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:
a 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 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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
BlvraBiliverdin reductase A; Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor; Belongs to the Gfo/Idh/MocA family. Biliverdin reductase subfamily. (295 aa)    
Predicted Functional Partners:
Hmox2
Heme oxygenase 2; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.
   
 
 0.991
Hmox1
Heme oxygenase 1; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.
     
 0.988
Blvrb
Biliverdin reductase B (Flavin reductase (NADPH)) (Predicted), isoform CRA_b.
   
 
 0.964
Ugt1a1
UDP-glucuronosyltransferase 1-1; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. Glucuronates opioids and bilirubin; Belongs to the UDP-glycosyltransferase family.
     
 0.948
RGD1559459
UDP-glucuronosyltransferase; Belongs to the UDP-glycosyltransferase family.
     
 0.929
Ugt2a1
UDP-glucuronosyltransferase; Belongs to the UDP-glycosyltransferase family.
   
 
 0.927
Ugt2b1
UDP-glucuronosyltransferase 2B1; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds; Belongs to the UDP-glycosyltransferase family.
     
 0.923
Ugt2b35
UDP-glucuronosyltransferase 2B15; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. Catalyzes the transfer of glucuronic acid from UDP- glucuronic acid to various aglycone molecules. Catalyzes the glucuronidation of monoterpenoid alcohols, such as (-)-borneol, (+)- menthol, and (-)- nopol. In addition, a number of simple phenolic compounds, such as hydroxybiphenyls, 7-hydroxylated coumarins, p- nitrophenol, and food-derived substances (e.g. naringenin and eugenol), and 4-methylumbelliferone are also sub [...]
     
 0.921
Ugt2b
UDP-glucuronosyltransferase 2B37; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. 2B37 is about 30-fold less active than 2B5 toward testosterone and dihydrotestosterone; Belongs to the UDP-glycosyltransferase family.
   
 
 0.920
G6pd
Glucose-6-phosphate 1-dehydrogenase; Cytosolic glucose-6-phosphate dehydrogenase that catalyzes the first and rate-limiting step of the oxidative branch within the pentose phosphate pathway/shunt, an alternative route to glycolysis for the dissimilation of carbohydrates and a major source of reducing power and metabolic intermediates for fatty acid and nucleic acid biosynthetic processes.
   
 
 0.702
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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