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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: Diacylglycerol lipase-beta

UniprotKB/SwissProt ID: Q8NCG7 (Q8NCG7)

Gene Name: DAGLB

Organism: Homo sapiens (Human)

Function: Lipase that catalyzes the hydrolysis of arachidonic acid (AA)-esterified diacylglycerols (DAGs) to produce the principal endocannabinoid, 2-arachidonoylglycerol (2-AG) which can be further cleaved by downstream enzymes to release arachidonic acid (AA) for cyclooxygenase (COX)-mediated eicosanoid production (PubMed:14610053). Preferentially hydrolyzes DAGs at the sn-1 position in a calcium-dependent manner and has negligible activity against other lipids including monoacylglycerols and phospholipids (PubMed:14610053). Plays a key role in the regulation of 2-AG and AA pools utilized by COX1/2 to generate lipid mediators of macrophage and microglia inflammatory responses. Also functions as a polyunsaturated fatty acids-specific triacylglycerol lipase in macrophages. Plays an important role to support the metabolic and signaling demands of macrophages (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cell membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR029058 AB_hydrolase_fold
IPR052214 DAG_Lipase-Related
IPR002921 Fungal_lipase-type

The S-nitrosylation sites of Q8NCG7

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 397 SAESEVLDVE C EVQDRLAHKG   
2 658 LDSVVSDRAA C VSCPAQGVSS   
3 661 VVSDRAACVS C PAQGVSSVDV