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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: E3 ubiquitin-protein ligase RGLG4

UniprotKB/SwissProt ID: Q9SAL0 (Q9SAL0)

Gene Name: RGLG4

Organism: Arabidopsis thaliana (Mouse-ear cress)

Function: Possesses E3 ubiquitin-protein ligase in vitro. Acts as upstream modulator of jasmonate (JA) signaling in response to various stimuli, such as JA-inhibited root growth, JA-inductive gene expression, coronatine-mediated pathogen susceptibility, wound-stimulated expression of JA-responsive genes and wound-induced JA biosynthesis (PubMed:22898498). Controls fumonisin B1 (FB1)-triggered programmed cell death (PCD) by modulating the JA signaling pathway. May mediate salicylic acid (SA) suppression of JA signaling in FB1-induced responses (PubMed:25788731). May mediate the formation of 'Lys-48'-linked multiubiquitin chains. Mediates the polyubiquitination and subsequent proteasomal degradation of the target protein GRXS17 (PubMed:27497447)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Nucleus

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR010734 Copine_C
IPR052079 E3_ligase/Copine_domain
IPR002035 VWF_A
IPR036465 vWFA_dom_sf
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD

The S-nitrosylation sites of Q9SAL0

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 102 WTGKTSFDGK C LHALGETSNP