BMI1_BOVIN
ID BMI1_BOVIN Reviewed; 326 AA.
AC Q32KX7;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Polycomb complex protein BMI-1;
DE AltName: Full=Polycomb group RING finger protein 4;
GN Name=BMI1; Synonyms=PCGF4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) 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; BC109871; AAI09872.1; -; mRNA.
DR RefSeq; NP_001033161.1; NM_001038072.1.
DR AlphaFoldDB; Q32KX7; -.
DR SMR; Q32KX7; -.
DR STRING; 9913.ENSBTAP00000020705; -.
DR PaxDb; Q32KX7; -.
DR PRIDE; Q32KX7; -.
DR Ensembl; ENSBTAT00000020705; ENSBTAP00000020705; ENSBTAG00000015584.
DR Ensembl; ENSBTAT00000068448; ENSBTAP00000058683; ENSBTAG00000015584.
DR Ensembl; ENSBTAT00000073960; ENSBTAP00000066261; ENSBTAG00000015584.
DR GeneID; 510666; -.
DR KEGG; bta:510666; -.
DR CTD; 648; -.
DR VEuPathDB; HostDB:ENSBTAG00000015584; -.
DR eggNOG; KOG2660; Eukaryota.
DR GeneTree; ENSGT00940000156042; -.
DR HOGENOM; CLU_046427_0_0_1; -.
DR InParanoid; Q32KX7; -.
DR OMA; DIDARYL; -.
DR OrthoDB; 1344247at2759; -.
DR TreeFam; TF324206; -.
DR Reactome; R-BTA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-BTA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-BTA-8953750; Transcriptional Regulation by E2F6.
DR Proteomes; UP000009136; Chromosome 13.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0031519; C:PcG protein complex; ISS:UniProtKB.
DR GO; GO:0035102; C:PRC1 complex; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0071535; F:RING-like zinc finger domain binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0097027; F:ubiquitin-protein transferase activator activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0006306; P:DNA methylation; IEA:Ensembl.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0030097; P:hemopoiesis; IEA:Ensembl.
DR GO; GO:0016573; P:histone acetylation; IEA:Ensembl.
DR GO; GO:0036353; P:histone H2A-K119 monoubiquitination; ISS:UniProtKB.
DR GO; GO:0006959; P:humoral immune response; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0033092; P:positive regulation of immature T cell proliferation in thymus; IEA:Ensembl.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:2000011; P:regulation of adaxial/abaxial pattern formation; IEA:Ensembl.
DR GO; GO:0021903; P:rostrocaudal neural tube patterning; IEA:Ensembl.
DR GO; GO:0048103; P:somatic stem cell division; IEA:Ensembl.
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 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_0000281859"
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 240..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; 36966 MW; F710D39A66A86DE1 CRC64;
MHRTTRIKIT ELNPHLMCVL CGGYFIDATT IIECLHSFCK TCIVRYLETS KYCPICDVQV
HKTRPLLNIR SDKTLQDIVY KLVPGLFKNE MKRRRDFYAA HPSADAANGS NEDRGEVADE
DKRIITDDEI ISLSIEFFDQ NRLDRKINKD KEKSKEEVND KRYLRCPAAM TVMHLRKFLR
SKMDIPNTFQ IDVMYEEEPL KDYYTLMDIA YIYTWRRNGP LPLKYRVRPT CKRMKISHQR
DGLTNTGELE SDSGSDKANS PAGGIPSTSS CLPSPSTPVQ SPHPQFPHIS STMNGTSSSP
SGNHQSSFAN RPRKSSVNGS SATSSG
