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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: Phospholipase B1, membrane-associated

UniprotKB/SwissProt ID: Q3TTY0 (Q3TTY0)

Gene Name: Plb1

Organism: Mus musculus (Mouse)

Function: Calcium-independent membrane-associated phospholipase that catalyzes complete diacylation of phospholipids by hydrolyzing both sn-1 and sn-2 fatty acyl chains attached to the glycerol backbone (phospholipase B activity) (By similarity). Has dual phospholipase and lysophospholipase activities toward diacylphospholipids. Preferentially cleaves sn-2 ester bonds over sn-1 bonds. Acts as a lipase toward glycerolipid substrates (By similarity). Hydrolyzes fatty acyl chains of diacylglycerols with preference for the sn-2 position and of triacylglycerols with not positional selectivity (By similarity). May also hydrolyze long chain retinyl esters such as retinyl palmitate (By similarity). May contribute to digestion of dietary phospholipids, glycerolipids and retinoids, facilitating lipid absorption at the brush border (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Apical cell membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR001087 GDSL
IPR008265 Lipase_GDSL_AS
IPR035547 Phospholipase_B
IPR038885 PLB1
IPR036514 SGNH_hydro_sf