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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: Acyl-protein thioesterase 1

UniprotKB/SwissProt ID: E5RGR0 (E5RGR0)

Gene Name: LYPLA1

Organism: Homo sapiens (Human)

Function: Acts as an acyl-protein thioesterase. Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Acts as a palmitoyl thioesterase that catalyzes depalmitoylation of proteins, such as ADRB2, KCNMA1 and SQSTM1. Acts as a negative regulator of autophagy by mediating palmitoylation of SQSTM1, decreasing affinity between SQSTM1 and ATG8 proteins and recruitment of ubiquitinated cargo proteins to autophagosomes. Acts as a lysophospholipase and hydrolyzes lysophosphatidylcholine (lyso-PC). Also hydrolyzes lysophosphatidylethanolamine (lyso-PE), lysophosphatidylinositol (lyso-PI) and lysophosphatidylserine (lyso-PS). Has much higher thioesterase activity than lysophospholipase activity. Contributes to the production of lysophosphatidic acid (LPA) during blood coagulation by recognizing and cleaving plasma phospholipids to generate lysophospholipids which in turn act as substrates for ENPP2 to produce LPA

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cell membrane. Cytoplasm. Endoplasmic reticulum. Nucleus membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR029058 AB_hydrolase_fold
IPR050565 LYPA1-2/EST-like
IPR003140 PLipase/COase/thioEstase