CPLM-000125

Genbank Nucleotide ID

Ubiquitin-conjugating enzyme E2 C

Protein Synonyms/Alias

UbcH10; Ubiquitin carrier protein C; Ubiquitin-protein ligase C

Homo sapiens (Human)

Position	Peptide	Type	References
80	VYEDLRYKLSLEFPS	ubiquitination	[1, 2, 3, 4]
97	PYNAPTVKFLTPCYH	ubiquitination	[5]
119	NICLDILKEKWSALY	ubiquitination	[2, 5, 6, 7, 8, 9]
121	CLDILKEKWSALYDV	ubiquitination	[1, 2, 3, 4, 5, 6, 8, 9, 10]
164	KNPTAFKKYLQETYS	ubiquitination	[5, 8]
172	YLQETYSKQVTSQEP	ubiquitination	[3, 5, 7, 8, 11]

[1] 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]
[2] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
[3] 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]
[4] 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]
[5] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[6] 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]
[7] 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]
[8] 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]
[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]
[10] 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]
[11] 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]

Functional Description

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 11'- and 'Lys-48'-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by initiating 'Lys-11'-linked polyubiquitin chains on APC/C substrates, leading to the degradation of APC/C substrates by the proteasome and promoting mitotic exit.

ACT_SITE 114 114 Glycyl thioester intermediate.
MOD_RES 2 2 N-acetylalanine.
MOD_RES 3 3 Phosphoserine.

3D-structure; Acetylation; Alternative splicing; ATP-binding; Cell cycle; Cell division; Complete proteome; Ligase; Mitosis; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation; Ubl conjugation pathway.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
GO:0005829; C:cytosol; TAS:Reactome.
GO:0005654; C:nucleoplasm; TAS:Reactome.
GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
GO:0051488; P:activation of anaphase-promoting complex activity; TAS:UniProtKB.
GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO:0008054; P:cyclin catabolic process; IDA:UniProtKB.
GO:0010458; P:exit from mitosis; IMP:UniProtKB.
GO:0010994; P:free ubiquitin chain polymerization; IDA:UniProtKB.
GO:0007094; P:mitotic spindle assembly checkpoint; TAS:Reactome.
GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO:0048015; P:phosphatidylinositol-mediated signaling; NAS:UniProtKB.
GO:0031536; P:positive regulation of exit from mitosis; IMP:UniProtKB.
GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
GO:0007051; P:spindle organization; NAS:UniProtKB.

IPR000608; UBQ-conjugat_E2.
IPR023313; UBQ-conjugating_AS.
IPR016135; UBQ-conjugating_enzyme/RWD.

PS00183; UBIQUITIN_CONJUGAT_1
PS50127; UBIQUITIN_CONJUGAT_2