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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: Peptidyl-prolyl cis-trans isomerase F, mitochondrial

UniprotKB/SwissProt ID: P29117 (P29117)

Gene Name: Ppif

Organism: Rattus norvegicus (Rat)

Function: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (By similarity). Involved in regulation of the mitochondrial permeability transition pore (mPTP) (PubMed:8567677, PubMed:9309684, PubMed:9820802). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated (PubMed:8567677, PubMed:9309684, PubMed:9820802). In cooperation with mitochondrial p53/TP53 is involved in activating oxidative stress-induced necrosis (PubMed:8567677, PubMed:9309684, PubMed:9820802). Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels (PubMed:8567677, PubMed:9309684, PubMed:9820802). Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis (PubMed:19228691)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Mitochondrion matrix

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR029000 Cyclophilin-like_dom_sf
IPR020892 Cyclophilin-type_PPIase_CS
IPR002130 Cyclophilin-type_PPIase_dom

The S-nitrosylation sites of P29117

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 202 KTSKKIVITD C GQLS------  CCCCCCCHHH H HHHCCCCCCC  2.54%