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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: 2-isopropylmalate synthase 1, chloroplastic

UniprotKB/SwissProt ID: Q9LPR4 (Q9LPR4)

Gene Name: IPMS1

Organism: Arabidopsis thaliana (Mouse-ear cress)

Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). Involved in Leu biosynthesis, but does not participate in the chain elongation of glucosinolates

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Plastid, chloroplast

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR050073 2-IPM_HCS-like
IPR013709 2-isopropylmalate_synth_dimer
IPR002034 AIPM/Hcit_synth_CS
IPR013785 Aldolase_TIM
IPR054691 LeuA/HCS_post-cat
IPR036230 LeuA_allosteric_dom_sf
IPR005671 LeuA_bact_synth
IPR000891 PYR_CT

The S-nitrosylation sites of Q9LPR4

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 226 SMVRFARSLG C EDVEFSPEDA   
2 410 LKHKGTYEII C PEEIGLERSN   
3 520 ADADGKEHVA C SIGTGPVDSA