Polycomb complex protein BMI-1 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P35226 (BMI1_HUMAN)

Last modified June 16, 2009. Version 91. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	326 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Component of the Polycomb group (PcG) multiprotein PRC1 complex, a complex 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.8 Ref.11
Subunit structure	Component of chromatin-associated class II polycomb repressive complex 1 (PRC1/hPRC-H) at least composed of PCGF2/RNF110, BMI1/PCGF4, CBX2/M33, CBX4/PC2, CBX8/PC3, PHC1, PHC2, PHC3, SCMH1, RING1 and RNF2/RING2. Also component of E3 ubiquitin ligase complex or human polycomb repressive complex 1-like at least composed of PHC2, BMI1, RING1 and RNF2. Interacts with SPOP. Part of a complex consisting of BMI1, CUL3 and SPOP. Interacts with E4F1. Ref.11 Ref.4 Ref.5 Ref.7 Ref.9
Subcellular location	Nucleus. Cytoplasm. Ref.11
Post-translational modification	May be polyubiquitinated; which does not lead to proteasomal degradation.
Involvement in disease	Cooperates with the MYC oncogene to produce B-lymphomas.
Sequence similarities	Contains 1 RING-type zinc finger.

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Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Disease	Proto-oncogene
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator Repressor
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of fibroblast proliferation Inferred from mutant phenotype. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW segment specification Traceable author statement. Source: ProtInc transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: MGI
Molecular function	protein binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 326

326

Polycomb complex protein BMI-1

PRO_0000055987

Regions

Zinc finger

18 – 57

RING-type

Region

164 – 228

Interaction with E4F1

Motif

81 – 95

Nuclear localization signal Potential

Compositional bias

251 – 326

Pro/Ser-rich

Amino acid modifications

Modified residue

251

Phosphoserine Ref.10

Modified residue

253

Phosphoserine Ref.10

Modified residue

255

Phosphoserine Ref.10

Natural variations

Natural variant

C → Y: dbSNP rs1042059.

VAR_052087

Experimental info

Sequence conflict

109

G → S in AAB27059. Ref.3

Sequence conflict

265

I → V in AAA19873. Ref.1

Secondary structure

326

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P35226-1 [UniParc].

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

326

36,949

        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

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References

	« Hide 'large scale' referencesShow '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: 8268912] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Erythrocyte.
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Muscle.
[3]	"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: 8390036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 12-300. Tissue: Thymus.
[4]	"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: 9121482] [Abstract] Cited for: INTERACTION WITH PHC2.
[5]	"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: 9199346] [Abstract] Cited for: INTERACTION WITH PHC2.
[6]	"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: 12167701] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC1 COMPLEX WITH PCGF2; CBX2; CBX4; CBX8; PHC1; PHC2; PHC3; SCMH1; RING1 AND RNF2.
[7]	"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: 15386022] [Abstract] Cited for: SUBUNIT, INTERACTION WITH PHC2.
[8]	"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: 16359901] [Abstract] Cited for: FUNCTION.
[9]	"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: 15897469] [Abstract] Cited for: INTERACTION WITH SPOP, IDENTIFICATION IN A COMPLEX WITH CUL3 AND SPOP, UBIQUITINATION.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251; SER-253 AND SER-255, MASS SPECTROMETRY. Tissue: Epithelium.
[11]	"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: 16882984] [Abstract] Cited for: FUNCTION, INTERACTION WITH E4F1, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

L13689 mRNA. Translation: AAA19873.1.
BC011652 mRNA. Translation: AAH11652.1.
S62198 mRNA. Translation: AAB27059.1.

IPI

IPI00017299.

PIR

I54339.

RefSeq

NP_005171.4.

UniGene

Hs.380403

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2H0D	X-ray	2.50	A	5-101	[»]

ModBase

Search...

PTM databases

PhosphoSite

P35226.

Proteomic databases

PRIDE

P35226.

Genome annotation databases

Ensembl

ENSG00000168283. Homo sapiens. [Contig view]

GeneID

648.

KEGG

hsa:648.

Organism-specific databases

GeneCards

GC10P022650.

H-InvDB

HIX0008701.

HGNC

HGNC:1066. BMI1.

HPA

CAB011120.

MIM

164831. gene.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P35226.

OMA

P35226. QSSFASR.

Gene expression databases

ArrayExpress

P35226.

Bgee

P35226.

CleanEx

HS_BMI1.

GermOnline

ENSG00000168283. Homo sapiens.

Family and domain databases

InterPro

IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR017907. Znf_RING_CS.
[Graphical view]

Pfam

PF00097. zf-C3HC4. 1 hit.
[Graphical view]

SMART

SM00184. RING. 1 hit.
[Graphical view]

PROSITE

PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

2628.

SOURCE

Search...

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Entry information

Entry name

BMI1_HUMAN

Accession

Primary (citable) accession number: P35226
Secondary accession number(s): Q16030, Q96F37

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	August 13, 2002
Last modified:	June 16, 2009
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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