GOT1

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; OMA:GOT1 - orthologs
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 43,488,191 bp [2] End 43,513,044 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right ventricle myocardium of left ventricle apex of heart cardiac muscle tissue of right atrium body of tongue right auricle of heart vastus lateralis muscle muscle of thigh Skeletal muscle tissue of rectus abdominis prefrontal cortex Top expressed in extraocular muscle right ventricle digastric muscle myocardium of ventricle medial vestibular nucleus temporal muscle sternocleidomastoid muscle pontine nuclei cardiac muscles deep cerebellar nuclei More reference expression data BioGPS 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 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 biosynthesis 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: 43.49 – 43.51 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/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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|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 [sic] 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2004Natur.429..375D. 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.