GOT1

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

GOT1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3II0, 3WZF
Identifiers
Aliases	GOT1, ASTQTL1, GIG18, cAspAT, cCAT, AST1, glutamic-oxaloacetic transaminase 1
External IDs	OMIM: 138180 MGI: 95791 HomoloGene: 1571 GeneCards: GOT1
Gene location (Human) Chr. Chromosome 10 (human)[1] Band 10q24.2 Start 99,396,870 bp[1] End 99,430,624 bp[1]
Gene location (Mouse) Chr. Chromosome 19 (mouse)[2] Band 19 C3|19 36.67 cM Start 43,499,752 bp[2] End 43,524,605 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • L-aspartate:2-oxoglutarate aminotransferase activity • L-cysteine:2-oxoglutarate aminotransferase activity • transaminase activity • catalytic activity • carboxylic acid binding • L-phenylalanine:2-oxoglutarate aminotransferase activity • phosphatidylserine decarboxylase activity • pyridoxal phosphate binding Cellular component • cytoplasm • axon terminus • mitochondrion • lysosome • extracellular exosome • cell nucleus • nucleoplasm • cytosol Biological process • Notch signaling pathway • gluconeogenesis • dicarboxylic acid metabolic process • aspartate metabolic process • aspartate catabolic process • cellular amino acid metabolic process • response to glucocorticoid • cellular amino acid biosynthetic process • biosynthetic process • 2-oxoglutarate metabolic process • oxaloacetate metabolic process • glutamate catabolic process to 2-oxoglutarate • aspartate biosynthetic process • fatty acid homeostasis • cellular response to insulin stimulus • glutamate catabolic process to aspartate • glutamate metabolic process • glycerol biosynthetic process • response to carbohydrate • positive regulation of transforming growth factor beta receptor signaling pathway • negative regulation of collagen biosynthetic process • response to immobilization stress • response to cadmium ion • negative regulation of cytosolic calcium ion concentration • negative regulation of mitochondrial depolarization • transdifferentiation • cellular response to mechanical stimulus • response to transition metal nanoparticle Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
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 Mb	Chr 19: 43.5 – 43.52 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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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|{{{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. GRCh38: Ensembl release 89: ENSG00000120053 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000025190 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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. "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. doi:10.1042/bj2700651. 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. S2CID 30300621.
• 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. doi:10.4269/ajtmh.2004.71.125. 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. S2CID 21495180.
• 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.