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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: Chaperone protein ClpC2, chloroplastic

UniprotKB/SwissProt ID: Q9SXJ7 (Q9SXJ7)

Gene Name: CLPC2

Organism: Arabidopsis thaliana (Mouse-ear cress)

Function: Molecular chaperone (PubMed:15304652, PubMed:21737456, PubMed:24599948). May act as a suppressor of FtsH-mediated thylakoid membrane biogenesis and may enhance photoinhibition (PubMed:15304652). Seems not involved in chloroplastic protein import (PubMed:15304652). Probable component of the TIC-associated stromal import motor involved in inner membrane translocation (PubMed:17376159). Has an ATPase activity, but no ADPase activity (PubMed:21737456). Interacts with transit peptides with a positional preference (PubMed:21737456, PubMed:22545953). Localization of the signal sequence at the N-terminal end of a protein seems mandatory for interaction to take place (PubMed:22545953)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Plastid, chloroplast stroma. Plastid, chloroplast membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR003593 AAA+_ATPase
IPR003959 ATPase_AAA_core
IPR019489 Clp_ATPase_C
IPR036628 Clp_N_dom_sf
IPR004176 Clp_R_dom
IPR001270 ClpA/B
IPR018368 ClpA/B_CS1
IPR028299 ClpA/B_CS2
IPR041546 ClpA/ClpB_AAA_lid
IPR050130 ClpA_ClpB
IPR027417 P-loop_NTPase
IPR001943 UVR_dom

The S-nitrosylation sites of Q9SXJ7

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 320 ILARRTKNNP C LIGEPGVGKT   
2 426 KPALARGELQ C IGATTIDEYR