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Aspartate aminotransferase, mitochondrial (mAspAT) (EC 2.6.1.1) (EC 2.6.1.7) (Fatty acid-binding protein) (FABP-1) (Glutamate oxaloacetate transaminase 2) (Kynurenine aminotransferase 4) (Kynurenine aminotransferase IV) (Kynurenine--oxoglutarate transaminase 4) (Kynurenine--oxoglutarate transaminase IV) (Plasma membrane-associated fatty acid-binding protein) (FABPpm) (Transaminase A)

 AATM_HUMAN              Reviewed;         430 AA.
P00505; B4DJA6; E7ERW2; Q53FL3; Q9BWA3;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 3.
17-JUN-2020, entry version 214.
RecName: Full=Aspartate aminotransferase, mitochondrial;
Short=mAspAT;
EC=2.6.1.1 {ECO:0000269|PubMed:26902786, ECO:0000269|PubMed:31422819};
EC=2.6.1.7;
AltName: Full=Fatty acid-binding protein;
Short=FABP-1;
AltName: Full=Glutamate oxaloacetate transaminase 2;
AltName: Full=Kynurenine aminotransferase 4;
AltName: Full=Kynurenine aminotransferase IV;
AltName: Full=Kynurenine--oxoglutarate transaminase 4;
AltName: Full=Kynurenine--oxoglutarate transaminase IV;
AltName: Full=Plasma membrane-associated fatty acid-binding protein;
Short=FABPpm;
AltName: Full=Transaminase A;
Flags: Precursor;
Name=GOT2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-346.
PubMed=3207426; DOI=10.1016/s0006-291x(88)81017-9;
Pol S., Bousquet-Lemercier B., Pave-Preux M., Pawlak A., Nalpas B.,
Berthelot P., Hanoune J., Barouki R.;
"Nucleotide sequence and tissue distribution of the human mitochondrial
aspartate aminotransferase mRNA.";
Biochem. Biophys. Res. Commun. 157:1309-1315(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLY-346.
TISSUE=Subthalamic nucleus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Gastric mucosa;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
Myers R.M., Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-428.
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 30-430, AND VARIANT GLY-346.
PubMed=4052435; DOI=10.1016/0167-4838(85)90172-4;
Martini F., Angelaccio S., Barra D., Pascarella S., Maras B., Doonan S.,
Bossa F.;
"The primary structure of mitochondrial aspartate aminotransferase from
human heart.";
Biochim. Biophys. Acta 832:46-51(1985).
[7]
FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=9537447; DOI=10.1002/hep.510270423;
Zhou S.L., Gordon R.E., Bradbury M., Stump D., Kiang C.L., Berk P.D.;
"Ethanol up-regulates fatty acid uptake and plasma membrane expression and
export of mitochondrial aspartate aminotransferase in HepG2 cells.";
Hepatology 27:1064-1074(1998).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73; LYS-90; LYS-159; LYS-234;
LYS-296; LYS-396 AND LYS-404, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 AND THR-333, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-48; TYR-96; SER-143 AND
THR-333, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-29, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[13]
FUNCTION, CATALYTIC ACTIVITY, INVOLVEMENT IN EIEE82, VARIANTS EIEE82
LEU-209 DEL; GLY-262; GLY-337 AND VAL-366, AND CHARACTERIZATION OF VARIANTS
EIEE82 GLY-262 AND VAL-366.
PubMed=31422819; DOI=10.1016/j.ajhg.2019.07.015;
van Karnebeek C.D.M., Ramos R.J., Wen X.Y., Tarailo-Graovac M.,
Gleeson J.G., Skrypnyk C., Brand-Arzamendi K., Karbassi F., Issa M.Y.,
van der Lee R., Droegemoeller B.I., Koster J., Rousseau J., Campeau P.M.,
Wang Y., Cao F., Li M., Ruiter J., Ciapaite J., Kluijtmans L.A.J.,
Willemsen M.A.A.P., Jans J.J., Ross C.J., Wintjes L.T., Rodenburg R.J.,
Huigen M.C.D.G., Jia Z., Waterham H.R., Wasserman W.W., Wanders R.J.A.,
Verhoeven-Duif N.M., Zaki M.S., Wevers R.A.;
"Bi-allelic GOT2 mutations cause a treatable malate-aspartate shuttle-
related encephalopathy.";
Am. J. Hum. Genet. 105:534-548(2019).
[14] {ECO:0000244|PDB:5AX8}
X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 30-430, BIOPHYSICOCHEMICAL
PROPERTIES, AND CATALYTIC ACTIVITY.
PubMed=26902786; DOI=10.5582/bst.2015.01150;
Jiang X., Wang J., Chang H., Zhou Y.;
"Recombinant expression, purification and crystallographic studies of the
mature form of human mitochondrial aspartate aminotransferase.";
Biosci. Trends 10:79-84(2016).
-!- FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan
metabolite L-kynurenine to form kynurenic acid (KA). As a member of the
malate-aspartate shuttle, it has a key role in the intracellular NAD(H)
redox balance. Is important for metabolite exchange between
mitochondria and cytosol, and for amino acid metabolism. Facilitates
cellular uptake of long-chain free fatty acids.
{ECO:0000269|PubMed:31422819, ECO:0000269|PubMed:9537447}.
-!- CATALYTIC ACTIVITY:
Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
Evidence={ECO:0000269|PubMed:26902786, ECO:0000269|PubMed:31422819};
-!- CATALYTIC ACTIVITY:
Reaction=2-oxoglutarate + L-kynurenine = 4-(2-aminophenyl)-2,4-
dioxobutanoate + L-glutamate; Xref=Rhea:RHEA:20964,
ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959,
ChEBI:CHEBI:58147; EC=2.6.1.7;
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 8.5. {ECO:0000269|PubMed:26902786};
Temperature dependence:
Optimum temperature is 47.5 degrees Celsius.
{ECO:0000269|PubMed:26902786};
-!- SUBUNIT: Homodimer.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:9537447}. Cell membrane
{ECO:0000269|PubMed:9537447}. Note=Exposure to alcohol promotes
translocation to the cell membrane. {ECO:0000269|PubMed:9537447}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P00505-1; Sequence=Displayed;
Name=2;
IsoId=P00505-2; Sequence=VSP_054848;
-!- INDUCTION: Up-regulated by long-time exposure to alcohol.
{ECO:0000269|PubMed:9537447}.
-!- DISEASE: Epileptic encephalopathy, early infantile, 82 (EIEE82)
[MIM:618721]: A form of epileptic encephalopathy, a heterogeneous group
of severe early-onset epilepsies characterized by refractory seizures,
neurodevelopmental impairment, and poor prognosis. Development is
normal prior to seizure onset, after which cognitive and motor delays
become apparent. EIEE82 is an autosomal recessive metabolic
encephalopathy characterized by epilepsy from the first year of life,
global developmental delay, hypotonia and feeding difficulties apparent
soon after birth, and intellectual and motor disabilities. Other
features include poor overall growth, progressive microcephaly and
biochemical abnormalities, including increased serum lactate and
ammonia. {ECO:0000269|PubMed:31422819}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
chloroplastic isozymes.
-!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
aminotransferase family. {ECO:0000305}.
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EMBL; M22632; AAA35568.1; -; mRNA.
EMBL; AK295993; BAG58768.1; -; mRNA.
EMBL; AK223271; BAD96991.1; -; mRNA.
EMBL; AC012183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000525; AAH00525.1; -; mRNA.
CCDS; CCDS10801.1; -. [P00505-1]
CCDS; CCDS67045.1; -. [P00505-2]
PIR; A31873; XNHUDM.
RefSeq; NP_001273149.1; NM_001286220.1. [P00505-2]
RefSeq; NP_002071.2; NM_002080.3. [P00505-1]
PDB; 5AX8; X-ray; 2.99 A; A/B/C/D=30-430.
PDBsum; 5AX8; -.
SMR; P00505; -.
BioGRID; 109068; 41.
IntAct; P00505; 17.
MINT; P00505; -.
STRING; 9606.ENSP00000245206; -.
DrugBank; DB02783; 4'-Deoxy-4'-Acetylyamino-Pyridoxal-5'-Phosphate.
DrugBank; DB00128; Aspartic acid.
DrugBank; DB00142; Glutamic acid.
DrugBank; DB00114; Pyridoxal phosphate.
DrugCentral; P00505; -.
TCDB; 9.A.70.1.1; the aspartate amino transferase (aat) family.
iPTMnet; P00505; -.
MetOSite; P00505; -.
PhosphoSitePlus; P00505; -.
SwissPalm; P00505; -.
BioMuta; GOT2; -.
DMDM; 308153643; -.
UCD-2DPAGE; P00505; -.
CPTAC; CPTAC-518; -.
CPTAC; CPTAC-519; -.
EPD; P00505; -.
jPOST; P00505; -.
MassIVE; P00505; -.
MaxQB; P00505; -.
PaxDb; P00505; -.
PeptideAtlas; P00505; -.
PRIDE; P00505; -.
ProteomicsDB; 17864; -.
ProteomicsDB; 51258; -. [P00505-1]
TopDownProteomics; P00505-1; -. [P00505-1]
Antibodypedia; 15396; 607 antibodies.
DNASU; 2806; -.
Ensembl; ENST00000245206; ENSP00000245206; ENSG00000125166. [P00505-1]
Ensembl; ENST00000434819; ENSP00000394100; ENSG00000125166. [P00505-2]
GeneID; 2806; -.
KEGG; hsa:2806; -.
UCSC; uc002eof.2; human. [P00505-1]
CTD; 2806; -.
DisGeNET; 2806; -.
EuPathDB; HostDB:ENSG00000125166.12; -.
GeneCards; GOT2; -.
HGNC; HGNC:4433; GOT2.
HPA; ENSG00000125166; Tissue enhanced (skeletal).
MIM; 138150; gene.
MIM; 618721; phenotype.
neXtProt; NX_P00505; -.
OpenTargets; ENSG00000125166; -.
PharmGKB; PA28818; -.
eggNOG; KOG1411; Eukaryota.
eggNOG; COG1448; LUCA.
GeneTree; ENSGT00950000183082; -.
HOGENOM; CLU_032440_1_2_1; -.
InParanoid; P00505; -.
KO; K14455; -.
OMA; VGACTIV; -.
OrthoDB; 1104596at2759; -.
PhylomeDB; P00505; -.
TreeFam; TF300641; -.
BioCyc; MetaCyc:HS04858-MONOMER; -.
Reactome; R-HSA-1614558; Degradation of cysteine and homocysteine.
Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
Reactome; R-HSA-70263; Gluconeogenesis.
Reactome; R-HSA-8963693; Aspartate and asparagine metabolism.
Reactome; R-HSA-8964539; Glutamate and glutamine metabolism.
BioGRID-ORCS; 2806; 138 hits in 787 CRISPR screens.
ChiTaRS; GOT2; human.
GeneWiki; GOT2; -.
GenomeRNAi; 2806; -.
Pharos; P00505; Tbio.
PRO; PR:P00505; -.
Proteomes; UP000005640; Chromosome 16.
RNAct; P00505; protein.
Bgee; ENSG00000125166; Expressed in vastus lateralis and 230 other tissues.
ExpressionAtlas; P00505; baseline and differential.
Genevisible; P00505; HS.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
GO; GO:0030315; C:T-tubule; IEA:Ensembl.
GO; GO:0016597; F:amino acid binding; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IDA:UniProtKB.
GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
GO; GO:0019470; P:4-hydroxyproline catabolic process; TAS:BHF-UCL.
GO; GO:0006532; P:aspartate biosynthetic process; IEA:Ensembl.
GO; GO:0006533; P:aspartate catabolic process; IDA:UniProtKB.
GO; GO:0006531; P:aspartate metabolic process; ISS:UniProtKB.
GO; GO:0008652; P:cellular amino acid biosynthetic process; TAS:Reactome.
GO; GO:0015908; P:fatty acid transport; IEP:UniProtKB.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0006094; P:gluconeogenesis; TAS:Reactome.
GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:Ensembl.
GO; GO:0019550; P:glutamate catabolic process to aspartate; IEA:Ensembl.
GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
GO; GO:0046487; P:glyoxylate metabolic process; TAS:Reactome.
GO; GO:0007595; P:lactation; IEA:Ensembl.
GO; GO:0006107; P:oxaloacetate metabolic process; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IDA:UniProtKB.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:0043278; P:response to morphine; IEA:Ensembl.
GO; GO:0014850; P:response to muscle activity; IEA:Ensembl.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
InterPro; IPR004839; Aminotransferase_I/II.
InterPro; IPR000796; Asp_trans.
InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
PANTHER; PTHR11879; PTHR11879; 1.
Pfam; PF00155; Aminotran_1_2; 1.
PRINTS; PR00799; TRANSAMINASE.
SUPFAM; SSF53383; SSF53383; 1.
PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Aminotransferase;
Cell membrane; Direct protein sequencing; Disease mutation; Epilepsy;
Lipid transport; Membrane; Methylation; Mitochondrion; Nitration;
Phosphoprotein; Polymorphism; Pyridoxal phosphate; Reference proteome;
Transferase; Transit peptide; Transport.
TRANSIT 1..29
/note="Mitochondrion"
/evidence="ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:4052435"
CHAIN 30..430
/note="Aspartate aminotransferase, mitochondrial"
/id="PRO_0000001215"
BINDING 65
/note="Substrate; via amide nitrogen"
/evidence="ECO:0000250"
BINDING 162
/note="Substrate"
/evidence="ECO:0000250"
BINDING 215
/note="Substrate"
/evidence="ECO:0000250"
BINDING 407
/note="Substrate"
/evidence="ECO:0000250"
MOD_RES 48
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:24275569"
MOD_RES 59
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 73
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000244|PubMed:19608861"
MOD_RES 73
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 82
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 90
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000244|PubMed:19608861"
MOD_RES 90
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 96
/note="Nitrated tyrosine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 96
/note="Phosphotyrosine; alternate"
/evidence="ECO:0000244|PubMed:24275569"
MOD_RES 107
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 107
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 122
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 122
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 143
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569"
MOD_RES 159
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000244|PubMed:19608861"
MOD_RES 159
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 185
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 185
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 227
/note="N6-succinyllysine"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 234
/note="N6-acetyllysine"
/evidence="ECO:0000244|PubMed:19608861"
MOD_RES 279
/note="N6-(pyridoxal phosphate)lysine; alternate"
/evidence="ECO:0000250"
MOD_RES 279
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 296
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000244|PubMed:19608861"
MOD_RES 296
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 302
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 309
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 309
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P12344"
MOD_RES 313
/note="Asymmetric dimethylarginine"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 333
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569"
MOD_RES 338
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 338
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 345
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 363
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 363
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 364
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 387
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 396
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000244|PubMed:19608861"
MOD_RES 396
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 404
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000244|PubMed:19608861"
MOD_RES 404
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
VAR_SEQ 83..125
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_054848"
VARIANT 2
/note="A -> S (in dbSNP:rs11558171)"
/id="VAR_055494"
VARIANT 188
/note="G -> S (in dbSNP:rs11076256)"
/id="VAR_031710"
VARIANT 209
/note="Missing (in EIEE82; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:31422819"
/id="VAR_083488"
VARIANT 262
/note="R -> G (in EIEE82; decreased glutamate oxaloacetate
transferase activity)"
/evidence="ECO:0000269|PubMed:31422819"
/id="VAR_083489"
VARIANT 337
/note="R -> G (in EIEE82; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:31422819"
/id="VAR_083490"
VARIANT 346
/note="V -> G (in dbSNP:rs30842)"
/evidence="ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:3207426, ECO:0000269|PubMed:4052435"
/id="VAR_031711"
VARIANT 366
/note="G -> V (in EIEE82; unknown pathological
significance; decreased glutamate oxaloacetate transferase
activity)"
/evidence="ECO:0000269|PubMed:31422819"
/id="VAR_083491"
VARIANT 428
/note="V -> A (in dbSNP:rs17849335)"
/evidence="ECO:0000269|PubMed:15489334"
/id="VAR_031712"
CONFLICT 110..111
/note="AE -> EA (in Ref. 6; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 255
/note="D -> N (in Ref. 6; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 258
/note="A -> T (in Ref. 3; BAD96991)"
/evidence="ECO:0000305"
CONFLICT 305
/note="E -> Q (in Ref. 6; AA sequence)"
/evidence="ECO:0000305"
HELIX 43..53
/evidence="ECO:0000244|PDB:5AX8"
HELIX 78..88
/evidence="ECO:0000244|PDB:5AX8"
TURN 89..91
/evidence="ECO:0000244|PDB:5AX8"
HELIX 103..114
/evidence="ECO:0000244|PDB:5AX8"
HELIX 119..123
/evidence="ECO:0000244|PDB:5AX8"
STRAND 126..132
/evidence="ECO:0000244|PDB:5AX8"
HELIX 133..148
/evidence="ECO:0000244|PDB:5AX8"
STRAND 153..159
/evidence="ECO:0000244|PDB:5AX8"
HELIX 165..172
/evidence="ECO:0000244|PDB:5AX8"
STRAND 175..180
/evidence="ECO:0000244|PDB:5AX8"
TURN 184..187
/evidence="ECO:0000244|PDB:5AX8"
HELIX 191..198
/evidence="ECO:0000244|PDB:5AX8"
STRAND 206..213
/evidence="ECO:0000244|PDB:5AX8"
HELIX 223..236
/evidence="ECO:0000244|PDB:5AX8"
STRAND 239..246
/evidence="ECO:0000244|PDB:5AX8"
TURN 247..251
/evidence="ECO:0000244|PDB:5AX8"
HELIX 254..257
/evidence="ECO:0000244|PDB:5AX8"
HELIX 259..266
/evidence="ECO:0000244|PDB:5AX8"
STRAND 272..276
/evidence="ECO:0000244|PDB:5AX8"
TURN 278..280
/evidence="ECO:0000244|PDB:5AX8"
TURN 284..287
/evidence="ECO:0000244|PDB:5AX8"
STRAND 288..294
/evidence="ECO:0000244|PDB:5AX8"
HELIX 298..315
/evidence="ECO:0000244|PDB:5AX8"
STRAND 316..318
/evidence="ECO:0000244|PDB:5AX8"
HELIX 321..332
/evidence="ECO:0000244|PDB:5AX8"
HELIX 334..364
/evidence="ECO:0000244|PDB:5AX8"
HELIX 372..376
/evidence="ECO:0000244|PDB:5AX8"
STRAND 379..383
/evidence="ECO:0000244|PDB:5AX8"
HELIX 388..398
/evidence="ECO:0000244|PDB:5AX8"
STRAND 406..409
/evidence="ECO:0000244|PDB:5AX8"
HELIX 410..412
/evidence="ECO:0000244|PDB:5AX8"
HELIX 415..428
/evidence="ECO:0000244|PDB:5AX8"
SEQUENCE 430 AA; 47518 MW; F559567ABF2DB346 CRC64;
MALLHSGRVL PGIAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA FKRDTNSKKM
NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK NLDKEYLPIG GLAEFCKASA ELALGENSEV
LKSGRFVTVQ TISGTGALRI GASFLQRFFK FSRDVFLPKP TWGNHTPIFR DAGMQLQGYR
YYDPKTCGFD FTGAVEDISK IPEQSVLLLH ACAHNPTGVD PRPEQWKEIA TVVKKRNLFA
FFDMAYQGFA SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTMVCKDADE
AKRVESQLKI LIRPMYSNPP LNGARIAAAI LNTPDLRKQW LQEVKVMADR IIGMRTQLVS
NLKKEGSTHN WQHITDQIGM FCFTGLKPEQ VERLIKEFSI YMTKDGRISV AGVTSSNVGY
LAHAIHQVTK


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