06400 | RB_HUMAN | DUF3452 PF11934 110-229, RB_A PF01858 375-573, RB_B PF01857 647-765, Rb_C PF08934 768-925 | Rb1 | 97874 | P13405 | RB_MOUSE | ENDOLIG | Endogenous ligands | Chromatin remodeling, Histone modification write | Histone ubiquitination | 19149898 | CREST-BRG1, L3MBTL1 | histone | # | # | 19149898 | Hypophosphorylated pRb can repress gene transcription at least partly by remodeling chromatin structure through its interactions with proteins such as HDAC1, BRM and BRG1. | # |
RBBP4
(details) |
9887 | retinoblastoma binding protein 4 | 5928 | Q09028 | RBBP4_HUMAN | CAF1C_H4-bd PF12265 19-88, WD40 PF00400 173-206 221-256 265-302 309-346 367-402 | Rbbp4 | 1194912 | Q60972 | RBBP4_MOUSE | WDR | WD repeat domain containing | Histone chaperone | # | 8858152 | NuRF, SWI/SNF_Brg1(I), SWI/SNF_Brg1(II), SWI/SNF_Brm, NuRD, mSin3A, core HDAC, mSin3A-like complex, PRC2, CAF-1 | histone | H4 | # | 8858152 | RbAp46 and RbAp48 (pRB-associated proteins p46 and p48, also known as RBBP7 and RBBP4, respectively) are highly homologous histone chaperones that play key roles in establishing and maintaining chromatin structure. Human p48 =RBBP4 can bind to histone H4 in the absence of CAF-1 p150 and p60. p48, also a known subunit of a histone deacetylase, copurifies with a chromatin assembly complex (CAC), which contains the three subunits of CAF-1 (p150, p60, p48) and H3 and H4, and promotes DNA replication-dependent chromatin assembly. | # |
RBBP5
(details) |
9888 | retinoblastoma binding protein 5 | 5929 | Q15291 | RBBP5_HUMAN | WD40 PF00400 29-52 62-94 | Rbbp5 | 1918367 | Q8BX09 | RBBP5_MOUSE | WDR | WD repeat domain containing | Histone modification write cofactor | Histone methylation | 19556245 | COMPASS, Menin-associated_HMT, MLL-HCF, CHD8, MLL2/3, COMPASS-like MLL1,2, MLL4/WBP7, COMPASS-like MLL3,4 | histone | H3K4 | H3K4me1, H3K4me2, H3K4me3 | 19556245 | A five-component 200-kDa MLL1 core complex containing human MLL1, WDR5, RbBP5, Ash2L, and DPY-30. | # |
RBBP7
(details) |
9890 | retinoblastoma binding protein 7 | 5931 | Q16576 | RBBP7_HUMAN | CAF1C_H4-bd PF12265 18-87, WD40 PF00400 172-205 220-255 264-301 308-345 366-402 | Rbbp7 | 1194910 | Q60973 | RBBP7_MOUSE | WDR | WD repeat domain containing | Histone chaperone | # | 18571423 | NuRF, NuRD, mSin3A, core HDAC, mSin3A-like complex, PRC2 | histone | H4 | # | 18571423 | RbAp46 and RbAp48 (pRB-associated proteins p46 and p48, also known as RBBP7 and RBBP4, respectively) are highly homologous histone chaperones that play key roles in establishing and maintaining chromatin structure. When a histone H3/H4 dimer (or tetramer) binds to RbAp46 or RbAp48, helix 1 of histone H4 unfolds to interact with the histone chaperone. | # |
RBFOX1
(details) |
9910 | RNA-binding motif protein, X chromosome (Glycoprotein p43) (Heterogeneous nuclear ribonucleoprotein G) (hnRNP G) [Cleaved into: RNA-binding motif protein, X chromosome, N-terminally processed] | 27316 | P38159 | RBMX_HUMAN | RRM_1 PF00076 10-80, RBM1CTR PF08081 169-221 | Rbmx | 1343044 | Q9WV02 | RBMX_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 12165565 | # | RNA | mRNA | # | 12165565 | Promotes exon 7 inclusion of SMN | New |
RBM11
(details) |
9897 | Splicing regulator RBM11 (RNA-binding motif protein 11) | 54033 | P57052 | RBM11_HUMAN | RRM_1 PF00076 12-80 | Rbm11 | 2447622 | Q80YT9 | RBM11_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 21984414 | # | RNA | mRNA | # | 21984414 | Regulates alternative splicing of Bcl-X and potentialy another genes during neuron and germ cell differentiation. | New |
RBM15
(details) |
14959 | RNA-binding protein 15 (One-twenty two protein 1) (RNA-binding motif protein 15) | 64783 | Q96T37 | RBM15_HUMAN | RRM_1 PF00076 182-245 376-444, SPOC PF07744 783-956 | Rbm15 | 2443205 | Q0VBL3 | RBM15_MOUSE | RBM | RNA binding motif containing | RNA modification | RNA methylation | 27602518 | WMM | RNA | A of mRNA | m6A | 27602518 | Recognition of RNA sites for m6A-methylation and recruitment of methylation complexes | New |
RBM15B
(details) |
24303 | Putative RNA-binding protein 15B (One-twenty two protein 3) (HsOTT3) (HuOTT3) (RNA-binding motif protein 15B) | 29890 | Q8NDT2 | RB15B_HUMAN | RRM_1 PF00076 339-408 420-480, SPOC PF07744 705-888 | Rbm15B | 1923598 | Q6PHZ5 | RB15B_MOUSE | RBM | RNA binding motif containing | RNA modification | RNA methylation | 27602518 | WMM | RNA | A of mRNA | m6A | 27602518 | Recognition of RNA sites for m6A-methylation and recruitment of methylation complexes | New |
RBM17
(details) |
16944 | Splicing factor 45 (45 kDa-splicing factor) (RNA-binding motif protein 17) | 84991 | Q96I25 | SPF45_HUMAN | G-patch PF01585 236-276, RRM_1 PF00076 328-383 | Rbm17 | 1924188 | Q8JZX4 | SPF45_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 17589525 | # | RNA | mRNA | # | 17589525 | Regulates alternative splicing of apoptosis regulator FAS | New |
RBM24
(details) |
21539 | RNA-binding protein 24 (RNA-binding motif protein 24) (RNA-binding region-containing protein 6) | 221662 | Q9BX46 | RBM24_HUMAN | RRM_1 PF00076 13-70 | Rbm24 | 3610364 | D3Z4I3 | RBM24_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 29104163, 26990106 | # | RNA | mRNA | # | 29104163, 26990106 | Promotes alternative splicing events of several pluripotency and/or differentiation genes. Mediates preferentially muscle-specific exon inclusion in numerous mRNAs important for striated cardiac and skeletal muscle cell differentiation | New |
RBM25
(details) |
23244 | RNA-binding protein 25 (Arg/Glu/Asp-rich protein of 120 kDa) (RED120) (Protein S164) (RNA-binding motif protein 25) (RNA-binding region-containing protein 7) | 58517 | P49756 | RBM25_HUMAN | RRM_1 PF00076 89-157, PWI PF01480 770-835 | Rbm25 | 1914289 | B2RY56 | RBM25_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 18663000 | # | RNA | RNA | # | 18663000 | alternative splicing site selection | New |
RBM4
(details) |
9901 | RNA-binding protein 4 (Lark homolog) (hLark) (RNA-binding motif protein 4) (RNA-binding motif protein 4a) | 5936 | Q9BWF3 | RBM4_HUMAN | RRM_1 PF00076 4-65 80-142, zf-CCHC PF00098 161-176 | Rbm4 | 1100865 | Q8C7Q4 | RBM4_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 16777844, 21518792 | # | RNA | RNA | # | 16777844, 21518792 | Modulates alternative 5'-splice site and exon selection. Activates exon skipping of the PTB pre-mRNA during muscle cell differentiation | New |
RBM5
(details) |
9902 | RNA-binding protein 5 (Protein G15) (Putative tumor suppressor LUCA15) (RNA-binding motif protein 5) (Renal carcinoma antigen NY-REN-9) | 10181 | P52756 | RBM5_HUMAN | RRM_1 PF00076 100-163 233-295, zf-RanBP PF00641 181-209, OCRE PF17780 456-507, G-patch PF01585 743-787 | Rbm5 | 1933204 | Q91YE7 | RBM5_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 18840686 | # | RNA | mRNA | # | 18840686 | Regulates the ratio of proapoptotic/antiapoptotic casp-2 splicing isoforms | New |
RBM7
(details) |
9904 | RNA-binding protein 7 (RNA-binding motif protein 7) | 10179 | Q9Y580 | RBM7_HUMAN | RRM_1 PF00076 12-81 | Rbm7 | 1914260 | Q9CQT2 | RBM7_MOUSE | RBM | RNA binding motif containing | RNA modification | RNA degradation, alternative splicing | 25578728 | # | RNA | snRNA | # | 25578728 | Component of exosome | New |
RBM8A
(details) |
9905 | RNA-binding protein 8A (Binder of OVCA1-1) (BOV-1) (RNA-binding motif protein 8A) (RNA-binding protein Y14) (Ribonucleoprotein RBM8A) | 9939 | Q9Y5S9 | RBM8A_HUMAN | RRM_1 PF00076 75-144 | Rbm8A | 1913129 | Q9CWZ3 | RBM8A_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 22203037 | # | RNA | mRNA | # | 22203037 | Production of the proapoptotic Bcl-x(S) splice variant. | New |
RBMY1A1
(details) |
9912 | RNA-binding motif protein, Y chromosome, family 1 member A1 (RNA-binding motif protein 1) (RNA-binding motif protein 2) (Y chromosome RNA recognition motif 1) (hRBMY) | 5940 | P0DJD3 | RBY1A_HUMAN | RRM_1 PF00076 10-79 | Rbmy | 104732 | O35698 | RBY1A_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 12165565 | # | RNA | mRNA | # | 12165565 | Regulates alternative splicing of SMN gene | New |
RBX1
(details) |
9928 | ring-box 1, E3 ubiquitin protein ligase | 9978 | P62877 | RBX1_HUMAN | zf-rbx1 PF12678 40-98 | Rbx1 | 1891829 | P62878 | RBX1_MOUSE | RNF | RING-type (C3HC4) zinc fingers | Histone modification write cofactor | Histone ubiquitination | 18593899 | # | histone | H3, H4 | H3ub, H4ub | 18593899 | Histones H3 and H4 are targets of the CUL4-DDB-RBX1 E3 ligase ( 34). It has been proposed that both DDB1-CUL4DDB2 and Ring2 ligases are recruited to UV-induced lesions to modify histones. | # |
RCC1
(details) |
1913 | regulator of chromosome condensation 1 | 1104 | P18754 | RCC1_HUMAN | RCC1 PF00415 35-82 86-134 138-187 191-257 259-309 313-358 364-414 | Rcc1 | 1913989 | Q8VE37 | RCC1_MOUSE | # | # | Chromatin remodeling | # | 11375490 | # | histone | H2A, H2B | # | # | Binds to histones H2A and H2B. | # |
RCOR1
(details) |
17441 | REST corepressor 1 | 23186 | Q9UKL0 | RCOR1_HUMAN | ELM2 PF01448 107-158, Myb_DNA-binding PF00249 194-237 385-428, REST_helical PF20878 311-375 | Rcor1 | 106340 | Q8CFE3 | RCOR1_MOUSE | # | # | Histone modification erase cofactor, Histone modification erase cofactor | Histone acetylation, Histone methylation | 10449787 | BHC, SCL, LSD-CoREST | histone | # | # | 10449787 | CoREST=RCOR1 may function as a repressor by recruiting, either directly or indirectly, histone deacetylase activity. | # |
RCOR3
(details) |
25594 | REST corepressor 3 | 55758 | Q9P2K3 | RCOR3_HUMAN | ELM2 PF01448 1-52, Myb_DNA-binding PF00249 88-131 289-332, REST_helical PF20878 215-278 | Rcor3 | 2441920 | Q6PGA0 | RCOR3_MOUSE | # | # | Histone modification erase cofactor | Histone acetylation | 23752268 | LSD-CoREST | histone | # | # | 23752268 | Part of the HDAC interactome. | # |
REST
(details) |
9966 | RE1-silencing transcription factor | 5978 | Q13127 | REST_HUMAN | zf-C2H2 PF00096 304-326 | Rest | 104897 | Q8VIG1 | REST_MOUSE | # | # | Histone modification erase cofactor, TF | Histone acetylation, TF activator, TF repressor | 12399542 | # | DNA | DNA motif | # | 12399542 | REST/NRSF can mediate repression, in part, through the association of its NH2-terminal repression domain with the mSin3/histone deacethylase 1,2 (HDAC1,2) complex. | # |
RFOX1
(details) |
18222 | RNA binding protein fox-1 homolog 1 (Ataxin-2-binding protein 1) (Fox-1 homolog A) (Hexaribonucleotide-binding protein 1) | 54715 | Q9NWB1 | RFOX1_HUMAN | RRM_1 PF00076 120-186, Fox-1_C PF12414 254-342 | Rbfox1 | 1926224 | Q9JJ43 | RFOX1_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 16537540 | # | RNA | mRNA | # | 16537540 | Activates inclusion of 4.1R exon 16 | New |
RING1
(details) |
10018 | ring finger protein 1 | 6015 | Q06587 | RING1_HUMAN | zf-C3HC4_2 PF13923 47-87, RAWUL PF16207 282-400 | Ring1 | 1101770 | O35730 | RING1_MOUSE | RNF | RING-type (C3HC4) zinc fingers | Histone modification write, Polycomb group (PcG) protein | Histone ubiquitination | 15386022 | PRC1, BCOR, RING2-L3MBTL2, RING2-FBRS | histone | H2AK119 | H2AK119ub | 15386022 | The complex hPRC1L (human Polycomb repressive complex 1-like) is composed of several Polycomb-group proteins including Ring1, Ring2, Bmi1 and HPH2. hPRC1L monoubiquitinates nucleosomal histone H2A at lysine 119. | # |
RLIM
(details) |
13429 | ring finger protein, LIM domain interacting | 51132 | Q9NVW2 | RNF12_HUMAN | zf-RING_2 PF13639 569-611 | Rlim | 1342291 | Q9WTV7 | RNF12_MOUSE | RNF | RING-type (C3HC4) zinc fingers | Histone modification erase cofactor | Histone acetylation | 10431247 | # | histone | # | # | # | Recruits the Sin3A/histone deacetylase corepressor complex. | # |
RMI1
(details) |
25764 | RecQ mediated genome instability 1 | 80010 | Q9H9A7 | RMI1_HUMAN | RMI1_N_N PF21000 16-62, RMI1_N_C PF08585 67-206, RMI1_C PF16099 481-623 | Rmi1 | 1921636 | Q9D4G9 | RMI1_MOUSE | # | # | DNA modification | # | 16537486 | # | DNA | # | # | 16537486 | # | # |
RNF168
(details) |
26661 | ring finger protein 168, E3 ubiquitin protein ligase | 165918 | Q8IYW5 | RN168_HUMAN | zf-C3HC4 PF00097 16-55 | Rnf168 | 1917488 | Q80XJ2 | RN168_MOUSE | RNF | RING-type (C3HC4) zinc fingers | Histone modification write | Histone ubiquitination | 22980979 | # | histone | H2AK13, H2AK15, H2AXK13, H2AXK15 | H2AK13ub, H2AK15ub, H2AXK13ub, H2AXK15ub | 22980979 | RNF8 and RNF168 targets histone H2A and H2AX. RNF8 is the first ligase recruited to the damage site, and RNF168 follows RNF8-dependent ubiquitination. This suggests that RNF8 initiates H2A/H2AX ubiquitination with K63-linked ubiquitin chains and RNF168 extends them. RNF8 is inactive toward nucleosomal H2A, whereas RNF168 catalyzes the monoubiquitination of the histones specifically on K13-15. | # |
RNF2
(details) |
10061 | ring finger protein 2 | 6045 | Q99496 | RING2_HUMAN | zf-C3HC4_2 PF13923 50-90, RAWUL PF16207 246-330 | Rnf2 | 1101759 | Q9CQJ4 | RING2_MOUSE | RNF | RING-type (C3HC4) zinc fingers | Histone modification write | Histone ubiquitination | 16943429 | PRC1, BCOR, RING2-L3MBTL2, RING2-FBRS, CHD8, MLL2/3, MLL4/WBP7 | histone | H2AK119 | H2AK119ub | 16943429 | RNF2 is the only BCOR complex PcG protein with a known enzymatic activity: an E3 ligase for the histone protein H2A (12, 78). Ub-H2A is thought to be involved in maintaining a repressed chromatin state. | # |
RNF20
(details) |
10062 | ring finger protein 20, E3 ubiquitin protein ligase | 56254 | Q5VTR2 | BRE1A_HUMAN | zf-C3HC4 PF00097 922-960 | Rnf20 | 1925927 | Q5DTM8 | BRE1A_MOUSE | RNF | RING-type (C3HC4) zinc fingers | Histone modification write | Histone ubiquitination | 16307923 | # | histone | H2BK120 | H2BK120ub1 | 16307923 | Two copies each of the E3 ligases RNF20 and RNF40 are present in the same complex catalyzing histone H2B-K120 monoubiquitination. The complex that catalyzes histone H2A-K119 monoubiquitination also contains two E3 ligases, Ring1 and Ring2. | # |
RNF40
(details) |
16867 | ring finger protein 40, E3 ubiquitin protein ligase | 9810 | O75150 | BRE1B_HUMAN | zf-C3HC4 PF00097 948-986 | Rnf40 | 2142048 | Q3U319 | BRE1B_MOUSE | RNF | RING-type (C3HC4) zinc fingers | Histone modification write cofactor | Histone ubiquitination | 16307923 | # | histone | H2BK121 | H2BK120ub2 | 16307923 | Two copies each of the E3 ligases RNF20 and RNF40 are present in the same complex catalyzing histone H2B-K120 monoubiquitination. The complex that catalyzes histone H2A-K119 monoubiquitination also contains two E3 ligases, Ring1 and Ring2. | # |
RNF8
(details) |
10071 | ring finger protein 8, E3 ubiquitin protein ligase | 9025 | O76064 | RNF8_HUMAN | FHA PF00498 38-109, zf-C3HC4_3 PF13920 400-446 | Rnf8 | 1929069 | Q8VC56 | RNF8_MOUSE | RNF | RING-type (C3HC4) zinc fingers | Histone modification write | Histone ubiquitination | 22980979 | # | histone | H2AK63, H2AXK63, H2AK48, H2AXK48 | H2AK63ub, H2AXK63ub, H2AK48ub, H2AXK48ub | 22980979 | Ubiquitin-dependent signaling during the DNA damage response (DDR) to double-strand breaks (DSBs) is initiated by two E3 ligases, RNF8 and RNF168, targeting histone H2A and H2AX. RNF8 is the first ligase recruited to the damage site, and RNF168 follows RNF8-dependent ubiquitination. This suggests that RNF8 initiates H2A/H2AX ubiquitination with K63-linked ubiquitin chains and RNF168 extends them. | # |
RNPS1
(details) |
10080 | RNA-binding protein with serine-rich domain 1 (SR-related protein LDC2) | 10921 | Q15287 | RNPS1_HUMAN | RRM_1 PF00076 164-233 | Rnps1 | 97960 | Q99M28 | RNPS1_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 22203037 | # | RNA | mRNA | # | 22203037 | Production of the proapoptotic Bcl-x(S) splice variant. | New |
RPS6KA3
(details) |
10432 | ribosomal protein S6 kinase, 90kDa, polypeptide 3 | 6197 | P51812 | KS6A3_HUMAN | Pkinase PF00069 68-327 422-679, Pkinase_C PF00433 351-387 | Rps6ka3 | 104557 | P18654 | KS6A3_MOUSE | # | # | Histone modification write cofactor | Histone phosphorylation | 10436156 | # | histone | H3S10 | H3S10ph | 10436156 | Is required for EGF-stimulated phosphorylation of CREB1 and histone H3 at 'Ser-10', which results in the subsequent transcriptional activation of several immediate-early genes. | # |
RPS6KA4
(details) |
10433 | ribosomal protein S6 kinase, 90kDa, polypeptide 4 | 8986 | O75676 | KS6A4_HUMAN | Pkinase PF00069 33-301 413-673, Pkinase_C PF00433 322-361 | Rps6ka4 | 1930076 | Q9Z2B9 | KS6A4_MOUSE | # | # | Histone modification write | Histone phosphorylation | 12773393 | # | histone | H3S10, H3S28 | H3S10ph, H3S28ph | 12773393 | The MSKs, particularly MSK2=RPS6KA4, but not RSK2, are the major histone H3 and HMG-14 kinases. | # |
RPS6KA5
(details) |
10434 | ribosomal protein S6 kinase, 90kDa, polypeptide 5 | 9252 | O75582 | KS6A5_HUMAN | Pkinase PF00069 49-318 426-687, Pkinase_C PF00433 339-377 | Rps6ka5 | 1920336 | Q8C050 | KS6A5_MOUSE | # | # | Histone modification write | Histone phosphorylation | 12773393 | # | histone | H2AS1, H3S10, H3S28 | H2AS1ph, H3S10ph, H3S28ph | 12773393 | The MSKs=(RPS6KA4, RPS6KA5), particularly MSK2, but not RSK2, are the major histone H3 and HMG-14 kinases. | # |
RPUSD3
(details) |
28437 | Mitochondrial mRNA pseudouridine synthase RPUSD3 (EC 5.4.99.-) (RNA pseudouridylate synthase domain-containing protein 3) | 285367 | Q6P087 | RUSD3_HUMAN | PseudoU_synth_2 PF00849 90-252 | Rpusd3 | 2141440 | Q14AI6 | RUSD3_MOUSE | RPUSD | RNA pseudouridylate synthase domain containing | RNA modification | RNA pseudouridinilation | 27974379 | # | RNA | mt--mRNA | U | 27974379 | Pseudouridinilation of mitochondrial mRNA | New |
RRP8
(details) |
29030 | ribosomal RNA processing 8, methyltransferase, homolog (yeast) | 23378 | O43159 | RRP8_HUMAN | Methyltransf_8 PF05148 239-456 | Rrp8 | 1914251 | Q9DB85 | RRP8_MOUSE | # | # | Histone modification cofactor | # | 18485871 | eNoSc | histone | H3ac | H3K9me2 | # | A component of the eNoSC complex, that mediates silencing of rDNA by recruiting histone-modifying enzymes, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. | # |
RSF1
(details) |
18118 | remodeling and spacing factor 1 | 51773 | Q96T23 | RSF1_HUMAN | WHIM1 PF15612 96-141, PHD PF00628 894-938 | Rsf1 | 2682305 | # | # | PHF | Zinc fingers, PHD-type | Histone modification read | # | 12972596 | RSF | histone | # | # | 12972596 | Recombinant RSF complex coimmunoprecipitates with core histones, and Rsf-1 alone also interacts with core histones. | # |
RSRC1
(details) |
24152 | Serine/Arginine-related protein 53 (SRrp53) (Arginine/serine-rich coiled-coil protein 1) | 51319 | Q96IZ7 | RSRC1_HUMAN | Rsrc1 | 1914130 | Q9DBU6 | RSRC1_MOUSE | # | # | RNA modification | Alternative splicing | 29522154 | # | RNA | mRNA | # | 29522154 | Regulates alternative splicing of E1A | New | |
RUVBL1
(details) |
10474 | RuvB-like AAA ATPase 1 | 8607 | Q9Y265 | RUVB1_HUMAN | TIP49 PF06068 14-368, TIP49_C PF17856 374-439 | Ruvbl1 | 1928760 | P60122 | RUVB1_MOUSE | INO80, AATP | INO80 complex subunits, ATPases / AAA-type | Chromatin remodeling, Histone modification write | Histone phosphorylation | 14695187 | Ino80, SWR, NuA4, NuA4-related complex, CHD8, MLL2/3, MLL4/WBP7, SRCAP | chromatin | # | # | 14695187 | The ability of TIP49=RUVBL1 to inhibit ITF-2 gene expression has been linked to decreased acetylation of histones in the vicinity of the TCF-binding sites in the ITF-2 promoter region. It has been suggested that TIP49 is an important cofactor in beta-catenin/TCF gene regulation in normal and neoplastic cells, likely functioning in chromatin remodeling. | # |
RUVBL2
(details) |
10475 | RuvB-like AAA ATPase 2 | 10856 | Q9Y230 | RUVB2_HUMAN | TIP49 PF06068 21-364, TIP49_C PF17856 370-435 | Ruvbl2 | 1342299 | Q9WTM5 | RUVB2_MOUSE | INO80, AATP | INO80 complex subunits, ATPases / AAA-type | Chromatin remodeling cofactor | # | 18026119 | Ino80, SWR, NuA4, NuA4-related complex, CHD8, MLL2/3, MLL4/WBP7, SRCAP | chromatin | # | # | 18026119 | The seven human INO80 complex components include TIP49A and TIP49B (previously identified as ‘RuvB-like’ proteins, and labeled RUVBL1 and RUVBL2). | # |
RYBP
(details) |
10480 | RING1 and YY1 binding protein | 23429 | Q8N488 | RYBP_HUMAN | zf-RanBP PF00641 22-45, YAF2_RYBP PF17219 146-178 | Rybp | 1929059 | Q8CCI5 | RYBP_MOUSE | # | # | Polycomb group (PcG) protein | # | 19098711 | BCOR, RING2-L3MBTL2, RING2-FBRS | # | # | # | 19098711 | RYBP (RING1- and YY1-binding protein), a member of the polycomb group (PcG), interacts with MDM2 and decreases MDM2-mediated p53 ubiquitination, leading to stabilization of p53 and an increase in p53 activity. | # |
SAFB
(details) |
10520 | scaffold attachment factor B | 6294 | Q15424 | SAFB1_HUMAN | SAP PF02037 31-65, RRM_1 PF00076 408-478 | Safb | 2146974 | D3YXK2 | SAFB1_MOUSE | RBM | RNA binding motif (RRM) containing | Chromatin remodeling | # | 24055346 | # | chromatin | # | # | # | The chromatine scaffold protein, a component of the DNA damage response cooperating with histone acetylation to allow for efficient γH2AX spreading. | # |
SAP130
(details) |
29813 | Sin3A-associated protein, 130kDa | 79595 | Q9H0E3 | SP130_HUMAN | SAP130_C PF16014 654-1033 | Sap130 | 1919782 | Q8BIH0 | SP130_MOUSE | # | # | Histone modification erase cofactor | Histone acetylation | 12724404 | # | histone | # | # | 12724404 | SAP130 has a repression domain at its C terminus that interacts with the mSin3A-HDAC complex and an N-terminal domain that probably mediates an interaction with a transcriptional activator. | # |
SAP18
(details) |
10530 | Sin3A-associated protein, 18kDa | 10284 | O00422 | SAP18_HUMAN | SAP18 PF06487 21-137 | Sap18 | 1277978 | O55128 | SAP18_MOUSE | # | # | Histone modification erase cofactor | Histone acetylation | 9150135 | mSin3A | histone | # | # | 9150135 | SAP18 Interacts with mSin3 and enhances the ability of mSin3-mediated repression of transcription. | # |
SAP25
(details) |
41908 | Sin3A-associated protein, 25kDa | 100316904 | Q8TEE9 | SAP25_HUMAN | SAP25 PF15476 17-193 | Sap25 | 3802945 | Q1EHW4 | SAP25_MOUSE | # | # | Histone modification erase cofactor | Histone acetylation | 16449650 | # | histone | # | # | 16449650 | SAP25 binds to the PAH1 domain of mSin3A, associates with the mSin3A-HDAC complex in vivo, and represses transcription when tethered to DNA. SAP25 is required for mSin3A-mediated, but not N-CoR-mediated, repression. | # |
SAP30
(details) |
10532 | Sin3A-associated protein, 30kDa | 8819 | O75446 | SAP30_HUMAN | zf-SAP30 PF13866 64-134, SAP30_Sin3_bdg PF13867 153-205 | Sap30 | 1929129 | O88574 | SAP30_MOUSE | # | # | Histone modification erase cofactor | Histone acetylation | 9651585 | mSin3A, mSin3A-like complex | histone | # | # | 9651585 | The human SAP30 complex is active in deacetylating core histone octamers. | # |
SAP30L
(details) |
25663 | SAP30-like | 79685 | Q9HAJ7 | SP30L_HUMAN | zf-SAP30 PF13866 26-95, SAP30_Sin3_bdg PF13867 114-166 | Sap30l | 1354709 | Q5SQF8 | SP30L_MOUSE | # | # | Histone modification erase cofactor | Histone acetylation | 16820529 | # | histone | # | # | 16820529 | SAP30L induces transcriptional repression, possibly via recruitment of Sin3A and histone deacetylases. A functional nucleolar localization signal in SAP30L means that SAP30L and SAP30 are able to target Sin3A to the nucleolus. | # |
SATB1
(details) |
10541 | SATB homeobox 1 | 6304 | Q01826 | SATB1_HUMAN | ULD PF16534 72-169, CUTL PF16557 177-248, CUT PF02376 371-446 493-568, Homeodomain PF00046 646-701 | Satb1 | 105084 | Q60611 | SATB1_MOUSE | CUT | Homeoboxes / CUT class | Chromatin remodeling cofactor | # | 15713622, 24055346, 12374985, 12374985, 24055346 | # | chromatin | # | # | # | Acts as a docking site for several chromatin remodeling enzymes and also by recruiting corepressors (HDACs) or coactivators (HATs) directly to promoters and enhancers. Forms chromatin loops. SATB1 also targets ACF1 and ISWI, subunits of CHRAC and ACF nucleosome mobilizing complexes. SAFB1 is a component of the DNA damage response and shows that SAFB1 cooperates with histone acetylation to allow for efficient γH2AX spreading. | # |
SATB2
(details) |
21637 | SATB homeobox 2 | 23314 | Q9UPW6 | SATB2_HUMAN | ULD PF16534 58-155, CUTL PF16557 162-234, CUT PF02376 360-435 482-557, Homeodomain PF00046 615-671 | Satb2 | 2679336 | Q8VI24 | SATB2_MOUSE | CUT | Homeoboxes / CUT class | Chromatin remodeling cofactor | # | 18255031 | # | chromatin | # | # | # | Cromatin remodeling in mouse. UniProt: Acts as a docking site for several chromatin remodeling enzymes and also by recruiting corepressors (HDACs) or coactivators (HATs) directly to promoters and enhancers. | # |
SCMH1
(details) |
19003 | sex comb on midleg homolog 1 (Drosophila) | 22955 | Q96GD3 | SCMH1_HUMAN | MBT PF02820 62-129 171-236, RBR PF17208 269-333, SLED PF12140 357-471, SAM_1 PF00536 592-656 | Scmh1 | 1352762 | Q8K214 | SCMH1_MOUSE | SAMD | Sterile alpha motif (SAM) domain containing | Polycomb group (PcG) protein | # | 23356856 | PRC1 | # | # | # | 23356856 | SCMH1 is part of a polycomb group complex 1 (PcG1) involved in transcriptional silencing and proteosomal degradation for the Geminin protein, important for regulation of replication and maintenance of undifferentiated states. | # |
SCML2
(details) |
10581 | sex comb on midleg-like 2 (Drosophila) | 10389 | Q9UQR0 | SCML2_HUMAN | MBT PF02820 67-134 176-241, RBR PF17208 281-321, SLED PF12140 355-464, SAM_1 PF00536 628-695 | # | # | # | # | SAMD | Sterile alpha motif (SAM) domain containing | Polycomb group (PcG) protein | # | 24727478 | PRC1 | # | # | # | 24727478 | Scml2 is a member of the Polycomb group of proteins involved in epigenetic gene silencing. Human Scml2 is a part of a multisubunit protein complex, PRC1 (Polycomb repressive complex 1), which is responsible for maintenance of gene repression, prevention of chromatin remodeling, preservation of the "stemness" of the cell, and cell differentiation. | # |
SCML4
(details) |
21397 | sex comb on midleg-like 4 (Drosophila) | 256380 | Q8N228 | SCML4_HUMAN | RBR PF17208 1-61, SLED PF12140 96-207, SAM_1 PF00536 343-410 | Scml4 | 2446140 | Q80VG1 | SCML4_MOUSE | SAMD | Sterile alpha motif (SAM) domain containing | Polycomb group (PcG) protein | # | # | # | # | # | # | # | Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. (Annotated by similarity.) | # |
SENP1
(details) |
17927 | SUMO1/sentrin specific peptidase 1 | 29843 | Q9P0U3 | SENP1_HUMAN | Peptidase_C48 PF02902 464-638 | Senp1 | 2445054 | P59110 | SENP1_MOUSE | # | # | Histone modification erase cofactor | Histone sumoylation | 15199155 | # | histone | H4 | # | 15199155 | SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1. | # |
SENP3
(details) |
17862 | SUMO1/sentrin/SMT3 specific peptidase 3 | 26168 | Q9H4L4 | SENP3_HUMAN | SENP3_5_N PF19722 306-387, Peptidase_C48 PF02902 400-570 | Senp3 | 2158736 | Q9EP97 | SENP3_MOUSE | # | # | Histone modification erase, Histone modification write cofactor | Histone sumoylation, Histone acetylation | # | CHD8, MLL2/3, MLL4/WBP7 | histone | H3 | H3ac | 18850004 | Facultative member of the MLL1/MLL complex (UniProt). | # |
SET
(details) |
10760 | SET nuclear proto-oncogene | 6418 | Q01105 | SET_HUMAN | NAP PF00956 92-234 | Set | 1860267 | Q9EQU5 | SET_MOUSE | # | # | Histone modification | # | 17320507 | # | histone | # | # | # | Classified as histone-modifying enzymes in paper. | # |
SETD1A
(details) |
29010 | SET domain containing 1A | 9739 | O15047 | SET1A_HUMAN | RRM_1 PF00076 97-166, N-SET PF11764 1419-1559, SET PF00856 1580-1685 | Setd1a | 2446244 | # | # | KMT, RBM | Chromatin-modifying enzymes / K-methyltransferases, RNA binding motif (RRM) containing | Histone modification write | Histone methylation | 17355966 | COMPASS | histone | H3K4 | H3K4me | 17355966 | The CFP1 complex contains human homologues of the COMPASS complex, including Set1A=SETD1A, Wdr5, Ash2, Rbbp5, and Wdr82 (previously denoted hSwd2). The human Set1A-CFP1 complex exhibits histone H3-Lys4 methyltransferase activity in vitro. | # |
SETD1B
(details) |
29187 | SET domain containing 1B | 23067 | Q9UPS6 | SET1B_HUMAN | RRM_1 PF00076 104-175, N-SET PF11764 1676-1821, SET PF00856 1839-1944 | Setd1b | 2652820 | Q8CFT2 | SET1B_MOUSE | KMT, RBM | Chromatin-modifying enzymes / K-methyltransferases, RNA binding motif (RRM) containing | Histone modification write | Histone methylation | 17355966 | COMPASS | histone | H3K4 | H3K4me | 17355966 | The extensive homology between Set1A and Set1B=SETD1B, particularly throughout the SET domain, suggests that Set1B functions as a histone methyltransferase. | # |
SETD2
(details) |
18420 | SET domain containing 2 | 29072 | Q9BYW2 | SETD2_HUMAN | AWS PF17907 1513-1547, SET PF00856 1561-1667, WW PF00397 2391-2421, SRI PF08236 2471-2552 | Setd2 | 1918177 | E9Q5F9 | SETD2_MOUSE | KMT | Chromatin-modifying enzymes / K-methyltransferases | Histone modification write | Histone methylation | 16118227 | # | histone | H3K36me2 | H3K36me3 | 16118227 | HYPB HMTase=SETD2 may coordinate histone methylation and transcriptional regulation in mammals. | # |
SETD3
(details) |
20493 | SET domain containing 3 | 84193 | Q86TU7 | SETD3_HUMAN | SET PF00856 105-314, Rubis-subs-bind PF09273 345-475 | Setd3 | 1289184 | Q91WC0 | SETD3_MOUSE | # | # | Histone modification write | Histone methylation | # | # | histone | H3K36 | H3K36me | # | Histone methyltransferase that methylates 'Lys-36' of histone H3 (H3K36me). H3 'Lys-36' methylation represents a specific tag for epigenetic transcriptional activation. (Annotated by similarity.) | # |
SETD5
(details) |
25566 | SET domain containing 5 | 55209 | Q9C0A6 | SETD5_HUMAN | SET PF00856 285-389 | Setd5 | 1920145 | Q5XJV7 | SETD5_MOUSE | # | # | Histone modification write | Histone methylation | 24680889 | # | histone | # | # | 24680889 | Encoding methyltransferases regulating histone modification. | # |
SETD6
(details) |
26116 | SET domain containing 6 | 79918 | Q8TBK2 | SETD6_HUMAN | SET PF00856 75-286, Rubis-subs-bind PF09273 328-465 | Setd6 | 1913333 | Q9CWY3 | SETD6_MOUSE | # | # | Chromatin remodeling, Histone modification write | Histone methylation | 21131967 | # | histone | # | # | 21131967 | SETD6 monomethylation of nuclear RelA at K310 attenuates NF-κB signaling by docking GLP (via its ankyrin repeats) at target genes to generate a silent chromatin state, effectively rendering chromatin-bound RelA inert. As deregulation of NF-κB is linked to pathologic inflammatory processes and cancer8 and SETD6 inhibits NF-κB signaling in diverse cell types, including primary human cells, SETD6 may provide a new link by which protein lysine methylation and chromatin regulation influence tumor suppression and anti-inflammatory respons. | # |
SETD7
(details) |
30412 | SET domain containing (lysine methyltransferase) 7 | 80854 | Q8WTS6 | SETD7_HUMAN | MORN PF02493 19-34 36-58 60-81, domain PF22648 110-184, SET PF00856 227-336 | Setd7 | 1920501 | Q8VHL1 | SETD7_MOUSE | KMT | Chromatin-modifying enzymes / K-methyltransferases | Histone modification write | Histone methylation | 11779497 | # | histone | H3K4 | H3K4me1 | 11779497 | SET7 methylates H3-K4 in vitro and in vivo. In addition, methylation of H3-K4 and H3-K9 inhibit each other. Furthermore, H3-K4 and H3-K9 methylation by SET7 and SUV39H1, respectively, have differential effects on subsequent histone acetylation by p300. May explain differential effects of H3-K4 and H3-K9 methylation on transcription. | # |
SETD8
(details) |
29489 | SET domain containing (lysine methyltransferase) 8 | 387893 | Q9NQR1 | SETD8_HUMAN | SET PF00856 268-378 | Setd8 | 1915206 | Q2YDW7 | SETD8_MOUSE | KMT | Chromatin-modifying enzymes / K-methyltransferases | Histone modification write | Histone methylation | 12086618 | # | histone | H4K20 | H4K20me1 | 12086618 | The encoding gene PR/SET07 =SETD8 of a human histone H4 lysine 20 methyltransferase. | # |
SETDB1
(details) |
10761 | SET domain, bifurcated 1 | 9869 | Q15047 | SETB1_HUMAN | DUF5604 PF18300 193-250, Tudor_5 PF18359 258-311, Tudor_4 PF18358 348-398, MBD PF01429 596-667, Pre-SET PF05033 683-798, SET PF00856 1199-1266 | Setdb1 | 1934229 | O88974 | SETB1_MOUSE | KMT, TDRD | Chromatin-modifying enzymes / K-methyltransferases, Tudor domain containing | Histone modification write | Histone methylation | 11959841 | # | histone | H3K9 | H3K9me3 | 11959841 | In vitro methylation of the N-terminal tail of histone H3 by SETDB1 is sufficient to enhance the binding of HP1 proteins, which requires both an intact chromodomain and chromoshadow domain. | # |
SETDB2
(details) |
20263 | SET domain, bifurcated 2 | 83852 | Q96T68 | SETB2_HUMAN | MBD PF01429 163-229, Pre-SET PF05033 247-359, SET PF00856 623-694 | Setdb2 | 2685139 | Q8C267 | SETB2_MOUSE | KMT | Chromatin-modifying enzymes / K-methyltransferases | Histone modification write | Histone methylation | 20404330 | # | histone | H3K9 | H3K9me3 | 20404330 | A member of the histone H3K9 methyltransferase family named CLLD8 (or SETDB2 or KMT1F). | # |
SETMAR
(details) |
10762 | SET domain and mariner transposase fusion gene | 6419 | Q53H47 | SETMR_HUMAN | Pre-SET PF05033 28-132, SET PF00856 148-263, HTH_48 PF17906 346-392, Transposase_1 PF01359 502-581 | Setmar | 1921979 | Q80UJ9 | SETMR_MOUSE | # | # | Histone modification write | Histone methylation | 16332963 | # | histone | H3K4, H3K36 | H3K4me, H3K36me | 16332963 | Metnase =SETMAR that has a SET domain and a transposase/nuclease domain. Metnase methylates histone H3 lysines 4 and 36, which are associated with open chromatin. Metnase increases resistance to ionizing radiation and increases nonhomologous end-joining repair of DNA doublestrand breaks. | # |
SF3B1
(details) |
10768 | splicing factor 3b, subunit 1, 155kDa | 23451 | O75533 | SF3B1_HUMAN | SF3b1 PF08920 327-453, domain PF22646 1086-1158 | Sf3b1 | 1932339 | Q99NB9 | SF3B1_MOUSE | # | # | RNA modification | # | 23568491 | B-WICH | RNA | # | # | 23568491 | Although the causative link between SF3B1 mutation and CLL pathogenesis remains unclear, several lines of evidence suggest SF3B1 mutation might be linked to genomic stability and epigenetic modification. | # |
SF3B3
(details) |
10770 | splicing factor 3b, subunit 3, 130kDa | 23450 | Q15393 | SF3B3_HUMAN | MMS1_N PF10433 77-591, CPSF_A PF03178 863-1180 | Sf3b3 | 1289341 | Q921M3 | SF3B3_MOUSE | # | # | RNA modification | # | 17643112 | # | RNA | # | # | 17643112 | # | # |
SFMBT1
(details) |
20255 | Scm-like with four mbt domains 1 | 51460 | Q9UHJ3 | SMBT1_HUMAN | MBT PF02820 54-121 166-234 279-351 388-454, SLED PF12140 501-616, SAM_1 PF00536 793-857 | Sfmbt1 | 1859609 | Q9JMD1 | SMBT1_MOUSE | # | # | Polycomb group (PcG) protein | # | 21423274 | SCL | histone | H4K20 | # | 21423274 | Table 1 in the reference. | # |
SFMBT2
(details) |
20256 | Scm-like with four mbt domains 2 | 57713 | Q5VUG0 | SMBT2_HUMAN | MBT PF02820 78-146 191-258 301-375 411-478, SLED PF12140 529-642, SAM_1 PF00536 823-885 | Sfmbt2 | 2447794 | Q5DTW2 | SMBT2_MOUSE | SAMD | Sterile alpha motif (SAM) domain containing | Histone modification read, Polycomb group (PcG) protein, TF | TF repressor | 23385818 | # | histone, DNA | H3K9me2, H3K9me3, H3K27me3, H4K20me2, H4K20me3 | H3, H4 | 23385818 | SFMBT2 binds preferentially to methylated histone H3 and H4 that are associated with transcriptional repression. Occupancy of SFMBT2 coincide with enrichment of diand tri-methylated H3K9 and H4K20 as well as tri-methylated H3K27 at the HOXB13 gene promoter. | # |
SFPQ
(details) |
10774 | splicing factor proline/glutamine-rich | 6421 | P23246 | SFPQ_HUMAN | RRM_1 PF00076 299-363 374-432, NOPS PF08075 444-496 | Sfpq | 1918764 | Q8VIJ6 | SFPQ_MOUSE | RBM | RNA binding motif (RRM) containing | Chromatin remodeling cofactor, RNA modification, TF | TF repressor | 22783022, 10858305, 8449401 | # | DNA, RNA | # | # | 22783022, 10858305, 8449401 | Four components of the Sin3a transcriptional repressor complex: SAP130, SUDS3, SFPQ, and TGIF2. Since the RNA splicing factors do not have an endogenous DNA relaxation activity, topoisomerase I (Chromatin remodeller) gets stimulated by the interaction with the PSF= SFPQ/p54nrb heterodimer. PSF=SFPQ is an essential pre-mRNA splicing factor required early in spliceosome formation. | # |
SFSWAP
(details) |
10790 | Splicing factor, suppressor of white-apricot homolog (Splicing factor, arginine/serine-rich 8) (Suppressor of white apricot protein homolog) | 6433 | Q12872 | SFSWA_HUMAN | DRY_EERY PF09750 34-153, Surp PF01805 210-255 458-502 | Sfswap | 101760 | Q3USH5 | SFSWA_MOUSE | # | # | RNA modification | Alternative splicing | 8940107 | # | RNA | mRNA | # | 8940107 | Regulates its own splicing, and also the splicing of fibronectin and CD45. Represses the splicing of MAPT/Tau exon 10 | New |
SHPRH
(details) |
19336 | SNF2 histone linker PHD RING helicase, E3 ubiquitin protein ligase | 257218 | Q149N8 | SHPRH_HUMAN | SNF2-rel_dom PF00176 307-985, Linker_histone PF00538 440-512, SHPRH_helical-1st PF21325 1003-1099, SHPRH_helical-2nd PF21324 1135-1361, zf-RING_UBOX PF13445 1432-1478, Helicase_C PF00271 1514-1622 | Shprh | 1917581 | Q7TPQ3 | SHPRH_MOUSE | RNF | RING-type (C3HC4) zinc fingers | Histone modification write cofactor | Histone ubiquitination | 17130289 | # | histone | # | # | 17130289 | SHPRH associates with PCNA, RAD18, and the ubiquitin-conjugating enzyme UBC13 (E2) and promotes methyl methanesulfonate (MMS)-induced PCNA polyubiquitination. | # |
SIN3A
(details) |
19353 | SIN3 transcription regulator family member A | 25942 | Q96ST3 | SIN3A_HUMAN | PAH PF02671 142-186 323-380 478-522, Sin3_corepress PF08295 551-647, Sin3a_C PF16879 885-1192 | Sin3a | 107157 | Q60520 | SIN3A_MOUSE | # | # | Histone modification erase cofactor, TF | Histone acetylation, TF activator, TF repressor | 12670868 | SWI/SNF_Brg1(I), SWI/SNF_Brm, mSin3A, mSin3A-like complex | histone, DNA | DNA motif | # | 12670868 | Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1. | # |
SIN3B
(details) |
19354 | SIN3 transcription regulator family member B | 23309 | O75182 | SIN3B_HUMAN | PAH PF02671 60-104 182-235 322-366, Sin3_corepress PF08295 394-447 435-521, Sin3a_C PF16879 775-1081 | Sin3b | 107158 | Q62141 | SIN3B_MOUSE | # | # | Histone modification erase cofactor, TF | Histone acetylation, TF repressor | 12670868 | mSin3A | histone, DNA | DNA motif | # | 12670868 | Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1. | # |
SIRT1
(details) |
14929 | sirtuin 1 | 23411 | Q96EB6 | SIR1_HUMAN | SIR2 PF02146 261-447 | Sirt1 | 2135607 | Q923E4 | SIR1_MOUSE | # | # | Histone modification erase, Histone modification write cofactor | Histone acetylation, Histone methylation | 15469825 | eNoSc | histone | H1K26ac, H3K9ac, H4K16ac | H1K26, H3K9, H4K16 | 15469825 | SirT1 deacetylates histone polypeptides with a preference for histone H4 lysine 16 (H4-K16Ac) and H3 lysine 9 (H3-K9Ac) in vitro. | # |
SIRT2
(details) |
10886 | sirtuin 2 | 22933 | Q8IXJ6 | SIR2_HUMAN | SIR2 PF02146 84-268 | Sirt2 | 1927664 | Q8VDQ8 | SIR2_MOUSE | # | # | Histone modification erase, Histone modification write cofactor | Histone acetylation, Histone methylation | 11427894 | # | histone | H3K18ac, H3K56ac, H4K16ac, H4K20me1 | H3K18, H3K56, H4K16, H4K20me2, H4K20me3 | 11427894 | Sir2 =SIRT2 is an NAD-dependent histone deacetylase that mediates transcriptional silencing at mating-type loci, telomeres and ribosomal gene clusters. | # |
SIRT6
(details) |
14934 | sirtuin 6 | 51548 | Q8N6T7 | SIR6_HUMAN | SIR2 PF02146 85-221 | Sirt6 | 1354161 | P59941 | SIR6_MOUSE | # | # | Histone modification erase | Histone acetylation | 18337721 | # | histone | H3K9ac, H3K56ac | H3K9, H3K56 | 18337721 | The human SIRT6 protein is an NAD+-dependent, histone H3 lysine 9 (H3K9) deacetylase that modulates telomeric chromatin. SIRT6 associates specifically with telomeres, and SIRT6 depletion leads to telomere dysfunction with end-to-end chromosomal fusions and premature cellular senescence. | # |
SIRT7
(details) |
14935 | sirtuin 7 | 51547 | Q9NRC8 | SIR7_HUMAN | SIR2 PF02146 140-273 | Sirt7 | 2385849 | Q8BKJ9 | SIR7_MOUSE | # | # | Histone modification erase | Histone acetylation | 22722849 | B-WICH | histone | H3K18ac | H3K18 | 22722849 | Genome-wide binding studies reveal that SIRT7 binds to promoters of a specific set of gene targets, where it deacetylates H3K18Ac and promotes transcriptional repression. | # |
SKP1
(details) |
10899 | S-phase kinase-associated protein 1 | 6500 | P63208 | SKP1_HUMAN | Skp1_POZ PF03931 3-68, Skp1 PF01466 113-160 | Akp1a | 103575 | Q9WTX5 | SKP1_MOUSE | # | # | Histone modification write cofactor | Histone ubiquitination | 16943429 | BCOR | histone | # | # | 16943429 | The proteins in the BCOR complex include the PcG and PcG-associated proteins NSPC1, RING1, RNF2, and RYBP as well as components of an SCF ubiquitin ligase, SKP1, and FBXL10. BCOR recruits a unique combination of enzymatic activities to chromatin targets: a PcG E3 ubiquitin ligase for histone H2A, a demethylase for histone H3 K36, and an SCF E3 ubiquitin ligase. | # |
SLU7
(details) |
16939 | Pre-mRNA-splicing factor SLU7 (hSlu7) | 10569 | O95391 | SLU7_HUMAN | Slu7 PF11708 160-432 | Slu7 | 2385598 | Q8BHJ9 | SLU7_MOUSE | # | # | RNA modification | Alternative splicing | 12764196 | # | RNA | mRNA | # | 12764196 | Regulates 3` splice site selection | New |
SMARCA1
(details) |
11097 | SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 | 6594 | P28370 | SMCA1_HUMAN | SNF2-rel_dom PF00176 186-465, Helicase_C PF00271 487-612, HAND PF09110 758-856, SLIDE PF09111 911-1028 | Smarca1 | 1935127 | Q6PGB8 | SMCA1_MOUSE | # | # | Chromatin remodeling, Histone modification erase | Histone acetylation | 15310751 | NuRF, CERF, CERF | chromatin | # | # | 15310751 | Mammalian genomes encode two imitation switch family chromatin remodeling proteins, SNF2H and SNF2L =SMARCA1. | # |
SMARCA2
(details) |
11098 | SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 | 6595 | P51531 | SMCA2_HUMAN | QLQ PF08880 174-208, HSA PF07529 438-508, BRK PF07533 591-633, SNF2-rel_dom PF00176 727-1021, Helicase_C PF00271 1051-1164, SnAC PF14619 1259-1326, Bromodomain PF00439 1421-1489 | Smarca2 | 99603 | Q6DIC0 | SMCA2_MOUSE | # | # | Histone modification read, TF | TF activator | 22464331 | BAF, nBAF, npBAF, WINAC, bBAF, SWI/SNF BRM-BRG1 | histone, DNA | H3, DNA motif | # | 22464331 | Fig. 5 in the reference. | # |
SMARCA4
(details) |
11100 | SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 | 6597 | P51532 | SMCA4_HUMAN | QLQ PF08880 172-205, HSA PF07529 461-532, BRK PF07533 612-653, SNF2-rel_dom PF00176 754-1051, Helicase_C PF00271 1081-1194, SnAC PF14619 1321-1388, Bromodomain PF00439 1477-1547 | Smarca4 | 88192 | Q3TKT4 | SMCA4_MOUSE | # | # | Histone modification read, TF | TF activator | 17582821 | BAF, nBAF, npBAF, PBAF, SWI/SNF_Brg1(I), SWI/SNF_Brg1(II), SWI/SNF_Brm, SWI/SNF-like_EPAFa, WINAC, SWI/SNF-like EPAFB, bBAF, SWI/SNF BRM-BRG1, CREST-BRG1 | histone | H3, H4 | # | 17582821 | The BRG1 =SMARCA4 bromodomain exhibits binding, albeit weak, to acetylated peptides that are derived from histones H3 and H4. | # |
SMARCA5
(details) |
11101 | SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5 | 8467 | O60264 | SMCA5_HUMAN | SNF2-rel_dom PF00176 183-462, Helicase_C PF00271 484-597, HAND PF09110 743-841, SLIDE PF09111 897-1011 | Smarca5 | 1935129 | Q91ZW3 | SMCA5_MOUSE | # | # | Chromatin remodeling | # | 10880450 | ACF, B-WICH, RSF, CHRAC, NoRC | chromatin | # | # | 10880450 | The DNA-binding properties of the p15–p17 complex are possibly relevant for incorporation of p15–p17 into chromatin, aided by the nucleosome remodeling activity of hSNF2H =SMARCA5 plus hACF1. | # |
SMARCAD1
(details) |
18398 | SWI/SNF-related, matrix-associated actin-dependent regulator of chromatin, subfamily a, containing DEAD/H box 1 | 56916 | Q9H4L7 | SMRCD_HUMAN | SNF2-rel_dom PF00176 500-786, Helicase_C PF00271 855-967 | Smarcad1 | 95453 | Q04692 | SMRCD_MOUSE | # | # | Chromatin remodeling | # | 22960744 | # | chromatin | # | # | 22960744 | The yeast Saccharomyces cerevisiae Fun30 protein and its human counterpart SMARCAD1, two ATP-dependent chromatin remodellers of the Snf2 ATPase family, are directly involved in the DSB response. | # |
SMARCAL1
(details) |
11102 | SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a-like 1 | 50485 | Q9NZC9 | SMAL1_HUMAN | HARP PF07443 245-304 344-397, SNF2-rel_dom PF00176 439-688, Helicase_C PF00271 714-822 | Smarcal1 | 1859183 | Q8BJL0 | SMAL1_MOUSE | # | # | Chromatin remodeling | # | 11799392 | # | chromatin | # | # | 11799392 | The unique constellation of findings constituting SIOD indicates that SMARCAL1 regulates the transcriptional activity of a particular subset of genes through chromatin remodeling during both development and later life. | # |
SMARCB1
(details) |
11103 | SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily b, member 1 | 6598 | Q12824 | SNF5_HUMAN | INI1_DNA-bd PF21459 12-104, SNF5 PF04855 180-373 | Smarcb1 | 1328366 | Q9Z0H3 | SNF5_MOUSE | # | # | Histone modification read | # | 21423274 | BAF, nBAF, npBAF, PBAF, SWI/SNF_Brg1(I), SWI/SNF_Brg1(II), SWI/SNF_Brm, SWI/SNF-like_EPAFa, WINAC, SWI/SNF-like EPAFB, bBAF, SWI/SNF BRM-BRG1 | histone | H3K56 | # | 21423274 | Table 1 in the reference (SMARCB1 =Snf5) | # |
SMARCC1
(details) |
11104 | SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 1 | 6599 | Q92922 | SMRC1_HUMAN | SWIRM-assoc_2 PF16496 31-165, SWIRM PF04433 459-537, Myb_DNA-binding PF00249 622-664, SWIRM-assoc_3 PF16498 705-772, SWIRM-assoc_1 PF16495 872-952 | Smarcc1 | 1203524 | P97496 | SMRC1_MOUSE | # | # | Chromatin remodeling cofactor | # | 10078207 | BAF, nBAF, npBAF, PBAF, SWI/SNF_Brg1(I), SWI/SNF_Brg1(II), SWI/SNF_Brm, SWI/SNF-like_EPAFa, WINAC, SWI/SNF-like EPAFB, bBAF, SWI/SNF BRM-BRG1 | chromatin | # | # | 10078207 | The addition of INI1, BAF155 =SMARCC1, and BAF170 to BRG1 increases remodeling activity to a level comparable to that of the whole hSWI/SNF complex. | # |
SMARCC2
(details) |
11105 | SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 2 | 6601 | Q8TAQ2 | SMRC2_HUMAN | SWIRM-assoc_2 PF16496 5-137, SWIRM PF04433 434-512, Myb_DNA-binding PF00249 600-642, SWIRM-assoc_3 PF16498 683-748, SWIRM-assoc_1 PF16495 864-945 | Smarcc2 | 1915344 | Q6PDG5 | SMRC2_MOUSE | # | # | Chromatin remodeling cofactor | # | 10078207 | BAF, nBAF, npBAF, PBAF, SWI/SNF_Brg1(I), SWI/SNF_Brg1(II), SWI/SNF_Brm, SWI/SNF-like_EPAFa, WINAC, SWI/SNF-like EPAFB, bBAF, SWI/SNF BRM-BRG1 | chromatin | # | # | 10078207 | The addition of INI1, BAF155, and BAF170 =SMARCC2 to BRG1 increases remodeling activity to a level comparable to that of the whole hSWI/SNF complex. | # |
SMARCD1
(details) |
11106 | SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 1 | 6602 | Q96GM5 | SMRD1_HUMAN | SWIB PF02201 294-364 | Smarcd1 | 1933623 | Q61466 | SMRD1_MOUSE | # | # | Chromatin remodeling | # | 12917342 | BAF, nBAF, npBAF, PBAF, SWI/SNF_Brg1(I), SWI/SNF_Brm, SWI/SNF-like_EPAFa, WINAC, SWI/SNF-like EPAFB, SWI/SNF BRM-BRG1 | chromatin | # | # | 12917342 | BAF60a =SMARCD1 possesses at least two interaction surfaces, one for GR and BRG1 and a second for BAF155 and BAF170. A GR mutant, GR(R488Q), that fails to interact with BAF60a=SMARCD1 in vitro has reduced chromatin-remodeling activity and reduced transcriptional activity from the promoter assembled as chromatin in vivo. | # |
SMARCD2
(details) |
11107 | SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 2 | 6603 | Q92925 | SMRD2_HUMAN | SWIB PF02201 310-379 | Smarcd2 | 1933621 | Q99JR8 | SMRD2_MOUSE | # | # | Chromatin remodeling cofactor | # | 20148946 | BAF, PBAF, SWI/SNF_Brg1(I), SWI/SNF_Brm, SWI/SNF-like EPAFB, bBAF, SWI/SNF BRM-BRG1 | chromatin | # | # | 20148946 | The SWI/SNF chromatin remodeling complexes are important regulators of transcription; they consist of large multisubunit assemblies containing either Brm or Brg1 as the catalytic ATPase subunit and a variable subset of approximately 10 Brg/Brm-associated factors (BAF). Among these factors, BAF60 proteins (BAF60a, BAF60b=SMARCD2 or BAF60c), which are found in most complexes, are thought to bridge interactions between transcription factors and SWI/SNF complexes. | # |
SMARCD3
(details) |
11108 | SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 3 | 6604 | Q6STE5 | SMRD3_HUMAN | SWIB PF02201 262-333 | Smarcd3 | 1914243 | Q6P9Z1 | SMRD3_MOUSE | # | # | Chromatin remodeling cofactor | # | 20148946 | BAF, nBAF, npBAF, PBAF, SWI/SNF_Brg1(I), SWI/SNF_Brm, SWI/SNF BRM-BRG1 | chromatin | # | # | 20148946 | The SWI/SNF chromatin remodeling complexes are important regulators of transcription; they consist of large multisubunit assemblies containing either Brm or Brg1 as the catalytic ATPase subunit and a variable subset of approximately 10 Brg/Brm-associated factors (BAF). Among these factors, BAF60 proteins (BAF60a, BAF60b or BAF60c=SMARCD3), which are found in most complexes, are thought to bridge interactions between transcription factors and SWI/SNF complexes. | # |
SMARCE1
(details) |
11109 | SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily e, member 1 | 6605 | Q969G3 | SMCE1_HUMAN | HMG_box PF00505 66-134 | Smarce1 | 1927347 | O54941 | SMCE1_MOUSE | # | # | Chromatin remodeling cofactor | # | 12672490 | BAF, nBAF, npBAF, PBAF, SWI/SNF_Brg1(I), SWI/SNF_Brg1(II), SWI/SNF_Brm, SWI/SNF-like_EPAFa, WINAC, SWI/SNF-like EPAFB, bBAF | chromatin | # | # | 12672490 | In addition to Swi2/Snf2 proteins, there is evidence that other core components are required for chromatin-remodeling activity. More recently, two additional human Swi/Snf members, BAF57 =SMARCE1 and BAF60a, have been shown to interact directly with regulatory proteins. | # |
SMEK1
(details) |
20219 | SMEK homolog 1, suppressor of mek1 (Dictyostelium) | 55671 | Q6IN85 | P4R3A_HUMAN | domain PF22972 5-101, PP4R3 PF04802 141-645 | Smek1 | 1915984 | Q6P2K6 | P4R3A_MOUSE | # | # | Histone modification erase cofactor | Histone phosphorylation | 18614045 | PPP4C-PPP4R2-PPP4R3A | histone | H2AFX | # | # | Member of PPP4C-PPP4R2-PPP4R3A PP4 complex which specifically dephosphorylates H2AFX phosphorylated on 'Ser-140' (gamma-H2AFX). | # |
SMEK2
(details) |
29267 | SMEK homolog 2, suppressor of mek1 (Dictyostelium) | 57223 | Q5MIZ7 | P4R3B_HUMAN | domain PF22972 5-101, PP4R3 PF04802 144-682 | Smek2 | 2144474 | Q922R5 | P4R3B_MOUSE | # | # | Histone modification erase cofactor | Histone phosphorylation | 18614045 | # | histone | H2AFX | # | # | Member of PPP4C-PPP4R2-PPP4R3B complex which dephosphorylates H2AFX. | # |
SMYD1
(details) |
20986 | SET and MYND domain containing 1 | 150572 | Q8NB12 | SMYD1_HUMAN | SET PF00856 18-252, zf-MYND PF01753 52-90 | Smyd1 | 104790 | P97443 | SMYD1_MOUSE | ZMYND, KMT | Zinc fingers, MYND-type, "Chromatin-modifying enzymes / K-methyltransferases" | Histone modification write | Histone methylation | 22498752 | # | histone | H3K4 | H3K4me | # | SMYD1 methylates histone H3 at Lys-4 (H3K4me), according to UniProt. | # |
SMYD2
(details) |
20982 | SET and MYND domain containing 2 | 56950 | Q9NRG4 | SMYD2_HUMAN | SET PF00856 18-240, zf-MYND PF01753 52-90 | Smyd2 | 1915889 | Q8R5A0 | SMYD2_MOUSE | ZMYND, KMT | Zinc fingers, MYND-type, Chromatin-modifying enzymes / K-methyltransferases | Histone modification write | Histone methylation | 18065756 | # | histone | H3K4, H3K36 | H3K4me, H3K36me2 | 18065756 | Some reports indicate that SMYD2 methylates p53 and histone H3. | # |
SMYD3
(details) |
15513 | SET and MYND domain containing 3 | 64754 | Q9H7B4 | SMYD3_HUMAN | SET PF00856 15-239, zf-MYND PF01753 49-87 | Smyd3 | 1916976 | Q9CWR2 | SMYD3_MOUSE | ZMYND, KMT | Zinc fingers, MYND-type, Chromatin-modifying enzymes / K-methyltransferases | Histone modification write | Histone methylation | 15235609 | # | histone | H3K4, H3K5 | H3K4me2, H3K4me3, H3K5me2, H3K5me3 | 15235609 | The SET domain of SMYD3 shows histone H3-lysine 4 (H3-K4)-specific methyltransferase activity, which is enhanced in the presence of the heat-shock protein HSP90A. | # |
SMYD4
(details) |
21067 | SET and MYND domain containing 4 | 114826 | Q8IYR2 | SMYD4_HUMAN | SET PF00856 244-574, zf-MYND PF01753 296-335 | Smyd4 | 2442796 | Q8BTK5 | SMYD4_MOUSE | ZMYND | Zinc fingers, MYND-type | Histone modification erase cofactor | Histone acetylation | 18714374 | # | # | # | # | # | SMYD4 interacts with HDAC1 and HDAC3. | # |
SNAI2
(details) |
11094 | snail family zinc finger 2 | 6591 | O43623 | SNAI2_HUMAN | zf-C2H2 PF00096 128-150 159-181 185-207 213-235 241-260 | Snai2 | 1096393 | P97469 | SNAI2_MOUSE | SNAI, ZNF | Snail homologs, Zinc fingers, C2H2-type | Histone modification erase cofactor | # | 15734731, 22986495 | # | histone | # | # | # | May recruit HDAC1. PHD12 interacts directly with Sin3A/HDAC, which in turn interacts with Snail2. | # |
SP1
(details) |
11205 | Sp1 transcription factor | # | P08047 | SP1_HUMAN | zf-C2H2 PF00096 656-680 686-708 | Sp1 | 98372 | O89090 | SP1_MOUSE | SP, ZNF | Specificity protein transcription factors, Zinc fingers, C2H2-type | Chromatin remodeling, TF | TF activator, TF repressor | 17827154, 18850004 | CREST-BRG1 | DNA | DNA motif | # | 17049555 | # | # |
SP100
(details) |
11206 | SP100 nuclear antigen | 6672 | P23497 | SP100_HUMAN | HSR PF03172 37-146, SAND PF01342 600-678, HMG_box_2 PF09011 697-752, HMG_box PF00505 769-837 | Sp100 | 109561 | O35892 | SP100_MOUSE | PHF | Zinc fingers, PHD-type | Chromatin remodeling cofactor | # | 9636146 | # | chromatin | # | # | 9636146 | There is an association between the PML/SP100 NBs and the chromatin nuclear compartment. This supports a model in which the NBs may play a role in certain aspects of chromatin dynamics. | # |
SP140
(details) |
17133 | SP140 nuclear body protein | 11262 | Q13342 | SP140_HUMAN | HSR PF03172 38-135, SAND PF01342 583-661, PHD PF00628 693-733, Bromodomain PF00439 779-833 | Sp140 | 3702467 | # | # | PHF | Zinc fingers, PHD-type | Histone modification read, TF | # | 22464331 | # | histone | H3 | # | 22464331 | Fig. 5 in the reference. | # |
SPEN
(details) |
17575 | spen family transcriptional repressor | 23013 | Q96T58 | MINT_HUMAN | RRM_1 PF00076 8-67 337-407 439-508 519-583, MINT_MID PF20809 2012-3467, MINT_RID PF20810 2366-2584 3009-3469, MINT_RAM7 PF20808 2654-2749, SPOC PF07744 3506-3662 | Spen | 1891706 | Q62504 | MINT_MOUSE | RBM | RNA binding motif (RRM) containing | Histone modification erase cofactor, TF | Histone acetylation, TF activator, TF repressor | 11331609 | # | histone | # | # | 11331609 | SHARP =SPEN recruits histone deacetylase activity. SHARP is a potent transcriptional repressor whose repression domain (RD) interacts directly with SMRT and at least five members of the NuRD complex including HDAC1 and HDAC2. | # |
SPOP
(details) |
11254 | speckle-type POZ protein | 8405 | O43791 | SPOP_HUMAN | domain PF22486 33-161, BTB PF00651 191-296 | Spop | 1343085 | Q6ZWS8 | SPOP_MOUSE | BTBD | BTB/POZ domain containing | Histone modification write | Histone ubiquitination | 15897469 | # | histone | MacroH2A1 | MacroH2A1ub | 15897469 | The E3 ubiquitin ligase consisting of SPOP and CULLIN3 is able to ubiquitinate the Polycomb group protein BMI1 and the variant histone MACROH2A. | # |
SRCAP
(details) |
16974 | Snf2-related CREBBP activator protein | 10847 | Q6ZRS2 | SRCAP_HUMAN | HSA PF07529 125-195, SNF2-rel_dom PF00176 621-906, Helicase_C PF00271 2044-2156 | Srcap | 2444036 | # | # | # | # | Chromatin remodeling, Histone modification erase | Histone acetylation | 17617668 | NuA4-related complex, SRCAP | histone | H2A.Z | # | 17617668 | The chromatin remodeling protein, SRCAP, is critical for deposition of the histone variant H2A.Z at promoters. | # |
SRRM4
(details) |
29389 | Serine/arginine repetitive matrix protein 4 (Medulloblastoma antigen MU-MB-2.76) (Neural-specific serine/arginine repetitive splicing factor of 100 kDa) (Neural-specific SR-related protein of 100 kDa) (nSR100) | 84530 | A7MD48 | SRRM4_HUMAN | SRRM_C PF15230 459-521 | Srrm4 | 1916205 | Q8BKA3 | SRRM4_MOUSE | # | # | RNA modification | Alternative splicing | 29961578 | # | RNA | mRNA | # | 29961578 | Regulates alternative splicing events in genes with important neuronal functions | New |
SRSF1
(details) |
10780 | serine/arginine-rich splicing factor 1 | 6426 | Q07955 | SRSF1_HUMAN | RRM_1 PF00076 18-85 123-184 | Srsf1 | 98283 | Q6PDM2 | SRSF1_MOUSE | SRSF, RBM | Serine/arginine-rich splicing factors, RNA binding motif (RRM) containing | RNA modification | # | 24706538 | # | RNA | # | # | 24706538 | H3S10 phosphorylation has been shown to promote the recruitment of per-mRNA-splicing factor SRp20 and alternative-splicing factor (ASF)/per-mRNAsplicing factor 2 (SF2) modular proteins to the chromosomes. | # |
SRSF10
(details) |
16713 | Serine/arginine-rich splicing factor 10 (40 kDa SR-repressor protein) (SRrp40) (FUS-interacting serine-arginine-rich protein 1) (Splicing factor SRp38) (Splicing factor, arginine/serine-rich 13A) (TLS-associated protein with Ser-Arg repeats) (TASR) (TLS-associated protein with SR repeats) (TLS-associated serine-arginine protein) (TLS-associated SR protein) | 10772 | O75494 | SRS10_HUMAN | RRM_1 PF00076 12-81 | Srsf10 | 1333805 | Q9R0U0 | SRS10_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 11684676 | # | RNA | mRNA | # | 11684676 | Regulates alternative splicing sites of E1A | New |
SRSF12
(details) |
21220 | Serine/arginine-rich splicing factor 12 (35 kDa SR repressor protein) (SRrp35) (Splicing factor, arginine/serine-rich 13B) (Splicing factor, arginine/serine-rich 19) | 135295 | Q8WXF0 | SRS12_HUMAN | RRM_1 PF00076 12-81 | Srsf12 | 2661424 | Q8C8K3 | SRS12_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 11684676 | # | RNA | mRNA | # | 11684676 | Regulates alternative splicing sites of E1A | New |
SRSF3
(details) |
10785 | serine/arginine-rich splicing factor 3 | 6428 | P84103 | SRSF3_HUMAN | RRM_1 PF00076 12-77 | Srsf3 | 98285 | P84104 | SRSF3_MOUSE | SRSF, RBM | Serine/arginine-rich splicing factors, RNA binding motif (RRM) containing | RNA modification | # | 24706538 | # | RNA | # | # | 24706538 | H3S10 phosphorylation has been shown to promote the recruitment of per-mRNA-splicing factor SRp20 and alternative-splicing factor (ASF)/per-mRNAsplicing factor 2 (SF2) modular proteins to the chromosomes. | # |
SRSF6
(details) |
10788 | Serine/arginine-rich splicing factor 6 (Pre-mRNA-splicing factor SRP55) (Splicing factor, arginine/serine-rich 6) | 6431 | Q13247 | SRSF6_HUMAN | RRM_1 PF00076 4-64 112-177 | Srsf6 | 1915246 | Q3TWW8 | SRSF6_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 22767602 | # | RNA | mRNA | # | 22767602 | Promotes Tau exon 10 inclusion | New |
SS18L1
(details) |
15592 | synovial sarcoma translocation gene on chromosome 18-like 1 | 26039 | O75177 | CREST_HUMAN | SSXT PF05030 12-73 | Ss18l1 | 2444061 | Q8BW22 | CREST_MOUSE | # | # | Chromatin remodeling | # | 23799466 | CREST-BRG1 | chromatin | # | # | 23799466 | - | # |
SS18L2
(details) |
15593 | synovial sarcoma translocation gene on chromosome 18-like 2 | 51188 | Q9UHA2 | S18L2_HUMAN | SSXT PF05030 12-73 | Deb1 | 1349474 | Q9D174 | S18L2_MOUSE | # | # | Chromatin remodeling | # | 19163965, 8666667 | # | chromatin | # | # | 15986999 | # | # |
SSRP1
(details) |
11327 | structure specific recognition protein 1 | 6749 | Q08945 | SSRP1_HUMAN | POB3_N PF17292 3-96, SSrecog PF03531 105-170, PH1_SSRP1-like PF21103 197-327, Rttp106-like_middle PF08512 340-427, HMG_box PF00505 547-615, SSRP1_C PF21092 663-709 | Ssrp1 | 107912 | Q08943 | SSRP1_MOUSE | # | # | Chromatin remodeling | # | 12934006 | FACT | histone | H3, H4 | # | 12934006 | Both FACT and Spt16 can bind to nucleosomes and H2A-H2B dimers, whereas SSRP1 can only bind to H3-H4 tetramers but not to intact nucleosomes. Possibly, upon FACT binding to the nucleosome in the transcribed region, Spt16 facilitates the H2A-H2B displacement, which promotes the interaction between SSRP1 and the “altered” nucleosome. | # |
STK4
(details) |
11408 | serine/threonine kinase 4 | 6789 | Q13043 | STK4_HUMAN | Pkinase PF00069 31-281, Mst1_SARAH PF11629 433-480 | Stk4 | 1929004 | Q9JI11 | STK4_MOUSE | # | # | Histone modification write | Histone phosphorylation | 12757711 | # | histone | H2AS14 | H2BS14ph | 12757711 | Mst1 =STK4 can phosphorylate H2B at S14 in vitro and in vivo, and the onset of H2B S14 phosphorylation is dependent upon cleavage of Mst1 by caspase-3. | # |
SUDS3
(details) |
29545 | suppressor of defective silencing 3 homolog (S. cerevisiae) | 64426 | Q9H7L9 | SDS3_HUMAN | Sds3 PF08598 61-186 | Suds3 | 1919204 | Q8BR65 | SDS3_MOUSE | # | # | Histone modification erase cofactor | Histone acetylation | 21239494 | mSin3A | histone | # | # | 21239494 | SDS3 is a key component of the histone deacetylase (HDAC)-dependent Sin3A co-repressor complex, serving to maintain its HDAC activity. | # |
SUPT16H
(details) |
11465 | suppressor of Ty 16 homolog (S. cerevisiae) | 11198 | Q9Y5B9 | SP16H_HUMAN | FACT-Spt16_Nlob PF14826 5-167, Peptidase_M24 PF00557 182-411, SPT16 PF08644 529-689, Rttp106-like_middle PF08512 809-895, SPT16_C PF21091 929-1031 | Supt16 | 1890948 | Q920B9 | SP16H_MOUSE | # | # | Histone modification read | # | 12934006 | WINAC, FACT | histone | H2A, H2B | # | 12934006 | Both FACT and Spt16=SUPT16H can bind to nucleosomes and H2A-H2B dimers, whereas SSRP1 can only bind to H3-H4 tetramers but not to intact nucleosomes. Possibly, upon FACT binding to the nucleosome in the transcribed region, Spt16 facilitates the H2A-H2B displacement, which promotes the interaction between SSRP1 and the “altered” nucleosome. | # |
SUPT3H
(details) |
11466 | suppressor of Ty 3 homolog (S. cerevisiae) | 8464 | O75486 | SUPT3_HUMAN | TFIID-18kDa PF02269 26-115 | # | # | # | # | # | # | Histone modification write cofactor | Histone acetylation | 11564863 | PCAF, SAGA, STAGA | histone | # | # | 11564863 | GCN5 is a histone acetyltransferase (HAT) originally identified in Saccharomyces cerevisiae and required for transcription of specific genes within chromatin as part of the SAGA (SPT-ADA-GCN5 acetylase) coactivator complex. Mammalian cells have two distinct GCN5 homologs (PCAF and GCN5L) that have been found in three different SAGA-like complexes (PCAF complex, TFTC [TATA-binding-protein-free TAFII-containing complex], and STAGA [SPT3-TAFII31-GCN5L acetylase]). | # |
SUPT6H
(details) |
11470 | suppressor of Ty 6 homolog (S. cerevisiae) | 6830 | Q7KZ85 | SPT6H_HUMAN | SPT6_acidic PF14632 19-126, HTH_44 PF14641 309-424, domain PF22706 565-743, YqgF PF14639 778-931, HHH_7 PF14635 935-1038, HHH_9 PF17674 1050-1139, S1 PF00575 1227-1282, SH2_2 PF14633 1297-1515 | Supt6 | 107726 | Q62383 | SPT6H_MOUSE | SH2D | SH2 domain containing | Histone modification erase cofactor | Histone methylation | 23503590 | # | histone | # | # | # | Coordinates H3K27 demethylation. | # |
SUPT7L
(details) |
30632 | suppressor of Ty 7 (S. cerevisiae)-like | 9913 | O94864 | ST65G_HUMAN | Bromo_TP PF07524 151-228 | Supt7l | 1919445 | Q9CZV5 | ST65G_MOUSE | # | # | Histone chaperone | # | 11564863 | TFTC-HAT, STAGA | histone | # | # | 11564863 | STAGA contains homologs of most yeast SAGA components, including two novel human proteins with histone-like folds and sequence relationships to yeast SPT7 and ADA1. STAGA preferentially acetylates histone H3 within nucleosomes. | # |
SUV39H1
(details) |
11479 | suppressor of variegation 3-9 homolog 1 (Drosophila) | 6839 | O43463 | SUV91_HUMAN | Chromo PF00385 43-91, Pre-SET PF05033 141-235, SET PF00856 255-366 | Suv39h1 | 1099440 | O54864 | SUV91_MOUSE | KMT | Chromatin-modifying enzymes / K-methyltransferases | Histone modification write, Histone modification write | Histone methylation, Histone phosphorylation | 10949293 | eNoSc | histone | H3S10, H3K9me1, H4 | H3K9me3 | 10949293 | In vivo, deregulated SUV39H1 or disrupted Suv39h activity modulate H3 serine 10 phosphorylation in native chromatin and induce aberrant mitotic divisions. | # |
SUV39H2
(details) |
17287 | suppressor of variegation 3-9 homolog 2 (Drosophila) | 79723 | Q9H5I1 | SUV92_HUMAN | Chromo PF00385 47-95, Pre-SET PF05033 149-242, SET PF00856 262-373 | Suv39h2 | 1890396 | Q9EQQ0 | SUV92_MOUSE | KMT | Chromatin-modifying enzymes / K-methyltransferases | Histone modification write | Histone methylation | 15107829 | # | histone | H3K9me1 | H3K9me3 | 15107829 | Suv39h proteins are histone methyltransferases that methylate histone H3 on lysine 9, resulting in transcriptional repression or silencing of target genes. | # |
SUV420H1
(details) |
24283 | suppressor of variegation 4-20 homolog 1 (Drosophila) | 51111 | Q4FZB7 | SV421_HUMAN | SET PF00856 209-308 | Suv420h1 | 2444557 | Q3U8K7 | SV421_MOUSE | KMT | Chromatin-modifying enzymes / K-methyltransferases | Histone modification write | Histone methylation | # | # | histone | H4K20 | H4K20me3 | # | Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. (Annotated by similarity.) | # |
SUV420H2
(details) |
28405 | suppressor of variegation 4-20 homolog 2 (Drosophila) | 84787 | Q86Y97 | SV422_HUMAN | SET PF00856 120-218 | Suv420h2 | 2385262 | Q6Q783 | SV422_MOUSE | KMT | Chromatin-modifying enzymes / K-methyltransferases | Histone modification write | Histone methylation | # | # | histone | H4K20 | H4K20me3 | # | Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. (Annotated by similarity.) | # |
SUZ12
(details) |
17101 | SUZ12 polycomb repressive complex 2 subunit | 23512 | Q15022 | SUZ12_HUMAN | VEFS-Box PF09733 548-680 | Suz12 | 1261758 | Q80U70 | SUZ12_MOUSE | ZNF | Zinc fingers, C2H2-type | Histone modification write cofactor, Histone modification write cofactor, Polycomb group (PcG) protein, TF | Histone methylation, Histone ubiquitination, TF repressor | 15385962 | PRC2 | DNA | DNA motif | # | 15385962 | SUZ12 is a recently identified Polycomb group (PcG) protein, which together with EZH2 and EED forms different Polycomb repressive complexes (PRC2/3). | # |
SYNCRIP
(details) |
16918 | synaptotagmin binding, cytoplasmic RNA interacting protein | 10492 | O60506 | HNRPQ_HUMAN | hnRNP_Q_AcD PF18360 34-103, RRM_1 PF00076 164-229 245-307 340-401 | Syncrip | 1891690 | Q7TMK9 | HNRPQ_MOUSE | RBM | RNA binding motif (RRM) containing | RNA modification | mRNA editing | 11134005, 11352648 | APOB_mRNA_editosome | RNA | mRNA | # | 11134005, 11352648 | GRY-RBP =HNRPQ has been shown to bind to apobec-1, the catalytic component of apoB mRNA editosome, in vivo and in vitro. | # |
TADA1
(details) |
30631 | transcriptional adaptor 1 | 117143 | Q96BN2 | TADA1_HUMAN | SAGA-Tad1 PF12767 7-107 136-193 | Tada1 | 1196415 | Q99LM9 | TADA1_MOUSE | # | # | Histone chaperone | # | 11564863 | STAGA | histone | H2A | # | 11564863 | Within STAGA are two novel histone fold-containing protein subunits: STAF65γ, which is encoded by the KIAA0764 gene of previously unknown function, and STAF42=TADA1, a novel histone H2A-like protein. | # |
TADA2A
(details) |
11531 | transcriptional adaptor 2A | 6871 | O75478 | TAD2A_HUMAN | Myb_DNA-binding PF00249 74-118, domain PF22941 165-240, SWIRM PF04433 375-440 | Tada2a | 2144471 | Q8CHV6 | TAD2A_MOUSE | # | # | Histone modification read, TF | TF activator | 19103755 | PCAF, ATAC | histone | H3 | # | 19103755 | The SANT domain of c-Myb has been shown to bind histone H3 tails and position them for acetylation. The SANT domains in ADA2a=TADA2A and ZZZ3/ATAC1 might enable the complex to associate with nucleosome tails in order to potentiate the catalytic activities of GCN5 and ATAC2, similar to what has been shown for the SANT domains in yeast Ada2 and Swi3. | # |
TADA2B
(details) |
30781 | transcriptional adaptor 2B | 93624 | Q86TJ2 | TAD2B_HUMAN | Myb_DNA-binding PF00249 68-112, domain PF22941 164-237 | Tada2b | 3035274 | # | # | # | # | Histone modification write cofactor | Histone acetylation | 17694077 | TFTC-HAT | histone | # | # | 17694077 | ADA2b =TADA2B is present in human STAGA/TFTC-type complexes. | # |
TADA3
(details) |
19422 | transcriptional adaptor 3 | 10474 | O75528 | TADA3_HUMAN | Ada3 PF10198 311-418 | Tada3 | 1915724 | Q8R0L9 | TADA3_MOUSE | # | # | Histone modification write cofactor | Histone acetylation | 11773077 | PCAF, TFTC-HAT, ATAC, STAGA | histone | # | # | 11773077 | Ada2 potentiates the Gcn5 catalytic activity and Ada3 =TADA3 facilitates nucleosomal acetylation and an expanded lysine specificity. | # |
TAF1
(details) |
11535 | TAF1 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 250kDa | 6872 | P21675 | TAF1_HUMAN | TBP-binding PF09247 27-87, DUF3591 PF12157 589-1050, zf-CCHC_6 PF15288 1282-1324, Bromodomain PF00439 1411-1492 1538-1613 | Taf1 | 1336878 | Q80UV9 | TAF1_MOUSE | KAT | Chromatin-modifying enzymes / K-acetyltransferases | Histone modification write | Histone acetylation | 11295558 | CHD8, MLL2/3, MLL4/WBP7 | histone | H3, H4 | H3ac, H4ac | 11295558 | TAFII250 has histone acetyltransferase (HAT) activity and can acetylate the tails of the core histones H3 and H4 in vitro. Both the N- and C-terminal kinase domains of TAFII250 are required for efficient transphosphorylation of RAP74 on serine residues. This suggests that the targeted phosphorylation of RAP74 by TAFII250 may provide a mechanism for signaling between components within the initiation complex to regulate transcription. | # |
TAF10
(details) |
11543 | TAF10 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 30kDa | 6881 | Q12962 | TAF10_HUMAN | TFIID_30kDa PF03540 128-177 | Taf10 | 1346320 | Q8K0H5 | TAF10_MOUSE | # | # | Histone chaperone, Histone modification write | Histone acetylation | 15099517 | PCAF, TFTC-HAT, SAGA, STAGA | histone | H3, H4 | # | 15099517 | SET9 can monomethylate the TBP-associated factor TAF10 at a single lysine residue located at the loop 2 region within the putative histone-fold domain of the protein. | # |
TAF12
(details) |
11545 | TAF12 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 20kDa | 6883 | Q16514 | TAF12_HUMAN | TFIID_20kDa PF03847 59-126 | Taf12 | 1913714 | Q8VE65 | TAF12_MOUSE | # | # | Histone chaperone, Histone modification write | Histone acetylation | 10594036 | PCAF, STAGA | histone | # | # | 10594036 | Heterodimerization requires the alpha2 and alpha3 helices of the hTAF(II)20 histone fold and is abolished by mutations in the hydrophobic face of the hTAF(II)20 alpha2 helix. Interaction with hTAF(II)20 requires a domain of hTAF(II)135 which shows sequence homology to H2A. | # |
TAF1L
(details) |
18056 | TAF1 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 210kDa-like | 138474 | Q8IZX4 | TAF1L_HUMAN | TBP-binding PF09247 26-86, DUF3591 PF12157 583-1047, zf-CCHC_6 PF15288 1278-1322, Bromodomain PF00439 1409-1488 1536-1612 | # | # | # | # | # | # | Histone modification read | # | 22464331 | # | histone | H1.4ac, H2Aac, H2Bac, H3ac, H4ac | # | 22464331 | Interacts (via bromo domains) with acetylated lysine residues on the N-terminus of histone H1.4, H2A, H2B, H3 and H4 (in vitro). | # |
TAF2
(details) |
11536 | TAF2 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 150kDa | 6873 | Q6P1X5 | TAF2_HUMAN | Taf2 | 2443028 | Q8C176 | TAF2_MOUSE | # | # | TF | # | # | TFTC-HAT | DNA | DNA motif | # | # | Added because it is a complex partner | # | |
TAF3
(details) |
17303 | TAF3 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 140kDa | 83860 | Q5VWG9 | TAF3_HUMAN | Bromo_TP PF07524 4-79, PHD PF00628 867-912 | Taf3 | 2388097 | Q5HZG4 | TAF3_MOUSE | PHF | Zinc fingers, PHD-type | Histone modification read | # | 21423274 | # | histone | H3K4me | # | 21423274 | Table 1 in the reference. | # |
TAF4
(details) |
11537 | TAF4 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 135kDa | 6874 | O00268 | TAF4_HUMAN | TAFH PF07531 592-680, TAF4 PF05236 833-1082 | # | # | # | # | # | # | Histone chaperone | # | 10594036 | TFTC-HAT, CHD8, MLL2/3, MLL4/WBP7 | histone | # | # | 10594036 | The histone fold region of hTAFII135 is required for coactivator activity in mammalian cells. | # |
TAF5
(details) |
11539 | TAF5 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 100kDa | 6877 | Q15542 | TAF5_HUMAN | TFIID_NTD2 PF04494 210-340, WD40 PF00400 466-498 535-571 577-612 618-655 660-697 703-739 | Taf5 | 2442144 | Q8C092 | TAF5_MOUSE | WDR | WD repeat domain containing | Histone modification write cofactor | Histone acetylation | 10373431 | TFTC-HAT | histone | # | # | 10373431 | TFTC, similar to other TBP-free TAFII complexes (yeast SAGA, hSTAGA, and hPCAF) contains the acetyltransferase hGCN5 and is able to acetylate histones in both a free and a nucleosomal context. A monoclonal antibody raised against hTAFII100 recognized hTAFII100=TAF5 not only in TFTC, but detected also a weak band in the PCAF complex. | # |
TAF5L
(details) |
17304 | TAF5-like RNA polymerase II, p300/CBP-associated factor (PCAF)-associated factor, 65kDa | 27097 | O75529 | TAF5L_HUMAN | TFIID_NTD2 PF04494 66-196, WD40 PF00400 269-296 334-370 379-412 418-454 459-496 501-538 | Taf5l | 1919039 | Q91WQ5 | TAF5L_MOUSE | WDR | WD repeat domain containing | Histone modification write cofactor | Histone acetylation | 10373431 | PCAF, TFTC-HAT, STAGA | histone | # | # | 10373431 | The PCAF complex contains hPAF65β=TAF5L, a WD40 repeat-containing factor having similarity to Htafii100(row=423) (5). Antibodies raised against hPAF65β revealed a band around 65 kDa in both the PCAF and the TFTC complexes. | # |
TAF6
(details) |
11540 | TAF6 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 80kDa | 6878 | P49848 | TAF6_HUMAN | TAF PF02969 12-76, TAF6_C PF07571 214-399 | Taf6 | 109129 | Q62311 | TAF6_MOUSE | # | # | Histone chaperone | # | 9611234 | TFTC-HAT, CHD8, MLL2/3, MLL4/WBP7 | DNA | # | # | 9611234 | The N-CoR/Sin3/HDAc complexes have a key role in the regulation of cellular proliferation and differentiation. N-CoR interacts directly with each of the basal factors, TFIIB and TAFII70 (=TAF6). | # |
TAF6L
(details) |
17305 | TAF6-like RNA polymerase II, p300/CBP-associated factor (PCAF)-associated factor, 65kDa | 10629 | Q9Y6J9 | TAF6L_HUMAN | TAF PF02969 10-73, TAF6_C PF07571 155-327 | Taf6l | 2444957 | Q8R2K4 | TAF6L_MOUSE | # | # | Histone chaperone | # | 12601814 | PCAF, TFTC-HAT, STAGA | histone | # | # | 12601814 | Human PAF65-alpha shows a strong sequence homology to TAFII80 and also contains a putative HFD. Thus, PAF65-alpha may also interact with TAFII32 in the TFTC complex. | # |
TAF7
(details) |
11541 | TAF7 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 55kDa | 6879 | Q15545 | TAF7_HUMAN | TAFII55_N PF04658 13-176 | Taf7 | 1346348 | Q9R1C0 | TAF7_MOUSE | # | # | Histone modification write cofactor, Histone modification write cofactor | Histone methylation, Histone acetylation | 22711989 | CHD8, MLL2/3, MLL4/WBP7 | histone | # | # | 22711989 | The largest transcription factor IID (TFIID) subunit, TBP-associated factor 1 (TAF1), possesses protein kinase and histone acetyltransferase (HAT) activities. | # |
TAF8
(details) |
17300 | TAF8 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 43kDa | 129685 | Q7Z7C8 | TAF8_HUMAN | Bromo_TP PF07524 32-105, TAF8_C PF10406 146-195 | Taf8 | 1926879 | Q9EQH4 | TAF8_MOUSE | # | # | Histone chaperone | # | 17375202 | # | histone | # | # | 17375202 | Present in a small TAF complex (SMAT), containing TAF8, TAF10 and SPT7L. | # |
TAF9
(details) |
11542 | TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa | 6880 | Q16594 | TAF9_HUMAN | TFIID-31kDa PF02291 10-130 | Taf9 | 1888697 | Q8VI33 | TAF9_MOUSE | # | # | Histone chaperone | # | 9674425 | PCAF, STAGA, CHD8, MLL2/3, MLL4/WBP7 | DNA | # | # | 9674425 | Histone-like TAFs, including TAFII31 =TAF9, are found within the PCAF histone acetylase complex. | # |
TAF9B
(details) |
17306 | TAF9B RNA polymerase II, TATA box binding protein (TBP)-associated factor, 31kDa | 51616 | Q9HBM6 | TAF9B_HUMAN | TFIID-31kDa PF02291 10-130 | Taf9b | 3039562 | Q6NZA9 | TAF9B_MOUSE | # | # | Histone chaperone | # | 15899866 | TFTC-HAT | histone | # | # | 15899866 | TAF9b (formerly TAF9L) is a bona fide TAF that has unique and overlapping roles with TAF9. | # |
TBL1XR1
(details) |
29529 | transducin (beta)-like 1 X-linked receptor 1 | 79718 | Q9BZK7 | TBL1R_HUMAN | LisH PF08513 6-32, WD40 PF00400 164-197 226-252 258-294 340-377 382-428 432-470 | Tbl1xr1 | 2441730 | Q8BHJ5 | TBL1R_MOUSE | WDR | WD repeat domain containing | # | # | 15601853 | # | histone | # | # | # | Targets Ncor repressive complex to deacethylated histones. | # |
TDG
(details) |
11700 | thymine-DNA glycosylase | 6996 | Q13569 | TDG_HUMAN | UDG PF03167 129-288 | Tdg | 108247 | P56581 | TDG_MOUSE | # | # | DNA modification | DNA hydroxymethylation | 22962365 | # | DNA | G:U, G:T, G:hmU | C, 5mC, 5hmC | 22962365 | The mammalian thymine DNA glycosylase (TDG) is implicated in active DNA demethylation via the base excision repair pathway. | # |
TDRD3
(details) |
20612 | tudor domain containing 3 | 81550 | Q9H7E2 | TDRD3_HUMAN | RMI1_N_C PF08585 1-72, domain PF22562 195-233, TUDOR PF00567 555-611 | Tdrd3 | 2444023 | Q91W18 | TDRD3_MOUSE | TDRD | Tudor domain containing | Histone modification read | # | 21172665 | # | histone | H3R17me2a, H4R3me2a | # | 21172665 | TDRD3 is an effector molecule for arginine-methylated histone marks. | # |
TDRD7
(details) |
30831 | tudor domain containing 7 | 23424 | Q8NHU6 | TDRD7_HUMAN | OST-HTH PF12872 7-72 236-274, TUDOR PF00567 462-582 653-775 912-1026 | Tdrd7 | 2140279 | Q8K1H1 | TDRD7_MOUSE | TDRD | Tudor domain containing | Histone modification read | # | 21423274 | # | histone | H3K9 | # | 21423274 | Table 1 in the reference. | # |
TDRKH
(details) |
11713 | tudor and KH domain containing | 11022 | Q9Y2W6 | TDRKH_HUMAN | KH_1 PF00013 54-116 126-190, TUDOR PF00567 305-423 | Tdrkh | 1919884 | Q80VL1 | TDRKH_MOUSE | TDRD | Tudor domain containing | RNA modification | # | 23714778 | # | RNA | piRNA | # | 23714778 | Piwi proteins and Piwi-interacting RNAs (piRNAs) repress transposition, regulate translation, and guide epigenetic programming in the germline. The evolutionarily conserved Tudor and KH domain-containing protein, Tdrkh (a.k.a. Tdrd2), is required for spermatogenesis and involved in piRNA biogenesis, the primary piRNA biogenesis pathway involves 3'→5' processing of 31-37 nt intermediates and that Tdrkh promotes this final step of piRNA biogenesis but not the ping-pong cycle. | # |
TET1
(details) |
29484 | tet methylcytosine dioxygenase 1 | 80312 | Q8NFU7 | TET1_HUMAN | zf-CXXC PF02008 585-625, Tet_JBP PF12851 1580-2051 | Tet1 | 1098693 | Q3URK3 | TET1_MOUSE | # | # | DNA modification | DNA hydroxymethylation | 23222540 | # | DNA | mC | hmC | 23222540 | Ten eleven translocation (TET) enzymes, including TET1, TET2 and TET3, convert 5-methylcytosine to 5-hydroxymethylcytosine and regulate gene transcription. | # |
TET2
(details) |
25941 | tet methylcytosine dioxygenase 2 | 54790 | Q6N021 | TET2_HUMAN | Tet_JBP PF12851 1290-1904 | Tet2 | 2443298 | Q4JK59 | TET2_MOUSE | # | # | DNA modification | DNA hydroxymethylation | 23222540 | # | DNA | mC | hmC | 23222540 | Ten eleven translocation (TET) enzymes, including TET1, TET2 and TET3, convert 5-methylcytosine to 5-hydroxymethylcytosine and regulate gene transcription. Downregulation of TET2 reduces the amount of histone 2B Ser 112 GlcNAc marks in vivo, which are associated with gene transcription regulation. | # |
TET3
(details) |
28313 | tet methylcytosine dioxygenase 3 | 200424 | O43151 | TET3_HUMAN | zf-CXXC PF02008 52-90, Tet_JBP PF12851 986-1697 | Tet3 | 2446229 | Q8BG87 | TET3_MOUSE | # | # | DNA modification | DNA hydroxymethylation | 23222540 | # | DNA | mC | hmC | 23222540 | Ten eleven translocation (TET) enzymes, including TET1, TET2 and TET3, convert 5-methylcytosine to 5-hydroxymethylcytosine and regulate gene transcription. There is a direct interaction of TET2 and TET3 with O-GlcNAc transferase (OGT). | # |
TEX10
(details) |
25988 | testis expressed 10 | 54881 | Q9NXF1 | TEX10_HUMAN | Ipi1_N PF12333 134-239 | Tex10 | 1344413 | Q3URQ0 | TEX10_MOUSE | # | # | Histone modification write cofactor, Histone modification write cofactor | Histone methylation, Histone acetylation | # | CHD8, MLL2/3, MLL4/WBP7 | histone | # | # | 22872859 | - | # |
TFDP1
(details) |
11749 | transcription factor Dp-1 | 7027 | Q14186 | TFDP1_HUMAN | E2F_TDP PF02319 113-193, DP PF08781 200-338 | Tfdp1 | 101934 | Q08639 | TFDP1_MOUSE | # | # | Histone modification | # | 24217316, 22325352 | RING2-L3MBTL2 | histone | # | # | 24217316, 22325352 | Part of a RING2 complex. | # |
TFPT
(details) |
13630 | TCF3 (E2A) fusion partner (in childhood Leukemia) | 29844 | P0C1Z6 | TFPT_HUMAN | Tfpt | 1916964 | Q3U1J1 | TFPT_MOUSE | INO80 | INO80 complex subunits | Chromatin remodeling cofactor, DNA modification | DNA hydroxymethylation | 16230350 | Ino80 | chromatin | # | # | 16230350 | Subunit Composition of the hINO80 Complex: These proteins included the “Pim-1 kinase-associated protein-associated protein 1” (PAPA-1, GI 13775202), Amida (also known as TCF3 =TFPT). | # | |
THRAP3
(details) |
22964 | Thyroid hormone receptor-associated protein 3 (BCLAF1 and THRAP3 family member 2) (Thyroid hormone receptor-associated protein complex 150 kDa component) (Trap150) | 9967 | Q9Y2W1 | TR150_HUMAN | THRAP3_BCLAF1 PF15440 107-862 | Tr150 | 2442637 | Q569Z6 | TR150_MOUSE | # | # | RNA modification | RNA degradation | 20123736 | # | RNA | mRNA | # | 20123736 | Mediates nuclear mRNA degradation | New |
TLE1
(details) |
11837 | transducin-like enhancer of split 1 (E(sp1) homolog, Drosophila) | 7088 | Q04724 | TLE1_HUMAN | TLE_N PF03920 18-132, WD40 PF00400 477-511 531-558 577-602 607-644 692-725 739-766 | Tle1 | 104636 | Q62440 | TLE1_MOUSE | WDR | WD repeat domain containing | Chromatin remodeling, Histone modification cofactor | # | 9334241, 17041588 | # | histone | H3 | # | 9334241, 17041588 | Native Groucho/TLE proteins interact specifically with histone H3 and not with other core histones. | # |
TLE2
(details) |
11838 | transducin-like enhancer of split 2 | 7089 | Q04725 | TLE2_HUMAN | TLE_N PF03920 18-130, WD40 PF00400 450-484 504-531 550-575 580-617 665-698 712-739 | Tle2 | 104635 | Q9WVB2 | TLE2_MOUSE | WDR | WD repeat domain containing | Histone modification cofactor | # | 17041588 | # | histone | H3 | H3K4, H3K9, H3K27me | 17041588 | CUL4-DDB1 complexes interact with multiple WD40-repeat proteins (WDRs) including TLE1-3, WDR5, L2DTL (also known as CDT2) and the Polycomb-group protein EED (also known as ESC). WDR5 and EED are core components of histone methylation complexes that are essential for histone H3 methylation and epigenetic control at K4 or K9 and K27, respectively. | # |
TLE4
(details) |
11840 | transducin-like enhancer of split 4 | 7091 | Q04727 | TLE4_HUMAN | TLE_N PF03920 24-138, WD40 PF00400 480-514 534-561 580-605 610-647 695-728 742-769 | Tle4 | 104633 | Q62441 | TLE4_MOUSE | WDR | WD repeat domain containing | Histone modification erase cofactor, TF | # | 24190972 | # | histone | H3ac, H4ac | # | 24190972 | Tle4 is the transcriptional repressor responsible for the establishment of the epigenetic repressive marks at the Ifng locus that result in silencing of Ifng gene expression. Tle proteins have been shown to oligomerize, to associate with amino-terminal domains of histone-modifying proteins, and to form higher-order structures as parts of repressive complexes. | # |
TLK1
(details) |
11841 | tousled-like kinase 1 | 9874 | Q9UKI8 | TLK1_HUMAN | Pkinase PF00069 458-734 | Tlk1 | 2441683 | Q8C0V0 | TLK1_MOUSE | # | # | Histone modification write | Histone phosphorylation | 11314006 | # | histone | H3S10 | H3S10ph | 11314006 | Purified TLK1B phosphorylates histone H3 at S(10) with high specificity both in a mix of core histones and in isolated chromatin, suggesting that histone H3 is a physiological substrate for TLK1B. | # |
TLK2
(details) |
11842 | tousled-like kinase 2 | 11011 | Q86UE8 | TLK2_HUMAN | Pkinase PF00069 464-741 | Tlk2 | 1346023 | O55047 | TLK2_MOUSE | # | # | Histone modification write | Histone phosphorylation | 12660173 | # | chromatin | # | # | 12660173 | There is a functional co-operation between ATM and Chk1 in propagation of a checkpoint response during S phase, suggesting that, through transient inhibition of Tlk kinases, the ATM-Chk1-Tlk pathway may regulate processes involved in chromatin assembly. | # |
TNP1
(details) |
11951 | transition protein 1 (during histone to protamine replacement) | 7141 | P09430 | STP1_HUMAN | TP1 PF02079 1-53 | Tnp1 | 98784 | P10856 | STP1_MOUSE | # | # | Chromatin remodeling | # | 12743712 | # | chromatin | # | # | 12743712 | Distinct roles for the two major transition nuclear proteins, TP1 = STP1 and TP2 = STP2, in histone displacement, sperm nuclear shaping, chromatin condensation, and maintenance of DNA integrity have been proposed. | # |
TNP2
(details) |
11952 | transition protein 2 (during histone to protamine replacement) | 7142 | Q05952 | STP2_HUMAN | TP2 PF01254 1-136 | Tnp2 | 98785 | P11378 | STP2_MOUSE | # | # | Chromatin remodeling | # | 12743712 | # | chromatin | # | # | 12743712 | Distinct roles for the two major transition nuclear proteins, TP1 = STP1 and TP2 = STP2, in histone displacement, sperm nuclear shaping, chromatin condensation, and maintenance of DNA integrity have been proposed. | # |
TONSL
(details) |
7801 | tonsoku-like, DNA repair protein | 4796 | Q96HA7 | TONSL_HUMAN | TPR_8 PF13181 202-235, domain PF13176 311-344, Ank_2 PF12796 529-628, LRR_6 PF13516 1097-1120 1128-1151 1248-1271 | Tonsl | 1919999 | Q6NZL6 | TONSL_MOUSE | ANKRD | Ankyrin repeat domain containing | Chromatin remodeling | # | 21113133 | # | histone | # | # | 21113133 | Mms22L associates with Nfkbil2 =TONSL, which may function as a scaffolding unit to bridge chromatin to multiple protein complexes. | # |
TOP2A
(details) |
11989 | topoisomerase (DNA) II alpha 170kDa | 7153 | P11388 | TOP2A_HUMAN | HATPase_c PF02518 80-176, DNA_gyraseB PF00204 265-425, Toprim PF01751 456-562, TOPRIM_C PF16898 574-711, DNA_topoisoIV PF00521 713-1171, DTHCT PF08070 1231-1511 | Top2a | 98790 | Q01320 | TOP2A_MOUSE | # | # | Chromatin remodeling | # | 11062478 | # | DNA | DNA | # | 11062478 | Histone deacetylase interacts directly with DNA topoisomerase II. | # |
TOP2B
(details) |
11990 | topoisomerase (DNA) II beta 180kDa | 7155 | Q02880 | TOP2B_HUMAN | HATPase_c PF02518 101-197, DNA_gyraseB PF00204 286-447, Toprim PF01751 477-583, TOPRIM_C PF16898 594-731, DNA_topoisoIV PF00521 734-1193, DTHCT PF08070 1447-1626 | Top2b | 98791 | Q64511 | TOP2B_MOUSE | # | # | Chromatin remodeling | # | 11062478 | WINAC | chromatin | # | # | 11062478 | Histone deacetylase interacts directly with DNA topoisomerase II. | # |
TP53
(details) |
11998 | tumor protein p53 | 7157 | P04637 | P53_HUMAN | P53_TAD PF08563 13-33, TAD2 PF18521 23-55, P53 PF00870 101-288, P53_tetramer PF07710 323-357 | Trp53 | 98834 | P02340 | P53_MOUSE | # | # | Histone modification write cofactor, TF | Histone acetylation, TF activator, TF repressor | 23870121 | # | histone | H3 | # | 23870121 | SET1 complex (SET1C)-mediated H3K4 trimethylation is dependent upon p53- and p300-mediated H3 acetylation. Complementary cell-based assays demonstrate a DNA-damage-induced p53-SET1C interaction, a corresponding enrichment of SET1C and H3K4me3 on a p53 target gene (p21/WAF1), and a corresponding codependency of H3K4 trimethylation and transcription upon p300 and SET1C. | # |
TP53BP1
(details) |
11999 | tumor protein p53 binding protein 1 | 7158 | Q12888 | TP53B_HUMAN | 53-BP1_Tudor PF09038 1481-1604, BRCT_3 PF18428 1866-1968 | Trp53bp1 | 1351320 | P70399 | TP53B_MOUSE | # | # | Histone modification read | # | 15525939 | # | histone | H4K79me2, H4K20me2 | # | 15525939 | In vitro, the 53BP1 =TP53BP1 tandem tudor domain binds histone H3 methylated on Lys 79 using residues that form the walls of the pocket; these residues are also required for recruitment of 53BP1 to DSBs. | # |
TRA2B
(details) |
10781 | Transformer-2 protein homolog beta (TRA-2 beta) (TRA2-beta) (hTRA2-beta) (Splicing factor, arginine/serine-rich 10) (Transformer-2 protein homolog B) | 6434 | P62995 | TRA2B_HUMAN | RRM_1 PF00076 122-190 | Tra2B | 106016 | P62996 | TRA2B_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 12165565 | # | RNA | mRNA | # | 12165565 | Promotes exon 7 inclusion of SMN | New |
TRIM16
(details) |
17241 | tripartite motif containing 16 | 10626 | O95361 | TRI16_HUMAN | zf-B_box PF00643 127-165, PRY PF13765 375-424, SPRY PF00622 426-543 | Trim16 | 2137356 | Q99PP9 | TRI16_MOUSE | TRIM | Tripartite motif containing / Tripartite motif containing | Histone modification write | Histone acetylation | 19147277, 20729920 | # | histone, DNA | # | # | # | Overexpression of this gene increases histone acetylation. TRIM16 has been identified as a DNA-binding protein with histone acetylase activity. | # |
TRIM24
(details) |
11812 | tripartite motif containing 24 | 8805 | O15164 | TIF1A_HUMAN | zf-B_box PF00643 221-258, PHD PF00628 829-870, Bromodomain PF00439 908-989 | Trim24 | 109275 | Q64127 | TIF1A_MOUSE | TRIM, RNF, PHF | Tripartite motif containing / Tripartite motif containing, RING-type (C3HC4) zinc fingers, Zinc fingers, PHD-type | Histone modification read | # | 22464331 | # | histone | H3K4, H3K23ac | # | 21164480 | Interacts with chromatin depending on histone H3 modifications, having the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac) (UniProt). | # |
TRIM27
(details) |
9975 | tripartite motif containing 27 | 5987 | P14373 | TRI27_HUMAN | zf-C3HC4_4 PF15227 16-56, zf-B_box PF00643 93-132, PRY PF13765 318-366, SPRY PF00622 370-482 | Trim27 | 97904 | Q62158 | TRI27_MOUSE | TRIM, RNF | Tripartite motif containing / Tripartite motif containing, RING-type (C3HC4) zinc fingers | Histone modification erase cofactor | Histone acetylation | 19351825 | # | # | # | # | # | The recruitment of HDAC1 to the TBP-2 promoter is mediated by a protein complex consisting of RET finger protein (RFP; also called TRIM27) and the trimeric transcription factor NF-Y. | # |
TRIM28
(details) |
16384 | tripartite motif containing 28 | 10155 | Q13263 | TIF1B_HUMAN | zf-RING_5 PF14634 65-122, zf-B_box PF00643 149-195 207-245, PHD PF00628 628-669 | Trim28 | 109274 | Q62318 | TIF1B_MOUSE | TRIM, RNF, PHF | Tripartite motif containing / Tripartite motif containing, RING-type (C3HC4) zinc fingers, Zinc fingers, PHD-type | Histone modification read | # | 22464331 | # | histone | H3 | # | 22464331 | Fig. 5 in the reference. | # |
TRIM33
(details) |
16290 | tripartite motif containing 33 | 51592 | Q9UPN9 | TRI33_HUMAN | zf-B_box PF00643 274-310, PHD PF00628 890-931, Bromodomain PF00439 967-1046 | Trim33 | 2137357 | Q99PP7 | TRI33_MOUSE | TRIM, PHF, RNF | Tripartite motif containing / Tripartite motif containing, Zinc fingers, PHD-type, RING-type (C3HC4) zinc fingers | Histone modification read | # | 23926104 | # | histone | H3K9me3, H3K18ac | # | 23926104 | TRIM33 helps recruit SMAD2/3 to chromatin via interaction of its PHD and Bromo domains with histone H3 trimethylated at lysine 9 (H3K9me3) and histone H3 acetylated at lysine 18 (H3K18ac), respectively. | # |
TRRAP
(details) |
12347 | transformation/transcription domain-associated protein | 8295 | Q9Y4A5 | TRRAP_HUMAN | Tra1_central PF20175 240-895, Tra1_ring PF20206 1003-2695, FAT PF02259 2851-3201, PI3_PI4_kinase PF00454 3531-3782 | Trrap | 2153272 | Q80YV3 | TRRAP_MOUSE | # | # | Histone modification write cofactor | Histone acetylation | 14966270 | SWR, PCAF, TFTC-HAT, NuA4, SAGA, NuA4-related complex, STAGA | histone | # | # | 14966270 | The complex(es) contain(s) other subunits shared with NuA4, including TRRAP, p400/hDomino, Brd8. | # |
TRUB2
(details) |
17170 | Mitochondrial mRNA pseudouridine synthase TRUB2 (EC 5.4.99.-) | 26995 | O95900 | TRUB2-HUMAN | TruB_N PF01509 88-231 | Trub2 | 2442186 | Q91WG3 | TRUB2_MOUSE | Pseudouridine synthases | Pseudouridine synthases | RNA modification | RNA pseudouridinilation | 27974379 | # | RNA | mt--mRNA | U | 27974379 | Pseudouridinilation of mitochondrial mRNA | New |
TSSK6
(details) |
30410 | testis-specific serine kinase 6 | 83983 | Q9BXA6 | TSSK6_HUMAN | Pkinase PF00069 12-267 | Tssk6 | 2148775 | Q925K9 | TSSK6_MOUSE | # | # | Histone modification write | Histone phosphorylation | 15870294 | # | histone | H1, H2A, H2AX, H3 | # | # | Phosphorylates histones H1, H2A, H2AX, and H3 but not H2B or H4 in vitro. | # |
TTK
(details) |
12401 | TTK protein kinase | 7272 | P33981 | TTK_HUMAN | Pkinase PF00069 525-791 | Ttk | 1194921 | P35761 | TTK_MOUSE | # | # | Histone modification write cofactor | Histone phosphorylation | 22732840 | # | histone | H2AT120 | H2AT120ph | 22732840 | Mps1 = TTK activity enhances H2A‐T120ph and is critical for Sgo1 recruitment to centromeres, thereby promoting Aurora B centromere recruitment in early mitosis. | # |
TYW5
(details) |
26754 | tRNA-yW synthesizing protein 5 | 129450 | A2RUC4 | TYW5_HUMAN | Cupin_8 PF13621 17-254 | Tyw5 | 1915986 | A2RSX7 | TYW5_MOUSE | # | # | RNA modification | # | 20972222 | # | RNA | # | # | 20972222 | Functional analyses of structure-based mutants have revealed the essential Arg residues participating in tRNA recognition by TYW5. These findings extend the repertoire of the tRNA modification enzyme into the Fe(II)/2-OG oxygenase superfamily. | # |
U2AF2
(details) |
23156 | Splicing factor U2AF 65 kDa subunit (U2 auxiliary factor 65 kDa subunit) (hU2AF(65)) (hU2AF65) (U2 snRNP auxiliary factor large subunit) | 11338 | P26368 | U2AF2_HUMAN | RRM_1 PF00076 151-225 261-330 400-459 | U2Af2 | 98886 | P26369 | U2AF2_MOUSE | RBM | RNA binding motif containing | RNA modification | Alternative splicing | 17579712, 16452196 | # | RNA | mRNA | # | 17579712, 16452196 | Regulates alternative splcing of FIR | New |
UBE2A
(details) |
12472 | ubiquitin-conjugating enzyme E2A | 7319 | P49459 | UBE2A_HUMAN | UQ_con PF00179 8-143 | Ube2a | 102959 | Q9Z255 | UBE2A_MOUSE | UBE2 | Ubiquitin-conjugating enzymes E2 | Histone modification write | Histone ubiquitination | 8797826 | # | histone | H2A, H2BK120 | H2BK120ub1 | 8797826 | RAD6 (=UBE2) has been identified as the first ubiquitin-conjugating enzyme, able to mono- and polyubiquitinate histones 2A and 2B in vitro. | # |
UBE2B
(details) |
12473 | ubiquitin-conjugating enzyme E2B | 7320 | P63146 | UBE2B_HUMAN | UQ_con PF00179 7-143 | Ube2b | 102944 | P63147 | UBE2B_MOUSE | UBE2 | Ubiquitin-conjugating enzymes E2 | Histone modification write | Histone ubiquitination | 8797826 | # | histone | H2A, H2BK121 | H2BK120ub2 | 8797826 | RAD6 (=UBE2) has been identified as the first ubiquitin-conjugating enzyme, able to mono- and polyubiquitinate histones 2A and 2B in vitro. | # |
UBE2D1
(details) |
12474 | ubiquitin-conjugating enzyme E2D 1 | 7321 | P51668 | UB2D1_HUMAN | UQ_con PF00179 5-141 | Ube2d1 | 2384911 | P61080 | UB2D1_MOUSE | UBE2 | Ubiquitin-conjugating enzymes E2 | Histone modification write | Histone ubiquitination | 22438555 | # | histone | H2BK48 | H2BK48ub | 22438555 | Ubiquitination of TP53. | # |
UBE2D3
(details) |
12476 | ubiquitin-conjugating enzyme E2D 3 | 7323 | P61077 | UB2D3_HUMAN | UQ_con PF00179 5-141 | Ube2d3 | 1913355 | P61079 | UB2D3_MOUSE | UBE2 | Ubiquitin-conjugating enzymes E2 | Histone modification write | Histone ubiquitination | 21772249 | # | histone | H2AK119 | H2AK119ub | 21772249 | Figure 7 in the reference (UBE2D3 =UbcH5c). | # |
UBE2E1
(details) |
12477 | ubiquitin-conjugating enzyme E2E 1 | 7324 | P51965 | UB2E1_HUMAN | UQ_con PF00179 51-187 | Ube2e1 | 107411 | P52482 | UB2E1_MOUSE | UBE2 | Ubiquitin-conjugating enzymes E2 | Histone modification write | Histone ubiquitination | 16307923 | # | histone | H2BK120 | H2BK120ub | 16307923 | The human RNF20/40 complex functions as the E3 ligase and UbcH6 (=UBE2E1) as the ubiquitin E2-conjugating enzyme for histone H2B-K120 monoubiquitination. | # |
UBE2H
(details) |
12484 | ubiquitin-conjugating enzyme E2H | 7328 | P62256 | UBE2H_HUMAN | UQ_con PF00179 30-144 | Ube2h | 104632 | P62257 | UBE2H_MOUSE | UBE2 | Ubiquitin-conjugating enzymes E2 | Histone modification write | Histone ubiquitination | 8132613 | # | histone | H2A, H2B | H2Aub, H2Bub | 8132613 | The capacity of the UBC8I UbcH2 enzymes to ubiquitinate histones in vitro raises makes it possible that these enzymes may be involved in this process in vivo. | # |
UBE2N
(details) |
12492 | ubiquitin-conjugating enzyme E2N | 7334 | P61088 | UBE2N_HUMAN | UQ_con PF00179 7-143 | Ube2n | 1934835 | P61089 | UBE2N_MOUSE | UBE2 | Ubiquitin-conjugating enzymes E2 | Histone modification write | Histone ubiquitination | 17709392 | # | histone | H2AX | H2AXub | 17709392 | TIP60 regulates the ubiquitination of H2AX via the ubiquitin-conjugating enzyme UBC13 (=UBE2N), which is induced by DNA damage. | # |
UBE2T
(details) |
25009 | ubiquitin-conjugating enzyme E2T (putative) | 29089 | Q9NPD8 | UBE2T_HUMAN | UQ_con PF00179 6-146 | Ube2t | 1914446 | Q9CQ37 | UBE2T_MOUSE | UBE2 | Ubiquitin-conjugating enzymes E2 | Histone modification write | Histone ubiquitination | 17938197 | # | histone | # | # | 17938197 | histone | # |
UBN1
(details) |
12506 | ubinuclein 1 | 29855 | Q9NPG3 | UBN1_HUMAN | HUN PF08729 118-170, UBN_AB PF14075 346-567 | Ubn1 | 1891307 | Q4G0F8 | UBN1_MOUSE | # | # | Histone modification write cofactor | Histone methylation | 19029251, 21807893 | # | histone | # | # | # | Binds to proliferation-promoting genes and associates with histone methyltransferase activity that methylates lysine 9 of histone H3. Human CABIN1 is a functional member of the human HIRA/UBN1/ASF1a histone H3.3 chaperone complex. | # |
UBR2
(details) |
21289 | ubiquitin protein ligase E3 component n-recognin 2 | 23304 | Q8IWV8 | UBR2_HUMAN | zf-UBR PF02207 99-167, ClpS PF02617 222-301, domain PF22960 778-872, PRT6_C PF18995 1309-1729 | Ubr2 | 1861099 | Q6WKZ8 | UBR2_MOUSE | UBR | Ubiquitin protein ligase E3 component n-recognins | Histone modification write | Histone ubiquitination | # | # | histone | H2A | # | # | Plays a critical role in chromatin inactivation and chromosome-wide transcriptional silencing during meiosis via ubiquitination of histone H2A. (Annotated by similarity.) | # |
UBR5
(details) |
16806 | ubiquitin protein ligase E3 component n-recognin 5 | 51366 | O95071 | UBR5_HUMAN | E3_UbLigase_EDD PF11547 183-228, PABP PF00658 2391-2450, HECT PF00632 2505-2799 | Ubr5 | 1918040 | Q80TP3 | UBR5_MOUSE | UBR | Ubiquitin protein ligase E3 component n-recognins | Chromatin remodeling, Histone modification write cofactor | Histone ubiquitination | 22884692 | # | histone | H2A, H2AX | H2Aub, H2AXub | 22884692 | Excessive spreading of a DNA-damage-associated chromatin modification can occur. TRIP12 and UBR5 are two suppressors of such spreading. | # |
UBR7
(details) |
20344 | ubiquitin protein ligase E3 component n-recognin 7 (putative) | 55148 | Q8N806 | UBR7_HUMAN | zf-UBR PF02207 46-112 | Ubr7 | 1913872 | Q8BU04 | UBR7_MOUSE | UBR | Ubiquitin protein ligase E3 component n-recognins | DNA modification cofactor | DNA methylation | 21745816 | # | DNA | # | # | 21745816 | Part of the DNMT1/USP7/UHRF1 complex which increases DNA methylation efficiency. | # |
UCHL5
(details) |
19678 | ubiquitin carboxyl-terminal hydrolase L5 | 51377 | Q9Y5K5 | UCHL5_HUMAN | Peptidase_C12 PF01088 8-209, UCH_C PF18031 265-309 | Uchl5 | 1914848 | Q9WUP7 | UCHL5_MOUSE | INO80 | INO80 complex subunits | Histone modification erase cofactor | Histone ubiquitination | 18922472 | Ino80 | histone | # | # | 18922472 | Deubiquitination by Uch37 is activated by proteasomal binding, which enables Uch37 to process polyubiquitin chains. In the nucleus Uch37 is also associated with the human Ino80 chromatin-remodeling complex (hINO80). In hINO80, Uch37 is held in an inactive state; however, it can be activated by transient interaction of the Ino80 complex with the proteasome. | # |
UHRF1
(details) |
12556 | ubiquitin-like with PHD and ring finger domains 1 | 29128 | Q96T88 | UHRF1_HUMAN | ubiquitin PF00240 2-75, TTD PF12148 133-285, PHD PF00628 318-363, SAD_SRA PF02182 417-585 | Uhrf1 | 1338889 | Q8VDF2 | UHRF1_MOUSE | RNF | RING-type (C3HC4) zinc fingers | Histone modification read, Histone modification write cofactor | Histone ubiquitination | 17967883 | # | histone, DNA | H3K9me3, H3R2, H3, mCG | H3ub | 17967883 | ICBP90 =UHRF1and its murine homologue Np95 are enriched in pericentric heterochromatin of interphase nuclei, and this localization is dependent on H3K9 methylation. | # |
UHRF2
(details) |
12557 | ubiquitin-like with PHD and ring finger domains 2, E3 ubiquitin protein ligase | 115426 | Q96PU4 | UHRF2_HUMAN | ubiquitin PF00240 2-74, TTD PF12148 125-311, PHD PF00628 347-392, SAD_SRA PF02182 445-614 | Uhrf2 | 1923718 | Q7TMI3 | UHRF2_MOUSE | RNF, PHF | RING-type (C3HC4) zinc fingers, Zinc fingers, PHD-type | Histone modification read | # | 15361834 | # | histone, DNA | H3K9me3, mCG | # | 15361834 | The SRA domain of the murine homologue of ICBP90=UHRF2, Np95, has histone H3-binding activity (Citterio et al., 2004). Methylated DNA twisted around histone H3 might be the primary target for Np95 and ICBP90 in vivo. | # |
UIMC1
(details) |
30298 | ubiquitin interaction motif containing 1 | 51720 | Q96RL1 | UIMC1_HUMAN | RAP80_UIM PF18282 73-125 | Uimc1 | 103185 | Q5U5Q9 | UIMC1_MOUSE | # | # | Histone modification read | # | 19015238 | BRCA1-A | histone | H2AK63ub, H2AXK63ub, H2BK63ub | # | 19015238 | The interaction between RAP80 =UIMC1 and ubiquitinated histones H2A and H2B is increased following DNA damage. | # |
USP11
(details) |
12609 | ubiquitin specific peptidase 11 | 8237 | P51784 | UBP11_HUMAN | DUSP PF06337 86-183, Ubiquitin_3 PF14836 199-285, UCH PF00443 309-927, USP7_C2 PF14533 493-596 | Usp11 | 2384312 | Q99K46 | UBP11_MOUSE | USP | Ubiquitin-specific peptidases | Histone modification erase cofactor | Histone ubiquitination | 20233726 | # | histone | # | # | 20233726 | USP11 is a chromatin-associated protein and its catalytic activity is required for its genome maintenance activities. USP11 may be a DUB that functions in the DNA damage response to double-strand breaks. | # |
USP12
(details) |
20485 | ubiquitin specific peptidase 12 | 219333 | O75317 | UBP12_HUMAN | UCH PF00443 39-366 | Usp12 | 1270128 | Q9D9M2 | UBP12_MOUSE | USP | Ubiquitin-specific peptidases | Histone modification erase | Histone ubiquitination | 22033037 | # | histone | H2Aub | H2A | 22033037 | Involved in H2A deubiquitination. | # |
USP15
(details) |
12613 | ubiquitin specific peptidase 15 | 9958 | Q9Y4E8 | UBP15_HUMAN | DUSP PF06337 27-118, Ubiquitin_3 PF14836 135-221, UCH PF00443 289-930, USP7_C2 PF14533 473-601 | Usp15 | 101857 | Q8R5H1 | UBP15_MOUSE | USP | Ubiquitin-specific peptidases | Histone modification erase | Histone ubiquitination | 24526689 | # | histone | H2BK120ub | H2BK120 | 24526689 | Enhanced Usp15 binding to ubH2B facilitates deubiquitination of ubH2B in free histones but not in nucleosomes. | # |
USP16
(details) |
12614 | ubiquitin specific peptidase 16 | 10600 | Q9Y5T5 | UBP16_HUMAN | zf-UBP PF02148 47-124, UCH PF00443 197-819 | Usp16 | 1921362 | Q99LG0 | UBP16_MOUSE | USP | Ubiquitin-specific peptidases | Histone modification erase | Histone ubiquitination | 10077596 | # | histone | H2Aub | H2A | 10077596 | Recombinant Ubp-M=USP16 is able to deubiquitinate histone H2A in vitro, and the phosphorylated form is also enzymatically active. | # |
USP17L2
(details) |
34434 | ubiquitin specific peptidase 17-like family member 2 | 377630 | Q6R6M4 | U17L2_HUMAN | UCH PF00443 81-372 | Usp17le | 3643640 | Q7M764 | U17PE_MOUSE | # | # | Histone modification erase cofactor | Histone ubiquitination | 21239494 | # | histone | # | # | 21239494 | SDS3 is a key component of the histone deacetylase (HDAC)-dependent Sin3A co-repressor complex, serving to maintain its HDAC activity. Both exogenous and endogenous functional interaction between deubiquitinating enzyme USP17 = USP17L2 and human SDS3 has been reported. | # |
USP21
(details) |
12620 | ubiquitin specific peptidase 21 | 27005 | Q9UK80 | UBP21_HUMAN | UCH PF00443 212-555 | Usp21 | 1353665 | Q9QZL6 | UBP21_MOUSE | USP | Ubiquitin-specific peptidases | Histone modification erase | Histone ubiquitination | # | # | histone | H2Aub | H2A | # | Deubiquitinates histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A releaves the repression of di- and trimethylation of histone H3 at 'Lys-4', resulting in regulation of transcriptional initiation. Regulates gene expression via histone H2A deubiquitination. (Annotated by similarity.) | # |
USP22
(details) |
12621 | ubiquitin specific peptidase 22 | 23326 | Q9UPT9 | UBP22_HUMAN | zf-UBP PF02148 63-123, UCH PF00443 176-517 | Usp22 | 2144157 | Q5DU02 | UBP22_MOUSE | USP | Ubiquitin-specific peptidases | Histone modification write cofactor | Histone ubiquitination | 18469533 | SAGA | histone | H2Aub, H2Bub | H2A, H2B | 18469533 | USP22 deubiquitylates histone H2A in addition to H2B. This supports a model in which the H2A ubiquitin hydrolase USP22 is coordinately expressed with Polycomb H2A ubiquitin ligases in order that the transcription of certain critical transforming genes be maintained in the face of the global repression mediated by Polycomb. | # |
USP3
(details) |
12626 | ubiquitin specific peptidase 3 | 9960 | Q9Y6I4 | UBP3_HUMAN | zf-UBP PF02148 29-107, UCH PF00443 160-508 | Usp3 | 2152450 | Q91W36 | UBP3_MOUSE | USP | Ubiquitin-specific peptidases | Histone modification write | Histone ubiquitination | 17980597 | # | histone | H2Aub, H2Bub | H2A, H2B | 17980597 | The ubiquitin-specific protease 3 USP3 is a deubiquitinating enzyme for uH2A and uH2B. USP3 dynamically associates with chromatin and deubiquitinates H2A/H2B in vivo. | # |
USP36
(details) |
20062 | ubiquitin specific peptidase 36 | 57602 | Q9P275 | UBP36_HUMAN | UCH PF00443 122-421 | Usp36 | 1919594 | B1AQJ2 | UBP36_MOUSE | USP | Ubiquitin-specific peptidases | Histone modification write cofactor | Histone ubiquitination | 22622177 | # | histone | H2Bub | H2B | 22622177 | Deubiquitination of histone H2B at the promoters of genes critical for cellular differentiation, thereby preventing histone H3 'Lys-4' trimethylation (H3K4). | # |
USP44
(details) |
20064 | ubiquitin specific peptidase 44 | 84101 | Q9H0E7 | UBP44_HUMAN | zf-UBP PF02148 28-91, UCH PF00443 273-675 | Usp44 | 3045318 | Q8C2S0 | UBP44_MOUSE | USP | Ubiquitin-specific peptidases | Histone modification erase | Histone ubiquitination | 22681888 | # | histone | H2Bub1 | H2B | 22681888 | USP44 is most likely an H2Bub1-specific DUB, whose downregulation during ESC differentiation contributes to increased H2Bub1 levels. | # |
USP46
(details) |
20075 | ubiquitin specific peptidase 46 | 64854 | P62068 | UBP46_HUMAN | UCH PF00443 35-362 | Usp46 | 1916977 | P62069 | UBP46_MOUSE | USP | Ubiquitin-specific peptidases | Histone modification erase | Histone ubiquitination | 22033037 | # | histone | H2Aub | H2A | 22033037 | Involved in H2A deubiquitination. | # |
USP49
(details) |
20078 | ubiquitin specific peptidase 49 | 25862 | Q70CQ1 | UBP49_HUMAN | zf-UBP PF02148 26-87, UCH PF00443 253-654 | Usp49 | 2685391 | Q6P9L4 | UBP49_MOUSE | USP | Ubiquitin-specific peptidases | Histone modification erase | Histone ubiquitination | 23824326 | # | histone | H2Bub | H2B | 23824326 | Ubiquitin-specific peptidase 49 (USP49) is a histone H2B-specific deubiquitinase and shows that H2B deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons. | # |
USP7
(details) |
12630 | ubiquitin specific peptidase 7 (herpes virus-associated) | 7874 | Q93009 | UBP7_HUMAN | domain PF22486 70-195, UCH PF00443 214-518, USP7_ICP0_bdg PF12436 620-867, USP7_C2 PF14533 877-1086 | Usp7 | 2182061 | Q6A4J8 | UBP7_MOUSE | USP | Ubiquitin-specific peptidases | Histone modification erase, DNA modification cofactor | Histone ubiquitination, DNA methylation | 15749019 | BCOR | histone, DNA | H2Bub | H2B | 15749019 | GMP synthetase stimulates histone H2B deubiquitylation by the epigenetic silencer USP7 | # |
UTY
(details) |
12638 | ubiquitously transcribed tetratricopeptide repeat containing, Y-linked | 7404 | O14607 | UTY_HUMAN | TPR_8 PF13181 202-235, JmjC PF02373 1080-1188, KDM6_C-hel PF21322 1195-1249, KDM6_GATAL PF21326 1267-1327 | Uty | 894810 | P79457 | UTY_MOUSE | TTC | Tetratricopeptide (TTC) repeat domain containing | Histone modification erase | Histone ubiquitination | 24798337 | # | histone | H3K27me | # | 24798337 | The Jumonji C lysine demethylases (KDMs) are 2-oxoglutarate- and Fe(II)-dependent oxygenases. KDM6A (UTX) and KDM6B (JMJD3) are KDM6 subfamily members that catalyze demethylation of Nϵ-methylated histone 3 lysine 27 (H3K27), a mark important for transcriptional repression. Despite reports stating that UTY (KDM6C) is inactive as a KDM, we demonstrate by biochemical studies, employing MS and NMR, that UTY (KDM6C) is an active KDM. Crystallographic analyses reveal that the UTY(KDM6C) active site is highly conserved with those of KDM6B and KDM6A. | # |
VDR
(details) |
12679 | vitamin D (1,25- dihydroxyvitamin D3) receptor | 7421 | P11473 | VDR_HUMAN | zf-C4 PF00105 23-91, Hormone_recep PF00104 227-403 | Vdr | 103076 | P48281 | VDR_MOUSE | NR | Nuclear hormone receptors | Chromatin remodeling cofactor, TF | # | 16252006 | # | histone | H2BK12ac, H3K14ac, H4K16ac | # | 16252006 | WINAC associates with chromatin through a physical interaction between the WSTF bromodomain and acetylated histones, which appears to be indispensable for VDR/promoter association for ligand-induced transrepression of 1α(OH)ase gene expression. | # |
VIRMA
(details) |
24500 | Protein virilizer homolog | 25962 | Q69YN4 | VIR_HUMAN | VIR_N PF15912 5-278 | Virma | 1913435 | A2AIV2 | VIR_MOUSE | ARMH | Armadillo like helical domain containing | RNA modification | RNA methylation | 29507755 | WMM | RNA | A of mRNA | m6A | 29507755 | Mediates methylation in 3'UTR and near stop codon | New |
VPS72
(details) |
11644 | vacuolar protein sorting 72 homolog (S. cerevisiae) | 6944 | Q15906 | VPS72_HUMAN | YL1 PF05764 7-212, YL1_C PF08265 291-319 | Vps72 | 1202305 | Q62481 | VPS72_MOUSE | # | # | Histone modification write cofactor | Histone acetylation | 14966270 | NuA4, NuA4-related complex | chromatin | # | # | 14966270 | The YL1 =VPS72 protein is a subunit of the TRRAP/TIP60 HAT complex. The YL1 protein is also present in cells as a subunit of the previously uncharacterized mammalian SRCAP complex, which bears a striking similarity to the S. cerevisiae SWR1 chromatin remodeling complex. | # |
VRK1
(details) |
12718 | vaccinia related kinase 1 | 7443 | Q99986 | VRK1_HUMAN | Pkinase PF00069 39-271 | Vrk1 | 1261847 | Q80X41 | VRK1_MOUSE | # | # | Histone modification write | Histone phosphorylation | 22194607 | # | histone | H3S10, H3T3 | H3S10ph, H3T3ph | # | Phosphorylates histones H3-S10, H3-T3. | # |
WAC
(details) |
17327 | WW domain containing adaptor with coiled-coil | 51322 | Q9BTA9 | WAC_HUMAN | WW PF00397 133-160 | Wac | 2387357 | Q924H7 | WAC_MOUSE | # | # | Histone modification write cofactor | Histone ubiquitination | 21329877 | # | histone | # | # | # | Regulates H2B ubiquitinations. | # |
WDR5
(details) |
12757 | WD repeat domain 5 | 11091 | P61964 | WDR5_HUMAN | WD40 PF00400 38-72 78-115 119-157 161-199 203-242 246-287 292-331 | Wdr5 | 2155884 | P61965 | WDR5_MOUSE | WDR | WD repeat domain containing | Histone modification read | # | 16946699 | ATAC, NSL, RING2-L3MBTL2, COMPASS, Menin-associated_HMT, MLL-HCF, CHD8, MLL2/3, COMPASS-like MLL1,2, MLL4/WBP7, COMPASS-like MLL3,4 | histone | H3K4, H3K4me1, H3K4me2, H3K4me3 | # | 16946699 | The WD40 domain of WDR5 represents a new class of histone methyl-lysine recognition domains that is important for recruiting H3K4 methyltransferases to K4-dimethylated histone H3 tail as well as for global and gene-specific K4 trimethylation. Here is given the crystal structures of full-length WDR5, WDR5Delta23 and its complexes with unmodified, mono-, di- and trimethylated histone H3K4 peptides. | # |
WDR77
(details) |
29652 | WD repeat domain 77 | 79084 | Q9BQA1 | MEP50_HUMAN | WD40 PF00400 122-153 160-196 | Wdr77 | 1917715 | Q99J09 | MEP50_MOUSE | WDR | WD repeat domain containing | Histone modification write | Histone methylation | 22009756 | methylosome | histone | H2A, H4 | H2Ame, H4me | # | Methylates histones H2A and H4 in Xenopus. | # |
WDR82
(details) |
28826 | WD repeat domain 82 | 80335 | Q6UXN9 | WDR82_HUMAN | WD40 PF00400 15-49 98-135 228-267 | Wdr82 | 1924555 | Q8BFQ4 | WDR82_MOUSE | WDR | WD repeat domain containing | Histone modification write cofactor | Histone methylation | 17355966 | COMPASS | histone | # | # | 17355966 | A mammalian Set1A complex analogous to the yeast Set1/COMPASS histone H3-Lys4 methyltransferase complex has previously been identified. WDR82 is a regulatory component of the SET1 complex implicated in the tethering of this complex to transcriptional start sites of active genes. | # |
WHSC1
(details) |
12766 | Wolf-Hirschhorn syndrome candidate 1 | 7468 | O96028 | NSD2_HUMAN | PWWP PF00855 221-299 881-972, HMG_box PF00505 454-505, domain PF23011 668-712 1241-1284, domain PF22908 716-763, domain PF23004 764-816, PHD PF00628 834-872, AWS PF17907 1022-1060, SET PF00856 1073-1180, C5HCH PF17982 1284-1328 | Whsc1 | 1276574 | Q8BVE8 | NSD2_MOUSE | PHF | Zinc fingers, PHD-type | Histone modification write | Histone methylation | 18172012 | # | histone | H3K27 | H3K27me | 18172012 | Multiple-myeloma-related WHSC1/MMSET isoform RE-IIBP is a histone methyltransferase with transcriptional repression activity. | # |
WHSC1L1
(details) |
12767 | Wolf-Hirschhorn syndrome candidate 1-like 1 | 54904 | Q9BZ95 | NSD3_HUMAN | PWWP PF00855 269-348 962-1050, domain PF23011 700-746, domain PF22908 749-798, domain PF23004 799-851, AWS PF17907 1104-1142, SET PF00856 1155-1262, C5HCH PF17982 1366-1410 | Whsc1l1 | 2142581 | Q6P2L6 | NSD3_MOUSE | # | # | Chromatin remodeling cofactor, TF | # | 16682010 | # | histone | H3K4, H3K27 | # | 16682010 | WHISTLE =WHSC1L1 di-methylates H3K4 and di-, and tri-methylates H3K27 of histones. | # |
WSB2
(details) |
19222 | WD repeat and SOCS box containing 2 | 55884 | Q9NYS7 | WSB2_HUMAN | WD40 PF00400 145-182 188-225 231-267 289-320 338-360, SOCS_box PF07525 367-401 | Wsb2 | 2144041 | O54929 | WSB2_MOUSE | WDR | WD repeat domain containing | Histone modification write | Histone ubiquitination | 21070969 | # | histone | # | # | # | May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, including histones. (Annotated by similarity). | # |
WTAP
(details) |
16846 | Pre-mRNA-splicing regulator WTAP (Female-lethal(2)D homolog) (hFL(2)D) (WT1-associated protein) (Wilms tumor 1-associating protein) | 9589 | Q15007 | FL2D_HUMAN | Wtap PF17098 68-223 | Wtap | 1926395 | Q9ER69 | FL2D_MOUSE | # | # | RNA modification | RNA methylation | 24407421 | WMM | RNA | A of mRNA | m6A | 24407421 | Regulates recruitment of the m6A methyltransferase complex to mRNA targets | New |
YAF2
(details) |
17363 | YY1 associated factor 2 | 10138 | Q8IY57 | YAF2_HUMAN | zf-RanBP PF00641 20-43, YAF2_RYBP PF17219 104-133 | Yaf2 | 1914307 | Q99LW6 | YAF2_MOUSE | # | # | Chromatin remodeling cofactor | # | 11593398 | BCOR, RING2-L3MBTL2, RING2-FBRS | chromatin | # | # | 11593398 | Both Myc and Yaf2 could play a role in chromatin remodeling complexes. | # |
YEATS2
(details) |
25489 | YEATS domain containing 2 | 55689 | Q9ULM3 | YETS2_HUMAN | YEATS PF03366 230-310, domain PF22951 1144-1241 | Yeats2 | 2447762 | Q3TUF7 | YETS2_MOUSE | # | # | Histone chaperone | # | 18838386, 29057918 | ATAC | histone | H3K27ac | # | 18838386, 29057918 | A YEATS2-NC2beta histone fold module that interacts with the TATA-binding protein (TBP) and negatively regulates transcription when recruited to a promoter. The p38 kinase-interacting protein (p38IP/FAM48A) is a novel component of STAGA with distant similarity to yeast Spt20.YEATS2 as a histone H3K27ac reader that regulates a transcriptional program essential for NSCLC tumorigenesis. | # |
YEATS4
(details) |
24859 | YEATS domain containing 4 | 8089 | O95619 | YETS4_HUMAN | YEATS PF03366 42-121 | Yeats4 | 1927224 | Q9CR11 | YETS4_MOUSE | # | # | Histone modification write cofactor | Histone acetylation | 14966270 | NuA4, NuA4-related complex, SRCAP | histone | # | # | 14966270 | The essential GAS41 =YEATS4 protein is a member of the AF9/ENL-related (YEATS) family, and associated to transcription/chromatin-modifying complexes, including yeast NuA4, NuA3, Sas2, SWI/SNF, TFIID/mediator/TFIIF, and human SWI/SNF complexes. | # |
YTHDC1
(details) |
30626 | YTH domain-containing protein 1 (Splicing factor YT521) (YT521-B) | 91746 | Q96MU7 | YTDC1_HUMAN | YTH PF04146 355-492 | Ythdc1 | 2443713 | E9Q5K9 | YTDC1_MOUSE | # | # | RNA modification | Alternative splicing | 20167602 | # | RNA | mRNA | m6A of mRNA | 20167602 | Regulates splicing site selection of vertabrate-specific exons. | New |
YWHAB
(details) |
12849 | tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, beta | 7529 | P31946 | 1433B_HUMAN | 14-3-3 PF00244 11-231 | Ywhab | 1891917 | Q9CQV8 | 1433B_MOUSE | # | # | Histone modification erase cofactor | Histone acetylation | 10869435 | # | histone | # | # | 10869435 | Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent (=YWHAB) cellular localization. | # |
YWHAE
(details) |
12851 | tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, epsilon | 7531 | P62258 | 1433E_HUMAN | 14-3-3 PF00244 10-232 | Ywhae | 894689 | P62259 | 1433E_MOUSE | # | # | Histone modification erase cofactor | Histone acetylation | 10869435 | # | histone | # | # | 10869435 | Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent (=YWHAE) cellular localization. | # |
YWHAZ
(details) |
12855 | tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, zeta | 7534 | P63104 | 1433Z_HUMAN | 14-3-3 PF00244 9-229 | Ywhaz | 109484 | P63101 | 1433Z_MOUSE | # | # | Histone modification read | # | 16246723 | # | histone | H3 | # | 16246723 | 14-3-3 =YWHAZ isoforms are proteins that bind modified H3 tail peptide tails in a strictly phosphorylation-dependent manner. | # |
YY1
(details) |
12856 | YY1 transcription factor | 7528 | P25490 | TYY1_HUMAN | zf-C2H2 PF00096 298-320 325-347 353-377 383-407 | Yy1 | 99150 | Q00899 | TYY1_MOUSE | INO80, ZNF | INO80 complex subunits, Zinc fingers, C2H2-type | Chromatin remodeling cofactor, TF | TF repressor | 11445535 | Ino80 | DNA | DNA motif | # | 11445535 | YY1 is complex comprising components of the evolutionarily conserved INO80 chromatin-remodeling complex. | # |
ZBTB16
(details) |
12930 | zinc finger and BTB domain containing 16 | 7704 | Q05516 | ZBT16_HUMAN | BTB PF00651 25-124, zf-C2H2_6 PF13912 461-483 518-540, zf-C2H2 PF00096 490-512 546-568 574-596, domain PF12874 630-652 | Zbtb16 | 103222 | # | # | ZBTB, ZNF, BTBD | Zinc fingers, C2H2-type, BTB/POZ domain containing | Histone modification erase cofactor | Histone acetylation | 9627120, 15467736 | # | histone | # | # | # | Recruites SMRT-mSin3-HDAC co-repressor complex. The repressive domains of PLZF function by recruiting N-CoR/Sin3A co-repressor complexes which in turn recruit histone deacetylases (HDACs). | # |
ZBTB33
(details) |
16682 | zinc finger and BTB domain containing 33 | 10009 | Q86T24 | KAISO_HUMAN | BTB PF00651 22-116 | Zbtb33 | 1927290 | Q8BN78 | KAISO_MOUSE | ZBTB, BTBD, ZNF | BTB/POZ domain containing, Zinc fingers, C2H2-type | Histone modification write cofactor, Histone modification erase cofactor, TF | Histone acetylation, Histone methylation, TF repressor | 14527417 | # | DNA | CG, mCG, DNA motif | # | 14527417 | Kaiso, a methyl CpG binding protein belonging to the BTB/POZ family of transcription factors, is a component of the human N-CoR complex. In vitro, the Kaiso/N-CoR complex binds specific CpG-rich sequences in a methylation-dependent manner. In vivo, Kaiso targets the N-CoR complex to the MTA2 gene promoter in a methylation-dependent manner. This repression also requires a functional N-CoR deacetylase complex, which brings about histone hypoacetylation and methylation of H3 lysine 9 to the MTA2 locus. | # |
ZBTB7A
(details) |
18078 | Zinc finger and BTB domain-containing protein 7A (Factor binding IST protein 1) (FBI-1) (Factor that binds to inducer of short transcripts protein 1) (HIV-1 1st-binding protein 1) (Leukemia/lymphoma-related factor) (POZ and Krueppel erythroid myeloid ontogenic factor) (POK erythroid myeloid ontogenic factor) (Pokemon) (Pokemon 1) (TTF-I-interacting peptide 21) (TIP21) (Zinc finger protein 857A) | 51341 | O95365 | ZBT7A_HUMAN | BTB PF00651 24-129, zf-C2H2 PF00096 410-432 438-460 | Zbtb7A | 1335091 | O88939 | ZBT7A_MOUSE | BTBD | BTB domain containing | RNA modification | Alternative splicing | 24514149 | # | RNA | mRNA | # | 24514149 | Regulates alternative splicing of BCL-X and apoptotic factors | New |
ZBTB7C
(details) |
31700 | zinc finger and BTB domain containing 7C | 201501 | A1YPR0 | ZBT7C_HUMAN | BTB PF00651 24-128, zf-C2H2 PF00096 392-414 448-469 | Zbtb7c | 2443302 | Q8VCZ7 | ZBT7C_MOUSE | ZBTB, ZNF, BTBD | Zinc fingers, C2H2-type, BTB/POZ domain containing | Histone modification cofactor | # | 21804610 | # | histone | # | # | 21804610 | Kr-pok =ZBTB7C competes with MIZ-1 in binding to these elements and represses transcription by inhibiting MIZ-1/p300 recruitment, which decreases the acetylation of histones H3 and H4. | # |
ZC3H13
(details) |
20368 | Zinc finger CCCH domain-containing protein 13 | 23091 | Q5T200 | ZC3HD_HUMAN | zf-CCCH PF00642 40-62 | Zc3h13 | 1914552 | E9Q784 | ZC3HD_MOUSE | ZC3H | Zinc fingers CCCH-type | RNA modification | RNA methylation | 29507755 | WMM | RNA | A of mRNA | m6A | 29507755 | Binds WTAP to RBM15 or RBM15B RNA-binding component | New |
ZCWPW1
(details) |
23486 | zinc finger, CW type with PWWP domain 1 | 55063 | Q9H0M4 | ZCPW1_HUMAN | zf-CW PF07496 256-302, PWWP PF00855 318-412 | Zcwpw1 | 2685899 | Q6IR42 | ZCPW1_MOUSE | # | # | Histone modification read | # | 21423274 | # | histone | H3K4me | # | 21423274 | Table 1 in the reference. | # |
ZFP57
(details) |
18791 | ZFP57 zinc finger protein | 346171 | Q9NU63 | ZFP57_HUMAN | KRAB PF01352 16-56, zf-C2H2 PF00096 91-113 119-141 147-169 175-197 300-322 328-350 | Zfp57 | 99204 | Q8C6P8 | ZFP57_MOUSE | # | # | TF | TF repressor | # | # | DNA | mC, DNA motif | # | # | Acts by controlling DNA methylation during the earliest multicellular stages of development at multiple imprinting control regions. (UniProt) | # |
ZGPAT
(details) |
15948 | zinc finger, CCCH-type with G patch domain | 84619 | Q8N5A5 | ZGPAT_HUMAN | zf-CCCH_4 PF18044 177-199, G-patch PF01585 333-376 | Zgpat | 2449939 | Q8VDM1 | ZGPAT_MOUSE | ZC3H, GPATCH | Zinc fingers, CCCH-type domain containing, "G patch domain containing" | TF | TF repressor | 22498752 | # | DNA | DNA motif | # | # | Recruits the chromatin multiprotein complex NuRD to target promoters. | # |
ZHX1
(details) |
12871 | zinc fingers and homeoboxes 1 | 11244 | Q9UKY1 | ZHX1_HUMAN | zf_C2H2_ZHX PF18387 99-151, Homeodomain PF00046 299-340 469-521 575-622 666-717, Homez PF11569 784-822 | Zhx1 | 109271 | P70121 | ZHX1_MOUSE | ZNF, ZFHX | Zinc fingers, C2H2-type, Homeoboxes / ZF class | Chromatin remodeling, Histone modification write cofactor | Histone acetylation, Histone methylation | 17303076 | # | histone | # | # | 17303076 | Presence of a PWWP domain is required for interaction of ZHX1. This domain may function as a site of protein–protein interaction and influence chromatin remodeling, and thereby facilitate the fine tuning of transcriptional processes. | # |
ZMYM2
(details) |
12989 | zinc finger, MYM-type 2 | 7750 | Q9UBW7 | ZMYM2_HUMAN | zf-FCS PF06467 328-364 371-412 422-457 465-504 534-571 637-674 681-716 725-762 766-803, DUF3504 PF12012 1190-1359 | Zmym2 | 1923257 | Q9CU65 | ZMYM2_MOUSE | ZMYM | Zinc fingers, MYM type | Histone modification erase cofactor, TF | Histone acetylation | 12493763 | BHC, LSD-CoREST | DNA | DNA motif | # | 12493763 | A family of HDAC1,2-associated complexes includes proteins with a putative role in DNA binding such as ZNF261/XFIM (=ZMYM3), ZNF198/FIM (=ZMYM2), and ZNF217. | # |
ZMYM3
(details) |
13054 | zinc finger, MYM-type 3 | 9203 | Q14202 | ZMYM3_HUMAN | zf-FCS PF06467 353-389 406-444 449-490 497-535 546-580 591-624 632-664 676-714 718-754, DUF3504 PF12012 1184-1354 | Zmym3 | 1927231 | Q9JLM4 | ZMYM3_MOUSE | ZMYM | Zinc fingers, MYM type | Histone modification erase cofactor | Histone acetylation | 12493763 | BHC | DNA | # | # | 12493763 | A family of HDAC1,2-associated complexes includes proteins with a putative role in DNA binding such as ZNF261/XFIM (=ZMYM3), ZNF198/FIM (=ZMYM2), and ZNF217. | # |
ZMYND11
(details) |
16966 | zinc finger, MYND-type containing 11 | 10771 | Q15326 | ZMY11_HUMAN | SAMD1_WH PF21524 18-68, Bromodomain PF00439 184-241, PWWP PF00855 281-351 | Zmynd11 | 1913755 | Q8R5C8 | ZMY11_MOUSE | ZMYND | Zinc fingers, MYND-type | Histone modification read | Histone methylation | 22498752 | # | histone | H3.3K36me3 | # | # | ZMYND11 recognizes and binds histone H3.3 trimethylated at Lys-36 (H3.3K36me3), according to UniProt. | # |
ZMYND8
(details) |
9397 | zinc finger, MYND-type containing 8 | 23613 | Q9ULU4 | PKCB1_HUMAN | PHD PF00628 91-130, Bromodomain PF00439 165-239, PWWP PF00855 280-348, DUF3544 PF12064 412-608 | Zmynd8 | 1918025 | # | # | ZMYND, PHF | Zinc fingers, MYND-type, "Zinc fingers, PHD-type" | Histone modification erase cofactor | Histone acetylation | 25123934 | # | histone | # | # | # | ZMYND8 is part of the NuRD complex. | # |
ZNF217
(details) |
13009 | zinc finger protein 217 | 7764 | O75362 | ZN217_HUMAN | zf-C2H2 PF00096 128-150 156-178 377-397 472-493 | # | # | # | # | ZNF | Zinc fingers, C2H2-type | Histone modification erase cofactor, TF | Histone acetylation, TF repressor | 12493763 | BHC, LSD-CoREST | DNA | # | # | 12493763 | A family of HDAC1,2-associated complexes includes proteins with a putative role in DNA binding such as ZNF261/XFIM (=ZMYM3), ZNF198/FIM (=ZMYM2), and ZNF217. | # |
ZNF516
(details) |
28990 | zinc finger protein 516 | 9658 | Q92618 | ZN516_HUMAN | zf-C2H2 PF00096 34-56 62-84 248-270 276-298 1098-1120 | Zfp516 | 2443957 | Q7TSH3 | ZN516_MOUSE | ZNF | Zinc fingers, C2H2-type | Histone modification erase cofactor, TF | Histone acetylation, TF repressor | 23752268 | LSD-CoREST | histone, DNA | # | # | 23752268 | Part of the HDAC interactome, TF annotation from Uniprot. | # |
ZNF532
(details) |
30940 | zinc finger protein 532 | 55205 | Q9HCE3 | ZN532_HUMAN | zf-C2H2_11 PF16622 1203-1226, zf-C2H2_6 PF13912 1264-1286 | Zfp532 | 3036282 | Q6NXK2 | ZN532_MOUSE | ZNF | Zinc fingers, C2H2-type | Histone modification erase cofactor | Histone acetylation | 25123934 | # | histone | # | # | # | A member of NuRD complex. | # |
ZNF541
(details) |
25294 | zinc finger protein 541 | 84215 | Q9H0D2 | ZN541_HUMAN | zf-C2H2 PF00096 140-162, zf-C2H2_6 PF13912 168-190 1289-1312, ELM2 PF01448 1055-1111 | Zfp541 | 3647699 | Q0GGX2 | ZN541_MOUSE | ZNF | Zinc fingers, C2H2-type | Chromatin remodeling | # | 18849567 | # | chromatin | # | # | # | Forms a complex with chromatin remodeling activity during spermatogenesis. UniProt: Component of some chromatin remodeling multiprotein complex that plays a role during spermatogenesis (by similarity). | # |
ZNF592
(details) |
28986 | zinc finger protein 592 | 9640 | Q92610 | ZN592_HUMAN | zf-C2H2_11 PF16622 1153-1176 | Zfp592 | 2443541 | Q8BHZ4 | ZN592_MOUSE | ZNF | Zinc fingers, C2H2-type | Histone modification erase cofactor | Histone acetylation | 25123934 | # | histone | # | # | # | A member of NuRD complex. | # |
ZNF687
(details) |
29277 | zinc finger protein 687 | 57592 | Q8N1G0 | ZN687_HUMAN | zf-C2H2 PF00096 993-1016 1200-1222, zf-C2H2_11 PF16622 1135-1158 | Zfp687 | 1925516 | Q9D2D7 | ZN687_MOUSE | # | # | Histone modification erase cofactor | Histone acetylation | 25123934 | # | histone | # | # | # | A member of NuRD complex. | # |
ZNF711
(details) |
13128 | zinc finger protein 711 | 7552 | Q9Y462 | ZN711_HUMAN | Zfx_Zfy_act PF04704 62-356, zf-C2H2 PF00096 383-405 505-527 562-584 590-613 619-641 676-698 704-727 733-755 | Zfp711 | 3045342 | A2ANX9 | ZN711_MOUSE | ZNF | Zinc fingers, C2H2-type | Histone modification erase cofactor | Histone acetylation | 20346720 | # | histone | # | # | 20346720 | The PHD domain of PHF8 binds to H3K4me3 and colocalizes with H3K4me3 at transcription initiation sites. Furthermore, PHF8 interacts with another XMLR protein, ZNF711, which binds to a subset of PHF8 target genes, including the XLMR gene JARID1C. | # |
ZNHIT1
(details) |
21688 | zinc finger, HIT-type containing 1 | 10467 | O43257 | ZNHI1_HUMAN | zf-HIT PF04438 113-141 | Znhit1 | 1917353 | Q8R331 | ZNHI1_MOUSE | ZNHIT | Zinc fingers, HIT-type | Chromatin remodeling cofactor, Histone modification erase cofactor | Histone acetylation | 15647280 | SRCAP | histone | # | # | 15647280 | YL1 protein is also present in cells as a subunit of the previously uncharacterized mammalian SRCAP complex, which bears a striking similarity to the recently described S. cerevisiae SWR1 chromatin remodeling complex and is composed of the SNF2-related SRCAP helicase, ARP6, ZnF/HIT1. | # |
ZRANB3
(details) |
25249 | zinc finger, RAN-binding domain containing 3 | 84083 | Q5FWF4 | ZRAB3_HUMAN | SNF2-rel_dom PF00176 40-299, Helicase_C PF00271 329-435, zf-RanBP PF00641 623-648, HNH PF01844 1014-1049 | Zranb3 | 1918362 | Q6NZP1 | ZRAB3_MOUSE | ZRANB | Zinc fingers, RAN-binding domain containing | Chromatin remodeling, Histone modification read cofactor | Histone methylation | 22705370 | # | histone | # | # | 22705370 | All four proteins (HARP, HARP-like domain (HPL), SMARCA1, RAD54L) belong to the SNF2 =ZRANB3 family, whose members participate in a variety of processes including chromatin remodeling, transcription, DNA repair, and recombination. | # |
ZZZ3
(details) |
24523 | zinc finger, ZZ-type containing 3 | 26009 | Q8IYH5 | ZZZ3_HUMAN | Myb_DNA-binding PF00249 655-703, ZZ PF00569 818-865 | Zzz3 | 1920453 | Q6KAQ7 | ZZZ3_MOUSE | ZZZ | Zinc fingers, ZZ-type | Histone modification read | # | 19103755 | ATAC | histone | # | # | 19103755 | The SANT domain of c-Myb has been shown to bind histone H3 tails and position them for acetylation (35). Moreover, the SANT domains in ADA2a and ZZZ3/ATAC1 might enable the complex to associate with nucleosome tails in order to potentiate the catalytic activities of GCN5 and ATAC2, similar to what has been shown for the SANT domains in yeast Ada2 and Swi3. | # |