Got2 (glutamic-oxaloacetic transaminase 2) - Rat Genome Database

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Gene: Got2 (glutamic-oxaloacetic transaminase 2) Rattus norvegicus
Symbol: Got2
Name: glutamic-oxaloacetic transaminase 2
RGD ID: 2722
Description: Enables several functions, including L-aspartate:2-oxoglutarate aminotransferase activity; anion binding activity; and identical protein binding activity. Involved in several processes, including dicarboxylic acid metabolic process; lactation; and response to insulin. Located in several cellular components, including T-tubule; mitochondrial inner membrane; and perikaryon. Part of protein-containing complex. Biomarker of acute kidney failure; neurodegenerative disease; obesity; and schizophrenia. Human ortholog(s) of this gene implicated in developmental and epileptic encephalopathy 82. Orthologous to human GOT2 (glutamic-oxaloacetic transaminase 2); PARTICIPATES IN gluconeogenesis pathway; 2-hydroxyglutaric aciduria pathway; argininosuccinic aciduria pathway; INTERACTS WITH 2,2',4,4',5,5'-hexachlorobiphenyl; 2,2,2-tetramine; 2,3,7,8-tetrachlorodibenzodioxine.
Type: protein-coding
RefSeq Status: VALIDATED
Previously known as: aspartate aminotransferase; aspartate aminotransferase, mitochondrial; ASPATA; FABP-1; FABPpm; fatty acid-binding protein; glutamate oxaloacetate transaminase 2; Glutamate oxaloacetate transaminase 2 mitochondrial (aspartate aminotransferase 2); glutamate oxaloacetate transaminase 2, mitochondrial; Glutamate oxaloacetate transaminase 2, mitochondrial (aspartate aminotransferase 2); glutamic-oxaloacetic transaminase 2, mitochondrial; glutamic-oxaloacetic transaminase 2, mitochondrial (aspartate aminotransferase 2); kynurenine aminotransferase 4; kynurenine aminotransferase IV; kynurenine--oxoglutarate transaminase 4; kynurenine--oxoglutarate transaminase IV; mAAT; mAspAT; plasma membrane-associated fatty acid-binding protein; transaminase A
RGD Orthologs
Green Monkey
Naked Mole-Rat
Alliance Genes
More Info more info ...
Latest Assembly: mRatBN7.2 - mRatBN7.2 Assembly
Rat AssemblyChrPosition (strand)SourceGenome Browsers
mRatBN7.2199,174,304 - 9,199,995 (+)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl199,174,311 - 9,199,994 (+)EnsemblmRatBN7.2 Ensembl
UTH_Rnor_SHR_Utx199,143,186 - 9,168,707 (+)NCBIRnor_SHRUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.0199,910,004 - 9,935,525 (+)NCBIRnor_SHRSPUTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.0199,196,308 - 9,221,830 (+)NCBIRnor_WKYUTH_Rnor_WKY_Bbb_1.0
Rnor_6.0199,587,637 - 9,613,323 (+)NCBIRnor6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 Ensembl199,587,653 - 9,613,340 (+)EnsemblRnor6.0rn6Rnor6.0
Rnor_5.0199,572,757 - 9,598,443 (+)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
RGSC_v3.4199,629,687 - 9,655,336 (+)NCBIRGSC3.4RGSC_v3.4rn4RGSC3.4
RGSC_v3.1199,634,512 - 9,660,162 (+)NCBI
Celera199,072,871 - 9,098,515 (+)NCBICelera
RH 3.4 Map1972.43RGD
Cytogenetic Map19p13NCBI
JBrowse: View Region in Genome Browser (JBrowse)

Gene-Chemical Interaction Annotations     Click to see Annotation Detail View
(-)-epigallocatechin 3-gallate  (ISO)
1,2-dimethylhydrazine  (ISO)
17alpha-ethynylestradiol  (ISO)
17beta-hydroxy-17-methylestra-4,9,11-trien-3-one  (ISO)
2,2',4,4',5,5'-hexachlorobiphenyl  (EXP,ISO)
2,2,2-tetramine  (EXP)
2,3,7,8-tetrachlorodibenzodioxine  (EXP,ISO)
2,4,6-trinitrobenzenesulfonic acid  (EXP)
3,3',4,4',5-pentachlorobiphenyl  (ISO)
4,4'-diaminodiphenylmethane  (EXP)
4,4'-sulfonyldiphenol  (ISO)
4-hydroxynon-2-enal  (ISO)
4-hydroxyphenyl retinamide  (ISO)
acrolein  (ISO)
acrylamide  (EXP)
all-trans-retinoic acid  (ISO)
Allylamine  (EXP)
alpha-pinene  (ISO)
amiodarone  (EXP)
amitriptyline  (EXP)
ammonium chloride  (EXP)
aniline  (EXP)
aristolochic acid A  (ISO)
arsane  (ISO)
arsenic atom  (ISO)
arsenite(3-)  (ISO)
arsenous acid  (ISO)
atrazine  (ISO)
benazepril  (EXP)
benzatropine  (ISO)
benzo[a]pyrene  (ISO)
bis(2-ethylhexyl) phthalate  (ISO)
bisphenol A  (EXP,ISO)
Bisphenol B  (ISO)
bisphenol F  (ISO)
Brodifacoum  (EXP)
C60 fullerene  (EXP)
cadmium dichloride  (ISO)
caffeine  (ISO)
cannabidiol  (ISO)
chlordecone  (ISO)
cisplatin  (EXP)
clomipramine  (EXP)
clozapine  (EXP,ISO)
cobalt dichloride  (ISO)
corn oil  (EXP)
Cuprizon  (ISO)
cyclosporin A  (ISO)
cypermethrin  (EXP)
dexamethasone  (ISO)
diarsenic trioxide  (ISO)
dibutyl phthalate  (EXP)
dicrotophos  (ISO)
diethyl maleate  (EXP)
diuron  (EXP)
doxorubicin  (ISO)
enzyme inhibitor  (ISO)
ethanol  (EXP,ISO)
febuxostat  (ISO)
fenofibrate  (EXP)
flavonoids  (EXP)
folic acid  (ISO)
fulvestrant  (ISO)
genistein  (ISO)
gentamycin  (EXP)
gold atom  (ISO)
gold(0)  (ISO)
haloperidol  (EXP,ISO)
hydrazine  (ISO)
hydroxyurea  (ISO)
imipramine  (EXP)
isoprenaline  (EXP)
ivermectin  (ISO)
ketoconazole  (EXP)
lead diacetate  (EXP)
lithium atom  (EXP)
lithium hydride  (EXP)
methamphetamine  (EXP)
mono(2-ethylhexyl) phthalate  (EXP)
niclosamide  (ISO)
nitrofen  (EXP)
ozone  (ISO)
p-toluidine  (EXP)
paracetamol  (ISO)
paraquat  (ISO)
permethrin  (EXP)
pirinixic acid  (ISO)
Propiverine  (EXP)
rotenone  (EXP)
sodium arsenite  (EXP,ISO)
sodium fluoride  (EXP,ISO)
streptozocin  (EXP)
sulfur dioxide  (EXP)
tetrachloromethane  (ISO)
thapsigargin  (ISO)
thioacetamide  (EXP)
topiramate  (EXP)
trimellitic anhydride  (ISO)
tunicamycin  (ISO)
valproic acid  (EXP,ISO)
vinclozolin  (EXP)
zearalenone  (ISO)
zinc atom  (ISO)
zinc(0)  (ISO)

Gene Ontology Annotations     Click to see Annotation Detail View

Cellular Component


References - curated
# Reference Title Reference Citation
1. Evidence that stimulation of gluconeogenesis by fatty acid is mediated through thermodynamic mechanisms. Berry MN, etal., FEBS Lett. 1988 Apr 11;231(1):19-24.
2. Acute endurance exercise increases plasma membrane fatty acid transport proteins in rat and human skeletal muscle. Bradley NS, etal., Am J Physiol Endocrinol Metab. 2012 Jan 15;302(2):E183-9. doi: 10.1152/ajpendo.00254.2011. Epub 2011 Oct 25.
3. Immunogold localization of mitochondrial aspartate aminotransferase in mitochondria and on the cell surface in normal rat tissues. Cechetto JD, etal., Histol Histopathol 2002 Apr;17(2):353-64.
4. Possible mechanism for the decrease of mitochondrial aspartate aminotransferase activity in ischemic and hypoxic rat retinas. Endo S, etal., Biochim Biophys Acta. 1999 Jul 8;1450(3):385-96.
5. Regulation of aminotransferase-glutamate dehydrogenase interactions by carbamyl phosphate synthase-I, Mg2+ plus leucine versus citrate and malate. Fahien LA, etal., J Biol Chem. 1985 May 25;260(10):6069-79.
6. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Gaudet P, etal., Brief Bioinform. 2011 Sep;12(5):449-62. doi: 10.1093/bib/bbr042. Epub 2011 Aug 27.
7. Rat ISS GO annotations from GOA human gene data--August 2006 GOA data from the GO Consortium
8. Structure, expression, and function of kynurenine aminotransferases in human and rodent brains. Han Q, etal., Cell Mol Life Sci. 2010 Feb;67(3):353-68. doi: 10.1007/s00018-009-0166-4. Epub 2009 Oct 15.
9. Dose-dependent effect of sulfur dioxide on brain damage induced by recurrent febrile seizures in rats. Han Y, etal., Neurosci Lett. 2014 Mar 20;563:149-54. doi: 10.1016/j.neulet.2013.12.042. Epub 2013 Dec 25.
10. Glutamate-synthesizing enzymes in GABAergic neurons of the neocortex: a double immunofluorescence study in the rat. Kaneko T and Mizuno N, Neuroscience. 1994 Aug;61(4):839-49.
11. KEGG: Kyoto Encyclopedia of Genes and Genomes KEGG
12. High-density rat radiation hybrid maps containing over 24,000 SSLPs, genes, and ESTs provide a direct link to the rat genome sequence. Kwitek AE, etal., Genome Res. 2004 Apr;14(4):750-7
13. Molecular cloning and in vivo expression of a precursor to rat mitochondrial aspartate aminotransferase. Mattingly JR Jr, etal., Biochem Biophys Res Commun 1987 Dec 31;149(3):859-65.
14. Neuronal and astrocytic shuttle mechanisms for cytosolic-mitochondrial transfer of reducing equivalents: current evidence and pharmacological tools. McKenna MC, etal., Biochem Pharmacol. 2006 Feb 14;71(4):399-407. Epub 2005 Dec 20.
15. Rat ISS GO annotations from MGI mouse gene data--August 2006 MGD data from the GO Consortium
16. Differential Neuroproteomic and Systems Biology Analysis of Spinal Cord Injury. Moghieb A, etal., Mol Cell Proteomics. 2016 Jul;15(7):2379-95. doi: 10.1074/mcp.M116.058115. Epub 2016 May 5.
17. Electronic Transfer of LocusLink and RefSeq Data NCBI rat LocusLink and RefSeq merged data July 26, 2002
18. The nature of the rate-limiting steps in the refolding of the cofactor-dependent protein aspartate aminotransferase. Oses-Prieto JA, etal., J Biol Chem. 2003 Dec 12;278(50):49988-99. Epub 2003 Sep 30.
19. Cisplatin binding and inactivation of mitochondrial glutamate oxaloacetate transaminase in cisplatin-induced rat nephrotoxicity. Ozaki T, etal., Biosci Biotechnol Biochem. 2013;77(8):1645-9. doi: 10.1271/bbb.130172. Epub 2013 Aug 7.
20. Nucleotide sequence and glucocorticoid regulation of the mRNAs for the isoenzymes of rat aspartate aminotransferase. Pave-Preux M, etal., J Biol Chem 1988 Nov 25;263(33):17459-66.
21. KEGG Annotation Import Pipeline Pipeline to import KEGG annotations from KEGG into RGD
22. SMPDB Annotation Import Pipeline Pipeline to import SMPDB annotations from SMPDB into RGD
23. Regulation of 2-oxoglutarate metabolism in rat liver by NADP-isocitrate dehydrogenase and aspartate aminotransferase. Rakhmanova TI and Popova TN, Biochemistry (Mosc). 2006 Feb;71(2):211-7.
24. GOA pipeline RGD automated data pipeline
25. ClinVar Automated Import and Annotation Pipeline RGD automated import pipeline for ClinVar variants, variant-to-disease annotations and gene-to-disease annotations
26. Data Import for Chemical-Gene Interactions RGD automated import pipeline for gene-chemical interactions
27. The effect of gestational age on expression of genes involved in uptake, trafficking and synthesis of fatty acids in the rat placenta. Rodríguez-Cruz M, etal., Gene. 2016 Oct 15;591(2):403-10. doi: 10.1016/j.gene.2016.06.034. Epub 2016 Jun 16.
28. Fatty acid transport proteins chronically relocate to the transverse-tubules in muscle from obese Zucker rats but are resistant to further insulin-induced translocation. Stefanyk LE, etal., Metabolism. 2013 Sep;62(9):1296-304. doi: 10.1016/j.metabol.2013.04.015. Epub 2013 Jun 3.
29. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Strausberg RL, etal., Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11.
30. Effects of sulfur dioxide on hypoxic pulmonary vascular structural remodeling. Sun Y, etal., Lab Invest. 2010 Jan;90(1):68-82. Epub 2009 Oct 12.
31. Proteomic analysis of post-nuclear supernatant fraction and percoll-purified membranes prepared from brain cortex of rats exposed to increasing doses of morphine. Ujcikova H, etal., Proteome Sci. 2014 Feb 14;12(1):11. doi: 10.1186/1477-5956-12-11.
32. Proteomic analysis for early neurodegenerative biomarker detection in an animal model. Vincenzetti S, etal., Biochimie. 2016 Feb;121:79-86. doi: 10.1016/j.biochi.2015.11.026. Epub 2015 Nov 26.
33. A combined metabonomic and proteomic approach identifies frontal cortex changes in a chronic phencyclidine rat model in relation to human schizophrenia brain pathology. Wesseling H, etal., Neuropsychopharmacology. 2013 Nov;38(12):2532-44. doi: 10.1038/npp.2013.160. Epub 2013 Jul 3.
34. Release of pyridoxal 5'-phosphate upon unfolding of mitochondrial aspartate aminotransferase. Wu TH, etal., Biochim Biophys Acta. 2003 Apr 11;1647(1-2):315-20.
35. Effects of heme oxygenase-1-modified bone marrow mesenchymal stem cells on microcirculation and energy metabolism following liver transplantation. Yang L, etal., World J Gastroenterol. 2017 May 21;23(19):3449-3467. doi: 10.3748/wjg.v23.i19.3449.
36. NAD+/NADH and NADP+/NADPH in cellular functions and cell death: regulation and biological consequences. Ying W Antioxid Redox Signal. 2008 Feb;10(2):179-206.
37. Change in the Lipid Transport Capacity of the Liver and Blood during Reproduction in Rats. Zhang Y, etal., Front Physiol. 2017 Jul 26;8:517. doi: 10.3389/fphys.2017.00517. eCollection 2017.
Additional References at PubMed
PMID:869894   PMID:1180875   PMID:1820020   PMID:2139228   PMID:2182221   PMID:2567216   PMID:2571576   PMID:2731362   PMID:3004464   PMID:4052435   PMID:4193185   PMID:7309704  
PMID:7470110   PMID:7759512   PMID:8274135   PMID:9537447   PMID:12865426   PMID:14651853   PMID:14701727   PMID:15489334   PMID:17634366   PMID:18614015   PMID:19142713   PMID:20458337  
PMID:20733562   PMID:20833797   PMID:22206666   PMID:22681889   PMID:23376485   PMID:23533145   PMID:26316108   PMID:29476059   PMID:31473978  


Comparative Map Data
(Rattus norvegicus - Norway rat)
Rat AssemblyChrPosition (strand)SourceGenome Browsers
mRatBN7.2199,174,304 - 9,199,995 (+)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl199,174,311 - 9,199,994 (+)EnsemblmRatBN7.2 Ensembl
UTH_Rnor_SHR_Utx199,143,186 - 9,168,707 (+)NCBIRnor_SHRUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.0199,910,004 - 9,935,525 (+)NCBIRnor_SHRSPUTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.0199,196,308 - 9,221,830 (+)NCBIRnor_WKYUTH_Rnor_WKY_Bbb_1.0
Rnor_6.0199,587,637 - 9,613,323 (+)NCBIRnor6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 Ensembl199,587,653 - 9,613,340 (+)EnsemblRnor6.0rn6Rnor6.0
Rnor_5.0199,572,757 - 9,598,443 (+)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
RGSC_v3.4199,629,687 - 9,655,336 (+)NCBIRGSC3.4RGSC_v3.4rn4RGSC3.4
RGSC_v3.1199,634,512 - 9,660,162 (+)NCBI
Celera199,072,871 - 9,098,515 (+)NCBICelera
RH 3.4 Map1972.43RGD
Cytogenetic Map19p13NCBI
(Homo sapiens - human)
Human AssemblyChrPosition (strand)SourceGenome Browsers
GRCh381658,707,131 - 58,734,316 (-)NCBIGRCh38GRCh38hg38GRCh38
GRCh38.p14 Ensembl1658,707,131 - 58,734,342 (-)EnsemblGRCh38hg38GRCh38
GRCh371658,741,035 - 58,768,220 (-)NCBIGRCh37GRCh37hg19GRCh37
Build 361657,298,536 - 57,325,747 (-)NCBINCBI36Build 36hg18NCBI36
Build 341657,298,537 - 57,325,641NCBI
Celera1643,241,839 - 43,268,969 (-)NCBICelera
Cytogenetic Map16q21NCBI
HuRef1644,606,528 - 44,633,785 (-)NCBIHuRef
CHM1_11660,147,934 - 60,175,160 (-)NCBICHM1_1
T2T-CHM13v2.01664,499,639 - 64,526,824 (-)NCBIT2T-CHM13v2.0
(Mus musculus - house mouse)
Mouse AssemblyChrPosition (strand)SourceGenome Browsers
GRCm39896,590,761 - 96,615,029 (-)NCBIGRCm39GRCm39mm39
GRCm39 Ensembl896,590,762 - 96,615,175 (-)EnsemblGRCm39 Ensembl
GRCm38895,864,133 - 95,888,401 (-)NCBIGRCm38GRCm38mm10GRCm38
GRCm38.p6 Ensembl895,864,134 - 95,888,547 (-)EnsemblGRCm38mm10GRCm38
MGSCv37898,388,037 - 98,412,265 (-)NCBIGRCm37MGSCv37mm9NCBIm37
MGSCv36898,753,266 - 98,777,494 (-)NCBIMGSCv36mm8
Celera8100,174,831 - 100,199,164 (-)NCBICelera
Cytogenetic Map8D1NCBI
cM Map847.79NCBI
(Chinchilla lanigera - long-tailed chinchilla)
Chinchilla AssemblyChrPosition (strand)SourceGenome Browsers
ChiLan1.0 EnsemblNW_00495543316,122,824 - 16,145,113 (-)EnsemblChiLan1.0
ChiLan1.0NW_00495543316,121,795 - 16,145,129 (-)NCBIChiLan1.0ChiLan1.0
(Pan paniscus - bonobo/pygmy chimpanzee)
Bonobo AssemblyChrPosition (strand)SourceGenome Browsers
NHGRI_mPanPan11674,113,908 - 74,140,940 (-)NCBINHGRI_mPanPan1
Mhudiblu_PPA_v01638,995,770 - 39,022,750 (-)NCBIMhudiblu_PPA_v0Mhudiblu_PPA_v0panPan3
PanPan1.11658,120,781 - 58,147,378 (-)NCBIpanpan1.1PanPan1.1panPan2
PanPan1.1 Ensembl1658,120,781 - 58,147,378 (-)Ensemblpanpan1.1panPan2
(Canis lupus familiaris - dog)
Dog AssemblyChrPosition (strand)SourceGenome Browsers
CanFam3.1257,968,833 - 57,994,219 (+)NCBICanFam3.1CanFam3.1canFam3CanFam3.1
CanFam3.1 Ensembl257,968,833 - 57,994,218 (+)EnsemblCanFam3.1canFam3CanFam3.1
Dog10K_Boxer_Tasha254,600,250 - 54,625,432 (+)NCBIDog10K_Boxer_Tasha
ROS_Cfam_1.0258,509,907 - 58,535,139 (+)NCBIROS_Cfam_1.0
ROS_Cfam_1.0 Ensembl258,509,974 - 58,535,138 (+)EnsemblROS_Cfam_1.0 Ensembl
UMICH_Zoey_3.1255,357,609 - 55,362,222 (+)NCBIUMICH_Zoey_3.1
UNSW_CanFamBas_1.0256,341,620 - 56,366,972 (+)NCBIUNSW_CanFamBas_1.0
UU_Cfam_GSD_1.0257,239,528 - 57,264,732 (+)NCBIUU_Cfam_GSD_1.0
(Sus scrofa - pig)
Pig AssemblyChrPosition (strand)SourceGenome Browsers
Sscrofa11.1 Ensembl620,407,200 - 20,432,067 (-)EnsemblSscrofa11.1susScr11Sscrofa11.1
Sscrofa11.1620,407,203 - 20,431,849 (-)NCBISscrofa11.1Sscrofa11.1susScr11Sscrofa11.1
Sscrofa10.2618,502,171 - 18,527,683 (-)NCBISscrofa10.2Sscrofa10.2susScr3
(Chlorocebus sabaeus - green monkey)
Green Monkey AssemblyChrPosition (strand)SourceGenome Browsers
ChlSab1.1544,645,721 - 44,670,917 (-)NCBIChlSab1.1ChlSab1.1chlSab2
ChlSab1.1 Ensembl544,645,602 - 44,670,918 (-)EnsemblChlSab1.1ChlSab1.1 EnsemblchlSab2
Vero_WHO_p1.0NW_02366604731,493,979 - 31,519,503 (+)NCBIVero_WHO_p1.0Vero_WHO_p1.0
(Heterocephalus glaber - naked mole-rat)
Naked Mole-Rat AssemblyChrPosition (strand)SourceGenome Browsers
HetGla_female_1.0 EnsemblNW_00462474627,558,005 - 27,586,257 (+)EnsemblHetGla_female_1.0HetGla_female_1.0 EnsemblhetGla2
HetGla 1.0NW_00462474627,557,994 - 27,586,257 (+)NCBIHetGla_female_1.0HetGla 1.0hetGla2


Variants in Got2
175 total Variants
miRNA Target Status

Predicted Target Of
Summary Value
Count of predictions:107
Count of miRNA genes:90
Interacting mature miRNAs:97
Prediction methods:Miranda, Rnahybrid
Result types:miRGate_prediction

The detailed report is available here: Full Report CSV TAB Printer

miRNA Target Status data imported from miRGate (
For more information about miRGate, see PMID:25858286 or access the full paper here.

QTLs in Region (mRatBN7.2)
The following QTLs overlap with this region.    Full Report CSV TAB Printer Gviewer
RGD IDSymbolNameLODP ValueTraitSub TraitChrStartStopSpecies
7411590Foco7Food consumption QTL 76.80.001eating behavior trait (VT:0001431)feed conversion ratio (CMO:0001312)19124688055Rat
10054132Srcrt9Stress Responsive Cort QTL 92.870.0017blood corticosterone amount (VT:0005345)plasma corticosterone level (CMO:0001173)19127355345Rat
631678Cm9Cardiac mass QTL 94.270.0001aorta mass (VT:0002845)aorta weight (CMO:0000076)19128982497Rat
631681Cm12Cardiac mass QTL 123.330.00053heart left ventricle mass (VT:0007031)heart left ventricle weight to body weight ratio (CMO:0000530)19128982497Rat
1549847Bss8Bone structure and strength QTL 84lumbar vertebra strength trait (VT:0010574)vertebra ultimate force (CMO:0001678)19131963836Rat
9590298Uminl5Urine mineral level QTL 53.590.001urine mineral amount (VT:0015086)urine electrolyte level (CMO:0000593)19136824771Rat
8552935Pigfal10Plasma insulin-like growth factor 1 level QTL 105.7blood insulin-like growth factor amount (VT:0010479)plasma insulin-like growth factor 1 level (CMO:0001299)19136824771Rat
9590250Scort11Serum corticosterone level QTL 1123.450.001blood corticosterone amount (VT:0005345)plasma corticosterone level (CMO:0001173)19136824771Rat
9590090Insglur8Insulin/glucose ratio QTL 810.810.001blood insulin amount (VT:0001560)calculated plasma insulin level (CMO:0002170)19136824771Rat
9589102Slep13Serum leptin concentration QTL 134.630.001blood leptin amount (VT:0005667)plasma leptin level (CMO:0000781)1956937445569374Rat
8694186Bw152Body weight QTL 1523.340.001body mass (VT:0001259)body weight gain (CMO:0000420)1956937445569374Rat
7247442Uae39Urinary albumin excretion QTL 39urine albumin amount (VT:0002871)urine albumin excretion rate (CMO:0000757)19218792746708701Rat
724566Uae12Urinary albumin excretion QTL 125urine albumin amount (VT:0002871)urine albumin level (CMO:0000130)19218792756457239Rat
61447Tcas1Tongue tumor susceptibility QTL 16.08tongue integrity trait (VT:0010553)squamous cell carcinoma of the tongue maximum tumor diameter (CMO:0001875)19231612147316121Rat
2317848Alcrsp21Alcohol response QTL 211.8999999761581420.05response to alcohol trait (VT:0010489)duration of loss of righting reflex (CMO:0002289)19320477748204777Rat
1331737Uae29Urinary albumin excretion QTL 295.5urine albumin amount (VT:0002871)urine albumin level (CMO:0000130)19409615555283277Rat
724518Uae19Urinary albumin excretion QTL 195.5urine albumin amount (VT:0002871)urine albumin excretion rate (CMO:0000757)19745724942983518Rat

Markers in Region
Rat AssemblyChrPosition (strand)SourceJBrowse
Cytogenetic Map19p13UniSTS
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2199,175,476 - 9,175,662 (+)MAPPERmRatBN7.2
Rnor_6.0199,588,810 - 9,588,995NCBIRnor6.0
Rnor_5.0199,573,930 - 9,574,115UniSTSRnor5.0
RGSC_v3.4199,630,826 - 9,631,011UniSTSRGSC3.4
Celera199,074,044 - 9,074,229UniSTS
RH 3.4 Map1972.63UniSTS
Cytogenetic Map19p13UniSTS
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2199,199,121 - 9,199,286 (+)MAPPERmRatBN7.2
mRatBN7.2X60,551,447 - 60,551,612 (+)MAPPERmRatBN7.2
Rnor_6.0X64,913,692 - 64,913,856NCBIRnor6.0
Rnor_6.0199,612,450 - 9,612,614NCBIRnor6.0
Rnor_5.0199,597,570 - 9,597,734UniSTSRnor5.0
Rnor_5.0X68,188,419 - 68,188,583UniSTSRnor5.0
RGSC_v3.4X83,244,343 - 83,244,507UniSTSRGSC3.4
RGSC_v3.4199,654,465 - 9,654,629UniSTSRGSC3.4
Celera199,097,642 - 9,097,806UniSTS
CeleraX60,969,715 - 60,969,879UniSTS
RH 3.4 Map1972.43UniSTS
Cytogenetic Map19p13UniSTS
Cytogenetic MapXq31UniSTS
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2199,193,738 - 9,193,819 (+)MAPPERmRatBN7.2
Rnor_6.0199,607,067 - 9,607,147NCBIRnor6.0
Rnor_5.0199,592,187 - 9,592,267UniSTSRnor5.0
RGSC_v3.4199,649,082 - 9,649,162UniSTSRGSC3.4
Celera199,092,258 - 9,092,338UniSTS
Cytogenetic Map19p13UniSTS


RNA-SEQ Expression
High: > 1000 TPM value   Medium: Between 11 and 1000 TPM
Low: Between 0.5 and 10 TPM   Below Cutoff: < 0.5 TPM

alimentary part of gastrointestinal system circulatory system endocrine system exocrine system hemolymphoid system hepatobiliary system integumental system musculoskeletal system nervous system renal system reproductive system respiratory system appendage
Medium 3 43 57 41 19 41 8 11 74 35 40 11 8
Low 1
Below cutoff


RefSeq Acc Id: ENSRNOT00000015956   ⟹   ENSRNOP00000015956
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl199,174,318 - 9,199,994 (+)Ensembl
Rnor_6.0 Ensembl199,587,653 - 9,613,340 (+)Ensembl
RefSeq Acc Id: ENSRNOT00000101698   ⟹   ENSRNOP00000096145
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl199,174,311 - 9,199,682 (+)Ensembl
RefSeq Acc Id: NM_013177   ⟹   NP_037309
RefSeq Status: VALIDATED
Rat AssemblyChrPosition (strand)Source
mRatBN7.2199,174,304 - 9,199,995 (+)NCBI
Rnor_6.0199,587,637 - 9,613,323 (+)NCBI
Rnor_5.0199,572,757 - 9,598,443 (+)NCBI
RGSC_v3.4199,629,687 - 9,655,336 (+)RGD
Celera199,072,871 - 9,098,515 (+)NCBI
RefSeq Acc Id: NP_037309   ⟸   NM_013177
- UniProtKB: Q64551 (UniProtKB/Swiss-Prot),   Q9QV50 (UniProtKB/Swiss-Prot),   P00507 (UniProtKB/Swiss-Prot),   A6JXY8 (UniProtKB/TrEMBL),   A0A8L2Q7Q0 (UniProtKB/TrEMBL)
- Sequence:
RefSeq Acc Id: ENSRNOP00000015956   ⟸   ENSRNOT00000015956
RefSeq Acc Id: ENSRNOP00000096145   ⟸   ENSRNOT00000101698
Protein Structures
Name Modeler Protein Id AA Range Protein Structure
AF-P00507-F1-model_v2 AlphaFold P00507 1-430 view protein structure


eQTL   View at Phenogen
WGCNA   View at Phenogen
Tissue/Strain Expression   View at Phenogen

Additional Information

Database Acc Id Source(s)
AGR Gene RGD:2722 AgrOrtholog
BioCyc Gene G2FUF-6555 BioCyc
BioCyc Pathway ASPARAGINE-DEG1-PWY-1 [L-asparagine degradation III (mammalian)] BioCyc
  ASPARTATE-DEG1-PWY [L-aspartate degradation I] BioCyc
  ASPARTATESYN-PWY [L-aspartate biosynthesis] BioCyc
  MALATE-ASPARTATE-SHUTTLE-PWY [malate/L-aspartate shuttle pathway] BioCyc
  PWY-5886 [3-(4-hydroxyphenyl)pyruvate biosynthesis] BioCyc
  PWY-6318 [L-phenylalanine degradation IV (mammalian, via side chain)] BioCyc
  TYRFUMCAT-PWY [L-tyrosine degradation I] BioCyc
Ensembl Genes ENSRNOG00000011782 Ensembl, ENTREZGENE, UniProtKB/TrEMBL
Ensembl Protein ENSRNOP00000015956 ENTREZGENE
  ENSRNOP00000015956.4 UniProtKB/TrEMBL
  ENSRNOP00000096145.1 UniProtKB/TrEMBL
Ensembl Transcript ENSRNOT00000015956 ENTREZGENE
  ENSRNOT00000015956.7 UniProtKB/TrEMBL
  ENSRNOT00000101698.1 UniProtKB/TrEMBL
Gene3D-CATH 3.40.640.10 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  3.90.1150.10 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
InterPro Aminotransferase_I/II UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Asp_trans UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  NHTrfase_class1_PyrdxlP-BS UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  PyrdxlP-dep_Trfase UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  PyrdxlP-dep_Trfase_dom1 UniProtKB/Swiss-Prot
  PyrdxlP-dep_Trfase_major UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  PyrdxlP-dep_Trfase_small UniProtKB/TrEMBL
KEGG Report rno:25721 UniProtKB/Swiss-Prot
  PTHR11879 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
Pfam Aminotran_1_2 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
PhenoGen Got2 PhenoGen
Superfamily-SCOP SSF53383 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
UniProt Secondary Q64551 UniProtKB/Swiss-Prot
  Q9QV50 UniProtKB/Swiss-Prot

Nomenclature History
Date Current Symbol Current Name Previous Symbol Previous Name Description Reference Status
2015-12-09 Got2  glutamic-oxaloacetic transaminase 2  Got2  glutamic-oxaloacetic transaminase 2, mitochondrial  Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2013-06-05 Got2  glutamic-oxaloacetic transaminase 2, mitochondrial  Got2  glutamic-oxaloacetic transaminase 2, mitochondrial (aspartate aminotransferase 2)  Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2008-09-26 Got2  glutamic-oxaloacetic transaminase 2, mitochondrial (aspartate aminotransferase 2)  Got2  glutamate oxaloacetate transaminase 2, mitochondrial  Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2006-03-30 Got2  glutamate oxaloacetate transaminase 2, mitochondrial    glutamate oxaloacetate transaminase 2  Name updated 1299863 APPROVED
2002-11-06 Got2  glutamate oxaloacetate transaminase 2    Glutamate oxaloacetate transaminase 2, mitochondrial (aspartate aminotransferase 2)  Name updated 625702 APPROVED
2002-06-10 Got2  Glutamate oxaloacetate transaminase 2, mitochondrial (aspartate aminotransferase 2)      Symbol and Name status set to approved 70586 APPROVED

RGD Curation Notes
Note Type Note Reference
gene_cellular_localization localized to the mitochondrion 632937
gene_regulation enzyme activity is not altered in response to glucocorticoid hormones 632939