CPLM-009301

Genbank Nucleotide ID

Ubiquitin-conjugating enzyme E2 D3

Protein Synonyms/Alias

Ubiquitin carrier protein D3; Ubiquitin-conjugating enzyme E2(17)KB 3; Ubiquitin-conjugating enzyme E2-17 kDa 3; Ubiquitin-protein ligase D3

Mus musculus (Mouse)

Position	Peptide	Type	References
8	MALKRINKELSDLAR	acetylation	[1]
8	MALKRINKELSDLAR	ubiquitination	[2]
133	IYKTDRDKYNRISRE	ubiquitination	[2]
144	ISREWTQKYAM****	ubiquitination	[2]

[1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
[2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]

Functional Description

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 11'-, as well as 'Lys-48'-linked polyubiquitination. Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Ubiquitin chain elongation is then performed by CDC34, building ubiquitin chains from the UBE2D3-primed NFKBIA- linked ubiquitin. Acts also as an initiator E2, in conjunction with RNF8, for the priming of PCNA. Monoubiquitination of PCNA, and its subsequent polyubiquitination, are essential events in the operation of the DNA damage tolerance (DDT) pathway that is activated after DNA damage caused by UV or chemical agents during S-phase. Associates with the BRCA1/BARD1 E3 ligase complex to perform ubiquitination at DNA damage sites following ionizing radiation leading to DNA repair. Targets DAPK3 for ubiquitination which influences promyelocytic leukemia protein nuclear body (PML- NB) formation in the nucleus. In conjunction with the MDM2 and TOPORS E3 ligases, functions ubiquitination of p53/TP53. Supports NRDP1-mediated ubiquitination and degradation of ERBB3 and of BRUCE which triggers apoptosis. In conjunction with the CBL E3 ligase, targets EGFR for polyubiquitination at the plasma membrane as well as during its internalization and transport on endosomes. In conjunction with the STUB1 E3 quality control E3 ligase, ubiquitinates unfolded proteins to catalyze their immediate destruction (By similarity).

ACT_SITE 85 85 Glycyl thioester intermediate (By
DISULFID 21 107 By similarity.

Apoptosis; ATP-binding; Cell membrane; Complete proteome; Disulfide bond; DNA damage; DNA repair; Endosome; Ligase; Membrane; Nucleotide-binding; Reference proteome; Ubl conjugation pathway.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
GO:0006513; P:protein monoubiquitination; IEA:Compara.

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

PS00183; UBIQUITIN_CONJUGAT_1
PS50127; UBIQUITIN_CONJUGAT_2