UB2D3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UB2D3_MOUSE
• UniProt AC: P61079
• Protein Name: Ubiquitin-conjugating enzyme E2 D3
• Gene Name: Ube2d3
• Organism: Mus musculus (Mouse).
• Sequence Length: 147
• Subcellular Localization: Cell membrane ; Peripheral membrane protein . Endosome membrane ; Peripheral membrane protein .
• Protein 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..
• Protein Sequence: MALKRINKELSDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDRDKYNRISREWTQKYAM

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Ubiquitination	MALKRINKELSDLAR CCHHHHHHHHHHHHH	58.63	-
8	Acetylation	MALKRINKELSDLAR CCHHHHHHHHHHHHH	58.63	22826441
8	Malonylation	MALKRINKELSDLAR CCHHHHHHHHHHHHH	58.63	26320211
11	Phosphorylation	KRINKELSDLARDPP HHHHHHHHHHHHCCC	31.50	22817900
80	Phosphorylation	IYHPNINSNGSICLD EECCCCCCCCEEHHH	38.48	23984901
83	Phosphorylation	PNINSNGSICLDILR CCCCCCCEEHHHHHH	17.87	26745281
85	S-nitrosylation	INSNGSICLDILRSQ CCCCCEEHHHHHHHC	2.75	24895380
91	Phosphorylation	ICLDILRSQWSPALT EHHHHHHHCCCCCHH	32.34	22817900
128	Ubiquitination	PEIARIYKTDRDKYN HHHHHHHCCCHHHHH	41.39	-
133	Acetylation	IYKTDRDKYNRISRE HHCCCHHHHHHHCHH	45.37	23954790
133	Ubiquitination	IYKTDRDKYNRISRE HHCCCHHHHHHHCHH	45.37	22790023
144	Ubiquitination	ISREWTQKYAM---- HCHHHHHHHCC----	27.83	22790023

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of UB2D3_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of UB2D3_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of UB2D3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TNAP3_MOUSE	Tnfaip3	physical	20185725

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.