UBE2O_HUMAN
ID UBE2O_HUMAN Reviewed; 1292 AA.
AC Q9C0C9; A6NDU5; Q69YP4; Q6PIZ2; Q86UA4; Q8N425; Q8TBN1; Q9BSW1; Q9H6E6;
AC Q9H7E4; Q9H9B2;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme;
DE EC=2.3.2.24 {ECO:0000269|PubMed:23455153, ECO:0000269|PubMed:24703950};
DE AltName: Full=E2/E3 hybrid ubiquitin-protein ligase UBE2O;
DE AltName: Full=Ubiquitin carrier protein O;
DE AltName: Full=Ubiquitin-conjugating enzyme E2 O;
DE AltName: Full=Ubiquitin-conjugating enzyme E2 of 230 kDa;
DE Short=Ubiquitin-conjugating enzyme E2-230K;
DE AltName: Full=Ubiquitin-protein ligase O;
GN Name=UBE2O; Synonyms=KIAA1734;
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 [LARGE SCALE MRNA], AND VARIANT SER-1207.
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 270-1292, AND VARIANT SER-1207.
RC TISSUE=Brain, and Skin;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 338-1292, AND VARIANT SER-1207.
RC TISSUE=Melanoma;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 448-1292, AND VARIANT SER-1207.
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 [7]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=11311559; DOI=10.1016/s0378-1119(01)00407-3;
RA Yokota T., Nagai H., Harada H., Mine N., Terada Y., Fujiwara H., Yabe A.,
RA Miyazaki K., Emi M.;
RT "Identification, tissue expression, and chromosomal position of a novel
RT gene encoding human ubiquitin-conjugating enzyme E2-230k.";
RL Gene 267:95-100(2001).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399; SER-401; SER-441 AND
RP SER-836, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87 AND SER-836, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87 AND SER-89, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-89 AND SER-896, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP FUNCTION.
RX PubMed=23452853; DOI=10.1016/j.cell.2013.01.051;
RA Hao Y.H., Doyle J.M., Ramanathan S., Gomez T.S., Jia D., Xu M., Chen Z.J.,
RA Billadeau D.D., Rosen M.K., Potts P.R.;
RT "Regulation of WASH-dependent actin polymerization and protein trafficking
RT by ubiquitination.";
RL Cell 152:1051-1064(2013).
RN [16]
RP FUNCTION.
RX PubMed=23381138; DOI=10.1038/cr.2013.21;
RA Zhang X., Zhang J., Zhang L., van Dam H., ten Dijke P.;
RT "UBE2O negatively regulates TRAF6-mediated NF-kappaB activation by
RT inhibiting TRAF6 polyubiquitination.";
RL Cell Res. 23:366-377(2013).
RN [17]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-1040.
RX PubMed=23455153; DOI=10.1038/emboj.2013.38;
RA Zhang X., Zhang J., Bauer A., Zhang L., Selinger D.W., Lu C.X.,
RA Ten Dijke P.;
RT "Fine-tuning BMP7 signalling in adipogenesis by UBE2O/E2-230K-mediated
RT monoubiquitination of SMAD6.";
RL EMBO J. 32:996-1007(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-89; SER-399; SER-401;
RP SER-515; SER-836 AND SER-896, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-87; SER-89; THR-488
RP AND THR-491, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [20]
RP FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP PHOSPHORYLATION, UBIQUITINATION, NUCLEAR LOCALIZATION SIGNAL, AND
RP MUTAGENESIS OF CYS-1040.
RX PubMed=24703950; DOI=10.1016/j.molcel.2014.03.002;
RA Mashtalir N., Daou S., Barbour H., Sen N.N., Gagnon J., Hammond-Martel I.,
RA Dar H.H., Therrien M., Affar E.B.;
RT "Autodeubiquitination protects the tumor suppressor BAP1 from cytoplasmic
RT sequestration mediated by the atypical ubiquitin ligase UBE2O.";
RL Mol. Cell 54:392-406(2014).
CC -!- FUNCTION: E2/E3 hybrid ubiquitin-protein ligase that displays both E2
CC and E3 ligase activities and mediates monoubiquitination of target
CC proteins (PubMed:23455153, PubMed:24703950). Negatively regulates
CC TRAF6-mediated NF-kappa-B activation independently of its E2 activity
CC (PubMed:23381138). Acts as a positive regulator of BMP7 signaling by
CC mediating monoubiquitination of SMAD6, thereby regulating adipogenesis
CC (PubMed:23455153). Mediates monoubiquitination at different sites of
CC the nuclear localization signal (NLS) of BAP1, leading to cytoplasmic
CC retention of BAP1. Also able to monoubiquitinate the NLS of other
CC chromatin-associated proteins, such as INO80 and CXXC1, affecting their
CC subcellular location (PubMed:24703950). Acts as a regulator of
CC retrograde transport by assisting the TRIM27:MAGEL2 E3 ubiquitin ligase
CC complex to mediate 'Lys-63'-linked ubiquitination of WASHC1, leading to
CC promote endosomal F-actin assembly (PubMed:23452853).
CC {ECO:0000269|PubMed:23381138, ECO:0000269|PubMed:23452853,
CC ECO:0000269|PubMed:23455153, ECO:0000269|PubMed:24703950}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-
CC cysteine + N(6)-monoubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.24; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388,
CC ECO:0000269|PubMed:23455153, ECO:0000269|PubMed:24703950};
CC -!- ACTIVITY REGULATION: inhibited by phenylarsine oxide (PAO).
CC {ECO:0000269|PubMed:24703950}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA
CC domain). Interacts with UBR2. {ECO:0000250|UniProtKB:Q6ZPJ3}.
CC -!- INTERACTION:
CC Q9C0C9; Q9UKG1: APPL1; NbExp=6; IntAct=EBI-2339946, EBI-741243;
CC Q9C0C9; P62879: GNB2; NbExp=6; IntAct=EBI-2339946, EBI-356942;
CC Q9C0C9; O60260-5: PRKN; NbExp=3; IntAct=EBI-2339946, EBI-21251460;
CC Q9C0C9; Q5VUG0: SFMBT2; NbExp=8; IntAct=EBI-2339946, EBI-12025260;
CC Q9C0C9; P40337-2: VHL; NbExp=3; IntAct=EBI-2339946, EBI-12157263;
CC Q9C0C9; O35182: Smad6; Xeno; NbExp=4; IntAct=EBI-2339946, EBI-4321242;
CC Q9C0C9; O35253: Smad7; Xeno; NbExp=2; IntAct=EBI-2339946, EBI-5274835;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24703950}. Nucleus
CC {ECO:0000269|PubMed:24703950}. Note=Mainly localizes to the cytoplasm.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle and
CC heart. {ECO:0000269|PubMed:11311559}.
CC -!- PTM: Phosphorylated. Phosphorylation affects subcellular location.
CC {ECO:0000269|PubMed:24703950}.
CC -!- PTM: Ubiquitinated: autoubiquitinates, possibly affecting its
CC subcellular location. {ECO:0000269|PubMed:24703950}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22237.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH25977.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH36820.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH51868.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14320.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14948.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15313.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB21825.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB051521; BAB21825.1; ALT_INIT; mRNA.
DR EMBL; AC090699; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471099; EAW89396.1; -; Genomic_DNA.
DR EMBL; BC004525; AAH04525.2; -; mRNA.
DR EMBL; BC022237; AAH22237.1; ALT_INIT; mRNA.
DR EMBL; BC025977; AAH25977.1; ALT_INIT; mRNA.
DR EMBL; BC036820; AAH36820.1; ALT_INIT; mRNA.
DR EMBL; BC051868; AAH51868.2; ALT_INIT; mRNA.
DR EMBL; AL832432; CAH10644.1; -; mRNA.
DR EMBL; AK022940; BAB14320.1; ALT_INIT; mRNA.
DR EMBL; AK024657; BAB14948.1; ALT_INIT; mRNA.
DR EMBL; AK025999; BAB15313.1; ALT_INIT; mRNA.
DR CCDS; CCDS32742.1; -.
DR RefSeq; NP_071349.3; NM_022066.3.
DR AlphaFoldDB; Q9C0C9; -.
DR SMR; Q9C0C9; -.
DR BioGRID; 121973; 230.
DR IntAct; Q9C0C9; 100.
DR MINT; Q9C0C9; -.
DR STRING; 9606.ENSP00000323687; -.
DR ChEMBL; CHEMBL4295940; -.
DR MoonDB; Q9C0C9; Predicted.
DR GlyGen; Q9C0C9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9C0C9; -.
DR MetOSite; Q9C0C9; -.
DR PhosphoSitePlus; Q9C0C9; -.
DR SwissPalm; Q9C0C9; -.
DR BioMuta; UBE2O; -.
DR DMDM; 209572710; -.
DR EPD; Q9C0C9; -.
DR jPOST; Q9C0C9; -.
DR MassIVE; Q9C0C9; -.
DR MaxQB; Q9C0C9; -.
DR PaxDb; Q9C0C9; -.
DR PeptideAtlas; Q9C0C9; -.
DR PRIDE; Q9C0C9; -.
DR ProteomicsDB; 80004; -.
DR Antibodypedia; 32408; 171 antibodies from 36 providers.
DR DNASU; 63893; -.
DR Ensembl; ENST00000319380.12; ENSP00000323687.6; ENSG00000175931.13.
DR GeneID; 63893; -.
DR KEGG; hsa:63893; -.
DR MANE-Select; ENST00000319380.12; ENSP00000323687.6; NM_022066.4; NP_071349.3.
DR UCSC; uc002jrm.5; human.
DR CTD; 63893; -.
DR DisGeNET; 63893; -.
DR GeneCards; UBE2O; -.
DR HGNC; HGNC:29554; UBE2O.
DR HPA; ENSG00000175931; Low tissue specificity.
DR MIM; 617649; gene.
DR neXtProt; NX_Q9C0C9; -.
DR OpenTargets; ENSG00000175931; -.
DR PharmGKB; PA142670651; -.
DR VEuPathDB; HostDB:ENSG00000175931; -.
DR eggNOG; KOG0895; Eukaryota.
DR GeneTree; ENSGT00940000160755; -.
DR HOGENOM; CLU_002088_1_0_1; -.
DR InParanoid; Q9C0C9; -.
DR OMA; KDHSDYQ; -.
DR OrthoDB; 808738at2759; -.
DR PhylomeDB; Q9C0C9; -.
DR TreeFam; TF325556; -.
DR BioCyc; MetaCyc:HS10987-MON; -.
DR BRENDA; 2.3.2.24; 2681.
DR PathwayCommons; Q9C0C9; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9C0C9; -.
DR SIGNOR; Q9C0C9; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 63893; 61 hits in 1084 CRISPR screens.
DR ChiTaRS; UBE2O; human.
DR GeneWiki; UBE2O; -.
DR GenomeRNAi; 63893; -.
DR Pharos; Q9C0C9; Tbio.
DR PRO; PR:Q9C0C9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9C0C9; protein.
DR Bgee; ENSG00000175931; Expressed in right hemisphere of cerebellum and 150 other tissues.
DR ExpressionAtlas; Q9C0C9; baseline and differential.
DR Genevisible; Q9C0C9; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IDA:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IMP:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase; Transport;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..1292
FT /note="(E3-independent) E2 ubiquitin-conjugating enzyme"
FT /id="PRO_0000280637"
FT DOMAIN 953..1113
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 812..882
FT /evidence="ECO:0000255"
FT MOTIF 512..536
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:24703950"
FT COMPBIAS 1..35
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..744
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..896
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1040
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 488
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 491
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 836
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 838
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPJ3"
FT MOD_RES 839
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPJ3"
FT MOD_RES 896
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 1207
FT /note="G -> S (in dbSNP:rs3803739)"
FT /evidence="ECO:0000269|PubMed:11214970,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_031184"
FT MUTAGEN 1040
FT /note="C->S: Loss of function."
FT /evidence="ECO:0000269|PubMed:23455153,
FT ECO:0000269|PubMed:24703950"
FT CONFLICT 50
FT /note="S -> F (in Ref. 1; BAB21825)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="E -> EQ (in Ref. 6; BAB15313)"
FT /evidence="ECO:0000305"
FT CONFLICT 1047
FT /note="W -> C (in Ref. 4; AAH22237)"
FT /evidence="ECO:0000305"
FT CONFLICT 1143
FT /note="E -> D (in Ref. 4; AAH25977)"
FT /evidence="ECO:0000305"
FT CONFLICT 1150
FT /note="A -> T (in Ref. 6; BAB14320)"
FT /evidence="ECO:0000305"
FT CONFLICT 1261
FT /note="L -> P (in Ref. 6; BAB14320)"
FT /evidence="ECO:0000305"
FT CONFLICT 1290
FT /note="E -> G (in Ref. 6; BAB14948)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1292 AA; 141293 MW; C9DF6395A32E9AB0 CRC64;
MADPAAPTPA APAPAQAPAP APEAVPAPAA APVPAPAPAS DSASGPSSDS GPEAGSQRLL
FSHDLVSGRY RGSVHFGLVR LIHGEDSDSE GEEEGRGSSG CSEAGGAGHE EGRASPLRRG
YVRVQWYPEG VKQHVKETKL KLEDRSVVPR DVVRHMRSTD SQCGTVIDVN IDCAVKLIGT
NCIIYPVNSK DLQHIWPFMY GDYIAYDCWL GKVYDLKNQI ILKLSNGARC SMNTEDGAKL
YDVCPHVSDS GLFFDDSYGF YPGQVLIGPA KIFSSVQWLS GVKPVLSTKS KFRVVVEEVQ
VVELKVTWIT KSFCPGGTDS VSPPPSVITQ ENLGRVKRLG CFDHAQRQLG ERCLYVFPAK
VEPAKIAWEC PEKNCAQGEG SMAKKVKRLL KKQVVRIMSC SPDTQCSRDH SMEDPDKKGE
SKTKSEAESA SPEETPDGSA SPVEMQDEGA EEPHEAGEQL PPFLLKEGRD DRLHSAEQDA
DDEAADDTDD TSSVTSSASS TTSSQSGSGT SRKKSIPLSI KNLKRKHKRK KNKITRDFKP
GDRVAVEVVT TMTSADVMWQ DGSVECNIRS NDLFPVHHLD NNEFCPGDFV VDKRVQSCPD
PAVYGVVQSG DHIGRTCMVK WFKLRPSGDD VELIGEEEDV SVYDIADHPD FRFRTTDIVI
RIGNTEDGAP HKEDEPSVGQ VARVDVSSKV EVVWADNSKT IILPQHLYNI ESEIEESDYD
SVEGSTSGAS SDEWEDDSDS WETDNGLVED EHPKIEEPPI PPLEQPVAPE DKGVVISEEA
ATAAVQGAVA MAAPMAGLME KAGKDGPPKS FRELKEAIKI LESLKNMTVE QLLTGSPTSP
TVEPEKPTRE KKFLDDIKKL QENLKKTLDN VAIVEEEKME AVPDVERKED KPEGQSPVKA
EWPSETPVLC QQCGGKPGVT FTSAKGEVFS VLEFAPSNHS FKKIEFQPPE AKKFFSTVRK
EMALLATSLP EGIMVKTFED RMDLFSALIK GPTRTPYEDG LYLFDIQLPN IYPAVPPHFC
YLSQCSGRLN PNLYDNGKVC VSLLGTWIGK GTERWTSKSS LLQVLISIQG LILVNEPYYN
EAGFDSDRGL QEGYENSRCY NEMALIRVVQ SMTQLVRRPP EVFEQEIRQH FSTGGWRLVN
RIESWLETHA LLEKAQALPN GVPKASSSPE PPAVAELSDS GQQEPEDGGP APGEASQGSD
SEGGAQGLAS ASRDHTDQTS ETAPDASVPP SVKPKKRRKS YRSFLPEKSG YPDIGFPLFP
LSKGFIKSIR GVLTQFRAAL LEAGMPECTE DK
