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  • 11.0 [archived version]
STRINGSTRING
BCAT1 BCAT1 OPLAH OPLAH BCAT2 BCAT2 GCLM GCLM GGT1 GGT1 GCLC GCLC GGT5 GGT5 GGCT GGCT GSS GSS LAP3 LAP3 ANPEP ANPEP
"GCLM" - Glutamate-cysteine ligase modifier subunit in Homo sapiens
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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GCLMGlutamate-cysteine ligase modifier subunit; Belongs to the aldo/keto reductase family. Glutamate-- cysteine ligase light chain subfamily (274 aa)    
Predicted Functional Partners:
GCLC
Glutamate-cysteine ligase catalytic subunit (637 aa)
     
  0.999
GSS
Glutathione synthetase; Belongs to the eukaryotic GSH synthase family (474 aa)
     
 
  0.974
BCAT1
Branched-chain-amino-acid aminotransferase, cytosolic; Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine (398 aa)
     
 
  0.942
BCAT2
Branched-chain-amino-acid aminotransferase, mitochondrial; Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids; Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family (392 aa)
     
 
  0.939
GGT1
Glutathione hydrolase 1 proenzyme; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione ( [...] (569 aa)
     
 
  0.931
GGT5
Glutathione hydrolase 5 proenzyme; Cleaves the gamma-glutamyl peptide bond of glutathione conjugates, but maybe not glutathione itself. Converts leukotriene C4 (LTC4) to leukotriene D4 (LTD4); Belongs to the gamma-glutamyltransferase family (587 aa)
     
 
  0.918
GGCT
Gamma-glutamylcyclotransferase; Catalyzes the formation of 5-oxoproline from gamma- glutamyl dipeptides and may play a significant role in glutathione homeostasis. Induces release of cytochrome c from mitochondria with resultant induction of apoptosis; Belongs to the gamma-glutamylcyclotransferase family (188 aa)
     
 
  0.909
OPLAH
5-oxoprolinase; Catalyzes the cleavage of 5-oxo-L-proline to form L- glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate (1288 aa)
     
 
  0.909
ANPEP
Aminopeptidase N; Broad specificity aminopeptidase which plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Also involved in the processing of various peptides including peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. May also be involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis and promote cholesterol crystallization; Aminopeptidases (967 aa)
     
 
  0.906
LAP3
Cytosol aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides; Belongs to the peptidase M17 family (519 aa)
   
 
  0.904
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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