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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: Magnesium-chelatase subunit ChlI-1, chloroplastic

UniprotKB/SwissProt ID: P16127 (P16127)

Gene Name: CHLI1

Organism: Arabidopsis thaliana (Mouse-ear cress)

Function: Involved in chlorophyll biosynthesis. Catalyzes the insertion of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. The magnesium-chelatase is a complex of three subunits, CHLI, CHLD and CHLH. The reaction takes place in two steps, with an ATP-dependent activation followed by an ATP-dependent chelation step. Possesses high affinity for ATP and may play a major role in chlorophyll biosynthesis. Does not bind abscisic acid (ABA), but is a positive regulator of ABA signaling (PubMed:11842180, PubMed:15815918, PubMed:17472958, PubMed:18846282, PubMed:23011401). May be involved in ABA signaling in the control of stomatal aperture, but does not seem to have an effect on ABA-induced gene expression (PubMed:24840863)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Plastid, chloroplast

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR003593 AAA+_ATPase
IPR045006 CHLI-like
IPR041628 ChlI/MoxR_AAA_lid
IPR011775 Mg_chelatase_ATPase-isu
IPR000523 Mg_chelatse_chII-like_cat_dom
IPR027417 P-loop_NTPase

The S-nitrosylation sites of P16127

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 354 RELKVKISRV C SELNVDGLRG