STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges:
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 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:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
PNLIPPancreatic lipase; Belongs to the AB hydrolase superfamily. Lipase family (465 aa)    
Predicted Functional Partners:
CLPS
Colipase; Colipase is a cofactor of pancreatic lipase. It allows the lipase to anchor itself to the lipid-water interface. Without colipase the enzyme is washed off by bile salts, which have an inhibitory effect on the lipase
   
 0.997
CEL
Bile salt-activated lipase; Catalyzes fat and vitamin absorption. Acts in concert with pancreatic lipase and colipase for the complete digestion of dietary triglycerides; Belongs to the type-B carboxylesterase/lipase family
   
 
 0.960
LIPE
Hormone-sensitive lipase; In adipose tissue and heart, it primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone production; Lipases
   
 
 0.959
LIPF
Lipase F, gastric type; Lipases
   
 
 0.946
MGLL
Monoglyceride lipase; Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes the endocannabinoid 2-arachidonoylglycerol, and thereby contributes to the regulation of endocannabinoid signaling, nociperception and perception of pain (By similarity). Regulates the levels of fatty acids that serve as signaling molecules and promote cancer cell migration, invasion and tumor growth; Lipases
     
 0.940
RBP2
Retinol-binding protein 2; Intracellular transport of retinol; Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family
     
 0.919
LPL
Lipoprotein lipase; The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL). Binding to heparin sulfate proteogylcans at the cell surface is vital to the function. The apolipoprotein, APOC2, acts as a coactivator of LPL activity in the presence of lipids on the luminal surface of vascular endothelium (By similarity); Belongs to the AB hydrolase superfamily. Lipase family
   
 
0.918
RBP1
Retinol-binding protein 1; Cytoplasmic retinol-binding protein. Accepts retinol from the transport protein STRA6, and thereby contributes to retinol uptake, storage and retinoid homeostasis; Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family
     
 0.917
RBP5
Retinol-binding protein 5; Intracellular transport of retinol; Fatty acid binding protein family
     
 0.906
AGK
Acylglycerol kinase, mitochondrial; Lipid kinase that can phosphorylate both monoacylglycerol and diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic acid (PA), respectively. Does not phosphorylate sphingosine. Independently of its lipid kinase activity, acts as a component of the TIM22 complex. The TIM22 complex mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane by forming a twin-pore translocase that uses the membrane potential as the external driving force. In the TIM22 complex, required for the import of a su [...]
     
 0.904
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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