CPLM-021960

Genbank Nucleotide ID

Ubiquitin-conjugating enzyme E2 T

Protein Synonyms/Alias

Cell proliferation-inducing gene 50 protein; Ubiquitin carrier protein T; Ubiquitin-protein ligase T

Homo sapiens (Human)

Position	Peptide	Type	References
28	GITCWQDKDQMDDLR	ubiquitination	[1]
48	GANTPYEKGVFKLEV	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8]
91	RICLDVLKLPPKGAW	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13]
136	SSEFKYNKPAFLKNA	ubiquitination	[5]
141	YNKPAFLKNARQWTE	ubiquitination	[5]
156	KHARQKQKADEEEML	ubiquitination	[3]
180	RVHNSTQKRKASQLV	ubiquitination	[12]
182	HNSTQKRKASQLVGI	ubiquitination	[4, 5, 7, 12]
191	SQLVGIEKKFHPDV*	acetylation	[8, 14]
191	SQLVGIEKKFHPDV*	ubiquitination	[2, 3, 7, 12]

[1] 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]
[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] 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]
[5] 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]
[6] 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]
[7] 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]
[8] 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]
[9] 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]
[10] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
[11] Proteomic snapshot of the EGF-induced ubiquitin network.
Argenzio E, Bange T, Oldrini B, Bianchi F, Peesari R, Mari S, Di Fiore PP, Mann M, Polo S.
Mol Syst Biol. 2011 Jan 18;7:462. [PMID: 21245847]
[12] 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]
[13] 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]
[14] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]

Functional Description

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. Involved in mitomycin-C (MMC)-induced DNA repair: acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. Also mediates monoubiquitination of FANCL and FANCI. May contribute to ubiquitination and degradation of BRCA1. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, but may prefer 'Lys-11'-, 'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination.

ACT_SITE 86 86 Glycyl thioester intermediate.
CROSSLNK 91 91 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 182 182 Glycyl lysine isopeptide (Lys-Gly)

3D-structure; ATP-binding; Complete proteome; DNA damage; DNA repair; Isopeptide bond; Ligase; Nucleotide-binding; Nucleus; Reference proteome; Ubl conjugation; Ubl conjugation pathway.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005654; C:nucleoplasm; TAS:Reactome.
GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
GO:0006281; P:DNA repair; IMP:UniProtKB.
GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
GO:0044314; P:protein K27-linked ubiquitination; IDA:UniProtKB.
GO:0035519; P:protein K29-linked ubiquitination; IDA:UniProtKB.
GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
GO:0085020; P:protein K6-linked ubiquitination; IDA:UniProtKB.
GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
GO:0006513; P:protein monoubiquitination; IDA:UniProtKB.

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

PS00183; UBIQUITIN_CONJUGAT_1
PS50127; UBIQUITIN_CONJUGAT_2