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Contents

   



(Top)
 


1 Function  





2 References  





3 Further reading  














Glutamic--pyruvic transaminase 2






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GPT2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesGPT2, ALT2, GPT 2, MRT49, glutamic pyruvate transaminase (alanine aminotransferase) 2, glutamic--pyruvic transaminase 2, NEDSPM
External IDsOMIM: 138210; MGI: 1915391; HomoloGene: 68832; GeneCards: GPT2; OMA:GPT2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_133443
NM_001142466

NM_173866

RefSeq (protein)

NP_001135938
NP_597700

NP_776291

Location (UCSC)Chr 16: 46.88 – 46.93 MbChr 8: 86.22 – 86.25 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Glutamic--pyruvic transaminase 2 is a protein that in humans is encoded by the GPT2 gene. [5]

Function[edit]

This gene encodes a mitochondrial alanine transaminase, a pyridoxal enzyme that catalyzes the reversible transamination between alanine and 2-oxoglutarate to generate pyruvate and glutamate. Alanine transaminases play roles in gluconeogenesis and amino acid metabolism in many tissues including skeletal muscle, kidney, and liver. Activating transcription factor 4 upregulates this gene under metabolic stress conditions in hepatocyte cell lines. A loss of function mutation in this gene has been associated with developmental encephalopathy. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Apr 2015].

References[edit]

  • ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  • ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  • ^ "Entrez Gene: Glutamic--pyruvic transaminase 2". Retrieved 2018-05-07.
  • Further reading[edit]

    • Yang RZ, Blaileanu G, Hansen BC, Shuldiner AR, Gong DW (March 2002). "cDNA cloning, genomic structure, chromosomal mapping, and functional expression of a novel human alanine aminotransferase". Genomics. 79 (3): 445–50. doi:10.1006/geno.2002.6722. PMID 11863375.
  • Ding Y, Zhao L, Mei H, Huang ZH, Zhang SL (November 2006). "Alterations of biliary biochemical constituents and cytokines in infantile hepatitis syndrome". World J. Gastroenterol. 12 (43): 7038–41. doi:10.3748/wjg.v12.i43.7038. PMC 4087351. PMID 17109502.
  • Fraser A, Ebrahim S, Smith GD, Lawlor DA (July 2007). "A comparison of associations of alanine aminotransferase and gamma-glutamyltransferase with fasting glucose, fasting insulin, and glycated hemoglobin in women with and without diabetes". Hepatology. 46 (1): 158–65. doi:10.1002/hep.21667. PMID 17596883. S2CID 12779974.
  • Glinghammar B, Rafter I, Lindström AK, Hedberg JJ, Andersson HB, Lindblom P, Berg AL, Cotgreave I (May 2009). "Detection of the mitochondrial and catalytically active alanine aminotransferase in human tissues and plasma". Int. J. Mol. Med. 23 (5): 621–31. doi:10.3892/ijmm_00000173. PMID 19360321.
  • Hendrickson SL, Lautenberger JA, Chinn LW, Malasky M, Sezgin E, Kingsley LA, Goedert JJ, Kirk GD, Gomperts ED, Buchbinder SP, Troyer JL, O'Brien SJ (September 2010). "Genetic variants in nuclear-encoded mitochondrial genes influence AIDS progression". PLOS ONE. 5 (9): e12862. Bibcode:2010PLoSO...512862H. doi:10.1371/journal.pone.0012862. PMC 2943476. PMID 20877624.
  • Salgado MC, Metón I, Anemaet IG, Baanante IV (2014). "Activating transcription factor 4 mediates up-regulation of alanine aminotransferase 2 gene expression under metabolic stress". Biochim. Biophys. Acta. 1839 (4): 288–96. doi:10.1016/j.bbagrm.2014.01.005. PMID 24418603.
  • Celis K, Shuldiner S, Haverfield EV, Cappell J, Yang R, Gong DW, Chung WK (September 2015). "Loss of function mutation in glutamic pyruvate transaminase 2 (GPT2) causes developmental encephalopathy". J. Inherit. Metab. Dis. 38 (5): 941–8. doi:10.1007/s10545-015-9824-x. PMC 4919120. PMID 25758935.

  • t
  • e
  • This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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