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
FABP9Fatty acid binding protein family (132 aa)    
Predicted Functional Partners:
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
    
 0.931
CYP2U1
Cytochrome P450 2U1; Catalyzes the hydroxylation of arachidonic acid, docosahexaenoic acid and other long chain fatty acids. May modulate the arachidonic acid signaling pathway and play a role in other fatty acid signaling processes; Cytochrome P450 family 2
      
 0.907
FABP4
Fatty acid-binding protein, adipocyte; Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus (By similarity); Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family
     
0.901
CYP2J2
Cytochrome P450 2J2; This enzyme metabolizes arachidonic acid predominantly via a NADPH-dependent olefin epoxidation to all four regioisomeric cis-epoxyeicosatrienoic acids. One of the predominant enzymes responsible for the epoxidation of endogenous cardiac arachidonic acid pools; Cytochrome P450 family 2
      
 0.806
CYP2R1
Vitamin D 25-hydroxylase; Has a D-25-hydroxylase activity on both forms of vitamin D, vitamin D(2) and D(3); Cytochrome P450 family 2
      
 0.800
SMTNL1
Smoothelin-like protein 1; Plays a role in the regulation of contractile properties of both striated and smooth muscles. When unphosphorylated, may inhibit myosin dephosphorylation. Phosphorylation at Ser-299 reduces this inhibitory activity (By similarity)
      
 0.648
PES1
Pescadillo homolog; Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome; Belongs to the pescadillo family
      
 0.635
KRBA1
Protein KRBA1; KRAB-A domain containing 1
      
 0.601
FABP6
Gastrotropin; Binds to bile acids and is involved in enterohepatic bile acid metabolism. Required for efficient apical to basolateral transport of conjugated bile acids in ileal enterocytes (By similarity). In vitro binds to bile acids in the order: deoxycholic acid > cholic acid > chenodeoxycholic acid and respective BA conjugation modifies affinities in the order taurine-conjugated > glycine-conjugated > unconjugated bile acids. Stimulates gastric acid and pepsinogen secretion (By similarity); Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family
      
 0.577
GOT2
Aspartate aminotransferase, mitochondrial; Catalyzes the irreversible transamination of the L- tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. Facilitates cellular uptake of long-chain free fatty acids; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family
   
  
 0.540
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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