UniProt Accession

 UBE2O_HUMAN; Q9C0C9; A6NDU5; Q69YP4; Q6PIZ2; Q86UA4; Q8N425; Q8TBN1; Q9BSW1; Q9H6E6; Q9H7E4; Q9H9B2 

Genbank Protein ID

 AB051521; AC090699; CH471099; BC004525; BC022237; BC025977; BC036820; BC051868; AL832432; AK022940; AK024657; AK025999 

Genbank Nucleotide ID

 BAB21825.1; EAW89396.1; AAH04525.2; AAH22237.1; AAH25977.1; AAH36820.1; AAH51868.2; CAH10644.1; BAB14320.1; BAB14948.1; BAB15313.1 

Protein Name

 Ubiquitin-conjugating enzyme E2 O 

Protein Synonyms/Alias

 Ubiquitin carrier protein O; Ubiquitin-conjugating enzyme E2 of 230 kDa; Ubiquitin-conjugating enzyme E2-230K; Ubiquitin-protein ligase O 

Gene Name

 UBE2O 

Gene Synonyms/Alias

 KIAA1734 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
132	QWYPEGVKQHVKETK	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8]
283	VQWLSGVKPVLSTKS	ubiquitination	[2, 5, 8]
360	CLYVFPAKVEPAKIA	ubiquitination	[6, 7, 9]
365	PAKVEPAKIAWECPE	ubiquitination	[6, 9]
373	IAWECPEKNCAQGEG	ubiquitination	[6]
521	KSIPLSIKNLKRKHK	ubiquitination	[2, 8]
593	PGDFVVDKRVQSCPD	ubiquitination	[6]
620	IGRTCMVKWFKLRPS	ubiquitination	[2, 4, 6, 8]
672	TEDGAPHKEDEPSVG	ubiquitination	[3, 6, 9]
809	AGKDGPPKSFRELKE	ubiquitination	[6]
815	PKSFRELKEAIKILE	ubiquitination	[2, 6, 8]
819	RELKEAIKILESLKN	ubiquitination	[2, 5, 6, 8]
825	IKILESLKNMTVEQL	ubiquitination	[1, 2, 3, 4, 6, 8]
846	SPTVEPEKPTREKKF	ubiquitination	[3]
852	EKPTREKKFLDDIKK	ubiquitination	[6]
859	KFLDDIKKLQENLKK	ubiquitination	[6]
865	KKLQENLKKTLDNVA	ubiquitination	[6]
866	KLQENLKKTLDNVAI	ubiquitination	[2, 3, 5, 8]
878	VAIVEEEKMEAVPDV	ubiquitination	[3]
990	DLFSALIKGPTRTPY	ubiquitination	[2, 3, 5, 6, 7, 8]
1154	ETHALLEKAQALPNG	ubiquitination	[6]
1233	ASVPPSVKPKKRRKS	ubiquitination	[3]
1235	VPPSVKPKKRRKSYR	ubiquitination	[3]
1248	YRSFLPEKSGYPDIG	ubiquitination	[3, 6, 7]
1263	FPLFPLSKGFIKSIR	ubiquitination	[6]
1267	PLSKGFIKSIRGVLT	ubiquitination	[6]

Reference

 [1] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [8] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [9] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 

Functional Description

 Catalyzes the covalent attachment of ubiquitin to other proteins (By similarity). 

Sequence Annotation

 ACT_SITE 1040 1040 Glycyl thioester intermediate (By
 MOD_RES 87 87 Phosphoserine.
 MOD_RES 89 89 Phosphoserine.
 MOD_RES 399 399 Phosphoserine.
 MOD_RES 401 401 Phosphoserine.
 MOD_RES 441 441 Phosphoserine.
 MOD_RES 836 836 Phosphoserine.
 MOD_RES 839 839 Phosphoserine (By similarity).
 MOD_RES 896 896 Phosphoserine.  

Keyword

 ATP-binding; Coiled coil; Complete proteome; Ligase; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation pathway. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 1292 AA 

Protein Sequence

Gene Ontology

 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004842; F:ubiquitin-protein ligase activity; IEA:EC. 

Interpro

 IPR000608; UBQ-conjugat_E2.
 IPR016135; UBQ-conjugating_enzyme/RWD. 

Pfam

 PF00179; UQ_con 

SMART

  

PROSITE

 PS00183; UBIQUITIN_CONJUGAT_1
 PS50127; UBIQUITIN_CONJUGAT_2 

PRINTS