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{{Infobox_gene}}
{{PBB_Controls
'''[[Aspartate aminotransferase]], cytoplasmic''' is an [[enzyme]] that in humans is encoded by the ''GOT1'' [[gene]].<ref name="pmid1974457">{{cite journal |vauthors=Bousquet-Lemercier B, Pol S, Pave-Preux M, Hanoune J, Barouki R | title = Properties of human liver cytosolic aspartate aminotransferase mRNAs generated by alternative polyadenylation site selection | journal = Biochemistry | volume = 29 | issue = 22 | pages = 5293–9 |date=Sep 1990 | pmid = 1974457 | pmc =  | doi =10.1021/bi00474a011 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: GOT1 glutamic-oxaloacetic transaminase 1, soluble (aspartate aminotransferase 1)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2805| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_GOT1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ajr.
| PDB = {{PDB2|1ajr}}, {{PDB2|1ajs}}
| Name = Glutamic-oxaloacetic transaminase 1, soluble (aspartate aminotransferase 1)
| HGNCid = 4432
| Symbol = GOT1
| AltSymbols =; GIG18
| OMIM = 138180
| ECnumber = 
| Homologene = 1571
| MGIid = 95791
| GeneAtlas_image1 = PBB_GE_GOT1_208813_at_tn.png
| Function = {{GNF_GO|id=GO:0004069 |text = aspartate transaminase activity}}
| Component = {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0006520 |text = amino acid metabolic process}} {{GNF_GO|id=GO:0006533 |text = aspartate catabolic process}} {{GNF_GO|id=GO:0009058 |text = biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2805
    | Hs_Ensembl = ENSG00000120053
    | Hs_RefseqProtein = NP_002070
    | Hs_RefseqmRNA = NM_002079
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 10
    | Hs_GenLoc_start = 101146648
    | Hs_GenLoc_end = 101180403
    | Hs_Uniprot = P17174
    | Mm_EntrezGene = 14718
    | Mm_Ensembl = ENSMUSG00000025190
    | Mm_RefseqmRNA = XM_994859
    | Mm_RefseqProtein = XP_999953
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 43553074
    | Mm_GenLoc_end = 43577820
    | Mm_Uniprot = Q3UJH8
  }}
}}
'''Glutamic-oxaloacetic transaminase 1, soluble (aspartate aminotransferase 1)''', also known as '''GOT1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GOT1 glutamic-oxaloacetic transaminase 1, soluble (aspartate aminotransferase 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2805| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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 cycle|urea]] and [[tricarboxylic acid cycle]]s. The two enzymes are homodimeric and show close homology.<ref name="entrez">{{cite web | title = Entrez Gene: GOT1 glutamic-oxaloacetic transaminase 1, soluble (aspartate aminotransferase 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2805| accessdate = }}</ref>
| summary_text = 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 cycle|urea]] and [[tricarboxylic acid cycle]]s. The two enzymes are homodimeric and show close homology.<ref name="entrez">{{cite web | title = Entrez Gene: GOT1 glutamic-oxaloacetic transaminase 1, soluble (aspartate aminotransferase 1)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2805| accessdate = }}</ref>
}}
}}
==Interactive pathway map==
{{GlycolysisGluconeogenesis_WP534|highlight=GOT1}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Panteghini M |title=Aspartate aminotransferase isoenzymes. |journal=Clin. Biochem. |volume=23 |issue= 4 |pages= 311-9 |year= 1990 |pmid= 2225456 |doi=  }}
*{{cite journal  | author=Panteghini M |title=Aspartate aminotransferase isoenzymes. |journal=Clin. Biochem. |volume=23 |issue= 4 |pages= 311–9 |year= 1990 |pmid= 2225456 |doi=10.1016/0009-9120(90)80062-N }}
*{{cite journal  | author=Doonan S, Barra D, Bossa F |title=Structural and genetic relationships between cytosolic and mitochondrial isoenzymes. |journal=Int. J. Biochem. |volume=16 |issue= 12 |pages= 1193-9 |year= 1985 |pmid= 6397370 |doi=  }}
*{{cite journal  |vauthors=Doonan S, Barra D, Bossa F |title=Structural and genetic relationships between cytosolic and mitochondrial isoenzymes. |journal=Int. J. Biochem. |volume=16 |issue= 12 |pages= 1193–9 |year= 1985 |pmid= 6397370 |doi=10.1016/0020-711X(84)90216-7 }}
*{{cite journal  | author=Kamei S, Ohkubo A, Yamanaka M |title=Apoenzyme of aspartate aminotransferase isozymes in serum and its diagnostic usefullness for hepatic diseases. |journal=Clin. Chim. Acta |volume=96 |issue= 1-2 |pages= 97-105 |year= 1979 |pmid= 225064 |doi= }}
*{{cite journal  |vauthors=Kamei S, Ohkubo A, Yamanaka M |title=Apoenzyme of aspartate aminotransferase isozymes in serum and its diagnostic usefullness for hepatic diseases. |journal=Clin. Chim. Acta |volume=96 |issue= 1–2 |pages= 97–105 |year= 1979 |pmid= 225064 |doi=10.1016/0009-8981(79)90058-5 }}
*{{cite journal  | author=Bousquet-Lemercier B, Pol S, Pavé-Preux M, ''et al.'' |title=Properties of human liver cytosolic aspartate aminotransferase mRNAs generated by alternative polyadenylation site selection. |journal=Biochemistry |volume=29 |issue= 22 |pages= 5293-9 |year= 1990 |pmid= 1974457 |doi= }}
*{{cite journal  |vauthors=Doyle JM, Schininà ME, Bossa F, Doonan S |title=The amino acid sequence of cytosolic aspartate aminotransferase from human liver. |journal=Biochem. J. |volume=270 |issue= 3 |pages= 651–7 |year= 1990 |pmid= 2241899 |doi= | pmc=1131781 }}
*{{cite journal  | author=Doyle JM, Schininà ME, Bossa F, Doonan S |title=The amino acid sequence of cytosolic aspartate aminotransferase from human liver. |journal=Biochem. J. |volume=270 |issue= 3 |pages= 651-7 |year= 1990 |pmid= 2241899 |doi=  }}
*{{cite journal  |vauthors=Pol S, Bousquet-Lemercier B, Pavé-Preux M |title=Chromosomal localization of human aspartate aminotransferase genes by in situ hybridization. |journal=Hum. Genet. |volume=83 |issue= 2 |pages= 159–64 |year= 1989 |pmid= 2777255 |doi=10.1007/BF00286710 |display-authors=etal}}
*{{cite journal  | author=Pol S, Bousquet-Lemercier B, Pavé-Preux M, ''et al.'' |title=Chromosomal localization of human aspartate aminotransferase genes by in situ hybridization. |journal=Hum. Genet. |volume=83 |issue= 2 |pages= 159-64 |year= 1989 |pmid= 2777255 |doi=  }}
*{{cite journal  |vauthors=Pol S, Bousquet-Lemercier B, Pave-Preux M |title=Nucleotide sequence and tissue distribution of the human mitochondrial aspartate aminotransferase mRNA. |journal=Biochem. Biophys. Res. Commun. |volume=157 |issue= 3 |pages= 1309–15 |year= 1989 |pmid= 3207426 |doi=10.1016/S0006-291X(88)81017-9 |display-authors=etal}}
*{{cite journal  | author=Pol S, Bousquet-Lemercier B, Pave-Preux M, ''et al.'' |title=Nucleotide sequence and tissue distribution of the human mitochondrial aspartate aminotransferase mRNA. |journal=Biochem. Biophys. Res. Commun. |volume=157 |issue= 3 |pages= 1309-15 |year= 1989 |pmid= 3207426 |doi=  }}
*{{cite journal  |vauthors=Andersson B, Wentland MA, Ricafrente JY |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107–13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 |display-authors=etal}}
*{{cite journal  | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal  |vauthors=Yu W, Andersson B, Worley KC |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353–8 |year= 1997 |pmid= 9110174 |doi=  10.1101/gr.7.4.353| pmc=139146  |display-authors=etal}}
*{{cite journal  | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi=  }}
*{{cite journal  |vauthors=Wang CY, Huang YQ, Shi JD |title=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. |journal=Am. J. Med. Genet. |volume=84 |issue= 5 |pages= 454–9 |year= 1999 |pmid= 10360399 |doi=10.1002/(SICI)1096-8628(19990611)84:5<454::AID-AJMG9>3.0.CO;2-D |display-authors=etal}}
*{{cite journal  | author=Wang CY, Huang YQ, Shi JD, ''et al.'' |title=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. |journal=Am. J. Med. Genet. |volume=84 |issue= 5 |pages= 454-9 |year= 1999 |pmid= 10360399 |doi=  }}
*{{cite journal  |vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  |vauthors=Miyake Y, Eguchi H, Shinchi K |title=Glucose intolerance and serum aminotransferase activities in Japanese men. |journal=J. Hepatol. |volume=38 |issue= 1 |pages= 18–23 |year= 2003 |pmid= 12480555 |doi=10.1016/S0168-8278(02)00323-9 |display-authors=etal}}
*{{cite journal  | author=Miyake Y, Eguchi H, Shinchi K, ''et al.'' |title=Glucose intolerance and serum aminotransferase activities in Japanese men. |journal=J. Hepatol. |volume=38 |issue= 1 |pages= 18-23 |year= 2003 |pmid= 12480555 |doi=  }}
*{{cite journal  |vauthors=Deloukas P, Earthrowl ME, Grafham DV |title=The DNA sequence and comparative analysis of human chromosome 10. |journal=Nature |volume=429 |issue= 6990 |pages= 375–81 |year= 2004 |pmid= 15164054 |doi= 10.1038/nature02462 |display-authors=etal}}
*{{cite journal  | author=Deloukas P, Earthrowl ME, Grafham DV, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 10. |journal=Nature |volume=429 |issue= 6990 |pages= 375-81 |year= 2004 |pmid= 15164054 |doi= 10.1038/nature02462 }}
*{{cite journal  |vauthors=Wu KL, Lu SN, Changchien CS |title=Sequential changes of serum aminotransferase levels in patients with severe acute respiratory syndrome. |journal=Am. J. Trop. Med. Hyg. |volume=71 |issue= 2 |pages= 125–8 |year= 2004 |pmid= 15306699 |doi=  |display-authors=etal}}
*{{cite journal  | author=Wu KL, Lu SN, Changchien CS, ''et al.'' |title=Sequential changes of serum aminotransferase levels in patients with severe acute respiratory syndrome. |journal=Am. J. Trop. Med. Hyg. |volume=71 |issue= 2 |pages= 125-8 |year= 2004 |pmid= 15306699 |doi=  }}
*{{cite journal  |vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  |vauthors=Totan A, Greabu M, Totan C, Spinu T |title=Salivary aspartate aminotransferase, alanine aminotransferase and alkaline phosphatase: possible markers in periodontal diseases? |journal=Clin. Chem. Lab. Med. |volume=44 |issue= 5 |pages= 612–5 |year= 2006 |pmid= 16681433 |doi= 10.1515/CCLM.2006.096 }}
*{{cite journal  | author=Totan A, Greabu M, Totan C, Spinu T |title=Salivary aspartate aminotransferase, alanine aminotransferase and alkaline phosphatase: possible markers in periodontal diseases? |journal=Clin. Chem. Lab. Med. |volume=44 |issue= 5 |pages= 612-5 |year= 2006 |pmid= 16681433 |doi= 10.1515/CCLM.2006.096 }}
*{{cite journal  |vauthors=Dubern B, Girardet JP, Tounian P |title=Insulin resistance and ferritin as major determinants of abnormal serum aminotransferase in severely obese children. |journal=International Journal of Pediatric Obesity |volume=1 |issue= 2 |pages= 77–82 |year= 2007 |pmid= 17907318 |doi=  10.1080/17477160600569594}}
*{{cite journal  | author=Dubern B, Girardet JP, Tounian P |title=Insulin resistance and ferritin as major determinants of abnormal serum aminotransferase in severely obese children. |journal=International journal of pediatric obesity : IJPO : an official journal of the International Association for the Study of Obesity |volume=1 |issue= 2 |pages= 77-82 |year= 2007 |pmid= 17907318 |doi=  }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=2805}}
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{{Transaminases}}


{{protein-stub}}
{{gene-10-stub}}
{{WikiDoc Sources}}

Latest revision as of 08:55, 31 August 2017

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Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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Wikidata
View/Edit Human

Aspartate aminotransferase, cytoplasmic is an enzyme that in humans is encoded by the GOT1 gene.[1][2]

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.[2]

Interactive pathway map

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

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<imagemap> Image:WP534.png
|{{{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. ↑ 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.
  2. ↑ 2.0 2.1 "Entrez Gene: GOT1 glutamic-oxaloacetic transaminase 1, soluble (aspartate aminotransferase 1)".

Further reading



Retrieved from "https://www.wikidoc.org/index.php?title=GOT1&oldid=1414346"