PCGF6
entrez
84108
canonical
uniprot
Q9BYE7
canonical
ensembl
ENSG00000156374
resolver
ensp
ENSP00000338845
resolver
ensp
ENSP00000358862
resolver
ensp
ENSP00000653210
resolver
ensp
ENSP00000653211
resolver
ensp
ENSP00000759839
resolver
genesymbol
PCGF6
resolver
genesymbol_syn
MBLR
resolver
genesymbol_syn
RNF134
resolver
hgnc
HGNC:21156
resolver
uniprot
A8K3R4
resolver
uniprot
Q5SYD1
resolver
uniprot
Q5SYD6
resolver
uniprot
Q96ID9
resolver
uniprot
Q96SJ1
resolver
uniprot_entry
PCGF6_HUMAN
resolver
uniprot_sec
A8K3R4
resolver
uniprot_sec
Q5SYD1
resolver
uniprot_sec
Q5SYD6
resolver
uniprot_sec
Q96ID9
resolver
uniprot_sec
Q96SJ1
resolver
amino_acid_sequence
MEGVAVVTAGSVGAAKTEGAAALPPPPPVSPPALTPAPAAGEEGPAPLSETGAPGCSGSRPPELEPERSLGRFRGRFEDEDEELEEEEELEEEEEEEEEDMSHFSLRLEGGRQDSEDEEERLINLSELTPYILCSICKGYLIDATTITECLHTFCKSCIVRHFYYSNRCPKCNIVVHQTQPLYNIRLDRQLQDIVYKLVINLEEREKKQMHDFYKERGLEVPKPAVPQPVPSSKGRSKKVLESVFRIPPELDMSLLLEFIGANEGTGHFKPLEKKFVRVSGEATIGHVEKFLRRKMGLDPACQVDIICGDHLLEQYQTLREIRRAIGDAAMQDGLLVLHYGLVVSPLKIT
uniprot
proteins
function
FUNCTION: Transcriptional repressor (PubMed:12167161). May modulate the levels of histone H3K4Me3 by activating KDM5D histone demethylase (PubMed:17320162). Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (PubMed:12167161). Within the PRC1-like complex, regulates RNF2 ubiquitin ligase activity (PubMed:26151332). {ECO:0000269|PubMed:12167161, ECO:0000269|PubMed:17320162, ECO:0000269|PubMed:26151332}.
uniprot
proteins
mass_dalton
39047
uniprot
proteins
mutagenesis
MUTAGEN 30; /note="S->A: Abolishes phosphorylation."; /evidence="ECO:0000269|PubMed:12167161"; MUTAGEN 57; /note="S->A: Does not abolish phosphorylation."; /evidence="ECO:0000269|PubMed:12167161"; MUTAGEN 59; /note="S->A: Does not abolish phosphorylation."; /evidence="ECO:0000269|PubMed:12167161"; MUTAGEN 69; /note="S->A: Does not abolish phosphorylation."; /evidence="ECO:0000269|PubMed:12167161
uniprot
proteins
post_translational_modification
PTM: Phosphorylated during mitosis. Phosphorylated on Ser-30 by CDK7 in vitro. {ECO:0000269|PubMed:12167161}.
uniprot
proteins
pubmed
12167161
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17320162
uniprot
proteins
pubmed
19636380
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21282530
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26151332
uniprot
proteins
pubmed
28112733
uniprot
proteins
sequence_length
350
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12167161, ECO:0000269|PubMed:21282530}.
uniprot
proteins