PCGF3_HUMAN
ID PCGF3_HUMAN Reviewed; 242 AA.
AC Q3KNV8; D3DVN1; O15262;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Polycomb group RING finger protein 3;
DE AltName: Full=RING finger protein 3A;
GN Name=PCGF3; Synonyms=RNF3, RNF3A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Abdul-Rauf M., Dyer M.J.;
RT "Interactions of the BCL7A protein with novel ring finger proteins.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION IN A PRC1-LIKE COMPLEX, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH CBX6; CBX7 AND CBX8.
RX PubMed=21282530; DOI=10.1074/mcp.m110.002642;
RA Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O.;
RT "Interaction proteomics analysis of polycomb proteins defines distinct PRC1
RT Complexes in mammalian cells.";
RL Mol. Cell. Proteomics 0:0-0(2011).
RN [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=26151332; DOI=10.1038/ncomms8621;
RA Taherbhoy A.M., Huang O.W., Cochran A.G.;
RT "BMI1-RING1B is an autoinhibited RING E3 ubiquitin ligase.";
RL Nat. Commun. 6:7621-7621(2015).
RN [6]
RP INTERACTION WITH BCORL1.
RX PubMed=27568929; DOI=10.1016/j.str.2016.07.011;
RA Wong S.J., Gearhart M.D., Taylor A.B., Nanyes D.R., Ha D.J., Robinson A.K.,
RA Artigas J.A., Lee O.J., Demeler B., Hart P.J., Bardwell V.J., Kim C.A.;
RT "KDM2B Recruitment of the Polycomb Group Complex, PRC1.1, Requires
RT Cooperation between PCGF1 and BCORL1.";
RL Structure 24:1795-1801(2016).
CC -!- FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like
CC complex, a complex class required to maintain the transcriptionally
CC repressive state of many genes, including Hox genes, throughout
CC development. PcG PRC1 complex acts via chromatin remodeling and
CC modification of histones; it mediates monoubiquitination of histone H2A
CC 'Lys-119', rendering chromatin heritably changed in its expressibility.
CC Within the PRC1-like complex, regulates RNF2 ubiquitin ligase activity
CC (PubMed:26151332). Plays a redundant role with PCGF5 as part of a PRC1-
CC like complex that mediates monoubiquitination of histone H2A 'Lys-119'
CC on the X chromosome and is required for normal silencing of one copy of
CC the X chromosome in XX females (By similarity).
CC {ECO:0000250|UniProtKB:Q8BTQ0, ECO:0000269|PubMed:26151332}.
CC -!- SUBUNIT: Component of a PRC1-like complex that contains PCGF3, RNF2 and
CC RYBP (PubMed:21282530, PubMed:26151332). Interacts with CBX6, CBX7 and
CC CBX8 (PubMed:21282530). Interacts with BCORL1 (PubMed:27568929).
CC {ECO:0000269|PubMed:21282530, ECO:0000269|PubMed:26151332,
CC ECO:0000269|PubMed:27568929}.
CC -!- INTERACTION:
CC Q3KNV8; Q6W2J9-4: BCOR; NbExp=3; IntAct=EBI-2339807, EBI-10208579;
CC Q3KNV8; O95503: CBX6; NbExp=2; IntAct=EBI-2339807, EBI-3951758;
CC Q3KNV8; O95931: CBX7; NbExp=2; IntAct=EBI-2339807, EBI-3923843;
CC Q3KNV8; Q9HC52: CBX8; NbExp=4; IntAct=EBI-2339807, EBI-712912;
CC Q3KNV8; Q8IXK0: PHC2; NbExp=3; IntAct=EBI-2339807, EBI-713786;
CC Q3KNV8; Q06587: RING1; NbExp=5; IntAct=EBI-2339807, EBI-752313;
CC Q3KNV8; Q99496: RNF2; NbExp=5; IntAct=EBI-2339807, EBI-722416;
CC Q3KNV8-2; P78364: PHC1; NbExp=5; IntAct=EBI-12818023, EBI-725403;
CC Q3KNV8-2; Q06587: RING1; NbExp=3; IntAct=EBI-12818023, EBI-752313;
CC Q3KNV8-2; Q99496: RNF2; NbExp=3; IntAct=EBI-12818023, EBI-722416;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21282530}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:Q8BTQ0}. Note=Recruited by the non-
CC coding RNA Xist to specific nuclear foci that probably correspond to
CC the inactivated X chromosome. {ECO:0000250|UniProtKB:Q8BTQ0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3KNV8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3KNV8-2; Sequence=VSP_023115;
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DR EMBL; AJ001019; CAA04477.1; -; mRNA.
DR EMBL; CH471131; EAW82652.1; -; Genomic_DNA.
DR EMBL; CH471131; EAW82653.1; -; Genomic_DNA.
DR EMBL; CH471131; EAW82656.1; -; Genomic_DNA.
DR EMBL; BC107061; AAI07062.1; -; mRNA.
DR CCDS; CCDS3339.2; -. [Q3KNV8-1]
DR RefSeq; NP_001304765.1; NM_001317836.1. [Q3KNV8-1]
DR RefSeq; NP_006306.2; NM_006315.5. [Q3KNV8-1]
DR AlphaFoldDB; Q3KNV8; -.
DR SMR; Q3KNV8; -.
DR BioGRID; 115618; 84.
DR DIP; DIP-52782N; -.
DR IntAct; Q3KNV8; 38.
DR MINT; Q3KNV8; -.
DR STRING; 9606.ENSP00000354724; -.
DR iPTMnet; Q3KNV8; -.
DR PhosphoSitePlus; Q3KNV8; -.
DR BioMuta; PCGF3; -.
DR DMDM; 121942537; -.
DR EPD; Q3KNV8; -.
DR jPOST; Q3KNV8; -.
DR MassIVE; Q3KNV8; -.
DR MaxQB; Q3KNV8; -.
DR PaxDb; Q3KNV8; -.
DR PeptideAtlas; Q3KNV8; -.
DR PRIDE; Q3KNV8; -.
DR ProteomicsDB; 61705; -. [Q3KNV8-1]
DR ProteomicsDB; 61706; -. [Q3KNV8-2]
DR Antibodypedia; 4972; 162 antibodies from 29 providers.
DR DNASU; 10336; -.
DR Ensembl; ENST00000362003.9; ENSP00000354724.5; ENSG00000185619.18. [Q3KNV8-1]
DR Ensembl; ENST00000470161.6; ENSP00000420489.2; ENSG00000185619.18. [Q3KNV8-1]
DR GeneID; 10336; -.
DR KEGG; hsa:10336; -.
DR MANE-Select; ENST00000362003.10; ENSP00000354724.5; NM_006315.7; NP_006306.2.
DR UCSC; uc003gbe.4; human. [Q3KNV8-1]
DR CTD; 10336; -.
DR DisGeNET; 10336; -.
DR GeneCards; PCGF3; -.
DR HGNC; HGNC:10066; PCGF3.
DR HPA; ENSG00000185619; Low tissue specificity.
DR neXtProt; NX_Q3KNV8; -.
DR OpenTargets; ENSG00000185619; -.
DR PharmGKB; PA34433; -.
DR VEuPathDB; HostDB:ENSG00000185619; -.
DR eggNOG; KOG2660; Eukaryota.
DR GeneTree; ENSGT00940000158395; -.
DR HOGENOM; CLU_046427_4_1_1; -.
DR InParanoid; Q3KNV8; -.
DR OMA; ILCNNEL; -.
DR OrthoDB; 1203951at2759; -.
DR PhylomeDB; Q3KNV8; -.
DR TreeFam; TF324206; -.
DR PathwayCommons; Q3KNV8; -.
DR SignaLink; Q3KNV8; -.
DR BioGRID-ORCS; 10336; 17 hits in 1119 CRISPR screens.
DR ChiTaRS; PCGF3; human.
DR GenomeRNAi; 10336; -.
DR Pharos; Q3KNV8; Tbio.
DR PRO; PR:Q3KNV8; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q3KNV8; protein.
DR Bgee; ENSG00000185619; Expressed in sural nerve and 194 other tissues.
DR ExpressionAtlas; Q3KNV8; baseline and differential.
DR Genevisible; Q3KNV8; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031519; C:PcG protein complex; IDA:UniProtKB.
DR GO; GO:0035102; C:PRC1 complex; IBA:GO_Central.
DR GO; GO:0000805; C:X chromosome; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036353; P:histone H2A-K119 monoubiquitination; ISS:UniProtKB.
DR GO; GO:0060819; P:inactivation of X chromosome by genomic imprinting; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR032443; RAWUL.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF16207; RAWUL; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Metal-binding; Nucleus; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..242
FT /note="Polycomb group RING finger protein 3"
FT /id="PRO_0000277864"
FT ZN_FING 17..56
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 115..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..242
FT /note="Interaction with BCORL1"
FT /evidence="ECO:0000269|PubMed:27568929"
FT VAR_SEQ 1
FT /note="M -> MEFPKM (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_023115"
SQ SEQUENCE 242 AA; 28115 MW; 202A607F571B249C CRC64;
MLTRKIKLWD INAHITCRLC SGYLIDATTV TECLHTFCRS CLVKYLEENN TCPTCRIVIH
QSHPLQYIGH DRTMQDIVYK LVPGLQEAEM RKQREFYHKL GMEVPGDIKG ETCSAKQHLD
SHRNGETKAD DSSNKEAAEE KPEEDNDYHR SDEQVSICLE CNSSKLRGLK RKWIRCSAQA
TVLHLKKFIA KKLNLSSFNE LDILCNEEIL GKDHTLKFVV VTRWRFKKAP LLLHYRPKMD
LL
