Reviewed,
UniProtKB/Swiss-Prot P35226 (BMI1_HUMAN)
Last modified
June 16, 2009.
Version 91.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
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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 |
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| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 326 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
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 | |
| 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. |
Ontologies
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 | 40 | RING-type | |||||||||||||||||||||||||||
| Region | 164 – 228 | 65 | Interaction with E4F1 | |||||||||||||||||||||||||||
| Motif | 81 – 95 | 15 | Nuclear localization signal Potential | |||||||||||||||||||||||||||
| Compositional bias | 251 – 326 | 76 | Pro/Ser-rich | |||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||
| Modified residue | 251 | 1 | Phosphoserine Ref.10 | |||||||||||||||||||||||||||
| Modified residue | 253 | 1 | Phosphoserine Ref.10 | |||||||||||||||||||||||||||
| Modified residue | 255 | 1 | Phosphoserine Ref.10 | |||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||
| Natural variant | 18 | 1 | C → Y: dbSNP rs1042059. | VAR_052087 | ||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||
| Sequence conflict | 109 | 1 | G → S in AAB27059. Ref.3 | |||||||||||||||||||||||||||
| Sequence conflict | 265 | 1 | I → V in AAA19873. Ref.1 | |||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||
| Beta strand | 6 – 8 | 3 | ||||||||||||||||||||||||||||
| Helix | 9 – 12 | 4 | ||||||||||||||||||||||||||||
| Helix | 13 – 15 | 3 | ||||||||||||||||||||||||||||
| Turn | 19 – 21 | 3 | ||||||||||||||||||||||||||||
| Beta strand | 22 – 24 | 3 | ||||||||||||||||||||||||||||
| Beta strand | 29 – 31 | 3 | ||||||||||||||||||||||||||||
| Turn | 32 – 34 | 3 | ||||||||||||||||||||||||||||
| Helix | 40 – 46 | 7 | ||||||||||||||||||||||||||||
| Turn | 54 – 56 | 3 | ||||||||||||||||||||||||||||
| Helix | 65 – 68 | 4 | ||||||||||||||||||||||||||||
| Beta strand | 69 – 71 | 3 | ||||||||||||||||||||||||||||
| Helix | 73 – 82 | 10 | ||||||||||||||||||||||||||||
| Helix | 86 – 100 | 15 | ||||||||||||||||||||||||||||
Sequences
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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: 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. |
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 | |||||||||||||
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| 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... | ||||||||||||
Entry information
| Entry name | BMI1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P35226 Secondary accession number(s): Q16030, Q96F37 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 10 Human chromosome 10: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


