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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: Cysteine desulfurase

UniprotKB/SwissProt ID: Q9Z1J3 (Q9Z1J3)

Gene Name: Nfs1

Organism: Mus musculus (Mouse)

Function: Mitochondrial cysteine desulfurase, of the core iron-sulfur cluster (ISC) assembly complex, that catalyzes the desulfuration of L-cysteine to L-alanine, as component of the cysteine desulfurase complex, leading to the formation of a cysteine persulfide intermediate at the active site cysteine residue and participates in the [2Fe-2S] clusters assembly on the scaffolding protein ISCU (PubMed:25597503). The persulfide is then transferred on the flexible Cys loop from the catalytic site of NFS1 to the surface of NFS1 (By similarity). After the NFS1-linked persulfide sulfur is transferred to one of the conserved Cys residues of the scaffold, a reaction assisted by FXN (PubMed:25597503). The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Mitochondrion

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR000192 Aminotrans_V_dom
IPR020578 Aminotrans_V_PyrdxlP_BS
IPR010240 Cys_deSase_IscS
IPR016454 Cysteine_dSase
IPR015424 PyrdxlP-dep_Trfase
IPR015421 PyrdxlP-dep_Trfase_major
IPR015422 PyrdxlP-dep_Trfase_small

The S-nitrosylation sites of Q9Z1J3

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 428 EEEVDYTAEK C IHHVKRLREM