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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: CDGSH iron-sulfur domain-containing protein 1

UniprotKB/SwissProt ID: Q91WS0 (Q91WS0)

Gene Name: Cisd1

Organism: Mus musculus (Mouse)

Function: L-cysteine transaminase that catalyzes the reversible transfer of the amino group from L-cysteine to the alpha-keto acid 2-oxoglutarate to respectively form 2-oxo-3-sulfanylpropanoate and L-glutamate (By similarity). The catalytic cycle occurs in the presence of pyridoxal 5'-phosphate (PLP) cofactor that facilitates transamination by initially forming an internal aldimine with the epsilon-amino group of active site Lys-55 residue on the enzyme (PLP-enzyme aldimine), subsequently displaced by formation of an external aldimine with the substrate amino group (PLP-L-cysteine aldimine). The external aldimine is further deprotonated to form a carbanion intermediate, which in the presence of 2-oxoglutarate regenerates PLP yielding final products 2-oxo-3-sulfanylpropanoate and L-glutamate. The proton transfer in carbanion intermediate is suggested to be controlled by the active site lysine residue, whereas PLP stabilizes carbanion structure through electron delocalization, also known as the electron sink effect (By similarity). Plays a key role in regulating maximal capacity for electron transport and oxidative phosphorylation (PubMed:17376863). May be involved in iron-sulfur cluster shuttling and/or in redox reactions. Can transfer the [2Fe-2S] cluster to an apo-acceptor protein only when in the oxidation state, likely serving as a redox sensor that regulates mitochondrial iron-sulfur cluster assembly and iron trafficking upon oxidative stress (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Mitochondrion outer membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR045131 CISD1/2
IPR018967 FeS-contain_CDGSH-typ
IPR019610 FeS-contain_mitoNEET_N
IPR042216 MitoNEET_CISD

The S-nitrosylation sites of Q91WS0

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 72 MEDLGDKAVY C RCWRSKKFPF  CCCCCCCCCC H HHHHHHHHHH  2.02% 21278135
2 83 RCWRSKKFPF C DGAHIKHNEE  CCCCCCCCCC H HHHHHHHHHH  4.86% 21278135