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
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. #
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. #
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. #
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. #
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 #
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. #
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. #
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. #
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). #
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. #
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. #
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. #
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. #
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, #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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.) #
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. #
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 . #
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. #
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. #
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. #
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. #
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. #
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). #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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). #
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. #
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. #
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. #
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. #
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. #
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). #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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). #
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. #
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. #
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. #
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. #
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 #
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. #
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. #
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. #
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 #
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. #
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. #
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). #
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). #
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. #
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). #
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. #
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. #
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. #
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. #
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 #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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). #
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.) #
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. #
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. #
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. #
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. #
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. #
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) #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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). #
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. #
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. #
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. #
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. #
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). #
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. #
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. #
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. #
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. #
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.) #
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). #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #
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. #