GOT1

GOT1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesGOT1, ASTQTL1, GIG18, cAspAT, cCAT, AST1, glutamic-oxaloacetic transaminase 1
External IDsMGI: 95791 HomoloGene: 1571 GeneCards: GOT1
Gene location (Human)
Chr.Chromosome 10 (human)[1]
Band10q24.2Start99,396,870 bp[1]
End99,430,624 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

2805

14718

Ensembl

ENSG00000120053

ENSMUSG00000025190

UniProt

P17174

P05201

RefSeq (mRNA)

NM_002079

NM_010324

RefSeq (protein)

NP_002070

NP_034454

Location (UCSC)Chr 10: 99.4 – 99.43 MbChr 19: 43.5 – 43.52 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Aspartate aminotransferase, cytoplasmic is an enzyme that in humans is encoded by the GOT1 gene.[5][6]

Glutamic-oxaloacetic transaminase is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, respectively. GOT plays a role in amino acid metabolism and the urea and tricarboxylic acid cycles. The two enzymes are homodimeric and show close homology.[6]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. [§ 1]

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GlycolysisGluconeogenesis_WP534go to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to WikiPathwaysgo to articlego to Entrezgo to article
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GlycolysisGluconeogenesis_WP534go to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to WikiPathwaysgo to articlego to Entrezgo to article
|{{{bSize}}}px|alt=Glycolysis and Gluconeogenesis edit]]
Glycolysis and Gluconeogenesis edit
  1. ↑ The interactive pathway map can be edited at WikiPathways: "GlycolysisGluconeogenesis_WP534".

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000120053 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000025190 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ Bousquet-Lemercier B, Pol S, Pave-Preux M, Hanoune J, Barouki R (Sep 1990). "Properties of human liver cytosolic aspartate aminotransferase mRNAs generated by alternative polyadenylation site selection". Biochemistry. 29 (22): 5293–9. doi:10.1021/bi00474a011. PMID 1974457.
  6. 1 2 "Entrez Gene: GOT1 glutamic-oxaloacetic transaminase 1, soluble (aspartate aminotransferase 1)".

Further reading

  • Panteghini M (1990). "Aspartate aminotransferase isoenzymes". Clin. Biochem. 23 (4): 311–9. doi:10.1016/0009-9120(90)80062-N. PMID 2225456.
  • Doonan S, Barra D, Bossa F (1985). "Structural and genetic relationships between cytosolic and mitochondrial isoenzymes". Int. J. Biochem. 16 (12): 1193–9. doi:10.1016/0020-711X(84)90216-7. PMID 6397370.
  • Kamei S, Ohkubo A, Yamanaka M (1979). "Apoenzyme of aspartate aminotransferase isozymes in serum and its diagnostic usefullness for hepatic diseases". Clin. Chim. Acta. 96 (1–2): 97–105. doi:10.1016/0009-8981(79)90058-5. PMID 225064.
  • Doyle JM, Schininà ME, Bossa F, Doonan S (1990). "The amino acid sequence of cytosolic aspartate aminotransferase from human liver". Biochem. J. 270 (3): 651–7. PMC 1131781. PMID 2241899.
  • Pol S, Bousquet-Lemercier B, Pavé-Preux M, et al. (1989). "Chromosomal localization of human aspartate aminotransferase genes by in situ hybridization". Hum. Genet. 83 (2): 159–64. doi:10.1007/BF00286710. PMID 2777255.
  • Pol S, Bousquet-Lemercier B, Pave-Preux M, et al. (1989). "Nucleotide sequence and tissue distribution of the human mitochondrial aspartate aminotransferase mRNA". Biochem. Biophys. Res. Commun. 157 (3): 1309–15. doi:10.1016/S0006-291X(88)81017-9. PMID 3207426.
  • Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
  • Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
  • Wang CY, Huang YQ, Shi JD, et al. (1999). "Genetic homogeneity, high-resolution mapping, and mutation analysis of the urofacial (Ochoa) syndrome and exclusion of the glutamate oxaloacetate transaminase gene (GOT1) in the critical region as the disease gene". Am. J. Med. Genet. 84 (5): 454–9. doi:10.1002/(SICI)1096-8628(19990611)84:5<454::AID-AJMG9>3.0.CO;2-D. PMID 10360399.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Miyake Y, Eguchi H, Shinchi K, et al. (2003). "Glucose intolerance and serum aminotransferase activities in Japanese men". J. Hepatol. 38 (1): 18–23. doi:10.1016/S0168-8278(02)00323-9. PMID 12480555.
  • Deloukas P, Earthrowl ME, Grafham DV, et al. (2004). "The DNA sequence and comparative analysis of human chromosome 10". Nature. 429 (6990): 375–81. doi:10.1038/nature02462. PMID 15164054.
  • Wu KL, Lu SN, Changchien CS, et al. (2004). "Sequential changes of serum aminotransferase levels in patients with severe acute respiratory syndrome". Am. J. Trop. Med. Hyg. 71 (2): 125–8. PMID 15306699.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Totan A, Greabu M, Totan C, Spinu T (2006). "Salivary aspartate aminotransferase, alanine aminotransferase and alkaline phosphatase: possible markers in periodontal diseases?". Clin. Chem. Lab. Med. 44 (5): 612–5. doi:10.1515/CCLM.2006.096. PMID 16681433.
  • Dubern B, Girardet JP, Tounian P (2007). "Insulin resistance and ferritin as major determinants of abnormal serum aminotransferase in severely obese children". International Journal of Pediatric Obesity. 1 (2): 77–82. doi:10.1080/17477160600569594. PMID 17907318.


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