BMI1_CHICK
ID BMI1_CHICK Reviewed; 326 AA.
AC Q5SDR3;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Polycomb complex protein BMI-1;
DE AltName: Full=Polycomb group RING finger protein 4;
GN Name=BMI1; Synonyms=PCGF4;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=White leghorn; TISSUE=Embryo;
RX PubMed=15533814; DOI=10.1016/j.modgep.2004.06.011;
RA Fraser P.E., Sauka-Spengler T.;
RT "Expression of the polycomb group gene bmi-1 in the early chick embryo.";
RL Gene Expr. Patterns 5:23-27(2004).
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-like complex, regulates the E3 ubiquitin-protein ligase
CC activity of RNF2/RING2. {ECO:0000250|UniProtKB:P35226}.
CC -!- SUBUNIT: Component of a PRC1-like complex.
CC {ECO:0000250|UniProtKB:P35226}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P35226}. Cytoplasm
CC {ECO:0000250|UniProtKB:P35226}.
CC -!- DEVELOPMENTAL STAGE: During early nervous system development, robust
CC expression was observed in the open neural plate and later in the
CC dorsal neural tube and much of the brain. Also present in the
CC developing heart primordia and the sensory placodes.
CC {ECO:0000269|PubMed:15533814}.
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DR EMBL; AY616032; AAU25821.1; -; mRNA.
DR RefSeq; NP_001007989.1; NM_001007988.1.
DR AlphaFoldDB; Q5SDR3; -.
DR SMR; Q5SDR3; -.
DR STRING; 9031.ENSGALP00000041259; -.
DR Ensembl; ENSGALT00000047281; ENSGALP00000051910; ENSGALG00000041267.
DR GeneID; 493647; -.
DR KEGG; gga:493647; -.
DR CTD; 648; -.
DR VEuPathDB; HostDB:geneid_493647; -.
DR eggNOG; KOG2660; Eukaryota.
DR GeneTree; ENSGT00940000156042; -.
DR HOGENOM; CLU_046427_0_0_1; -.
DR InParanoid; Q5SDR3; -.
DR OMA; DIDARYL; -.
DR OrthoDB; 1344247at2759; -.
DR PhylomeDB; Q5SDR3; -.
DR Reactome; R-GGA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-GGA-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-GGA-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-GGA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-GGA-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-GGA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-GGA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-GGA-8953750; Transcriptional Regulation by E2F6.
DR PRO; PR:Q5SDR3; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000041267; Expressed in ovary and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0036353; P:histone H2A-K119 monoubiquitination; ISS:UniProtKB.
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:0051443; P:positive regulation of ubiquitin-protein transferase activity; ISS:UniProtKB.
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; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..326
FT /note="Polycomb complex protein BMI-1"
FT /id="PRO_0000296629"
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; 36885 MW; 4046712599642314 CRC64;
MHRTTRIKIT ELNPHLMCVL CGGYFIDATT IIECLHSFCK TCIVRYLETS KYCPICDVQV
HKTRPLLNIR SDKTLQDIVY KLVPGLFKNE MKRRRDFYAA HPSADAANGS NEDRGEVADE
DKRIITDDEI ISLSIEFFDQ NRLERKGNKE KEKSKEEVND KRYLRCPAAM TVMHLRKFLR
SKMDIPNTFQ IDVMYEEEPL KDYYTLMDIA YIYTWRRNGP LPLKYRVRPT CKRMKIGHQR
EGLSNSGELE SDSGSDKASS PAGGLPSTSS CLPSPSTPVQ SPHPQFPHIS STMNGTSSSP
GSNHQSSFTN RARKSSINGS SATSSG
