GOT1

Glutamic-oxaloacetic transaminase 1, soluble (aspartate aminotransferase 1)
PDB rendering based on 1ajr.
Available structures PDB 1ajr, 1ajs
Identifiers
Symbols	GOT1; GIG18
External IDs	OMIM: 138180 MGI: 95791 HomoloGene: 1571 GeneCards: GOT1 Gene
EC number	2.6.1.1
Gene Ontology Molecular function • L-aspartate:2-oxoglutarate aminotransferase activity • L-aspartate:2-oxoglutarate aminotransferase activity • L-aspartate:2-oxoglutarate aminotransferase activity • phosphatidylserine decarboxylase activity • pyridoxal phosphate binding • carboxylic acid binding Cellular component • soluble fraction • cytoplasm • lysosome • cytosol • axon terminus Biological process • carbohydrate metabolic process • glucose metabolic process • gluconeogenesis • 2-oxoglutarate metabolic process • oxaloacetate metabolic process • glycerol biosynthetic process • aspartate metabolic process • aspartate biosynthetic process • aspartate catabolic process • glutamate metabolic process • cellular amino acid biosynthetic process • biosynthetic process • glutamate catabolic process to aspartate • glutamate catabolic process to 2-oxoglutarate • cellular response to insulin stimulus • cellular nitrogen compound metabolic process • response to glucocorticoid stimulus • fatty acid homeostasis Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2805	14718
Ensembl	ENSG00000120053	ENSMUSG00000025190
UniProt	P17174	Q3UJH8
RefSeq (mRNA)	NM_002079	NM_010324.2
RefSeq (protein)	NP_002070	NP_034454.2
Location (UCSC)	Chr 10: 101.16 – 101.19 Mb	Chr 19: 43.57 – 43.6 Mb
PubMed search	[1]	[2]

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

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.

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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1131781. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139146. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• 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 : IJPO : an official journal of the International Association for the Study of Obesity 1 (2): 77–82. PMID 17907318.