| 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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
|
ARID1A
(details) |
11110 | AT rich interactive domain 1A (SWI-like) | 8289 | O14497 | ARI1A_HUMAN | ARID PF01388 1018-1104, BAF250_C PF12031 1970-2222 | Arid1a | 1935147 | A2BH40 | ARI1A_MOUSE | ARID | # | Chromatin remodeling cofactor | # | 18448678 | BAF, nBAF, npBAF, PBAF, SWI/SNF_Brg1(I), SWI/SNF_Brg1(II), SWI/SNF_Brm, WINAC, bBAF, SWI/SNF BRM-BRG1 | DNA | DNA motif | # | 18448678 | BAF250a=ARID1A mediated chromatin remodeling plays a critical role in maintaining a particular chromatin configuration of its target genes that is essential for ES pluripotency and mesoderm formation. | # |
|
ARID1B
(details) |
18040 | AT rich interactive domain 1B (SWI1-like) | 57492 | Q8NFD5 | ARI1B_HUMAN | ARID PF01388 1137-1223, BAF250_C PF12031 2006-2266 | Arid1b | 1926129 | # | # | ARID | # | Histone modification write | Histone ubiquitination | 20086098 | BAF, nBAF, npBAF, PBAF, SWI/SNF-like_EPAFa, SWI/SNF-like EPAFB, SWI/SNF BRM-BRG1 | histone, DNA | H2BK120, DNA motif | # | 20086098 | The characteristic member of human SWI/SNF-A is BAF250/ARID1, of which there are two isoforms, BAF250a/ARID1a and BAF250b/ARID1b. The immunopurified BAF250b E3 ubiquitin ligase was found to target histone H2B at lysine 120 for monoubiquitination in vitro. | # |
|
EID1
(details) |
1191 | EP300 interacting inhibitor of differentiation 1 | 23741 | Q9Y6B2 | EID1_HUMAN | Eid1 | 1889651 | Q9DCR4 | EID1_MOUSE | # | # | Histone modification write cofactor | Histone acetylation | 11073990 | # | histone | # | # | 11073990 | Inhibition of MyoD may be explained by EID-1's ability to bind and inhibit p300's histone acetylase activity, an essential MyoD coactivator. Thus, EID-1 binds both Rb and p300 and is a novel repressor of MyoD function. | # | |
|
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. | # |
|
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. | # |