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Protein

Polycomb complex protein BMI-1

Gene

BMI1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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 (PubMed:15386022, PubMed:16359901, PubMed:26151332, PubMed:16714294, PubMed:21772249, PubMed:25355358, PubMed:27827373). The complex composed of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with nucleosomal histone H2A (PubMed:21772249, PubMed:25355358). In the PRC1-like complex, regulates the E3 ubiquitin-protein ligase activity of RNF2/RING2 (PubMed:15386022, PubMed:26151332, PubMed:21772249).8 Publications

Miscellaneous

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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri18 – 57RING-typePROSITE-ProRule annotationAdd BLAST40

GO - Molecular functioni

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

GO - Biological processi

  • hemopoiesis Source: UniProtKB
  • histone H2A-K119 monoubiquitination Source: UniProtKB
  • negative regulation of G0 to G1 transition Source: Reactome
  • negative regulation of gene expression, epigenetic Source: UniProtKB
  • negative regulation of transcription by RNA polymerase II Source: UniProtKB
  • positive regulation of fibroblast proliferation Source: BHF-UCL
  • positive regulation of ubiquitin-protein transferase activity Source: UniProtKB
  • regulation of gene expression Source: BHF-UCL
  • segment specification Source: ProtInc
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionChromatin regulator, Repressor
Biological processTranscription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-4551638 SUMOylation of chromatin organization proteins
R-HSA-4570464 SUMOylation of RNA binding proteins
R-HSA-8939243 RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known
R-HSA-8943724 Regulation of PTEN gene transcription
R-HSA-8953750 Transcriptional Regulation by E2F6
SIGNORiP35226

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
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000168283.13
HGNCiHGNC:1066 BMI1
MIMi164831 gene
neXtProtiNX_P35226

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi62K → A: Strongly decreases histone H2A ubiquitination; when associated with A-64. 1 Publication1
Mutagenesisi64R → A: Mildly decreases histone H2A ubiquitination. Strongly decreases histone H2A ubiquitination; when associated with A-62. 2 Publications1
Mutagenesisi73K → N: Increases stimulation of RNF2 ubiquitin ligase activity; when associated with E-77. 1 Publication1
Mutagenesisi77D → E: Increases stimulation of RNF2 ubiquitin ligase activity; when associated with N-73. 1 Publication1
Mutagenesisi165R → E: Decreases affinity for PHC2. Abolishes interaction with PHC2; when associated with E-174. 1 Publication1
Mutagenesisi170M → E: Strongly decreases affinity for PHC2. 1 Publication1
Mutagenesisi174H → E: Strongly decreases affinity for PHC2. Abolishes interaction with PHC2; when associated with E-165. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi100532731
648
OpenTargetsiENSG00000168283
PharmGKBiPA25376

Polymorphism and mutation databases

BioMutaiBMI1
DMDMi22258801

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000559871 – 326Polycomb complex protein BMI-1Add BLAST326

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

EPDiP35226
MaxQBiP35226
PaxDbiP35226
PeptideAtlasiP35226
PRIDEiP35226
ProteomicsDBi54991

PTM databases

iPTMnetiP35226
PhosphoSitePlusiP35226

Expressioni

Gene expression databases

BgeeiENSG00000168283
CleanExiHS_BMI1
ExpressionAtlasiP35226 baseline and differential
GenevisibleiP35226 HS

Organism-specific databases

HPAiCAB011120
HPA030471
HPA030472

Interactioni

Subunit structurei

Component of a PRC1-like complex (PubMed:12167701, PubMed:15386022, PubMed:19636380, PubMed:21282530, PubMed:26151332, PubMed:21772249, PubMed:25355358). Identified in a PRC1-like HPRC-H complex with CBX2, CBX4, CBX8, PHC1, PHC2, PHC3 RING1 and RNF2 (PubMed:12167701). Interacts with RNF2/RING2 (PubMed:16714294, PubMed:21772249, PubMed:25355358). Interacts with RING1 (By similarity). Part of a complex that contains RNF2, UB2D3 and BMI1, where RNF2 and BMI1 form a tight heterodimer, and UB2D3 interacts only with RNF2 (PubMed:21772249, PubMed:25355358). The complex composed of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with nucleosomal histone H2A (PubMed:21772249, PubMed:25355358). Interacts with CBX7 and CBX8 (PubMed:19636380). Interacts with SPOP (PubMed:15897469). Part of a complex consisting of BMI1, CUL3 and SPOP (PubMed:15897469). Interacts with E4F1 (PubMed:16882984). Interacts with PHC2 (PubMed:9121482, PubMed:9199346, PubMed:27827373).By similarity13 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • RING-like zinc finger domain binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107116, 393 interactors
1529410, 5 interactors
CORUMiP35226
DIPiDIP-41879N
IntActiP35226, 48 interactors
MINTiP35226
STRINGi9606.ENSP00000365851

Structurei

Secondary structure

1326
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 8Combined sources3
Helixi9 – 12Combined sources4
Helixi13 – 15Combined sources3
Turni19 – 21Combined sources3
Beta strandi22 – 24Combined sources3
Beta strandi29 – 31Combined sources3
Turni32 – 34Combined sources3
Beta strandi36 – 39Combined sources4
Helixi40 – 46Combined sources7
Turni47 – 49Combined sources3
Turni54 – 56Combined sources3
Helixi65 – 68Combined sources4
Beta strandi69 – 71Combined sources3
Helixi73 – 82Combined sources10
Helixi86 – 100Combined sources15
Beta strandi130 – 137Combined sources8
Helixi140 – 142Combined sources3
Helixi147 – 150Combined sources4
Beta strandi162 – 167Combined sources6
Helixi172 – 182Combined sources11
Beta strandi189 – 199Combined sources11
Helixi206 – 213Combined sources8
Beta strandi217 – 229Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H0DX-ray2.50A5-101[»]
2NA1NMR-A121-235[»]
3RPGX-ray2.65B1-109[»]
4R8PX-ray3.28K/M2-109[»]
5FR6X-ray2.51A121-235[»]
ProteinModelPortaliP35226
SMRiP35226
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35226

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni162 – 182Interaction with PHC21 PublicationAdd BLAST21
Regioni164 – 228Interaction with E4F11 PublicationAdd BLAST65

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi81 – 95Nuclear localization signalSequence analysisAdd BLAST15

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi251 – 326Pro/Ser-richAdd BLAST76

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri18 – 57RING-typePROSITE-ProRule annotationAdd BLAST40

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2660 Eukaryota
ENOG410XPCN LUCA
GeneTreeiENSGT00550000074463
HOGENOMiHOG000231945
HOVERGENiHBG052826
InParanoidiP35226
KOiK11459
OrthoDBiEOG091G09IB
PhylomeDBiP35226
TreeFamiTF324206

Family and domain databases

Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR032443 RAWUL
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
PfamiView protein in Pfam
PF16207 RAWUL, 1 hit
SMARTiView protein in SMART
SM00184 RING, 1 hit
PROSITEiView protein in PROSITE
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti109G → S in AAB27059 (PubMed:8390036).Curated1
Sequence conflicti265I → V in AAA19873 (PubMed:8268912).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05208718C → Y. Corresponds to variant dbSNP:rs1042059Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13689 mRNA Translation: AAA19873.1
AK313235 mRNA Translation: BAG36046.1
AL158211 Genomic DNA No translation available.
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.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiBMI1_HUMAN
AccessioniPrimary (citable) accession number: P35226
Secondary accession number(s): Q16030, Q5T8Z3, Q96F37
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: August 13, 2002
Last modified: June 20, 2018
This is version 192 of the entry and version 2 of the sequence. See 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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