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Pnliprp2 Pnliprp2 Lpl Lpl Pnlip Pnlip Pnliprp1 Pnliprp1 Lipc Lipc Pla1a Pla1a Lipg Lipg Liph Liph Lipi Lipi
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Pnliprp2Pancreatic lipase-related protein 2; Lipase with broad substrate specificity. Can hydrolyze both phospholipids and galactolipids. Shows a preference for 1,2- didodecanoylphosphatidylethanolamine and 1,2- didodecanoylphosphatidylglycerol, and has low activity towards 1,2- didodecanoylphosphatidylcholine (in vitro). Belongs to the AB hydrolase superfamily. Lipase family. (479 aa)
LplLipoprotein lipase; Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans. (474 aa)
PnlipPancreatic triacylglycerol lipase; Plays an important role in fat metabolism. It preferentially splits the esters of long-chain fatty acids at positions 1 and 3, producing mainly 2-monoacylglycerol and free fatty acids, and shows considerably higher activity against insoluble emulsified substrates than against soluble ones. (465 aa)
Pnliprp1Inactive pancreatic lipase-related protein 1; May function as inhibitor of dietary triglyceride digestion. Lacks detectable lipase activity (in vitro) (By similarity). Belongs to the AB hydrolase superfamily. Lipase family. (473 aa)
LipcHepatic triacylglycerol lipase; Hepatic lipase has the capacity to catalyze hydrolysis of phospholipids, mono-, di-, and triglycerides, and acyl-CoA thioesters. It is an important enzyme in HDL metabolism. Hepatic lipase binds heparin. (510 aa)
Pla1aPhospholipase A1 member A; Hydrolyzes the ester bond at the sn-1 position of glycerophospholipids and produces 2-acyl lysophospholipids. Hydrolyzes phosphatidylserine (PS) in the form of liposomes and 1-acyl-2 lysophosphatidylserine (lyso-PS), but not triolein, phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidic acid (PA) or phosphatidylinositol (PI). Hydrolysis of lyso-PS in peritoneal mast cells activated by receptors for IgE leads to stimulate histamine production. (456 aa)
LipgEndothelial lipase; Has phospholipase and triglyceride lipase activities. Hydrolyzes high density lipoproteins (HDL) more efficiently than other lipoproteins. Binds heparin (By similarity). (493 aa)
LiphLipase member H; Hydrolyzes specifically phosphatidic acid (PA) to produce lysophosphatidic acid (LPA); Belongs to the AB hydrolase superfamily. Lipase family. (451 aa)
LipiLipase, member H (Predicted). (476 aa)
Your Current Organism:
Rattus norvegicus
NCBI taxonomy Id: 10116
Other names: Buffalo rat, Norway rat, R. norvegicus, Rattus PC12 clone IS, Rattus sp. strain Wistar, Sprague-Dawley rat, Wistar rats, brown rat, laboratory rat, rat, rats, zitter rats
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