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P35226 (BMI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·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
RING finger protein 51
Gene names
Name:BMI1
Synonyms:PCGF4, RNF51
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length326 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. Ref.11 Ref.13 Ref.16

Subunit structure

Component of a PRC1-like complex. Interacts with RING1 and RING2 By similarity. Interacts vwith CBX7 and CBX8. Interacts with SPOP. Part of a complex consisting of BMI1, CUL3 and SPOP. Interacts with E4F1. Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16

Subcellular location

Nucleus. Cytoplasm Ref.13 Ref.15.

Post-translational modification

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

Miscellaneous

The hPRC-H complex purification reported by Ref.9 probably presents a mixture of different PRC1-like complexes.

Sequence similarities

Contains 1 RING-type zinc finger.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

hemopoiesis

Inferred from expression pattern PubMed 15334543. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.14. Source: UniProtKB

positive regulation of fibroblast proliferation

Inferred from mutant phenotype PubMed 17420273. Source: BHF-UCL

positive regulation of ubiquitin-protein ligase activity

Inferred from direct assay Ref.16. Source: UniProtKB

regulation of gene expression

Inferred from mutant phenotype PubMed 17420273. Source: BHF-UCL

segment specification

Traceable author statement PubMed 7715727. Source: ProtInc

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPRC1 complex

Inferred from direct assay Ref.9Ref.14. Source: UniProtKB

PcG protein complex

Inferred from direct assay Ref.15. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 10445843Ref.15. Source: UniProtKB

ubiquitin ligase complex

Inferred from direct assay Ref.16. Source: UniProtKB

   Molecular_functionRING-like zinc finger domain binding

Inferred from physical interaction Ref.16. Source: UniProtKB

zinc ion binding

Inferred from direct assay Ref.16. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 326326Polycomb complex protein BMI-1
PRO_0000055987

Regions

Zinc finger18 – 5740RING-type
Region164 – 22865Interaction with E4F1
Motif81 – 9515Nuclear localization signal Potential
Compositional bias251 – 32676Pro/Ser-rich

Natural variations

Natural variant181C → Y.
Corresponds to variant rs1042059 [ dbSNP | Ensembl ].
VAR_052087

Experimental info

Sequence conflict1091G → S in AAB27059. Ref.6
Sequence conflict2651I → V in AAA19873. Ref.1

Secondary structure

...................... 326
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35226 [UniParc].

Last modified August 13, 2002. Version 2.
Checksum: 030A7D396BADA543

FASTA32636,949
        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 
DKRIITDDEI ISLSIEFFDQ NRLDRKVNKD KEKSKEEVND KRYLRCPAAM TVMHLRKFLR 

       190        200        210        220        230        240 
SKMDIPNTFQ IDVMYEEEPL KDYYTLMDIA YIYTWRRNGP LPLKYRVRPT CKRMKISHQR 

       250        260        270        280        290        300 
DGLTNAGELE SDSGSDKANS PAGGIPSTSS CLPSPSTPVQ SPHPQFPHIS STMNGTSNSP 

       310        320 
SGNHQSSFAN RPRKSSVNGS SATSSG 

« Hide

References

« Hide 'large scale' references
[1]"Characterization and chromosomal localization of the human proto-oncogene BMI-1."
Alkema M.J., Wiegand J., Raap A.K., Berns A., van Lohuizen M.
Hum. Mol. Genet. 2:1597-1603(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Erythrocyte.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
Tissue: Muscle.
[6]"flvi-2, a target of retroviral insertional mutagenesis in feline thymic lymphosarcomas, encodes bmi-1."
Levy L.S., Lobelle-Rich P.A., Overbaugh J.
Oncogene 8:1833-1838(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 12-300.
Tissue: Thymus.
[7]"Identification and characterization of interactions between the vertebrate polycomb-group protein BMI1 and human homologs of polyhomeotic."
Gunster M.J., Satijn D.P.E., Hamer K.M., den Blaauwen J.L., de Bruijn D., Alkema M.J., van Lohuizen M., van Driel R., Otte A.P.
Mol. Cell. Biol. 17:2326-2335(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PHC2.
[8]"RING1 is associated with the polycomb group protein complex and acts as a transcriptional repressor."
Satijn D.P.E., Gunster M.J., van der Vlag J., Hamer K.M., Schul W., Alkema M.J., Saurin A.J., Freemont P.S., van Driel R., Otte A.P.
Mol. Cell. Biol. 17:4105-4113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PHC2.
[9]"The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans."
Levine S.S., Weiss A., Erdjument-Bromage H., Shao Z., Tempst P., Kingston R.E.
Mol. Cell. Biol. 22:6070-6078(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A PRC1-LIKE HPRC-H COMPLEX WITH CBX2; CBX4; CBX8; PHC1; PHC2; PHC3; RING1 AND RNF2.
[10]"Role of histone H2A ubiquitination in Polycomb silencing."
Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P., Jones R.S., Zhang Y.
Nature 431:873-878(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A PRC1-LIKE COMPLEX.
[11]"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: FUNCTION.
[12]"Stable X chromosome inactivation involves the PRC1 Polycomb complex and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase."
Hernandez-Munoz I., Lund A.H., van der Stoop P., Boutsma E., Muijrers I., Verhoeven E., Nusinow D.A., Panning B., Marahrens Y., van Lohuizen M.
Proc. Natl. Acad. Sci. U.S.A. 102:7635-7640(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPOP, IDENTIFICATION IN A COMPLEX WITH CUL3 AND SPOP, UBIQUITINATION.
[13]"E4F1: a novel candidate factor for mediating BMI1 function in primitive hematopoietic cells."
Chagraoui J., Niessen S.L., Lessard J., Girard S., Coulombe P., Sauvageau M., Meloche S., Sauvageau G.
Genes Dev. 20:2110-2120(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH E4F1, SUBCELLULAR LOCATION.
[14]"Several distinct polycomb complexes regulate and co-localize on the INK4a tumor suppressor locus."
Maertens G.N., El Messaoudi-Aubert S., Racek T., Stock J.K., Nicholls J., Rodriguez-Niedenfuhr M., Gil J., Peters G.
PLoS ONE 4:E6380-E6380(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A PRC1-LIKE COMPLEX, INTERACTION WITH CBX7 AND CBX8.
[15]"Interaction proteomics analysis of polycomb proteins defines distinct PRC1 Complexes in mammalian cells."
Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O.
Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A PRC1-LIKE COMPLEX, SUBCELLULAR LOCATION.
[16]"Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex."
Li Z., Cao R., Wang M., Myers M.P., Zhang Y., Xu R.M.
J. Biol. Chem. 281:20643-20649(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 5-101 IN COMPLEX WITH RNF2 AND ZINC IONS, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L13689 mRNA. Translation: AAA19873.1.
AK313235 mRNA. Translation: BAG36046.1.
AL158211 Genomic DNA. Translation: CAI15958.1.
CH471072 Genomic DNA. Translation: EAW86148.1.
CH471072 Genomic DNA. Translation: EAW86150.1.
CH471072 Genomic DNA. Translation: EAW86151.1.
CH471072 Genomic DNA. Translation: EAW86154.1.
BC011652 mRNA. Translation: AAH11652.1.
AH004292 mRNA. Translation: AAB27059.1.
PIRI54339.
RefSeqNP_001190991.1. NM_001204062.1.
NP_005171.4. NM_005180.8.
UniGeneHs.380403.
Hs.731287.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2H0DX-ray2.50A5-101[»]
3RPGX-ray2.65B1-109[»]
ProteinModelPortalP35226.
SMRP35226. Positions 6-103, 126-227.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107116. 58 interactions.
1529410. 1 interaction.
DIPDIP-41879N.
IntActP35226. 35 interactions.
MINTMINT-158260.
STRING9606.ENSP00000365851.

PTM databases

PhosphoSiteP35226.

Polymorphism databases

DMDM22258801.

Proteomic databases

PaxDbP35226.
PRIDEP35226.

Protocols and materials databases

DNASU648.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376663; ENSP00000365851; ENSG00000168283.
GeneID100532731.
648.
KEGGhsa:100532731.
hsa:648.
UCSCuc001irh.3. human.

Organism-specific databases

CTD100532731.
648.
GeneCardsGC10P022605.
HGNCHGNC:1066. BMI1.
HPACAB011120.
HPA030472.
MIM164831. gene.
neXtProtNX_P35226.
PharmGKBPA25376.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG304672.
HOGENOMHOG000231945.
HOVERGENHBG052826.
InParanoidP35226.
KOK11459.
OMARVRPNCK.
PhylomeDBP35226.
TreeFamTF324206.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.

Gene expression databases

ArrayExpressP35226.
BgeeP35226.
CleanExHS_BMI1.
GenevestigatorP35226.

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

EvolutionaryTraceP35226.
GeneWikiBMI1.
NextBio2628.
PROP35226.
SOURCESearch...

Entry information

Entry nameBMI1_HUMAN
AccessionPrimary (citable) accession number: P35226
Secondary accession number(s): Q16030, Q5T8Z3, Q96F37
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: August 13, 2002
Last modified: April 16, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM