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GOT1

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

GOT1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
3II0, 3WZF

Identifiers

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]
Band	10q24.2	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]
Band	19 C3\|19 36.67 cM	End	43,513,044 bp^[2]

RNA expression pattern

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

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


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

Species

Human

Mouse


2805


14718


ENSG00000120053


ENSMUSG00000025190


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]

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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|alt=Glycolysis and Gluconeogenesis edit]]

Glycolysis and Gluconeogenesis edit

^ The interactive pathway map can be edited at WikiPathways: "GlycolysisGluconeogenesis_WP534".

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000120053 – Ensembl, May 2017

^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000025190 – Ensembl, May 2017

^ "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.

^ 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.

^ ^a ^b "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.

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