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STRING protein interaction network
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 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
protein homology
Your Input:
Gene Fusion
GLULGlutamine synthetase; This enzyme has 2 functions: it catalyzes the production of glutamine and 4-aminobutanoate (gamma-aminobutyric acid, GABA), the latter in a pyridoxal phosphate-independent manner (By similarity). Essential for proliferation of fetal skin fibroblasts; Belongs to the glutamine synthetase family (373 aa)    
Predicted Functional Partners:
Glutamate dehydrogenase 1, mitochondrial; Mitochondrial glutamate dehydrogenase that converts L- glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle. May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity); Belongs to the Glu/Leu/Phe/Val dehydrogenases family
Glutamate dehydrogenase 2, mitochondrial; Important for recycling the chief excitatory neurotransmitter, glutamate, during neurotransmission; Belongs to the Glu/Leu/Phe/Val dehydrogenases family
Amidophosphoribosyltransferase; Phosphoribosyl pyrophosphate amidotransferase; In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family
Glutaminase liver isoform, mitochondrial; Plays an important role in the regulation of glutamine catabolism. Promotes mitochondrial respiration and increases ATP generation in cells by catalyzing the synthesis of glutamate and alpha-ketoglutarate. Increases cellular anti-oxidant function via NADH and glutathione production. May play a role in preventing tumor proliferation; Ankyrin repeat domain containing
Glutaminase kidney isoform, mitochondrial; Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate in the brain. Isoform 2 lacks catalytic activity; Ankyrin repeat domain containing
Carbamoyl-phosphate synthase [ammonia], mitochondrial; Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell
4-aminobutyrate aminotransferase, mitochondrial; Catalyzes the conversion of gamma-aminobutyrate and L- beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate and beta-alanine; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family
Delta-1-pyrroline-5-carboxylate synthase; Bifunctional enzyme that converts glutamate to glutamate 5-semialdehyde, an intermediate in the biosynthesis of proline, ornithine and arginine
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1; Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins. Regulates the circadian expression of clock genes ARNTL/BMAL1 and CRY1
Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial; Irreversible conversion of delta-1-pyrroline-5- carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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