BMI1B_DANRE
ID BMI1B_DANRE Reviewed; 324 AA.
AC Q7T3E6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Polycomb complex protein BMI-1-B;
DE AltName: Full=Polycomb group RING finger protein 4-B;
GN Name=bmi1b; Synonyms=pcgf4b;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2003) 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 In the PRC1 complex, it is required to stimulate the E3 ubiquitin-
CC protein ligase activity of rnf2 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of a PRC1-like complex. Homodimer. Interacts with
CC cbx2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; BC053151; AAH53151.1; -; mRNA.
DR RefSeq; NP_001074220.1; NM_001080751.1.
DR AlphaFoldDB; Q7T3E6; -.
DR SMR; Q7T3E6; -.
DR BioGRID; 90317; 3.
DR STRING; 7955.ENSDARP00000115422; -.
DR PaxDb; Q7T3E6; -.
DR Ensembl; ENSDART00000185792; ENSDARP00000157311; ENSDARG00000013076.
DR GeneID; 394249; -.
DR KEGG; dre:394249; -.
DR CTD; 394249; -.
DR ZFIN; ZDB-GENE-040116-4; bmi1b.
DR eggNOG; KOG2660; Eukaryota.
DR GeneTree; ENSGT00940000156042; -.
DR InParanoid; Q7T3E6; -.
DR Reactome; R-DRE-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DRE-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-DRE-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-DRE-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-DRE-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-DRE-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-DRE-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-DRE-8953750; Transcriptional Regulation by E2F6.
DR PRO; PR:Q7T3E6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 2.
DR Bgee; ENSDARG00000013076; Expressed in ovary and 28 other tissues.
DR ExpressionAtlas; Q7T3E6; baseline.
DR GO; GO:0031519; C:PcG protein complex; ISS:UniProtKB.
DR GO; GO:0035102; C:PRC1 complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0021549; P:cerebellum development; IGI:ZFIN.
DR GO; GO:0036353; P:histone H2A-K119 monoubiquitination; IBA:GO_Central.
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 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; Metal-binding; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..324
FT /note="Polycomb complex protein BMI-1-B"
FT /id="PRO_0000296631"
FT ZN_FING 18..57
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 232..324
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 254..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 324 AA; 36655 MW; D7EBF2D3FC3E1EBA CRC64;
MHRTTRIKIT ELNPHLMCVL CGGYFIDATT IVECLHSFCK MCIVRYLETS KYCPICDVQV
HKTKPLLNIR SDKTLQDIVY KLVPGLFKNE MKRRRDFYAE HPVDATNGSN EDRGEVSDED
KRIIADDEII SLSIEFFDQK KLDGKDGEEK ESTKEVTVKR YLQCPAAMTV MHLRKFLRSK
MDIPCTFQIE VMYEDEPLKD YYTLMDIAYI YTWRRNGPLP LKYRVRPGCK KIKLSSPRND
MSGGRRPDTE SDSSSDKPNS PSIVAAPSTS SSMPSPNTPV QSTHPSFPHI STINGVSAKV
GHNGQTPFSS KVCKTSHNGS NSLG