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Q9C0C9 (UBE2O_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E2/E3 hybrid ubiquitin-protein ligase UBE2O

EC=6.3.2.-
EC=6.3.2.19
Alternative name(s):
Ubiquitin carrier protein O
Ubiquitin-conjugating enzyme E2 O
Ubiquitin-conjugating enzyme E2 of 230 kDa
Short name=Ubiquitin-conjugating enzyme E2-230K
Ubiquitin-protein ligase O
Gene names
Name:UBE2O
Synonyms:KIAA1734
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1292 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E2/E3 hybrid ubiquitin-protein ligase that displays both E2 and E3 ligase activities and mediates monoubiquitination of target proteins (Ref.17, Ref.18). Negatively regulates TRAF6-mediated NF-kappa-B activation independently of its E2 activity (Ref.16). Acts as a positive regulator of BMP7 signaling by mediating monoubiquitination of SMAD6, thereby regulating adipogenesis (Ref.17). Mediates monoubiquitination at different sites of the nuclear localization signal (NLS) of BAP1, leading to cytoplasmic retention of BAP1. Also able to monoubiquitinate the NLS of other chromatin-associated proteins, such as INO80 and CXXC1, affecting their subcellular location (Ref.18). Acts as a regulator of retrograde transport by assisting the TRIM27:MAGEL2 E3 ubiquitin ligase complex to mediate 'Lys-63'-linked ubiquitination of WASH1, leading to promote endosomal F-actin assembly (Ref.15). Ref.15 Ref.16 Ref.17 Ref.18

Catalytic activity

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.

Enzyme regulation

inhibited by phenylarsine oxide (PAO). Ref.18

Pathway

Protein modification; protein ubiquitination.

Subcellular location

Cytoplasm. Nucleus. Note: Mainly localizes to the cytoplasm. Ref.18

Tissue specificity

Predominantly expressed in skeletal muscle and heart. Ref.7

Post-translational modification

Phosphorylated. Phosphorylation affects subcellular location. Ref.18

Ubiquitinated: autoubiquitinates, possibly affecting its subcellulat location. Ref.18

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Sequence caution

The sequence AAH22237.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH25977.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH36820.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH51868.2 differs from that shown. Reason: Erroneous initiation.

The sequence BAB14320.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB14948.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB15313.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB21825.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTransport
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.17. Source: IntAct

ubiquitin-protein transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Smad6O351824EBI-2339946,EBI-4321242From a different organism.
Smad7O352532EBI-2339946,EBI-5274835From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12921292E2/E3 hybrid ubiquitin-protein ligase UBE2O
PRO_0000280637

Regions

Coiled coil812 – 88271 Potential
Motif512 – 53625Nuclear localization signal Ref.18
Compositional bias2 – 4342Ala-rich

Sites

Active site10401Glycyl thioester intermediate

Amino acid modifications

Modified residue871Phosphoserine Ref.11 Ref.12 Ref.14
Modified residue891Phosphoserine Ref.11 Ref.12 Ref.14
Modified residue3991Phosphoserine Ref.9
Modified residue4011Phosphoserine Ref.9
Modified residue4411Phosphoserine Ref.9
Modified residue8361Phosphoserine Ref.9 Ref.11
Modified residue8391Phosphoserine By similarity
Modified residue8961Phosphoserine Ref.14

Natural variations

Natural variant12071G → S. Ref.1 Ref.4 Ref.5 Ref.6
Corresponds to variant rs3803739 [ dbSNP | Ensembl ].
VAR_031184

Experimental info

Mutagenesis10401C → S: Loss of function. Ref.17 Ref.18
Sequence conflict501S → F in BAB21825. Ref.1
Sequence conflict6751E → EQ in BAB15313. Ref.6
Sequence conflict10471W → C in AAH22237. Ref.4
Sequence conflict11431E → D in AAH25977. Ref.4
Sequence conflict11501A → T in BAB14320. Ref.6
Sequence conflict12611L → P in BAB14320. Ref.6
Sequence conflict12901E → G in BAB14948. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q9C0C9 [UniParc].

Last modified October 14, 2008. Version 3.
Checksum: C9DF6395A32E9AB0

FASTA1,292141,293
        10         20         30         40         50         60 
MADPAAPTPA APAPAQAPAP APEAVPAPAA APVPAPAPAS DSASGPSSDS GPEAGSQRLL 

        70         80         90        100        110        120 
FSHDLVSGRY RGSVHFGLVR LIHGEDSDSE GEEEGRGSSG CSEAGGAGHE EGRASPLRRG 

       130        140        150        160        170        180 
YVRVQWYPEG VKQHVKETKL KLEDRSVVPR DVVRHMRSTD SQCGTVIDVN IDCAVKLIGT 

       190        200        210        220        230        240 
NCIIYPVNSK DLQHIWPFMY GDYIAYDCWL GKVYDLKNQI ILKLSNGARC SMNTEDGAKL 

       250        260        270        280        290        300 
YDVCPHVSDS GLFFDDSYGF YPGQVLIGPA KIFSSVQWLS GVKPVLSTKS KFRVVVEEVQ 

       310        320        330        340        350        360 
VVELKVTWIT KSFCPGGTDS VSPPPSVITQ ENLGRVKRLG CFDHAQRQLG ERCLYVFPAK 

       370        380        390        400        410        420 
VEPAKIAWEC PEKNCAQGEG SMAKKVKRLL KKQVVRIMSC SPDTQCSRDH SMEDPDKKGE 

       430        440        450        460        470        480 
SKTKSEAESA SPEETPDGSA SPVEMQDEGA EEPHEAGEQL PPFLLKEGRD DRLHSAEQDA 

       490        500        510        520        530        540 
DDEAADDTDD TSSVTSSASS TTSSQSGSGT SRKKSIPLSI KNLKRKHKRK KNKITRDFKP 

       550        560        570        580        590        600 
GDRVAVEVVT TMTSADVMWQ DGSVECNIRS NDLFPVHHLD NNEFCPGDFV VDKRVQSCPD 

       610        620        630        640        650        660 
PAVYGVVQSG DHIGRTCMVK WFKLRPSGDD VELIGEEEDV SVYDIADHPD FRFRTTDIVI 

       670        680        690        700        710        720 
RIGNTEDGAP HKEDEPSVGQ VARVDVSSKV EVVWADNSKT IILPQHLYNI ESEIEESDYD 

       730        740        750        760        770        780 
SVEGSTSGAS SDEWEDDSDS WETDNGLVED EHPKIEEPPI PPLEQPVAPE DKGVVISEEA 

       790        800        810        820        830        840 
ATAAVQGAVA MAAPMAGLME KAGKDGPPKS FRELKEAIKI LESLKNMTVE QLLTGSPTSP 

       850        860        870        880        890        900 
TVEPEKPTRE KKFLDDIKKL QENLKKTLDN VAIVEEEKME AVPDVERKED KPEGQSPVKA 

       910        920        930        940        950        960 
EWPSETPVLC QQCGGKPGVT FTSAKGEVFS VLEFAPSNHS FKKIEFQPPE AKKFFSTVRK 

       970        980        990       1000       1010       1020 
EMALLATSLP EGIMVKTFED RMDLFSALIK GPTRTPYEDG LYLFDIQLPN IYPAVPPHFC 

      1030       1040       1050       1060       1070       1080 
YLSQCSGRLN PNLYDNGKVC VSLLGTWIGK GTERWTSKSS LLQVLISIQG LILVNEPYYN 

      1090       1100       1110       1120       1130       1140 
EAGFDSDRGL QEGYENSRCY NEMALIRVVQ SMTQLVRRPP EVFEQEIRQH FSTGGWRLVN 

      1150       1160       1170       1180       1190       1200 
RIESWLETHA LLEKAQALPN GVPKASSSPE PPAVAELSDS GQQEPEDGGP APGEASQGSD 

      1210       1220       1230       1240       1250       1260 
SEGGAQGLAS ASRDHTDQTS ETAPDASVPP SVKPKKRRKS YRSFLPEKSG YPDIGFPLFP 

      1270       1280       1290 
LSKGFIKSIR GVLTQFRAAL LEAGMPECTE DK 

« Hide

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-1207.
Tissue: Brain.
[2]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 270-1292, VARIANT SER-1207.
Tissue: Brain and Skin.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 338-1292, VARIANT SER-1207.
Tissue: Melanoma.
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 448-1292, VARIANT SER-1207.
[7]"Identification, tissue expression, and chromosomal position of a novel gene encoding human ubiquitin-conjugating enzyme E2-230k."
Yokota T., Nagai H., Harada H., Mine N., Terada Y., Fujiwara H., Yabe A., Miyazaki K., Emi M.
Gene 267:95-100(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION, TISSUE SPECIFICITY.
[8]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399; SER-401; SER-441 AND SER-836, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-89 AND SER-836, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87 AND SER-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-89 AND SER-896, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Regulation of WASH-dependent actin polymerization and protein trafficking by ubiquitination."
Hao Y.H., Doyle J.M., Ramanathan S., Gomez T.S., Jia D., Xu M., Chen Z.J., Billadeau D.D., Rosen M.K., Potts P.R.
Cell 152:1051-1064(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"UBE2O negatively regulates TRAF6-mediated NF-kappaB activation by inhibiting TRAF6 polyubiquitination."
Zhang X., Zhang J., Zhang L., van Dam H., ten Dijke P.
Cell Res. 23:366-377(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Fine-tuning BMP7 signalling in adipogenesis by UBE2O/E2-230K-mediated monoubiquitination of SMAD6."
Zhang X., Zhang J., Bauer A., Zhang L., Selinger D.W., Lu C.X., Ten Dijke P.
EMBO J. 32:996-1007(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-1040.
[18]"Autodeubiquitination protects the tumor suppressor BAP1 from cytoplasmic sequestration mediated by the atypical ubiquitin ligase UBE2O."
Mashtalir N., Daou S., Barbour H., Sen N.N., Gagnon J., Hammond-Martel I., Dar H.H., Therrien M., Affar E.B.
Mol. Cell 54:392-406(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, PHOSPHORYLATION, UBIQUITINATION, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF CYS-1040.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB051521 mRNA. Translation: BAB21825.1. Different initiation.
AC090699 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89396.1.
BC004525 mRNA. Translation: AAH04525.2.
BC022237 mRNA. Translation: AAH22237.1. Different initiation.
BC025977 mRNA. Translation: AAH25977.1. Different initiation.
BC036820 mRNA. Translation: AAH36820.1. Different initiation.
BC051868 mRNA. Translation: AAH51868.2. Different initiation.
AL832432 mRNA. Translation: CAH10644.1.
AK022940 mRNA. Translation: BAB14320.1. Different initiation.
AK024657 mRNA. Translation: BAB14948.1. Different initiation.
AK025999 mRNA. Translation: BAB15313.1. Different initiation.
CCDSCCDS32742.1.
RefSeqNP_071349.3. NM_022066.3.
UniGeneHs.16130.

3D structure databases

ProteinModelPortalQ9C0C9.
SMRQ9C0C9. Positions 936-1150.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121973. 25 interactions.
IntActQ9C0C9. 25 interactions.

PTM databases

PhosphoSiteQ9C0C9.

Polymorphism databases

DMDM209572710.

Proteomic databases

MaxQBQ9C0C9.
PaxDbQ9C0C9.
PRIDEQ9C0C9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000319380; ENSP00000323687; ENSG00000175931.
GeneID63893.
KEGGhsa:63893.
UCSCuc002jrl.4. human.

Organism-specific databases

CTD63893.
GeneCardsGC17M074385.
H-InvDBHIX0020035.
HGNCHGNC:29554. UBE2O.
HPAHPA023605.
neXtProtNX_Q9C0C9.
PharmGKBPA142670651.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5078.
HOVERGENHBG080116.
InParanoidQ9C0C9.
KOK10581.
OMACAQGEGS.
OrthoDBEOG7GN2KX.
PhylomeDBQ9C0C9.
TreeFamTF325556.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkQ9C0C9.
UniPathwayUPA00143.

Gene expression databases

BgeeQ9C0C9.
CleanExHS_UBE2O.
GenevestigatorQ9C0C9.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBE2O. human.
GeneWikiUBE2O.
GenomeRNAi63893.
NextBio65578.
PROQ9C0C9.

Entry information

Entry nameUBE2O_HUMAN
AccessionPrimary (citable) accession number: Q9C0C9
Secondary accession number(s): A6NDU5 expand/collapse secondary AC list , Q69YP4, Q6PIZ2, Q86UA4, Q8N425, Q8TBN1, Q9BSW1, Q9H6E6, Q9H7E4, Q9H9B2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: October 14, 2008
Last modified: July 9, 2014
This is version 106 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM