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Protein

Polycomb complex protein BMI-1

Gene

BMI1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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/RING2.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri18 – 5740RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • RING-like zinc finger domain binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • cellular protein metabolic process Source: Reactome
  • chromatin modification Source: UniProtKB-KW
  • hemopoiesis Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of fibroblast proliferation Source: BHF-UCL
  • positive regulation of ubiquitin-protein transferase activity Source: UniProtKB
  • post-translational protein modification Source: Reactome
  • protein sumoylation Source: Reactome
  • regulation of gene expression Source: BHF-UCL
  • segment specification Source: ProtInc
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_169436. Oxidative Stress Induced Senescence.
REACT_355174. SUMOylation of DNA damage response and repair proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Polycomb complex protein BMI-1
Alternative name(s):
Polycomb group RING finger protein 4
RING finger protein 51
Gene namesi
Name:BMI1
Synonyms:PCGF4, RNF51
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:1066. BMI1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • PcG protein complex Source: UniProtKB
  • PRC1 complex Source: UniProtKB
  • ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA25376.

Polymorphism and mutation databases

BioMutaiBMI1.
DMDMi22258801.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 326326Polycomb complex protein BMI-1PRO_0000055987Add
BLAST

Post-translational modificationi

Monoubiquitinated (By similarity). May be polyubiquitinated; which does not lead to proteasomal degradation.By similarity1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiP35226.
PaxDbiP35226.
PRIDEiP35226.

PTM databases

PhosphoSiteiP35226.

Expressioni

Gene expression databases

BgeeiP35226.
CleanExiHS_BMI1.
ExpressionAtlasiP35226. baseline and differential.
GenevestigatoriP35226.

Organism-specific databases

HPAiCAB011120.
HPA030472.

Interactioni

Subunit structurei

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.By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CBX4O002574EBI-2341576,EBI-722425
CBX4O00257-32EBI-2341576,EBI-4392727
CBX6O955033EBI-2341576,EBI-3951758
CBX7O959317EBI-2341576,EBI-3923843
CBX8Q9HC5213EBI-2341576,EBI-712912
NDEL1Q9GZM83EBI-2341576,EBI-928842
PHC2Q8IXK05EBI-2341576,EBI-713786
PTENP604843EBI-2341576,EBI-696162
RING1Q0658714EBI-2341576,EBI-752313
RNF2Q994969EBI-2341576,EBI-722416
UBCP0CG482EBI-2341576,EBI-3390054
USP11P517847EBI-2341576,EBI-306876
USP7Q930097EBI-2341576,EBI-302474
VPS11Q9H2702EBI-2341576,EBI-373380

Protein-protein interaction databases

BioGridi107116. 360 interactions.
DIPiDIP-41879N.
IntActiP35226. 37 interactions.
MINTiMINT-158260.
STRINGi9606.ENSP00000365851.

Structurei

Secondary structure

1
326
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83Combined sources
Helixi9 – 124Combined sources
Helixi13 – 153Combined sources
Turni19 – 213Combined sources
Beta strandi22 – 243Combined sources
Beta strandi29 – 313Combined sources
Turni32 – 343Combined sources
Beta strandi36 – 394Combined sources
Helixi40 – 467Combined sources
Turni47 – 493Combined sources
Turni54 – 563Combined sources
Helixi65 – 684Combined sources
Beta strandi69 – 713Combined sources
Helixi73 – 8210Combined sources
Helixi86 – 10015Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H0DX-ray2.50A5-101[»]
3RPGX-ray2.65B1-109[»]
4R8PX-ray3.28K/M2-109[»]
ProteinModelPortaliP35226.
SMRiP35226. Positions 6-103.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35226.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni164 – 22865Interaction with E4F1Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi81 – 9515Nuclear localization signalSequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi251 – 32676Pro/Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri18 – 5740RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG304672.
GeneTreeiENSGT00550000074463.
HOGENOMiHOG000231945.
HOVERGENiHBG052826.
InParanoidiP35226.
KOiK11459.
PhylomeDBiP35226.
TreeFamiTF324206.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35226-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHRTTRIKIT ELNPHLMCVL CGGYFIDATT IIECLHSFCK TCIVRYLETS
60 70 80 90 100
KYCPICDVQV HKTRPLLNIR SDKTLQDIVY KLVPGLFKNE MKRRRDFYAA
110 120 130 140 150
HPSADAANGS NEDRGEVADE DKRIITDDEI ISLSIEFFDQ NRLDRKVNKD
160 170 180 190 200
KEKSKEEVND KRYLRCPAAM TVMHLRKFLR SKMDIPNTFQ IDVMYEEEPL
210 220 230 240 250
KDYYTLMDIA YIYTWRRNGP LPLKYRVRPT CKRMKISHQR DGLTNAGELE
260 270 280 290 300
SDSGSDKANS PAGGIPSTSS CLPSPSTPVQ SPHPQFPHIS STMNGTSNSP
310 320
SGNHQSSFAN RPRKSSVNGS SATSSG
Length:326
Mass (Da):36,949
Last modified:August 13, 2002 - v2
Checksum:i030A7D396BADA543
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1091G → S in AAB27059 (PubMed:8390036).Curated
Sequence conflicti265 – 2651I → V in AAA19873 (PubMed:8268912).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181C → Y.
Corresponds to variant rs1042059 [ dbSNP | Ensembl ].
VAR_052087

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS7138.1.
PIRiI54339.
RefSeqiNP_001190991.1. NM_001204062.1.
NP_005171.4. NM_005180.8.
UniGeneiHs.380403.
Hs.731287.

Genome annotation databases

EnsembliENST00000376663; ENSP00000365851; ENSG00000168283.
GeneIDi100532731.
648.
KEGGihsa:100532731.
hsa:648.
UCSCiuc001irh.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS7138.1.
PIRiI54339.
RefSeqiNP_001190991.1. NM_001204062.1.
NP_005171.4. NM_005180.8.
UniGeneiHs.380403.
Hs.731287.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H0DX-ray2.50A5-101[»]
3RPGX-ray2.65B1-109[»]
4R8PX-ray3.28K/M2-109[»]
ProteinModelPortaliP35226.
SMRiP35226. Positions 6-103.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107116. 360 interactions.
DIPiDIP-41879N.
IntActiP35226. 37 interactions.
MINTiMINT-158260.
STRINGi9606.ENSP00000365851.

PTM databases

PhosphoSiteiP35226.

Polymorphism and mutation databases

BioMutaiBMI1.
DMDMi22258801.

Proteomic databases

MaxQBiP35226.
PaxDbiP35226.
PRIDEiP35226.

Protocols and materials databases

DNASUi648.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000376663; ENSP00000365851; ENSG00000168283.
GeneIDi100532731.
648.
KEGGihsa:100532731.
hsa:648.
UCSCiuc001irh.3. human.

Organism-specific databases

CTDi100532731.
648.
GeneCardsiGC10P022611.
HGNCiHGNC:1066. BMI1.
HPAiCAB011120.
HPA030472.
MIMi164831. gene.
neXtProtiNX_P35226.
PharmGKBiPA25376.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG304672.
GeneTreeiENSGT00550000074463.
HOGENOMiHOG000231945.
HOVERGENiHBG052826.
InParanoidiP35226.
KOiK11459.
PhylomeDBiP35226.
TreeFamiTF324206.

Enzyme and pathway databases

ReactomeiREACT_169436. Oxidative Stress Induced Senescence.
REACT_355174. SUMOylation of DNA damage response and repair proteins.

Miscellaneous databases

EvolutionaryTraceiP35226.
GeneWikiiBMI1.
NextBioi2628.
PROiP35226.
SOURCEiSearch...

Gene expression databases

BgeeiP35226.
CleanExiHS_BMI1.
ExpressionAtlasiP35226. baseline and differential.
GenevestigatoriP35226.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiBMI1_HUMAN
AccessioniPrimary (citable) accession number: P35226
Secondary accession number(s): Q16030, Q5T8Z3, Q96F37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: August 13, 2002
Last modified: May 27, 2015
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

The hPRC-H complex purification reported by PubMed:12167701 probably presents a mixture of different PRC1-like complexes.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.