BRE1B_HUMAN
ID BRE1B_HUMAN Reviewed; 1001 AA.
AC O75150; A0A024QZG0; Q6AHZ6; Q6N005; Q7L3T6; Q8N615; Q96T18; Q9BSV9; Q9HC82;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 5.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=E3 ubiquitin-protein ligase BRE1B;
DE Short=BRE1-B;
DE EC=2.3.2.27 {ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:19410543};
DE AltName: Full=95 kDa retinoblastoma-associated protein;
DE Short=RBP95;
DE AltName: Full=RING finger protein 40;
DE AltName: Full=RING-type E3 ubiquitin transferase BRE1B {ECO:0000305};
GN Name=RNF40; Synonyms=BRE1B, KIAA0661;
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] (ISOFORM 3), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, SUBUNIT, INTERACTION WITH RB1, AND MUTAGENESIS OF LEU-109;
RP CYS-111 AND GLU-113.
RC TISSUE=Fetal brain;
RX PubMed=10944455; DOI=10.1006/bbrc.2000.3242;
RA Wen H., Ao S.;
RT "RBP95, a novel leucine zipper protein, binds to the retinoblastoma
RT protein.";
RL Biochem. Biophys. Res. Commun. 275:141-148(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Teratocarcinoma;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix, and Rectum tumor;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Mammary gland, Skin, and Uterus;
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND IDENTIFICATION IN A COMPLEX WITH
RP RNF20 AND UBE2E1.
RX PubMed=16307923; DOI=10.1016/j.molcel.2005.09.025;
RA Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H., Tempst P.,
RA Reinberg D.;
RT "Monoubiquitination of human histone H2B: the factors involved and their
RT roles in HOX gene regulation.";
RL Mol. Cell 20:601-611(2005).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=19410543; DOI=10.1016/j.cell.2009.02.027;
RA Kim J., Guermah M., McGinty R.K., Lee J.S., Tang Z., Milne T.A.,
RA Shilatifard A., Muir T.W., Roeder R.G.;
RT "RAD6-mediated transcription-coupled H2B ubiquitylation directly stimulates
RT H3K4 methylation in human cells.";
RL Cell 137:459-471(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP INTERACTION WITH WAC.
RX PubMed=21329877; DOI=10.1016/j.molcel.2011.01.024;
RA Zhang F., Yu X.;
RT "WAC, a functional partner of RNF20/40, regulates histone H2B
RT ubiquitination and gene transcription.";
RL Mol. Cell 41:384-397(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-578 AND LYS-579, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Component of the RNF20/40 E3 ubiquitin-protein ligase complex
CC that mediates monoubiquitination of 'Lys-120' of histone H2B
CC (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic
CC transcriptional activation and is also prerequisite for histone H3
CC 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It
CC thereby plays a central role in histone code and gene regulation. The
CC RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation
CC with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with
CC UBE2E1/UBCH are contradictory. Required for transcriptional activation
CC of Hox genes. {ECO:0000269|PubMed:16307923,
CC ECO:0000269|PubMed:19410543}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:16307923,
CC ECO:0000269|PubMed:19410543};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the RNF20/40 complex (also known as BRE1 complex)
CC probably composed of 2 copies of RNF20/BRE1A and 2 copies of
CC RNF40/BRE1B. Interacts with UBE2E1/UBCH6. Interacts with RB1 and WAC.
CC {ECO:0000269|PubMed:10944455, ECO:0000269|PubMed:16307923,
CC ECO:0000269|PubMed:19410543, ECO:0000269|PubMed:21329877}.
CC -!- INTERACTION:
CC O75150; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-744408, EBI-746752;
CC O75150; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-744408, EBI-10187270;
CC O75150; Q8IYE0-2: CCDC146; NbExp=3; IntAct=EBI-744408, EBI-10247802;
CC O75150; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-744408, EBI-11988027;
CC O75150; Q68J44: DUSP29; NbExp=3; IntAct=EBI-744408, EBI-1054321;
CC O75150; P42858: HTT; NbExp=12; IntAct=EBI-744408, EBI-466029;
CC O75150; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-744408, EBI-16439278;
CC O75150; Q09161: NCBP1; NbExp=4; IntAct=EBI-744408, EBI-464743;
CC O75150; P06400: RB1; NbExp=3; IntAct=EBI-744408, EBI-491274;
CC O75150; Q5VTR2: RNF20; NbExp=10; IntAct=EBI-744408, EBI-2372238;
CC O75150; Q86XK3: SFR1; NbExp=3; IntAct=EBI-744408, EBI-1104535;
CC O75150; Q7KZS0: UBE2I; NbExp=6; IntAct=EBI-744408, EBI-10180829;
CC O75150; Q6PEW1: ZCCHC12; NbExp=3; IntAct=EBI-744408, EBI-748373;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10944455}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O75150-1; Sequence=Displayed;
CC Name=3;
CC IsoId=O75150-3; Sequence=VSP_016682, VSP_016683;
CC Name=4;
CC IsoId=O75150-4; Sequence=VSP_016681;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at higher level
CC in testis, heart and pancreas, while it is only weakly expressed in
CC lung, skeletal muscle and small intestine.
CC {ECO:0000269|PubMed:10944455}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31636.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAE45869.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR EMBL; AF122819; AAG13723.1; -; mRNA.
DR EMBL; AB014561; BAA31636.2; ALT_INIT; mRNA.
DR EMBL; AK027406; BAB55092.1; -; mRNA.
DR EMBL; BX640763; CAE45869.1; ALT_SEQ; mRNA.
DR EMBL; CR627431; CAH10518.1; -; mRNA.
DR EMBL; AC106886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471192; EAW52197.1; -; Genomic_DNA.
DR EMBL; CH471192; EAW52200.1; -; Genomic_DNA.
DR EMBL; BC004527; AAH04527.2; -; mRNA.
DR EMBL; BC006133; AAH06133.1; -; mRNA.
DR EMBL; BC011769; AAH11769.1; -; mRNA.
DR EMBL; BC018647; AAH18647.1; -; mRNA.
DR EMBL; BC030802; AAH30802.2; -; mRNA.
DR CCDS; CCDS10691.1; -. [O75150-1]
DR CCDS; CCDS55994.1; -. [O75150-4]
DR PIR; JC7363; JC7363.
DR RefSeq; NP_001193962.1; NM_001207033.1.
DR RefSeq; NP_001193963.1; NM_001207034.1. [O75150-4]
DR RefSeq; NP_001273501.1; NM_001286572.2. [O75150-1]
DR RefSeq; NP_055586.1; NM_014771.3. [O75150-1]
DR AlphaFoldDB; O75150; -.
DR SMR; O75150; -.
DR BioGRID; 115149; 165.
DR CORUM; O75150; -.
DR IntAct; O75150; 63.
DR MINT; O75150; -.
DR STRING; 9606.ENSP00000325677; -.
DR GlyGen; O75150; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75150; -.
DR MetOSite; O75150; -.
DR PhosphoSitePlus; O75150; -.
DR BioMuta; RNF40; -.
DR EPD; O75150; -.
DR jPOST; O75150; -.
DR MassIVE; O75150; -.
DR PaxDb; O75150; -.
DR PeptideAtlas; O75150; -.
DR PRIDE; O75150; -.
DR ProteomicsDB; 49814; -. [O75150-1]
DR ProteomicsDB; 49815; -. [O75150-3]
DR ProteomicsDB; 49816; -. [O75150-4]
DR Antibodypedia; 13809; 275 antibodies from 32 providers.
DR DNASU; 9810; -.
DR Ensembl; ENST00000324685.11; ENSP00000325677.6; ENSG00000103549.22. [O75150-1]
DR Ensembl; ENST00000357890.9; ENSP00000350563.5; ENSG00000103549.22. [O75150-4]
DR GeneID; 9810; -.
DR KEGG; hsa:9810; -.
DR MANE-Select; ENST00000324685.11; ENSP00000325677.6; NM_014771.4; NP_055586.1.
DR UCSC; uc002dzq.4; human. [O75150-1]
DR CTD; 9810; -.
DR DisGeNET; 9810; -.
DR GeneCards; RNF40; -.
DR HGNC; HGNC:16867; RNF40.
DR HPA; ENSG00000103549; Low tissue specificity.
DR MIM; 607700; gene.
DR neXtProt; NX_O75150; -.
DR OpenTargets; ENSG00000103549; -.
DR PharmGKB; PA34440; -.
DR VEuPathDB; HostDB:ENSG00000103549; -.
DR eggNOG; KOG0978; Eukaryota.
DR GeneTree; ENSGT00390000002866; -.
DR InParanoid; O75150; -.
DR OMA; THIEIMT; -.
DR OrthoDB; 782448at2759; -.
DR PhylomeDB; O75150; -.
DR TreeFam; TF323183; -.
DR PathwayCommons; O75150; -.
DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR SignaLink; O75150; -.
DR SIGNOR; O75150; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 9810; 371 hits in 1122 CRISPR screens.
DR ChiTaRS; RNF40; human.
DR GeneWiki; RNF40; -.
DR GenomeRNAi; 9810; -.
DR Pharos; O75150; Tbio.
DR PRO; PR:O75150; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O75150; protein.
DR Bgee; ENSG00000103549; Expressed in ventricular zone and 149 other tissues.
DR ExpressionAtlas; O75150; baseline and differential.
DR Genevisible; O75150; HS.
DR GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0019898; C:extrinsic component of membrane; IEA:Ensembl.
DR GO; GO:0033503; C:HULC complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0017075; F:syntaxin-1 binding; IEA:Ensembl.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0071894; P:histone H2B conserved C-terminal lysine ubiquitination; IBA:GO_Central.
DR GO; GO:0033523; P:histone H2B ubiquitination; IDA:UniProtKB.
DR GO; GO:0010390; P:histone monoubiquitination; IDA:UniProtKB.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IEA:Ensembl.
DR GO; GO:1902916; P:positive regulation of protein polyubiquitination; IEA:Ensembl.
DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23163; PTHR23163; 1.
DR Pfam; PF00097; zf-C3HC4; 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 Acetylation; Alternative splicing; Chromatin regulator; Coiled coil;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..1001
FT /note="E3 ubiquitin-protein ligase BRE1B"
FT /id="PRO_0000055839"
FT ZN_FING 948..987
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 44..91
FT /evidence="ECO:0000255"
FT COILED 189..377
FT /evidence="ECO:0000255"
FT COILED 437..525
FT /evidence="ECO:0000255"
FT COILED 627..946
FT /evidence="ECO:0000255"
FT COMPBIAS 604..619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3U319"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VTR2"
FT MOD_RES 355
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5VTR2"
FT MOD_RES 517
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3U319"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VTR2"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U319"
FT CROSSLNK 578
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 579
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 332..431
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016681"
FT VAR_SEQ 822..838
FT /note="DAQLLTVQKLEEKERAL -> WPPPACRLELERWGSWP (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:10944455"
FT /id="VSP_016682"
FT VAR_SEQ 839..1001
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10944455"
FT /id="VSP_016683"
FT VARIANT 463
FT /note="R -> H (in dbSNP:rs11556801)"
FT /id="VAR_055021"
FT VARIANT 615
FT /note="R -> Q (in dbSNP:rs7195142)"
FT /id="VAR_055022"
FT MUTAGEN 109
FT /note="L->S: Abolishes interaction with RB1."
FT /evidence="ECO:0000269|PubMed:10944455"
FT MUTAGEN 111
FT /note="C->M: Abolishes interaction with RB1."
FT /evidence="ECO:0000269|PubMed:10944455"
FT MUTAGEN 113
FT /note="E->Q: Abolishes interaction with RB1."
FT /evidence="ECO:0000269|PubMed:10944455"
FT CONFLICT 56
FT /note="N -> D (in Ref. 3; BAB55092)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="R -> L (in Ref. 1; AAG13723)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="L -> P (in Ref. 3; BAB55092)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="S -> G (in Ref. 3; BAB55092)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="E -> K (in Ref. 4; CAH10518)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="K -> E (in Ref. 4; CAE45869)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="S -> F (in Ref. 4; CAE45869)"
FT /evidence="ECO:0000305"
FT CONFLICT 714
FT /note="D -> N (in Ref. 3; BAB55092)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1001 AA; 113678 MW; 408A6E5A9CC25E41 CRC64;
MSGPGNKRAA GDGGSGPPEK KLSREEKTTT TLIEPIRLGG ISSTEEMDLK VLQFKNKKLA
ERLEQRQACE DELRERIEKL EKRQATDDAT LLIVNRYWAQ LDETVEALLR CHESQGELSS
APEAPGTQEG PTCDGTPLPE PGTSELRDPL LMQLRPPLSE PALAFVVALG ASSSEEVELE
LQGRMEFSKA AVSRVVEASD RLQRRVEELC QRVYSRGDSE PLSEAAQAHT RELGRENRRL
QDLATQLQEK HHRISLEYSE LQDKVTSAET KVLEMETTVE DLQWDIEKLR KREQKLNKHL
AEALEQLNSG YYVSGSSSGF QGGQITLSMQ KFEMLNAELE ENQELANSRM AELEKLQAEL
QGAVRTNERL KVALRSLPEE VVRETGEYRM LQAQFSLLYN ESLQVKTQLD EARGLLLATK
NSHLRHIEHM ESDELGLQKK LRTEVIQLED TLAQVRKEYE MLRIEFEQNL AANEQAGPIN
REMRHLISSL QNHNHQLKGD AQRYKRKLRE VQAEIGKLRA QASGSAHSTP NLGHPEDSGV
SAPAPGKEEG GPGPVSTPDN RKEMAPVPGT TTTTTSVKKE ELVPSEEDFQ GITPGAQGPS
SRGREPEARP KRELREREGP SLGPPPVASA LSRADREKAK VEETKRKESE LLKGLRAELK
KAQESQKEMK LLLDMYKSAP KEQRDKVQLM AAERKAKAEV DELRSRIREL EERDRRESKK
IADEDALRRI RQAEEQIEHL QRKLGATKQE EEALLSEMDV TGQAFEDMQE QNGRLLQQLR
EKDDANFKLM SERIKANQIH KLLREEKDEL GEQVLGLKSQ VDAQLLTVQK LEEKERALQG
SLGGVEKELT LRSQALELNK RKAVEAAQLA EDLKVQLEHV QTRLREIQPC LAESRAAREK
ESFNLKRAQE DISRLRRKLE KQRKVEVYAD ADEILQEEIK EYKARLTCPC CNTRKKDAVL
TKCFHVFCFE CVRGRYEARQ RKCPKCNAAF GAHDFHRIYI S
