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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: Persulfide dioxygenase ETHE1 homolog, mitochondrial

UniprotKB/SwissProt ID: Q9C8L4 (Q9C8L4)

Gene Name: GLY3

Organism: Arabidopsis thaliana (Mouse-ear cress)

Function: Sulfur dioxygenase that plays an essential role in hydrogen sulfide catabolism in the mitochondrial matrix. Hydrogen sulfide (H(2)S) gives rise to cysteine persulfide residues. ETHE1 consumes molecular oxygen to catalyze the oxidation of the persulfide, once it has been transferred to a thiophilic acceptor, such as glutathione (R-SSH). Plays an important role in metabolic homeostasis in mitochondria by metabolizing hydrogen sulfide and preventing the accumulation of supraphysiological H(2)S levels that have toxic effects, due to the inhibition of cytochrome c oxidase. Required for normal endosperm development in seed, and thereby also required for normal embryo development

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Mitochondrion

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR001279 Metallo-B-lactamas
IPR051682 Mito_Persulfide_Diox
IPR044528 POD-like_MBL-fold
IPR036866 RibonucZ/Hydroxyglut_hydro

The S-nitrosylation sites of Q9C8L4

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 170 VRATPGHTAG C VTYVTGEGAD