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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: Non-selective voltage-gated ion channel VDAC1

UniprotKB/SwissProt ID: Q60932 (Q60932)

Gene Name: Vdac1

Organism: Mus musculus (Mouse)

Function: Non-selective voltage-gated ion channel that mediates the transport of anions and cations through the mitochondrion outer membrane and plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective (By similarity). Binds various signaling molecules, including the sphingolipid ceramide, the phospholipid phosphatidylcholine, and the sterols cholesterol and oxysterol (PubMed:34799735). In depolarized mitochondria, acts downstream of PRKN and PINK1 to promote mitophagy or prevent apoptosis; polyubiquitination by PRKN promotes mitophagy, while monoubiquitination by PRKN decreases mitochondrial calcium influx which ultimately inhibits apoptosis (PubMed:32047033). May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis (PubMed:10716730, PubMed:15477379, PubMed:18988731). May mediate ATP export from cells (By similarity). Part of a complex composed of HSPA9, ITPR1 and VDAC1 that regulates mitochondrial calcium-dependent apoptosis by facilitating calcium transport from the ER lumen to the mitochondria intermembrane space thus providing calcium for the downstream calcium channel MCU that directly releases it into mitochondria matrix (PubMed:29907098) Catalyzes the scrambling of phospholipids across the outer mitochondrial membrane; the mechanism is unrelated to channel activity and is capable of translocating both anionic and zwitterionic phospholipids

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Mitochondrion outer membrane. Cell membrane. Membrane raft

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR023614 Porin_dom_sf
IPR001925 Porin_Euk
IPR027246 Porin_Euk/Tom40

The S-nitrosylation sites of Q60932

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 140 GYKREHINLG C DVDFDIAGPS  CCHHHHHHHH H HHCCCCCCHH  5.33% 24895380
21278135
2 245 AAKYQVDPDA C FSAKVNNSSL  CCHHHHHHHH H HHCCCCCCHH  3.45% 24895380
22588120
21278135