BMI1_HUMAN
ID BMI1_HUMAN Reviewed; 326 AA.
AC P35226; Q16030; Q5T8Z3; Q96F37;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Polycomb complex protein BMI-1;
DE AltName: Full=Polycomb group RING finger protein 4;
DE AltName: Full=RING finger protein 51;
GN Name=BMI1; Synonyms=PCGF4, RNF51;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Erythrocyte;
RX PubMed=8268912; DOI=10.1093/hmg/2.10.1597;
RA Alkema M.J., Wiegand J., Raap A.K., Berns A., van Lohuizen M.;
RT "Characterization and chromosomal localization of the human proto-oncogene
RT BMI-1.";
RL Hum. Mol. Genet. 2:1597-1603(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-300.
RC TISSUE=Thymus;
RX PubMed=8390036;
RA Levy L.S., Lobelle-Rich P.A., Overbaugh J.;
RT "flvi-2, a target of retroviral insertional mutagenesis in feline thymic
RT lymphosarcomas, encodes bmi-1.";
RL Oncogene 8:1833-1838(1993).
RN [7]
RP INTERACTION WITH PHC2.
RX PubMed=9121482; DOI=10.1128/mcb.17.4.2326;
RA Gunster M.J., Satijn D.P.E., Hamer K.M., den Blaauwen J.L., de Bruijn D.,
RA Alkema M.J., van Lohuizen M., van Driel R., Otte A.P.;
RT "Identification and characterization of interactions between the vertebrate
RT polycomb-group protein BMI1 and human homologs of polyhomeotic.";
RL Mol. Cell. Biol. 17:2326-2335(1997).
RN [8]
RP INTERACTION WITH PHC2, AND SUBCELLULAR LOCATION.
RX PubMed=9199346; DOI=10.1128/mcb.17.7.4105;
RA Satijn D.P.E., Gunster M.J., van der Vlag J., Hamer K.M., Schul W.,
RA Alkema M.J., Saurin A.J., Freemont P.S., van Driel R., Otte A.P.;
RT "RING1 is associated with the polycomb group protein complex and acts as a
RT transcriptional repressor.";
RL Mol. Cell. Biol. 17:4105-4113(1997).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A PRC1-LIKE
RP HPRC-H COMPLEX WITH CBX2; CBX4; CBX8; PHC1; PHC2; PHC3; RING1 AND RNF2.
RX PubMed=12167701; DOI=10.1128/mcb.22.17.6070-6078.2002;
RA Levine S.S., Weiss A., Erdjument-Bromage H., Shao Z., Tempst P.,
RA Kingston R.E.;
RT "The core of the polycomb repressive complex is compositionally and
RT functionally conserved in flies and humans.";
RL Mol. Cell. Biol. 22:6070-6078(2002).
RN [10]
RP IDENTIFICATION IN A PRC1-LIKE COMPLEX, AND FUNCTION.
RX PubMed=15386022; DOI=10.1038/nature02985;
RA Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P., Jones R.S.,
RA Zhang Y.;
RT "Role of histone H2A ubiquitination in Polycomb silencing.";
RL Nature 431:873-878(2004).
RN [11]
RP FUNCTION.
RX PubMed=16359901; DOI=10.1016/j.molcel.2005.12.002;
RA Cao R., Tsukada Y., Zhang Y.;
RT "Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing.";
RL Mol. Cell 20:845-854(2005).
RN [12]
RP INTERACTION WITH SPOP, IDENTIFICATION IN A COMPLEX WITH CUL3 AND SPOP, AND
RP UBIQUITINATION.
RX PubMed=15897469; DOI=10.1073/pnas.0408918102;
RA Hernandez-Munoz I., Lund A.H., van der Stoop P., Boutsma E., Muijrers I.,
RA Verhoeven E., Nusinow D.A., Panning B., Marahrens Y., van Lohuizen M.;
RT "Stable X chromosome inactivation involves the PRC1 Polycomb complex and
RT requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:7635-7640(2005).
RN [13]
RP FUNCTION, INTERACTION WITH E4F1, AND SUBCELLULAR LOCATION.
RX PubMed=16882984; DOI=10.1101/gad.1453406;
RA Chagraoui J., Niessen S.L., Lessard J., Girard S., Coulombe P.,
RA Sauvageau M., Meloche S., Sauvageau G.;
RT "E4F1: a novel candidate factor for mediating BMI1 function in primitive
RT hematopoietic cells.";
RL Genes Dev. 20:2110-2120(2006).
RN [14]
RP IDENTIFICATION IN A PRC1-LIKE COMPLEX, AND INTERACTION WITH CBX7 AND CBX8.
RX PubMed=19636380; DOI=10.1371/journal.pone.0006380;
RA Maertens G.N., El Messaoudi-Aubert S., Racek T., Stock J.K., Nicholls J.,
RA Rodriguez-Niedenfuhr M., Gil J., Peters G.;
RT "Several distinct polycomb complexes regulate and co-localize on the INK4a
RT tumor suppressor locus.";
RL PLoS ONE 4:E6380-E6380(2009).
RN [15]
RP IDENTIFICATION IN A PRC1-LIKE COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=21282530; DOI=10.1074/mcp.m110.002642;
RA Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O.;
RT "Interaction proteomics analysis of polycomb proteins defines distinct PRC1
RT Complexes in mammalian cells.";
RL Mol. Cell. Proteomics 0:0-0(2011).
RN [16]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF LYS-73 AND ASP-77.
RX PubMed=26151332; DOI=10.1038/ncomms8621;
RA Taherbhoy A.M., Huang O.W., Cochran A.G.;
RT "BMI1-RING1B is an autoinhibited RING E3 ubiquitin ligase.";
RL Nat. Commun. 6:7621-7621(2015).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 5-101 IN COMPLEX WITH RNF2 AND
RP ZINC IONS, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=16714294; DOI=10.1074/jbc.m602461200;
RA Li Z., Cao R., Wang M., Myers M.P., Zhang Y., Xu R.M.;
RT "Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex.";
RL J. Biol. Chem. 281:20643-20649(2006).
RN [18] {ECO:0007744|PDB:3RPG}
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 1-109 IN COMPLEX WITH ZINC IONS;
RP RNF2 AND UB2D3, FUNCTION, AND MUTAGENESIS OF LYS-62 AND ARG-64.
RX PubMed=21772249; DOI=10.1038/emboj.2011.243;
RA Bentley M.L., Corn J.E., Dong K.C., Phung Q., Cheung T.K., Cochran A.G.;
RT "Recognition of UbcH5c and the nucleosome by the Bmi1/Ring1b ubiquitin
RT ligase complex.";
RL EMBO J. 30:3285-3297(2011).
RN [19] {ECO:0007744|PDB:4R8P}
RP X-RAY CRYSTALLOGRAPHY (3.28 ANGSTROMS) OF 2-109 IN COMPLEX WITH THE
RP NUCLEOSOME; RNF2; UB2D3 AND ZINC IONS, FUNCTION, AND MUTAGENESIS OF ARG-64.
RX PubMed=25355358; DOI=10.1038/nature13890;
RA McGinty R.K., Henrici R.C., Tan S.;
RT "Crystal structure of the PRC1 ubiquitylation module bound to the
RT nucleosome.";
RL Nature 514:591-596(2014).
RN [20] {ECO:0007744|PDB:2NA1, ECO:0007744|PDB:5FR6}
RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 121-235, STRUCTURE BY NMR OF
RP 121-235 IN COMPLEX WITH PHC2, FUNCTION, AND MUTAGENESIS OF ARG-165; MET-170
RP AND HIS-174.
RX PubMed=27827373; DOI=10.1038/ncomms13343;
RA Gray F., Cho H.J., Shukla S., He S., Harris A., Boytsov B., Jaremko L.,
RA Jaremko M., Demeler B., Lawlor E.R., Grembecka J., Cierpicki T.;
RT "BMI1 regulates PRC1 architecture and activity through homo- and hetero-
RT oligomerization.";
RL Nat. Commun. 7:13343-13343(2016).
CC -!- FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like
CC complex, a complex class required to maintain the transcriptionally
CC repressive state of many genes, including Hox genes, throughout
CC development. PcG PRC1 complex acts via chromatin remodeling and
CC modification of histones; it mediates monoubiquitination of histone H2A
CC 'Lys-119', rendering chromatin heritably changed in its expressibility
CC (PubMed:15386022, PubMed:16359901, PubMed:26151332, PubMed:16714294,
CC PubMed:21772249, PubMed:25355358, PubMed:27827373). The complex
CC composed of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity
CC only with nucleosomal histone H2A (PubMed:21772249, PubMed:25355358).
CC In the PRC1-like complex, regulates the E3 ubiquitin-protein ligase
CC activity of RNF2/RING2 (PubMed:15386022, PubMed:26151332,
CC PubMed:21772249). {ECO:0000269|PubMed:15386022,
CC ECO:0000269|PubMed:16359901, ECO:0000269|PubMed:16714294,
CC ECO:0000269|PubMed:16882984, ECO:0000269|PubMed:21772249,
CC ECO:0000269|PubMed:25355358, ECO:0000269|PubMed:26151332,
CC ECO:0000269|PubMed:27827373}.
CC -!- SUBUNIT: Component of a PRC1-like complex (PubMed:12167701,
CC PubMed:15386022, PubMed:19636380, PubMed:21282530, PubMed:26151332,
CC PubMed:21772249, PubMed:25355358). Identified in a PRC1-like HPRC-H
CC complex with CBX2, CBX4, CBX8, PHC1, PHC2, PHC3 RING1 and RNF2
CC (PubMed:12167701). Interacts with RNF2/RING2 (PubMed:16714294,
CC PubMed:21772249, PubMed:25355358). Interacts with RING1 (By
CC similarity). Part of a complex that contains RNF2, UB2D3 and BMI1,
CC where RNF2 and BMI1 form a tight heterodimer, and UB2D3 interacts only
CC with RNF2 (PubMed:21772249, PubMed:25355358). The complex composed of
CC RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with
CC nucleosomal histone H2A (PubMed:21772249, PubMed:25355358). Interacts
CC with CBX7 and CBX8 (PubMed:19636380). Interacts with SPOP
CC (PubMed:15897469). Part of a complex consisting of BMI1, CUL3 and SPOP
CC (PubMed:15897469). Interacts with E4F1 (PubMed:16882984). Interacts
CC with PHC2 (PubMed:9121482, PubMed:9199346, PubMed:27827373). Interacts
CC with zinc finger protein ZNF277 (By similarity). May be part of a
CC complex including at least ZNF277, BMI1 and RNF2/RING2 (By similarity).
CC {ECO:0000250|UniProtKB:P25916, ECO:0000269|PubMed:12167701,
CC ECO:0000269|PubMed:15386022, ECO:0000269|PubMed:15897469,
CC ECO:0000269|PubMed:16714294, ECO:0000269|PubMed:16882984,
CC ECO:0000269|PubMed:19636380, ECO:0000269|PubMed:21282530,
CC ECO:0000269|PubMed:21772249, ECO:0000269|PubMed:25355358,
CC ECO:0000269|PubMed:26151332, ECO:0000269|PubMed:27827373,
CC ECO:0000269|PubMed:9121482, ECO:0000269|PubMed:9199346}.
CC -!- INTERACTION:
CC P35226; O00257: CBX4; NbExp=8; IntAct=EBI-2341576, EBI-722425;
CC P35226; O00257-3: CBX4; NbExp=2; IntAct=EBI-2341576, EBI-4392727;
CC P35226; O95503: CBX6; NbExp=8; IntAct=EBI-2341576, EBI-3951758;
CC P35226; O95931: CBX7; NbExp=12; IntAct=EBI-2341576, EBI-3923843;
CC P35226; Q9HC52: CBX8; NbExp=30; IntAct=EBI-2341576, EBI-712912;
CC P35226; P68400: CSNK2A1; NbExp=2; IntAct=EBI-2341576, EBI-347804;
CC P35226; O75031: HSF2BP; NbExp=3; IntAct=EBI-2341576, EBI-7116203;
CC P35226; Q9HCE1: MOV10; NbExp=4; IntAct=EBI-2341576, EBI-1055820;
CC P35226; Q9GZM8: NDEL1; NbExp=3; IntAct=EBI-2341576, EBI-928842;
CC P35226; P78364: PHC1; NbExp=6; IntAct=EBI-2341576, EBI-725403;
CC P35226; Q8IXK0: PHC2; NbExp=9; IntAct=EBI-2341576, EBI-713786;
CC P35226; O94906: PRPF6; NbExp=8; IntAct=EBI-2341576, EBI-536755;
CC P35226; P60484: PTEN; NbExp=7; IntAct=EBI-2341576, EBI-696162;
CC P35226; Q06587: RING1; NbExp=22; IntAct=EBI-2341576, EBI-752313;
CC P35226; Q99496: RNF2; NbExp=21; IntAct=EBI-2341576, EBI-722416;
CC P35226; P0CG48: UBC; NbExp=2; IntAct=EBI-2341576, EBI-3390054;
CC P35226; P51784: USP11; NbExp=7; IntAct=EBI-2341576, EBI-306876;
CC P35226; Q93009: USP7; NbExp=8; IntAct=EBI-2341576, EBI-302474;
CC P35226; Q9H270: VPS11; NbExp=2; IntAct=EBI-2341576, EBI-373380;
CC P35226; Q9P202: WHRN; NbExp=3; IntAct=EBI-2341576, EBI-310886;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16882984,
CC ECO:0000269|PubMed:9199346}. Cytoplasm {ECO:0000269|PubMed:16882984}.
CC -!- INDUCTION: Down-regulated by oxidative stress.
CC {ECO:0000250|UniProtKB:P25916}.
CC -!- PTM: Monoubiquitinated (By similarity). May be polyubiquitinated; which
CC does not lead to proteasomal degradation. {ECO:0000250,
CC ECO:0000269|PubMed:15897469}.
CC -!- MISCELLANEOUS: The hPRC-H complex purification reported by
CC PubMed:12167701 probably presents a mixture of different PRC1-like
CC complexes.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BMI1ID807ch10p12.html";
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DR EMBL; L13689; AAA19873.1; -; mRNA.
DR EMBL; AK313235; BAG36046.1; -; mRNA.
DR EMBL; AL158211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86148.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86150.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86151.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86154.1; -; Genomic_DNA.
DR EMBL; BC011652; AAH11652.1; -; mRNA.
DR EMBL; AH004292; AAB27059.1; -; mRNA.
DR CCDS; CCDS7138.1; -.
DR PIR; I54339; I54339.
DR RefSeq; NP_001190991.1; NM_001204062.1.
DR RefSeq; NP_005171.4; NM_005180.8.
DR PDB; 2H0D; X-ray; 2.50 A; A=5-101.
DR PDB; 2NA1; NMR; -; A=121-235.
DR PDB; 3RPG; X-ray; 2.65 A; B=1-109.
DR PDB; 4R8P; X-ray; 3.28 A; K/M=2-109.
DR PDB; 5FR6; X-ray; 2.51 A; A=121-235.
DR PDB; 6WI7; X-ray; 1.70 A; A=1-104.
DR PDB; 6WI8; X-ray; 3.09 A; A/B=1-104.
DR PDB; 7ND1; NMR; -; H=4-104.
DR PDBsum; 2H0D; -.
DR PDBsum; 2NA1; -.
DR PDBsum; 3RPG; -.
DR PDBsum; 4R8P; -.
DR PDBsum; 5FR6; -.
DR PDBsum; 6WI7; -.
DR PDBsum; 6WI8; -.
DR PDBsum; 7ND1; -.
DR AlphaFoldDB; P35226; -.
DR SMR; P35226; -.
DR BioGRID; 107116; 478.
DR BioGRID; 1529410; 16.
DR CORUM; P35226; -.
DR DIP; DIP-41879N; -.
DR IntAct; P35226; 961.
DR MINT; P35226; -.
DR STRING; 9606.ENSP00000365851; -.
DR ChEMBL; CHEMBL4295749; -.
DR GlyGen; P35226; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P35226; -.
DR PhosphoSitePlus; P35226; -.
DR BioMuta; BMI1; -.
DR DMDM; 22258801; -.
DR EPD; P35226; -.
DR jPOST; P35226; -.
DR MassIVE; P35226; -.
DR MaxQB; P35226; -.
DR PaxDb; P35226; -.
DR PeptideAtlas; P35226; -.
DR PRIDE; P35226; -.
DR ProteomicsDB; 54991; -.
DR Antibodypedia; 4554; 965 antibodies from 46 providers.
DR DNASU; 648; -.
DR Ensembl; ENST00000376663.8; ENSP00000365851.3; ENSG00000168283.14.
DR GeneID; 100532731; -.
DR GeneID; 648; -.
DR KEGG; hsa:100532731; -.
DR KEGG; hsa:648; -.
DR MANE-Select; ENST00000376663.8; ENSP00000365851.3; NM_005180.9; NP_005171.4.
DR UCSC; uc001irh.4; human.
DR CTD; 100532731; -.
DR CTD; 648; -.
DR DisGeNET; 100532731; -.
DR DisGeNET; 648; -.
DR GeneCards; BMI1; -.
DR HGNC; HGNC:1066; BMI1.
DR HPA; ENSG00000168283; Low tissue specificity.
DR MIM; 164831; gene.
DR neXtProt; NX_P35226; -.
DR OpenTargets; ENSG00000168283; -.
DR PharmGKB; PA25376; -.
DR VEuPathDB; HostDB:ENSG00000168283; -.
DR eggNOG; KOG2660; Eukaryota.
DR GeneTree; ENSGT00940000156042; -.
DR HOGENOM; CLU_046427_0_0_1; -.
DR InParanoid; P35226; -.
DR OMA; DIDARYL; -.
DR OrthoDB; 1344247at2759; -.
DR PhylomeDB; P35226; -.
DR TreeFam; TF324206; -.
DR PathwayCommons; P35226; -.
DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-HSA-4655427; SUMOylation of DNA methylation proteins.
DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
DR SignaLink; P35226; -.
DR SIGNOR; P35226; -.
DR BioGRID-ORCS; 100532731; 17 hits in 606 CRISPR screens.
DR BioGRID-ORCS; 648; 44 hits in 1113 CRISPR screens.
DR EvolutionaryTrace; P35226; -.
DR GeneWiki; BMI1; -.
DR Pharos; P35226; Tbio.
DR PRO; PR:P35226; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P35226; protein.
DR Bgee; ENSG00000168283; Expressed in germinal epithelium of ovary and 209 other tissues.
DR ExpressionAtlas; P35226; baseline and differential.
DR Genevisible; P35226; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031519; C:PcG protein complex; IDA:UniProtKB.
DR GO; GO:0035102; C:PRC1 complex; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR GO; GO:0071535; F:RING-like zinc finger domain binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0097027; F:ubiquitin-protein transferase activator activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR GO; GO:0006306; P:DNA methylation; IEA:Ensembl.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0030097; P:hemopoiesis; IEP:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; IEA:Ensembl.
DR GO; GO:0036353; P:histone H2A-K119 monoubiquitination; IMP:UniProtKB.
DR GO; GO:0006959; P:humoral immune response; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:BHF-UCL.
DR GO; GO:0033092; P:positive regulation of immature T cell proliferation in thymus; IEA:Ensembl.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:2000011; P:regulation of adaxial/abaxial pattern formation; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0021903; P:rostrocaudal neural tube patterning; IEA:Ensembl.
DR GO; GO:0007379; P:segment specification; TAS:ProtInc.
DR GO; GO:0048103; P:somatic stem cell division; IEA:Ensembl.
DR Gene3D; 3.30.40.10; -; 1.
DR IDEAL; IID00450; -.
DR InterPro; IPR032443; RAWUL.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF16207; RAWUL; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Cytoplasm; Metal-binding; Nucleus;
KW Proto-oncogene; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..326
FT /note="Polycomb complex protein BMI-1"
FT /id="PRO_0000055987"
FT ZN_FING 18..57
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 162..182
FT /note="Interaction with PHC2"
FT /evidence="ECO:0000269|PubMed:27827373"
FT REGION 164..228
FT /note="Interaction with E4F1"
FT /evidence="ECO:0000269|PubMed:16882984"
FT REGION 236..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 81..95
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 244..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 18
FT /note="C -> Y (in dbSNP:rs1042059)"
FT /id="VAR_052087"
FT MUTAGEN 62
FT /note="K->A: Strongly decreases histone H2A ubiquitination;
FT when associated with A-64."
FT /evidence="ECO:0000269|PubMed:21772249"
FT MUTAGEN 64
FT /note="R->A: Mildly decreases histone H2A ubiquitination.
FT Strongly decreases histone H2A ubiquitination; when
FT associated with A-62."
FT /evidence="ECO:0000269|PubMed:21772249,
FT ECO:0000269|PubMed:25355358"
FT MUTAGEN 73
FT /note="K->N: Increases stimulation of RNF2 ubiquitin ligase
FT activity; when associated with E-77."
FT /evidence="ECO:0000269|PubMed:26151332"
FT MUTAGEN 77
FT /note="D->E: Increases stimulation of RNF2 ubiquitin ligase
FT activity; when associated with N-73."
FT /evidence="ECO:0000269|PubMed:26151332"
FT MUTAGEN 165
FT /note="R->E: Decreases affinity for PHC2. Abolishes
FT interaction with PHC2; when associated with E-174."
FT /evidence="ECO:0000269|PubMed:27827373"
FT MUTAGEN 170
FT /note="M->E: Strongly decreases affinity for PHC2."
FT /evidence="ECO:0000269|PubMed:27827373"
FT MUTAGEN 174
FT /note="H->E: Strongly decreases affinity for PHC2.
FT Abolishes interaction with PHC2; when associated with E-
FT 165."
FT /evidence="ECO:0000269|PubMed:27827373"
FT CONFLICT 109
FT /note="G -> S (in Ref. 6; AAB27059)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="I -> V (in Ref. 1; AAA19873)"
FT /evidence="ECO:0000305"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:6WI7"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:6WI7"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:6WI7"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:6WI7"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:6WI7"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:6WI7"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:6WI7"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:6WI7"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:6WI7"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:6WI7"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:6WI7"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:6WI7"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:6WI7"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:6WI7"
FT HELIX 86..100
FT /evidence="ECO:0007829|PDB:6WI7"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:5FR6"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:2NA1"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:2NA1"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:5FR6"
FT HELIX 172..182
FT /evidence="ECO:0007829|PDB:5FR6"
FT STRAND 189..199
FT /evidence="ECO:0007829|PDB:5FR6"
FT HELIX 206..213
FT /evidence="ECO:0007829|PDB:5FR6"
FT STRAND 217..229
FT /evidence="ECO:0007829|PDB:5FR6"
SQ SEQUENCE 326 AA; 36949 MW; 030A7D396BADA543 CRC64;
MHRTTRIKIT ELNPHLMCVL CGGYFIDATT IIECLHSFCK TCIVRYLETS KYCPICDVQV
HKTRPLLNIR SDKTLQDIVY KLVPGLFKNE MKRRRDFYAA HPSADAANGS NEDRGEVADE
DKRIITDDEI ISLSIEFFDQ NRLDRKVNKD KEKSKEEVND KRYLRCPAAM TVMHLRKFLR
SKMDIPNTFQ IDVMYEEEPL KDYYTLMDIA YIYTWRRNGP LPLKYRVRPT CKRMKISHQR
DGLTNAGELE SDSGSDKANS PAGGIPSTSS CLPSPSTPVQ SPHPQFPHIS STMNGTSNSP
SGNHQSSFAN RPRKSSVNGS SATSSG
