BMI1_MOUSE
ID BMI1_MOUSE Reviewed; 324 AA.
AC P25916;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Polycomb complex protein BMI-1;
DE AltName: Full=Polycomb group RING finger protein 4;
GN Name=Bmi1; Synonyms=Bmi-1, Pcgf4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1904009; DOI=10.1016/0092-8674(91)90383-a;
RA Haupt Y., Alexander W.S., Barri G., Klinken S.P., Adams J.M.;
RT "Novel zinc finger gene implicated as myc collaborator by retrovirally
RT accelerated lymphomagenesis in E mu-myc transgenic mice.";
RL Cell 65:753-763(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1904008; DOI=10.1016/0092-8674(91)90382-9;
RA van Lohuiizen M., Verbbeek S., Scheijen B., Wientjens E., Gulden H.,
RA Berns A.;
RT "Identification of cooperating oncogenes in E mu-myc transgenic mice by
RT provirus tagging.";
RL Cell 65:737-752(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hematopoietic;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP RECONSTITUTION OF A PRC1-LIKE COMPLEX, AND INTERACTION WITH RING1; RNF2;
RP CBX8 AND PHC2.
RX PubMed=16359901; DOI=10.1016/j.molcel.2005.12.002;
RA Cao R., Tsukada Y., Zhang Y.;
RT "Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing.";
RL Mol. Cell 20:845-854(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-108 IN COMPLEX WITH RNF2 AND
RP ZINC IONS, FUNCTION, INTERACTION WITH RING1, MONOUBIQUITINATION,
RP POLYUBIQUITINATION IN THE PRESENCE OF UBE2D3 AND RING2, AND SUBUNIT.
RX PubMed=16710298; DOI=10.1038/sj.emboj.7601144;
RA Buchwald G., van der Stoop P., Weichenrieder O., Perrakis A.,
RA van Lohuizen M., Sixma T.K.;
RT "Structure and E3-ligase activity of the Ring-Ring complex of polycomb
RT proteins Bmi1 and Ring1b.";
RL EMBO J. 25:2465-2474(2006).
RN [6] {ECO:0000305}
RP INTERACTION WITH ZNF277, AND INDUCTION.
RX PubMed=20808772; DOI=10.1371/journal.pone.0012373;
RA Negishi M., Saraya A., Mochizuki S., Helin K., Koseki H., Iwama A.;
RT "A novel zinc finger protein Zfp277 mediates transcriptional repression of
RT the Ink4a/arf locus through polycomb repressive complex 1.";
RL PLoS ONE 5:e12373-e12373(2010).
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 (By
CC similarity). {ECO:0000250|UniProtKB:P35226,
CC ECO:0000269|PubMed:16710298}.
CC -!- SUBUNIT: Component of a PRC1-like complex (PubMed:16359901). Identified
CC in a PRC1-like HPRC-H complex with CBX2, CBX4, CBX8, PHC1, PHC2, PHC3,
CC RING1 and RNF2 (By similarity). Interacts with RNF2/RING2
CC (PubMed:16359901, PubMed:16710298). Interacts with RING1
CC (PubMed:16359901, PubMed:16710298). Part of a complex that contains
CC RNF2, UB2D3 and BMI1, where RNF2 and BMI1 form a tight heterodimer, and
CC UB2D3 interacts only with RNF2. The complex composed of RNF2, UB2D3 and
CC BMI1 binds nucleosomes, and has activity only with nucleosomal histone
CC H2A. Interacts with CBX7 and CBX8 (PubMed:16359901). Interacts with
CC SPOP. Part of a complex consisting of BMI1, CUL3 and SPOP. Interacts
CC with E4F1 (By similarity). Interacts with PHC2 (PubMed:16359901).
CC Interacts with zinc finger protein ZNF277 (PubMed:20808772). May be
CC part of a complex including at least ZNF277, BMI1 and RNF2/RING2
CC (PubMed:20808772). {ECO:0000250|UniProtKB:P35226,
CC ECO:0000269|PubMed:16359901, ECO:0000269|PubMed:16710298,
CC ECO:0000269|PubMed:20808772}.
CC -!- INTERACTION:
CC P25916; Q9QXV1: Cbx8; NbExp=3; IntAct=EBI-927401, EBI-1216641;
CC P25916; O88509: Dnmt3b; NbExp=2; IntAct=EBI-927401, EBI-7987547;
CC P25916; Q60848: Hells; NbExp=2; IntAct=EBI-927401, EBI-3043887;
CC P25916; Q9QWH1: Phc2; NbExp=3; IntAct=EBI-927401, EBI-642357;
CC P25916; O35730: Ring1; NbExp=4; IntAct=EBI-927401, EBI-929310;
CC P25916; Q9CQJ4: Rnf2; NbExp=17; IntAct=EBI-927401, EBI-927321;
CC P25916; Q8IXK0: PHC2; Xeno; NbExp=2; IntAct=EBI-927401, EBI-713786;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P35226}. Cytoplasm
CC {ECO:0000250|UniProtKB:P35226}.
CC -!- TISSUE SPECIFICITY: Detected in most organs with high expression levels
CC in thymus, heart, brain and testis.
CC -!- INDUCTION: Down-regulated by oxidative stress.
CC {ECO:0000269|PubMed:20808772}.
CC -!- PTM: May be polyubiquitinated; which does not lead to proteasomal
CC degradation (By similarity). Monoubiquitinated. {ECO:0000250,
CC ECO:0000269|PubMed:16710298}.
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DR EMBL; M64067; AAA37299.1; -; Genomic_DNA.
DR EMBL; M64068; AAA37301.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M64279; AAA37300.1; -; mRNA.
DR EMBL; BC053708; AAH53708.1; -; mRNA.
DR EMBL; BC056384; AAH56384.1; -; mRNA.
DR CCDS; CCDS15711.1; -.
DR PIR; A39523; A39523.
DR RefSeq; NP_031578.2; NM_007552.4.
DR RefSeq; XP_006497374.1; XM_006497311.2.
DR RefSeq; XP_006497375.1; XM_006497312.3.
DR PDB; 2CKL; X-ray; 2.00 A; A=1-108.
DR PDBsum; 2CKL; -.
DR AlphaFoldDB; P25916; -.
DR SMR; P25916; -.
DR BioGRID; 198359; 29.
DR CORUM; P25916; -.
DR DIP; DIP-132N; -.
DR IntAct; P25916; 21.
DR MINT; P25916; -.
DR STRING; 10090.ENSMUSP00000028071; -.
DR iPTMnet; P25916; -.
DR PhosphoSitePlus; P25916; -.
DR EPD; P25916; -.
DR PaxDb; P25916; -.
DR PeptideAtlas; P25916; -.
DR PRIDE; P25916; -.
DR ProteomicsDB; 273502; -.
DR DNASU; 12151; -.
DR Ensembl; ENSMUST00000028071; ENSMUSP00000028071; ENSMUSG00000026739.
DR Ensembl; ENSMUST00000051929; ENSMUSP00000110300; ENSMUSG00000026739.
DR GeneID; 12151; -.
DR KEGG; mmu:12151; -.
DR UCSC; uc008ily.1; mouse.
DR CTD; 648; -.
DR MGI; MGI:88174; Bmi1.
DR VEuPathDB; HostDB:ENSMUSG00000026739; -.
DR eggNOG; KOG2660; Eukaryota.
DR GeneTree; ENSGT00940000156042; -.
DR HOGENOM; CLU_046427_0_0_1; -.
DR InParanoid; P25916; -.
DR OMA; DIDARYL; -.
DR OrthoDB; 1344247at2759; -.
DR PhylomeDB; P25916; -.
DR TreeFam; TF324206; -.
DR Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-MMU-8953750; Transcriptional Regulation by E2F6.
DR BioGRID-ORCS; 12151; 4 hits in 76 CRISPR screens.
DR EvolutionaryTrace; P25916; -.
DR PRO; PR:P25916; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P25916; protein.
DR Bgee; ENSMUSG00000026739; Expressed in animal zygote and 308 other tissues.
DR ExpressionAtlas; P25916; baseline and differential.
DR Genevisible; P25916; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0031519; C:PcG protein complex; IDA:MGI.
DR GO; GO:0035102; C:PRC1 complex; ISO:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI.
DR GO; GO:0071535; F:RING-like zinc finger domain binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0097027; F:ubiquitin-protein transferase activator activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0097190; P:apoptotic signaling pathway; IGI:MGI.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR GO; GO:0006306; P:DNA methylation; IMP:MGI.
DR GO; GO:0048706; P:embryonic skeletal system development; IGI:MGI.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IGI:MGI.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; ISO:MGI.
DR GO; GO:0030097; P:hemopoiesis; IEA:Ensembl.
DR GO; GO:0016573; P:histone acetylation; IGI:MGI.
DR GO; GO:0036353; P:histone H2A-K119 monoubiquitination; ISS:UniProtKB.
DR GO; GO:0016574; P:histone ubiquitination; IDA:MGI.
DR GO; GO:0006959; P:humoral immune response; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IGI:MGI.
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; IDA:MGI.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:HGNC-UCL.
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; IMP:HGNC-UCL.
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; IGI:MGI.
DR GO; GO:0021903; P:rostrocaudal neural tube patterning; IMP:MGI.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR GO; GO:0048103; P:somatic stem cell division; IMP:MGI.
DR DisProt; DP01316; -.
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 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Cytoplasm; Metal-binding; Nucleus;
KW Proto-oncogene; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..324
FT /note="Polycomb complex protein BMI-1"
FT /id="PRO_0000055988"
FT ZN_FING 18..57
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 160..180
FT /note="Interaction with PHC2"
FT /evidence="ECO:0000250|UniProtKB:P35226"
FT REGION 162..226
FT /note="Interaction with E4F1"
FT /evidence="ECO:0000250|UniProtKB:P35226"
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 242..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:2CKL"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:2CKL"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:2CKL"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:2CKL"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:2CKL"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:2CKL"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2CKL"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:2CKL"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:2CKL"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:2CKL"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:2CKL"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:2CKL"
FT HELIX 86..100
FT /evidence="ECO:0007829|PDB:2CKL"
SQ SEQUENCE 324 AA; 36708 MW; AD7DECDB6B29DCE5 CRC64;
MHRTTRIKIT ELNPHLMCVL CGGYFIDATT IIECLHSFCK TCIVRYLETS KYCPICDVQV
HKTRPLLNIR SDKTLQDIVY KLVPGLFKNE MKRRRDFYAA HPSADAANGS NEDRGEVADE
EKRIITDDEI ISLSIEFFDQ SRLDRKVNKE KPKEEVNDKR YLRCPAAMTV MHLRKFLRSK
MDIPNTFQID VMYEEEPLKD YYTLMDIAYI YTWRRNGPLP LKYRVRPTCK RMKMSHQRDG
LTNAGELESD SGSDKANSPA GGVPSTSSCL PSPSTPVQSP HPQFPHISST MNGTSNSPSA
NHQSSFASRP RKSSLNGSSA TSSG
