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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: GPI-anchor transamidase

UniprotKB/SwissProt ID: Q92643 (Q92643)

Gene Name: PIGK

Organism: Homo sapiens (Human)

Function: Catalytic subunit of the glycosylphosphatidylinositol-anchor (GPI-anchor) transamidase (GPI-T) complex that catalyzes the formation of the linkage between a proprotein and a GPI-anchor and participates in GPI anchored protein biosynthesis (PubMed:10793132, PubMed:11483512, PubMed:12582175, PubMed:34576938, PubMed:35165458, PubMed:35551457, PubMed:37684232, PubMed:9356492). Recognizes diverse proproteins at a C-terminal signal peptide (CSP) region that lacks consensus sequence and replaces it with a GPI-anchor via a transamidation reaction (PubMed:35165458, PubMed:35551457, PubMed:37684232). Transamidation catalysis reaction follows a two-phase mechanism (PubMed:37684232). In the acyl-enzyme phase, the carbonyl group of the proproteins's omega-site undergoes a nucleophilic attack forming an enzyme-substrate thioester bond (PubMed:37684232). Followed by a general acid catalysis that allows CSP releasing, regenerating the carbonyl, and forming the acyl-enzyme intermediate (PubMed:37684232). In the GPI-anchor attachment phase, the amino group of the GPI-anchor's ethanolamine phosphate, the one on third mannose (EtNP3), mediates a nucleophilic attack on the carbonyl of the acyl-enzyme intermediate, replacing the CSP, allowing GPI-anchor attachment to the omega-residue, therefore forming the product and freeing the enzyme (PubMed:37684232)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Endoplasmic reticulum membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR028361 GPI_transamidase
IPR001096 Peptidase_C13