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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: Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial

UniprotKB/SwissProt ID: Q8R1S0 (Q8R1S0)

Gene Name: Coq6

Organism: Mus musculus (Mouse)

Function: FAD-dependent monooxygenase required for two non-consecutive steps during ubiquinone biosynthesis. Required for the C5-ring hydroxylation during ubiquinone biosynthesis by catalyzing the hydroxylation of 4-hydroxy-3-(all-trans-decaprenyl)benzoic acid to 3,4-dihydroxy-5-(all-trans-decaprenyl)benzoic acid. Also acts downstream of COQ4, for the C1-hydroxylation during ubiquinone biosynthesis by catalyzing the hydroxylation of 2-methoxy-6-(all-trans-decaprenyl)phenol to 2-methoxy-6-(all-trans-decaprenyl)benzene-1,4-diol. The electrons required for the hydroxylation reaction are funneled indirectly to COQ6 from NADPH via a ferredoxin/ferredoxin reductase system composed of FDX2 and FDXR

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Mitochondrion inner membrane. Golgi apparatus. Cell projection

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR002938 FAD-bd
IPR036188 FAD/NAD-bd_sf
IPR018168 Ubi_Hdrlase_CS
IPR010971 UbiH/COQ6
IPR051205 UbiH/COQ6_monooxygenase
IPR000689 UbQ_mOase_COQ6

The S-nitrosylation sites of Q8R1S0

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 116 LSSFGAWDHI C NMRCKAFRRM  CCHHHHHHHH H HHHHHHHHHH  2.88% 21278135