ID   Q6IB93_HUMAN            Unreviewed;       326 AA.
AC   Q6IB93;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   04-NOV-2026, entry version 105.
DE   RecName: Full=Polycomb complex protein BMI-1 {ECO:0000256|ARBA:ARBA00039211};
DE   AltName: Full=Polycomb group RING finger protein 4 {ECO:0000256|ARBA:ARBA00042731};
GN   Name=COMMD3 {ECO:0000313|EMBL:CAG33192.1};
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 {ECO:0000313|EMBL:CAG33192.1};
RN   [1] {ECO:0000313|EMBL:CAG33192.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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       The complex composed of RNF2, UB2D3 and BMI1 binds nucleosomes, and has
CC       activity only with nucleosomal histone H2A. In the PRC1-like complex,
CC       regulates the E3 ubiquitin-protein ligase activity of RNF2/RING2.
CC       {ECO:0000256|ARBA:ARBA00045235}.
CC   -!- SUBUNIT: Component of a PRC1-like complex. Identified in a PRC1-like
CC       HPRC-H complex with CBX2, CBX4, CBX8, PHC1, PHC2, PHC3 RING1 and RNF2.
CC       Interacts with RNF2/RING2. Interacts with RING1. Part of a complex that
CC       contains RNF2, UB2D3 and BMI1, where RNF2 and BMI1 form a tight
CC       heterodimer, and UB2D3 interacts only with RNF2. The complex composed
CC       of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with
CC       nucleosomal histone H2A. Interacts with CBX7 and CBX8. Interacts with
CC       SPOP. Part of a complex consisting of BMI1, CUL3 and SPOP. Interacts
CC       with E4F1. Interacts with PHC2. Interacts with zinc finger protein
CC       ZNF277. May be part of a complex including at least ZNF277, BMI1 and
CC       RNF2/RING2. {ECO:0000256|ARBA:ARBA00064957}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR456911; CAG33192.1; -; mRNA.
DR   SMR; Q6IB93; -.
DR   PeptideAtlas; Q6IB93; -.
DR   OrthoDB; 1917519at2759; -.
DR   CDD; cd17165; RAWUL_PCGF4; 1.
DR   CDD; cd16736; RING-HC_PCGF4; 1.
DR   FunFam; 3.10.20.90:FF:000106; Polycomb complex protein BMI-1; 1.
DR   FunFam; 3.30.40.10:FF:000082; Polycomb group ring finger 2; 1.
DR   Gene3D; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR032443; RAWUL.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR10825:SF21; POLYCOMB COMPLEX PROTEIN BMI-1; 1.
DR   PANTHER; PTHR10825; RING FINGER DOMAIN-CONTAINING, POLYCOMB GROUP COMPONENT; 1.
DR   Pfam; PF16207; RAWUL; 1.
DR   Pfam; PF13923; zf-C3HC4_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   GO; GO:0035102; C:PRC1 complex; IEA:UniProtKB-ARBA.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; IEA:UniProtKB-ARBA.
DR   AlphaFoldDB; Q6IB93; -.
DR   EMDB; EMD-34207; -.
PE   2: Evidence at transcript level;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          18..57
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          236..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..278
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..326
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   326 AA;  36922 MW;  AEE46F18B64F849B CRC64;
     MHRTTRIKIT ELNPHLMCVL CGGYFIDATT IIECLHSFCK TCIVRYLETS KYCPICDVQV
     HKTRPLLNIR SDKTLQDIVY KLVPGLFKNE MKRRRDFYAA HPSADAANGS SEDRGEVADE
     DKRIITDDEI ISLSIEFFDQ NRLDRKVNKD KEKSKEEVND KRYLRCPAAM TVMHLRKFLR
     SKMDIPNTFQ IDVMYEEEPL KDYYTLMDIA YIYTWRRNGP LPLKYRVRPT CKRMKISHQR
     DGLTNAGELE SDSGSDKANS PAGGIPSTSS CLPSPSTPVQ SPHPQFPHIS STMNGTSNSP
     SGNHQSSFAN RPRKSSVNGS SATSSG
//