UEV1C_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UEV1C_ARATH
• UniProt AC: Q9SJ44
• Protein Name: Ubiquitin-conjugating enzyme E2 variant 1C
• Gene Name: UEV1C
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 145
• Protein Description: Has no ubiquitin ligase activity on its own. The heterodimer with UBC catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. May play a role in the control of progress through the cell cycle and differentiation. May play a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage..
• Protein Sequence: MTLGSGSSVVVPRNFRLLEELERGEKGIGDGTVSYGMDDGDDIYMRSWTGTIIGPHNTVHEGRIYQLKLFCDKDYPEKPPTVRFHSRINMTCVNHDTGVVDSKKFGVLANWQRQYTMEDILTQLKKEMAASHNRKLVQPPEGTFF

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
2	Phosphorylation	------MTLGSGSSV ------CCCCCCCEE	39.56	30291188
5	Phosphorylation	---MTLGSGSSVVVP ---CCCCCCCEEEEC	38.32	30291188
7	Phosphorylation	-MTLGSGSSVVVPRN -CCCCCCCEEEECCC	22.96	19376835
8	Phosphorylation	MTLGSGSSVVVPRNF CCCCCCCEEEECCCH	23.58	19376835
128	Sulfoxidation	LTQLKKEMAASHNRK HHHHHHHHHHHCCCC	5.32	25693801

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

Oops, there are no upstream regulatory protein records of UEV1C_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of UEV1C_ARATH !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of UEV1C_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of UEV1C_ARATH !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2, AND MASSSPECTROMETRY.
PubMed: 19376835