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HOGA1 protein (human) - STRING interaction network
"HOGA1" - 4-hydroxy-2-oxoglutarate aldolase, mitochondrial in Homo sapiens
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second shell of interactors
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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HOGA14-hydroxy-2-oxoglutarate aldolase, mitochondrial; Catalyzes the final step in the metabolic pathway of hydroxyproline (327 aa)    
Predicted Functional Partners:
GRHPR
Glyoxylate reductase/hydroxypyruvate reductase; Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase and D-glycerate dehydrogenase enzymatic activities. Reduces hydroxypyruvate to D-glycerate, glyoxylate to glycolate oxidizes D-glycerate to hydroxypyruvate (328 aa)
   
 
  0.991
AGXT
Alanine-glyoxylate aminotransferase (392 aa)
   
 
  0.981
HAO1
Hydroxyacid oxidase 1; Has 2-hydroxyacid oxidase activity. Most active on the 2-carbon substrate glycolate, but is also active on 2-hydroxy fatty acids, with high activity towards 2-hydroxy palmitate and 2- hydroxy octanoate (370 aa)
   
 
  0.935
HAO2
Hydroxyacid oxidase 2; Catalyzes the oxidation of L-alpha-hydroxy acids as well as, more slowly, that of L-alpha-amino acids; Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family (351 aa)
   
 
  0.934
GOT1
Aspartate aminotransferase, cytoplasmic; Biosynthesis of L-glutamate from L-aspartate or L- cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis. Using L-cysteine as substrate, regulates levels of mercaptopyruvate, an important source of hydrogen sulfide. Mercaptopyruvate is converted into H(2)S via the action of 3- [...] (413 aa)
   
 
  0.930
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 (430 aa)
   
 
  0.921
DAO
D-amino-acid oxidase; Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D- amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids; Belongs to the DAMOX/DASOX family (347 aa)
   
 
  0.863
AGXT2
Alanine--glyoxylate aminotransferase 2, mitochondrial; Can metabolize asymmetric dimethylarginine (ADMA) via transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this activity provides mechanism through which the kidney regulates blood pressure; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family (514 aa)
     
 
  0.819
C12orf65
Probable peptide chain release factor C12orf65, mitochondrial; May act as a codon-independent translation release factor that has lost all stop codon specificity and directs the termination of translation in mitochondrion. May help rescuing stalled mitoribosomes during translation (By similarity) (166 aa)
     
   
  0.811
TUFM
Elongation factor Tu, mitochondrial; This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily (455 aa)
   
   
  0.794
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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