Protein Name:
Acyl-protein thioesterase 1
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UniprotKB/SwissProt ID: O75608 (O75608)
Gene Name:
LYPLA1
Organism: Homo sapiens (Human)
Function: Acts as an acyl-protein thioesterase (PubMed:19439193, PubMed:20418879). Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS (PubMed:20418879). Acts as a palmitoyl thioesterase that catalyzes depalmitoylation of proteins, such as ADRB2, KCNMA1 and SQSTM1 (PubMed:22399288, PubMed:27481942, PubMed:37802024). 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 (PubMed:37802024). Acts as a lysophospholipase and hydrolyzes lysophosphatidylcholine (lyso-PC) (PubMed:19439193). Also hydrolyzes lysophosphatidylethanolamine (lyso-PE), lysophosphatidylinositol (lyso-PI) and lysophosphatidylserine (lyso-PS) (By similarity). Has much higher thioesterase activity than lysophospholipase activity (PubMed:19439193). 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 (PubMed:21393252)
Other Modifications: View all modification sites in dbPTM
Protein Subcellular Localization: Cytoplasm. Cell membrane. Nucleus membrane. Endoplasmic reticulum
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Graphical Visualization of S-nitrosylation Sites:
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The S-nitrosylation sites of O75608
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| No. |
Position |
S-nitrosylated Peptide |
Secondary Structure of S-nitrosylated Peptide |
Solvent Accessibility of nitrosylated Site |
PubMed ID |
| 1 |
144 |
QKLAGVTALS C WLPLRASFPQ |
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| 2 |
211 |
KTYEGMMHSS C QQEMMDVKQF |
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