ID BMI1_PONAB Reviewed; 326 AA.
AC Q5R8L2;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 24-JAN-2024, entry version 104.
DE RecName: Full=Polycomb complex protein BMI-1;
DE AltName: Full=Polycomb group RING finger protein 4;
GN Name=BMI1; Synonyms=PCGF4;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-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:0000250|UniProtKB:P35226}.
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 (By similarity). Interacts with RING1 (By
CC similarity). Part of a complex that contains RNF2, UB2D3 and BMI1,
CC where RNF2 and BMI1 form a tight heterodimer, and UB2D3 interacts only
CC with RNF2. The complex composed of RNF2, UB2D3 and BMI1 binds
CC nucleosomes, and has activity only with nucleosomal histone H2A.
CC Interacts with CBX7 and CBX8. Interacts with SPOP. Part of a complex
CC consisting of BMI1, CUL3 and SPOP. Interacts with E4F1. Interacts with
CC PHC2 (By similarity). Interacts with zinc finger protein ZNF277 (By
CC similarity). May be part of a complex including at least ZNF277, BMI1
CC and RNF2/RING2 (By similarity). {ECO:0000250|UniProtKB:P25916,
CC ECO:0000250|UniProtKB:P35226}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P35226}. Cytoplasm
CC {ECO:0000250|UniProtKB:P35226}.
CC -!- INDUCTION: Down-regulated by oxidative stress.
CC {ECO:0000250|UniProtKB:P25916}.
CC -!- PTM: May be polyubiquitinated; which does not lead to proteasomal
CC degradation. Monoubiquitinated. {ECO:0000250}.
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DR EMBL; CR859740; CAH91898.1; -; mRNA.
DR RefSeq; NP_001126098.1; NM_001132626.1.
DR AlphaFoldDB; Q5R8L2; -.
DR SMR; Q5R8L2; -.
DR STRING; 9601.ENSPPYP00000002492; -.
DR Ensembl; ENSPPYT00000002567.3; ENSPPYP00000002492.2; ENSPPYG00000002144.3.
DR GeneID; 100173052; -.
DR KEGG; pon:100173052; -.
DR CTD; 648; -.
DR eggNOG; KOG2660; Eukaryota.
DR GeneTree; ENSGT00940000156042; -.
DR HOGENOM; CLU_046427_0_0_1; -.
DR InParanoid; Q5R8L2; -.
DR OrthoDB; 460116at2759; -.
DR TreeFam; TF324206; -.
DR Proteomes; UP000001595; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031519; C:PcG protein complex; ISS:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; ISS:UniProtKB.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; ISS:UniProtKB.
DR CDD; cd17165; RAWUL_PCGF4; 1.
DR CDD; cd16736; RING-HC_PCGF4; 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.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Cytoplasm; Metal-binding; Nucleus; Proto-oncogene;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..326
FT /note="Polycomb complex protein BMI-1"
FT /id="PRO_0000296628"
FT ZN_FING 18..57
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 162..182
FT /note="Interaction with PHC2"
FT /evidence="ECO:0000250|UniProtKB:P35226"
FT REGION 164..228
FT /note="Interaction with E4F1"
FT /evidence="ECO:0000250|UniProtKB:P35226"
FT REGION 236..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 81..95
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 244..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 326 AA; 36949 MW; 030A7D396BADA543 CRC64;
MHRTTRIKIT ELNPHLMCVL CGGYFIDATT IIECLHSFCK TCIVRYLETS KYCPICDVQV
HKTRPLLNIR SDKTLQDIVY KLVPGLFKNE MKRRRDFYAA HPSADAANGS NEDRGEVADE
DKRIITDDEI ISLSIEFFDQ NRLDRKVNKD KEKSKEEVND KRYLRCPAAM TVMHLRKFLR
SKMDIPNTFQ IDVMYEEEPL KDYYTLMDIA YIYTWRRNGP LPLKYRVRPT CKRMKISHQR
DGLTNAGELE SDSGSDKANS PAGGIPSTSS CLPSPSTPVQ SPHPQFPHIS STMNGTSNSP
SGNHQSSFAN RPRKSSVNGS SATSSG
//
