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P25916 (BMI1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polycomb complex protein BMI-1
Alternative name(s):
Polycomb group RING finger protein 4
Gene names
Name:Bmi1
Synonyms:Bmi-1, Pcgf4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length324 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. In the PRC1 complex, it is required to stimulate the E3 ubiquitin-protein ligase activity of RNF2/RING2 By similarity. Ref.5

Subunit structure

Component of a PRC1-like complex. Interacts with RING1 and RING2. Interacts vwith CBX7 and CBX8. Interacts with SPOP. Part of a complex consisting of BMI1, CUL3 and SPOP. Interacts with E4F1 By similarity. Ref.4 Ref.5

Subcellular location

Nucleus. Cytoplasm By similarity.

Tissue specificity

Detected in most organs with high expression levels in thymus, heart, brain and testis.

Post-translational modification

May be polyubiquitinated; which does not lead to proteasomal degradation By similarity. Monoubiquitinated.

Sequence similarities

Contains 1 RING-type zinc finger.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   DiseaseProto-oncogene
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionChromatin regulator
Repressor
   PTMUbl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbrain development

Inferred from mutant phenotype PubMed 7926765. Source: MGI

cellular process

Traceable author statement PubMed 7926765. Source: MGI

embryonic skeletal system development

Inferred from genetic interaction PubMed 11290297. Source: MGI

embryonic skeletal system morphogenesis

Inferred from genetic interaction PubMed 11290297. Source: MGI

histone acetylation

Inferred from genetic interaction PubMed 16687444. Source: MGI

histone ubiquitination

Inferred from direct assay Ref.4. Source: MGI

humoral immune response

Inferred from mutant phenotype PubMed 7926765. Source: MGI

in utero embryonic development

Inferred from genetic interaction PubMed 11290297. Source: MGI

negative regulation of apoptotic signaling pathway

Inferred from genetic interaction PubMed 11290297. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 9312051PubMed 9367786. Source: MGI

positive regulation of B cell proliferation

Inferred from mutant phenotype PubMed 15964995. Source: HGNC

positive regulation of immature T cell proliferation in thymus

Inferred from mutant phenotype PubMed 15964995. Source: HGNC

positive regulation of ubiquitin-protein ligase activity

Inferred from sequence or structural similarity. Source: UniProtKB

rostrocaudal neural tube patterning

Inferred from mutant phenotype PubMed 8887324. Source: MGI

skeletal system development

Inferred from mutant phenotype PubMed 7926765. Source: MGI

somatic stem cell division

Inferred from mutant phenotype PubMed 12714971. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPcG protein complex

Inferred from direct assay Ref.4PubMed 16624538. Source: MGI

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

heterochromatin

Inferred from direct assay PubMed 18311137. Source: MGI

nuclear body

Inferred from direct assay PubMed 12183370. Source: MGI

nucleus

Inferred from sequence orthology PubMed 9367786. Source: MGI

ubiquitin ligase complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionchromatin binding

Inferred from direct assay Ref.4. Source: MGI

sequence-specific DNA binding

Inferred from direct assay PubMed 20956546. Source: MGI

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 324324Polycomb complex protein BMI-1
PRO_0000055988

Regions

Zinc finger18 – 5740RING-type
Region162 – 22665Interaction with E4F1 By similarity
Motif81 – 9515Nuclear localization signal Potential
Compositional bias249 – 32476Pro/Ser-rich

Secondary structure

...................... 324
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P25916 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: AD7DECDB6B29DCE5

FASTA32436,708
        10         20         30         40         50         60 
MHRTTRIKIT ELNPHLMCVL CGGYFIDATT IIECLHSFCK TCIVRYLETS KYCPICDVQV 

        70         80         90        100        110        120 
HKTRPLLNIR SDKTLQDIVY KLVPGLFKNE MKRRRDFYAA HPSADAANGS NEDRGEVADE 

       130        140        150        160        170        180 
EKRIITDDEI ISLSIEFFDQ SRLDRKVNKE KPKEEVNDKR YLRCPAAMTV MHLRKFLRSK 

       190        200        210        220        230        240 
MDIPNTFQID VMYEEEPLKD YYTLMDIAYI YTWRRNGPLP LKYRVRPTCK RMKMSHQRDG 

       250        260        270        280        290        300 
LTNAGELESD SGSDKANSPA GGVPSTSSCL PSPSTPVQSP HPQFPHISST MNGTSNSPSA 

       310        320 
NHQSSFASRP RKSSLNGSSA TSSG 

« Hide

References

« Hide 'large scale' references
[1]"Novel zinc finger gene implicated as myc collaborator by retrovirally accelerated lymphomagenesis in E mu-myc transgenic mice."
Haupt Y., Alexander W.S., Barri G., Klinken S.P., Adams J.M.
Cell 65:753-763(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Identification of cooperating oncogenes in E mu-myc transgenic mice by provirus tagging."
van Lohuiizen M., Verbbeek S., Scheijen B., Wientjens E., Gulden H., Berns A.
Cell 65:737-752(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain and Hematopoietic.
[4]"Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing."
Cao R., Tsukada Y., Zhang Y.
Mol. Cell 20:845-854(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: RECONSTITUTION OF A PRC1-LIKE COMPLEX, INTERACTION WITH RING1; RNF2; CBX8 AND PHC2.
[5]"Structure and E3-ligase activity of the Ring-Ring complex of polycomb proteins Bmi1 and Ring1b."
Buchwald G., van der Stoop P., Weichenrieder O., Perrakis A., van Lohuizen M., Sixma T.K.
EMBO J. 25:2465-2474(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-108 IN COMPLEX WITH RNF2 AND ZINC IONS, FUNCTION, INTERACTION WITH RING1, MONOUBIQUITINATION, POLYUBIQUITINATION IN THE PRESENCE OF UBE2D3 AND RING2, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64067 Genomic DNA. Translation: AAA37299.1.
M64068 Genomic DNA. Translation: AAA37301.1. Sequence problems.
M64279 mRNA. Translation: AAA37300.1.
BC053708 mRNA. Translation: AAH53708.1.
BC056384 mRNA. Translation: AAH56384.1.
PIRA39523.
RefSeqNP_031578.2. NM_007552.4.
XP_006497374.1. XM_006497311.1.
XP_006497375.1. XM_006497312.1.
UniGeneMm.289584.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CKLX-ray2.00A1-108[»]
ProteinModelPortalP25916.
SMRP25916. Positions 6-103, 126-225.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198359. 26 interactions.
DIPDIP-132N.
IntActP25916. 17 interactions.

PTM databases

PhosphoSiteP25916.

Proteomic databases

PaxDbP25916.
PRIDEP25916.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028071; ENSMUSP00000028071; ENSMUSG00000026739.
ENSMUST00000051929; ENSMUSP00000110300; ENSMUSG00000026739.
GeneID12151.
KEGGmmu:12151.
UCSCuc008ily.1. mouse.

Organism-specific databases

CTD648.
MGIMGI:88174. Bmi1.

Phylogenomic databases

eggNOGNOG304672.
HOGENOMHOG000231945.
HOVERGENHBG052826.
InParanoidP25916.
KOK11459.
OMARVRPNCK.
OrthoDBEOG77T14W.
PhylomeDBP25916.
TreeFamTF324206.

Gene expression databases

ArrayExpressP25916.
BgeeP25916.
CleanExMM_BMI1.
GenevestigatorP25916.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP25916.
NextBio280483.
PROP25916.
SOURCESearch...

Entry information

Entry nameBMI1_MOUSE
AccessionPrimary (citable) accession number: P25916
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: April 16, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot