STRINGSTRING
DPEP1 DPEP1 GGTLC1 GGTLC1 CHAC2 CHAC2 GGT1 GGT1 GGT2 GGT2 GGT1-2 GGT1-2 GGTLC2 GGTLC2 GGTLC3 GGTLC3 CHAC1 CHAC1 GGT5 GGT5 GGT7 GGT7
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:
DPEP1Dipeptidase 1; Hydrolyzes a wide range of dipeptides. Implicated in the renal metabolism of glutathione and its conjugates. Converts leukotriene D4 to leukotriene E4; it may play an important role in the regulation of leukotriene activity. (411 aa)
GGTLC1Gamma-glutamyltransferase light chain 1. (225 aa)
CHAC2Glutathione-specific gamma-glutamylcyclotransferase 2; Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides. (184 aa)
GGT1Glutathione hydrolase 1 heavy chain; 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)
GGT2Inactive glutathione hydrolase 2; Isoform 1, isoform 2 and isoform 3 lack catalytic activity due to its inability to undergo the autocatalytic cleavage needed to produce a mature, enzymatically active heterodimer. (569 aa)
GGT1-2Gamma-glutamyltransferase 1. (569 aa)
GGTLC2Gamma-glutamyltransferase light chain 2; Belongs to the gamma-glutamyltransferase family. (218 aa)
GGTLC3Gamma-glutamyltransferase light chain family member 3. (225 aa)
CHAC1Glutathione-specific gamma-glutamylcyclotransferase 1; Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides. Glutathione depletion is an important factor for apoptosis initiation and execution. Acts as a pro-apoptotic component of the unfolded protein response pathway by mediating the pro-apoptotic effects of the ATF4-ATF3-DDIT3/CHOP cascade. Negative regulator of Notch signaling pathway involved in embryonic neurogenesis: acts by inhibiting Notch cleavage by furin, maintaining Not [...] (222 aa)
GGT5Glutathione hydrolase 5 heavy chain; Cleaves the gamma-glutamyl peptide bond of glutathione conjugates, but maybe not glutathione itself. Converts leukotriene C4 (LTC4) to leukotriene D4 (LTD4). (587 aa)
GGT7Glutathione hydrolase 7 heavy chain; Cleaves glutathione conjugates; Belongs to the gamma-glutamyltransferase family. (662 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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