Full text data of UBE2O
UBE2O
(KIAA1734)
[Confidence: high (present in two of the MS resources)]
Ubiquitin-conjugating enzyme E2 O; 6.3.2.19 (Ubiquitin carrier protein O; Ubiquitin-conjugating enzyme E2 of 230 kDa; Ubiquitin-conjugating enzyme E2-230K; Ubiquitin-protein ligase O)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ubiquitin-conjugating enzyme E2 O; 6.3.2.19 (Ubiquitin carrier protein O; Ubiquitin-conjugating enzyme E2 of 230 kDa; Ubiquitin-conjugating enzyme E2-230K; Ubiquitin-protein ligase O)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00028307
IPI00028307 Hypothetical protein FLJ12878 ubiquitin conjugating enzyme activity, ubiquitin cycle soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00028307 Hypothetical protein FLJ12878 ubiquitin conjugating enzyme activity, ubiquitin cycle soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
Q9C0C9
ID UBE2O_HUMAN Reviewed; 1292 AA.
AC Q9C0C9; A6NDU5; Q69YP4; Q6PIZ2; Q86UA4; Q8N425; Q8TBN1; Q9BSW1;
read moreAC Q9H6E6; Q9H7E4; Q9H9B2;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 22-JAN-2014, entry version 100.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 O;
DE EC=6.3.2.19;
DE AltName: Full=Ubiquitin carrier protein 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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large 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.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA 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
RT the 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RP 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
RT project: 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
RP 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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
RP 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Yabe A., Miyazaki K., Emi M.;
RT "Identification, tissue expression, and chromosomal position of a
RT novel 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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399; SER-401; SER-441
RP AND SER-836, AND MASS SPECTROMETRY.
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-89 AND SER-836,
RP AND MASS SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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,
RP AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC diphosphate + protein N-ubiquityllysine.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- INTERACTION:
CC O35182:Smad6 (xeno); NbExp=4; IntAct=EBI-2339946, EBI-4321242;
CC O35253:Smad7 (xeno); NbExp=2; IntAct=EBI-2339946, EBI-5274835;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle and
CC heart.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22237.1; Type=Erroneous initiation;
CC Sequence=AAH25977.1; Type=Erroneous initiation;
CC Sequence=AAH36820.1; Type=Erroneous initiation;
CC Sequence=AAH51868.2; Type=Erroneous initiation;
CC Sequence=BAB14320.1; Type=Erroneous initiation;
CC Sequence=BAB14948.1; Type=Erroneous initiation;
CC Sequence=BAB15313.1; Type=Erroneous initiation;
CC Sequence=BAB21825.1; Type=Erroneous initiation;
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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 RefSeq; NP_071349.3; NM_022066.3.
DR UniGene; Hs.16130; -.
DR ProteinModelPortal; Q9C0C9; -.
DR SMR; Q9C0C9; 936-1150.
DR IntAct; Q9C0C9; 25.
DR PhosphoSite; Q9C0C9; -.
DR DMDM; 209572710; -.
DR PaxDb; Q9C0C9; -.
DR PRIDE; Q9C0C9; -.
DR Ensembl; ENST00000319380; ENSP00000323687; ENSG00000175931.
DR GeneID; 63893; -.
DR KEGG; hsa:63893; -.
DR UCSC; uc002jrl.4; human.
DR CTD; 63893; -.
DR GeneCards; GC17M074385; -.
DR H-InvDB; HIX0020035; -.
DR HGNC; HGNC:29554; UBE2O.
DR HPA; HPA023605; -.
DR neXtProt; NX_Q9C0C9; -.
DR PharmGKB; PA142670651; -.
DR eggNOG; COG5078; -.
DR HOVERGEN; HBG080116; -.
DR InParanoid; Q9C0C9; -.
DR KO; K10581; -.
DR OMA; DLQHIWP; -.
DR OrthoDB; EOG7GN2KX; -.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; Q9C0C9; -.
DR UniPathway; UPA00143; -.
DR ChiTaRS; UBE2O; human.
DR GeneWiki; UBE2O; -.
DR GenomeRNAi; 63893; -.
DR NextBio; 65578; -.
DR PRO; PR:Q9C0C9; -.
DR Bgee; Q9C0C9; -.
DR CleanEx; HS_UBE2O; -.
DR Genevestigator; Q9C0C9; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:UniProtKB-EC.
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; PS00183; UBIQUITIN_CONJUGAT_1; FALSE_NEG.
DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Complete proteome; Ligase;
KW Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1 1292 Ubiquitin-conjugating enzyme E2 O.
FT /FTId=PRO_0000280637.
FT COILED 812 882 Potential.
FT COMPBIAS 2 43 Ala-rich.
FT ACT_SITE 1040 1040 Glycyl thioester intermediate (By
FT similarity).
FT MOD_RES 87 87 Phosphoserine.
FT MOD_RES 89 89 Phosphoserine.
FT MOD_RES 399 399 Phosphoserine.
FT MOD_RES 401 401 Phosphoserine.
FT MOD_RES 441 441 Phosphoserine.
FT MOD_RES 836 836 Phosphoserine.
FT MOD_RES 839 839 Phosphoserine (By similarity).
FT MOD_RES 896 896 Phosphoserine.
FT VARIANT 1207 1207 G -> S (in dbSNP:rs3803739).
FT /FTId=VAR_031184.
FT CONFLICT 50 50 S -> F (in Ref. 1; BAB21825).
FT CONFLICT 675 675 E -> EQ (in Ref. 6; BAB15313).
FT CONFLICT 1047 1047 W -> C (in Ref. 4; AAH22237).
FT CONFLICT 1143 1143 E -> D (in Ref. 4; AAH25977).
FT CONFLICT 1150 1150 A -> T (in Ref. 6; BAB14320).
FT CONFLICT 1261 1261 L -> P (in Ref. 6; BAB14320).
FT CONFLICT 1290 1290 E -> G (in Ref. 6; BAB14948).
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
//
ID UBE2O_HUMAN Reviewed; 1292 AA.
AC Q9C0C9; A6NDU5; Q69YP4; Q6PIZ2; Q86UA4; Q8N425; Q8TBN1; Q9BSW1;
read moreAC Q9H6E6; Q9H7E4; Q9H9B2;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 22-JAN-2014, entry version 100.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 O;
DE EC=6.3.2.19;
DE AltName: Full=Ubiquitin carrier protein 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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large 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.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA 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
RT the 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RP 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
RT project: 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
RP 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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
RP 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Yabe A., Miyazaki K., Emi M.;
RT "Identification, tissue expression, and chromosomal position of a
RT novel 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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399; SER-401; SER-441
RP AND SER-836, AND MASS SPECTROMETRY.
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-89 AND SER-836,
RP AND MASS SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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,
RP AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC diphosphate + protein N-ubiquityllysine.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- INTERACTION:
CC O35182:Smad6 (xeno); NbExp=4; IntAct=EBI-2339946, EBI-4321242;
CC O35253:Smad7 (xeno); NbExp=2; IntAct=EBI-2339946, EBI-5274835;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle and
CC heart.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22237.1; Type=Erroneous initiation;
CC Sequence=AAH25977.1; Type=Erroneous initiation;
CC Sequence=AAH36820.1; Type=Erroneous initiation;
CC Sequence=AAH51868.2; Type=Erroneous initiation;
CC Sequence=BAB14320.1; Type=Erroneous initiation;
CC Sequence=BAB14948.1; Type=Erroneous initiation;
CC Sequence=BAB15313.1; Type=Erroneous initiation;
CC Sequence=BAB21825.1; Type=Erroneous initiation;
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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 RefSeq; NP_071349.3; NM_022066.3.
DR UniGene; Hs.16130; -.
DR ProteinModelPortal; Q9C0C9; -.
DR SMR; Q9C0C9; 936-1150.
DR IntAct; Q9C0C9; 25.
DR PhosphoSite; Q9C0C9; -.
DR DMDM; 209572710; -.
DR PaxDb; Q9C0C9; -.
DR PRIDE; Q9C0C9; -.
DR Ensembl; ENST00000319380; ENSP00000323687; ENSG00000175931.
DR GeneID; 63893; -.
DR KEGG; hsa:63893; -.
DR UCSC; uc002jrl.4; human.
DR CTD; 63893; -.
DR GeneCards; GC17M074385; -.
DR H-InvDB; HIX0020035; -.
DR HGNC; HGNC:29554; UBE2O.
DR HPA; HPA023605; -.
DR neXtProt; NX_Q9C0C9; -.
DR PharmGKB; PA142670651; -.
DR eggNOG; COG5078; -.
DR HOVERGEN; HBG080116; -.
DR InParanoid; Q9C0C9; -.
DR KO; K10581; -.
DR OMA; DLQHIWP; -.
DR OrthoDB; EOG7GN2KX; -.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; Q9C0C9; -.
DR UniPathway; UPA00143; -.
DR ChiTaRS; UBE2O; human.
DR GeneWiki; UBE2O; -.
DR GenomeRNAi; 63893; -.
DR NextBio; 65578; -.
DR PRO; PR:Q9C0C9; -.
DR Bgee; Q9C0C9; -.
DR CleanEx; HS_UBE2O; -.
DR Genevestigator; Q9C0C9; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:UniProtKB-EC.
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; PS00183; UBIQUITIN_CONJUGAT_1; FALSE_NEG.
DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Complete proteome; Ligase;
KW Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1 1292 Ubiquitin-conjugating enzyme E2 O.
FT /FTId=PRO_0000280637.
FT COILED 812 882 Potential.
FT COMPBIAS 2 43 Ala-rich.
FT ACT_SITE 1040 1040 Glycyl thioester intermediate (By
FT similarity).
FT MOD_RES 87 87 Phosphoserine.
FT MOD_RES 89 89 Phosphoserine.
FT MOD_RES 399 399 Phosphoserine.
FT MOD_RES 401 401 Phosphoserine.
FT MOD_RES 441 441 Phosphoserine.
FT MOD_RES 836 836 Phosphoserine.
FT MOD_RES 839 839 Phosphoserine (By similarity).
FT MOD_RES 896 896 Phosphoserine.
FT VARIANT 1207 1207 G -> S (in dbSNP:rs3803739).
FT /FTId=VAR_031184.
FT CONFLICT 50 50 S -> F (in Ref. 1; BAB21825).
FT CONFLICT 675 675 E -> EQ (in Ref. 6; BAB15313).
FT CONFLICT 1047 1047 W -> C (in Ref. 4; AAH22237).
FT CONFLICT 1143 1143 E -> D (in Ref. 4; AAH25977).
FT CONFLICT 1150 1150 A -> T (in Ref. 6; BAB14320).
FT CONFLICT 1261 1261 L -> P (in Ref. 6; BAB14320).
FT CONFLICT 1290 1290 E -> G (in Ref. 6; BAB14948).
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
//