Full text data of GOT2
GOT2
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Aspartate aminotransferase, mitochondrial; mAspAT; 2.6.1.1; 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; Flags: Precursor)
Aspartate aminotransferase, mitochondrial; mAspAT; 2.6.1.1; 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; Flags: Precursor)
UniProt
P00505
ID AATM_HUMAN Reviewed; 430 AA.
AC P00505; Q53FL3; Q9BWA3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-OCT-2010, sequence version 3.
DT 22-JAN-2014, entry version 152.
DE RecName: Full=Aspartate aminotransferase, mitochondrial;
DE Short=mAspAT;
DE EC=2.6.1.1;
DE EC=2.6.1.7;
DE AltName: Full=Fatty acid-binding protein;
DE Short=FABP-1;
DE AltName: Full=Glutamate oxaloacetate transaminase 2;
DE AltName: Full=Kynurenine aminotransferase 4;
DE AltName: Full=Kynurenine aminotransferase IV;
DE AltName: Full=Kynurenine--oxoglutarate transaminase 4;
DE AltName: Full=Kynurenine--oxoglutarate transaminase IV;
DE AltName: Full=Plasma membrane-associated fatty acid-binding protein;
DE Short=FABPpm;
DE AltName: Full=Transaminase A;
DE Flags: Precursor;
GN Name=GOT2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-346.
RX PubMed=3207426; DOI=10.1016/S0006-291X(88)81017-9;
RA Pol S., Bousquet-Lemercier B., Pave-Preux M., Pawlak A., Nalpas B.,
RA Berthelot P., Hanoune J., Barouki R.;
RT "Nucleotide sequence and tissue distribution of the human
RT mitochondrial aspartate aminotransferase mRNA.";
RL Biochem. Biophys. Res. Commun. 157:1309-1315(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastric mucosa;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-428.
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 30-430, AND VARIANT GLY-346.
RX PubMed=4052435; DOI=10.1016/0167-4838(85)90172-4;
RA Martini F., Angelaccio S., Barra D., Pascarella S., Maras B.,
RA Doonan S., Bossa F.;
RT "The primary structure of mitochondrial aspartate aminotransferase
RT from human heart.";
RL Biochim. Biophys. Acta 832:46-51(1985).
RN [6]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9537447; DOI=10.1002/hep.510270423;
RA Zhou S.L., Gordon R.E., Bradbury M., Stump D., Kiang C.L., Berk P.D.;
RT "Ethanol up-regulates fatty acid uptake and plasma membrane expression
RT and export of mitochondrial aspartate aminotransferase in HepG2
RT cells.";
RL Hepatology 27:1064-1074(1998).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73; LYS-90; LYS-159;
RP LYS-234; LYS-296; LYS-396 AND LYS-404, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Catalyzes the irreversible transamination of the L-
CC tryptophan metabolite L-kynurenine to form kynurenic acid (KA).
CC Plays a key role in amino acid metabolism. Important for
CC metabolite exchange between mitochondria and cytosol. Facilitates
CC cellular uptake of long-chain free fatty acids.
CC -!- CATALYTIC ACTIVITY: L-aspartate + 2-oxoglutarate = oxaloacetate +
CC L-glutamate.
CC -!- CATALYTIC ACTIVITY: L-kynurenine + 2-oxoglutarate = 4-(2-
CC aminophenyl)-2,4-dioxobutanoate + L-glutamate.
CC -!- COFACTOR: Pyridoxal phosphate.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. Cell membrane.
CC Note=Exposure to alcohol promotes translocation to the cell
CC membrane.
CC -!- INDUCTION: Up-regulated by long-time exposure to alcohol.
CC -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial
CC and chloroplastic isozymes.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M22632; AAA35568.1; -; mRNA.
DR EMBL; AK223271; BAD96991.1; -; mRNA.
DR EMBL; BC000525; AAH00525.1; -; mRNA.
DR PIR; A31873; XNHUDM.
DR RefSeq; NP_001273149.1; NM_001286220.1.
DR RefSeq; NP_002071.2; NM_002080.3.
DR UniGene; Hs.599470; -.
DR ProteinModelPortal; P00505; -.
DR SMR; P00505; 30-430.
DR IntAct; P00505; 7.
DR MINT; MINT-1406848; -.
DR STRING; 9606.ENSP00000245206; -.
DR DrugBank; DB00128; L-Aspartic Acid.
DR DrugBank; DB00142; L-Glutamic Acid.
DR DrugBank; DB00114; Pyridoxal Phosphate.
DR PhosphoSite; P00505; -.
DR DMDM; 308153643; -.
DR UCD-2DPAGE; P00505; -.
DR PaxDb; P00505; -.
DR PRIDE; P00505; -.
DR DNASU; 2806; -.
DR Ensembl; ENST00000245206; ENSP00000245206; ENSG00000125166.
DR GeneID; 2806; -.
DR KEGG; hsa:2806; -.
DR UCSC; uc002eof.1; human.
DR CTD; 2806; -.
DR GeneCards; GC16M058741; -.
DR H-InvDB; HIX0013095; -.
DR HGNC; HGNC:4433; GOT2.
DR HPA; HPA018139; -.
DR MIM; 138150; gene.
DR neXtProt; NX_P00505; -.
DR PharmGKB; PA28818; -.
DR eggNOG; COG1448; -.
DR HOGENOM; HOG000185898; -.
DR HOVERGEN; HBG000951; -.
DR InParanoid; P00505; -.
DR KO; K14455; -.
DR OMA; RVGAFTM; -.
DR OrthoDB; EOG74J980; -.
DR PhylomeDB; P00505; -.
DR Reactome; REACT_111217; Metabolism.
DR ChiTaRS; Got2; human.
DR GeneWiki; GOT2; -.
DR GenomeRNAi; 2806; -.
DR NextBio; 11061; -.
DR PRO; PR:P00505; -.
DR ArrayExpress; P00505; -.
DR Bgee; P00505; -.
DR CleanEx; HS_GOT2; -.
DR Genevestigator; P00505; -.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IDA:UniProtKB.
DR GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR GO; GO:0019470; P:4-hydroxyproline catabolic process; TAS:BHF-UCL.
DR GO; GO:0006532; P:aspartate biosynthetic process; IEA:Ensembl.
DR GO; GO:0006533; P:aspartate catabolic process; IDA:UniProtKB.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; TAS:Reactome.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
DR GO; GO:0015908; P:fatty acid transport; IEP:UniProtKB.
DR GO; GO:0006094; P:gluconeogenesis; TAS:Reactome.
DR GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:Ensembl.
DR GO; GO:0019550; P:glutamate catabolic process to aspartate; IEA:Ensembl.
DR GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IDA:UniProtKB.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR000796; Asp_trans.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR PANTHER; PTHR11879; PTHR11879; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminotransferase; Cell membrane; Complete proteome;
KW Direct protein sequencing; Lipid transport; Membrane; Mitochondrion;
KW Nitration; Polymorphism; Pyridoxal phosphate; Reference proteome;
KW Transferase; Transit peptide; Transport.
FT TRANSIT 1 29 Mitochondrion.
FT CHAIN 30 430 Aspartate aminotransferase,
FT mitochondrial.
FT /FTId=PRO_0000001215.
FT BINDING 65 65 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 162 162 Substrate (By similarity).
FT BINDING 215 215 Substrate (By similarity).
FT BINDING 407 407 Substrate (By similarity).
FT MOD_RES 59 59 N6-acetyllysine (By similarity).
FT MOD_RES 73 73 N6-acetyllysine.
FT MOD_RES 82 82 N6-acetyllysine (By similarity).
FT MOD_RES 90 90 N6-acetyllysine.
FT MOD_RES 96 96 Nitrated tyrosine (By similarity).
FT MOD_RES 107 107 N6-acetyllysine (By similarity).
FT MOD_RES 122 122 N6-acetyllysine (By similarity).
FT MOD_RES 159 159 N6-acetyllysine.
FT MOD_RES 185 185 N6-acetyllysine (By similarity).
FT MOD_RES 234 234 N6-acetyllysine.
FT MOD_RES 279 279 N6-(pyridoxal phosphate)lysine; alternate
FT (By similarity).
FT MOD_RES 279 279 N6-acetyllysine; alternate (By
FT similarity).
FT MOD_RES 296 296 N6-acetyllysine.
FT MOD_RES 302 302 N6-acetyllysine (By similarity).
FT MOD_RES 309 309 N6-acetyllysine; alternate (By
FT similarity).
FT MOD_RES 309 309 N6-succinyllysine; alternate (By
FT similarity).
FT MOD_RES 338 338 N6-acetyllysine (By similarity).
FT MOD_RES 345 345 N6-acetyllysine (By similarity).
FT MOD_RES 363 363 N6-acetyllysine (By similarity).
FT MOD_RES 364 364 N6-acetyllysine (By similarity).
FT MOD_RES 387 387 N6-acetyllysine (By similarity).
FT MOD_RES 396 396 N6-acetyllysine.
FT MOD_RES 404 404 N6-acetyllysine.
FT VARIANT 2 2 A -> S (in dbSNP:rs11558171).
FT /FTId=VAR_055494.
FT VARIANT 188 188 G -> S (in dbSNP:rs11076256).
FT /FTId=VAR_031710.
FT VARIANT 346 346 V -> G (in dbSNP:rs30842).
FT /FTId=VAR_031711.
FT VARIANT 428 428 V -> A (in dbSNP:rs17849335).
FT /FTId=VAR_031712.
FT CONFLICT 110 111 AE -> EA (in Ref. 5; AA sequence).
FT CONFLICT 255 255 D -> N (in Ref. 5; AA sequence).
FT CONFLICT 258 258 A -> T (in Ref. 2; BAD96991).
FT CONFLICT 305 305 E -> Q (in Ref. 5; AA sequence).
SQ 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
//
ID AATM_HUMAN Reviewed; 430 AA.
AC P00505; Q53FL3; Q9BWA3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-OCT-2010, sequence version 3.
DT 22-JAN-2014, entry version 152.
DE RecName: Full=Aspartate aminotransferase, mitochondrial;
DE Short=mAspAT;
DE EC=2.6.1.1;
DE EC=2.6.1.7;
DE AltName: Full=Fatty acid-binding protein;
DE Short=FABP-1;
DE AltName: Full=Glutamate oxaloacetate transaminase 2;
DE AltName: Full=Kynurenine aminotransferase 4;
DE AltName: Full=Kynurenine aminotransferase IV;
DE AltName: Full=Kynurenine--oxoglutarate transaminase 4;
DE AltName: Full=Kynurenine--oxoglutarate transaminase IV;
DE AltName: Full=Plasma membrane-associated fatty acid-binding protein;
DE Short=FABPpm;
DE AltName: Full=Transaminase A;
DE Flags: Precursor;
GN Name=GOT2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-346.
RX PubMed=3207426; DOI=10.1016/S0006-291X(88)81017-9;
RA Pol S., Bousquet-Lemercier B., Pave-Preux M., Pawlak A., Nalpas B.,
RA Berthelot P., Hanoune J., Barouki R.;
RT "Nucleotide sequence and tissue distribution of the human
RT mitochondrial aspartate aminotransferase mRNA.";
RL Biochem. Biophys. Res. Commun. 157:1309-1315(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastric mucosa;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-428.
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 30-430, AND VARIANT GLY-346.
RX PubMed=4052435; DOI=10.1016/0167-4838(85)90172-4;
RA Martini F., Angelaccio S., Barra D., Pascarella S., Maras B.,
RA Doonan S., Bossa F.;
RT "The primary structure of mitochondrial aspartate aminotransferase
RT from human heart.";
RL Biochim. Biophys. Acta 832:46-51(1985).
RN [6]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9537447; DOI=10.1002/hep.510270423;
RA Zhou S.L., Gordon R.E., Bradbury M., Stump D., Kiang C.L., Berk P.D.;
RT "Ethanol up-regulates fatty acid uptake and plasma membrane expression
RT and export of mitochondrial aspartate aminotransferase in HepG2
RT cells.";
RL Hepatology 27:1064-1074(1998).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73; LYS-90; LYS-159;
RP LYS-234; LYS-296; LYS-396 AND LYS-404, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Catalyzes the irreversible transamination of the L-
CC tryptophan metabolite L-kynurenine to form kynurenic acid (KA).
CC Plays a key role in amino acid metabolism. Important for
CC metabolite exchange between mitochondria and cytosol. Facilitates
CC cellular uptake of long-chain free fatty acids.
CC -!- CATALYTIC ACTIVITY: L-aspartate + 2-oxoglutarate = oxaloacetate +
CC L-glutamate.
CC -!- CATALYTIC ACTIVITY: L-kynurenine + 2-oxoglutarate = 4-(2-
CC aminophenyl)-2,4-dioxobutanoate + L-glutamate.
CC -!- COFACTOR: Pyridoxal phosphate.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. Cell membrane.
CC Note=Exposure to alcohol promotes translocation to the cell
CC membrane.
CC -!- INDUCTION: Up-regulated by long-time exposure to alcohol.
CC -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial
CC and chloroplastic isozymes.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M22632; AAA35568.1; -; mRNA.
DR EMBL; AK223271; BAD96991.1; -; mRNA.
DR EMBL; BC000525; AAH00525.1; -; mRNA.
DR PIR; A31873; XNHUDM.
DR RefSeq; NP_001273149.1; NM_001286220.1.
DR RefSeq; NP_002071.2; NM_002080.3.
DR UniGene; Hs.599470; -.
DR ProteinModelPortal; P00505; -.
DR SMR; P00505; 30-430.
DR IntAct; P00505; 7.
DR MINT; MINT-1406848; -.
DR STRING; 9606.ENSP00000245206; -.
DR DrugBank; DB00128; L-Aspartic Acid.
DR DrugBank; DB00142; L-Glutamic Acid.
DR DrugBank; DB00114; Pyridoxal Phosphate.
DR PhosphoSite; P00505; -.
DR DMDM; 308153643; -.
DR UCD-2DPAGE; P00505; -.
DR PaxDb; P00505; -.
DR PRIDE; P00505; -.
DR DNASU; 2806; -.
DR Ensembl; ENST00000245206; ENSP00000245206; ENSG00000125166.
DR GeneID; 2806; -.
DR KEGG; hsa:2806; -.
DR UCSC; uc002eof.1; human.
DR CTD; 2806; -.
DR GeneCards; GC16M058741; -.
DR H-InvDB; HIX0013095; -.
DR HGNC; HGNC:4433; GOT2.
DR HPA; HPA018139; -.
DR MIM; 138150; gene.
DR neXtProt; NX_P00505; -.
DR PharmGKB; PA28818; -.
DR eggNOG; COG1448; -.
DR HOGENOM; HOG000185898; -.
DR HOVERGEN; HBG000951; -.
DR InParanoid; P00505; -.
DR KO; K14455; -.
DR OMA; RVGAFTM; -.
DR OrthoDB; EOG74J980; -.
DR PhylomeDB; P00505; -.
DR Reactome; REACT_111217; Metabolism.
DR ChiTaRS; Got2; human.
DR GeneWiki; GOT2; -.
DR GenomeRNAi; 2806; -.
DR NextBio; 11061; -.
DR PRO; PR:P00505; -.
DR ArrayExpress; P00505; -.
DR Bgee; P00505; -.
DR CleanEx; HS_GOT2; -.
DR Genevestigator; P00505; -.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IDA:UniProtKB.
DR GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR GO; GO:0019470; P:4-hydroxyproline catabolic process; TAS:BHF-UCL.
DR GO; GO:0006532; P:aspartate biosynthetic process; IEA:Ensembl.
DR GO; GO:0006533; P:aspartate catabolic process; IDA:UniProtKB.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; TAS:Reactome.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
DR GO; GO:0015908; P:fatty acid transport; IEP:UniProtKB.
DR GO; GO:0006094; P:gluconeogenesis; TAS:Reactome.
DR GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:Ensembl.
DR GO; GO:0019550; P:glutamate catabolic process to aspartate; IEA:Ensembl.
DR GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IDA:UniProtKB.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR000796; Asp_trans.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR PANTHER; PTHR11879; PTHR11879; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminotransferase; Cell membrane; Complete proteome;
KW Direct protein sequencing; Lipid transport; Membrane; Mitochondrion;
KW Nitration; Polymorphism; Pyridoxal phosphate; Reference proteome;
KW Transferase; Transit peptide; Transport.
FT TRANSIT 1 29 Mitochondrion.
FT CHAIN 30 430 Aspartate aminotransferase,
FT mitochondrial.
FT /FTId=PRO_0000001215.
FT BINDING 65 65 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 162 162 Substrate (By similarity).
FT BINDING 215 215 Substrate (By similarity).
FT BINDING 407 407 Substrate (By similarity).
FT MOD_RES 59 59 N6-acetyllysine (By similarity).
FT MOD_RES 73 73 N6-acetyllysine.
FT MOD_RES 82 82 N6-acetyllysine (By similarity).
FT MOD_RES 90 90 N6-acetyllysine.
FT MOD_RES 96 96 Nitrated tyrosine (By similarity).
FT MOD_RES 107 107 N6-acetyllysine (By similarity).
FT MOD_RES 122 122 N6-acetyllysine (By similarity).
FT MOD_RES 159 159 N6-acetyllysine.
FT MOD_RES 185 185 N6-acetyllysine (By similarity).
FT MOD_RES 234 234 N6-acetyllysine.
FT MOD_RES 279 279 N6-(pyridoxal phosphate)lysine; alternate
FT (By similarity).
FT MOD_RES 279 279 N6-acetyllysine; alternate (By
FT similarity).
FT MOD_RES 296 296 N6-acetyllysine.
FT MOD_RES 302 302 N6-acetyllysine (By similarity).
FT MOD_RES 309 309 N6-acetyllysine; alternate (By
FT similarity).
FT MOD_RES 309 309 N6-succinyllysine; alternate (By
FT similarity).
FT MOD_RES 338 338 N6-acetyllysine (By similarity).
FT MOD_RES 345 345 N6-acetyllysine (By similarity).
FT MOD_RES 363 363 N6-acetyllysine (By similarity).
FT MOD_RES 364 364 N6-acetyllysine (By similarity).
FT MOD_RES 387 387 N6-acetyllysine (By similarity).
FT MOD_RES 396 396 N6-acetyllysine.
FT MOD_RES 404 404 N6-acetyllysine.
FT VARIANT 2 2 A -> S (in dbSNP:rs11558171).
FT /FTId=VAR_055494.
FT VARIANT 188 188 G -> S (in dbSNP:rs11076256).
FT /FTId=VAR_031710.
FT VARIANT 346 346 V -> G (in dbSNP:rs30842).
FT /FTId=VAR_031711.
FT VARIANT 428 428 V -> A (in dbSNP:rs17849335).
FT /FTId=VAR_031712.
FT CONFLICT 110 111 AE -> EA (in Ref. 5; AA sequence).
FT CONFLICT 255 255 D -> N (in Ref. 5; AA sequence).
FT CONFLICT 258 258 A -> T (in Ref. 2; BAD96991).
FT CONFLICT 305 305 E -> Q (in Ref. 5; AA sequence).
SQ 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
//
MIM
138150
*RECORD*
*FIELD* NO
138150
*FIELD* TI
*138150 GLUTAMATE OXALOACETATE TRANSAMINASE, MITOCHONDRIAL; GOT2
;;ASPARTATE AMINOTRANSFERASE, MITOCHONDRIAL
read more*FIELD* TX
CLONING
By starch gel electrophoresis, Davidson et al. (1970) demonstrated
polymorphism of mitochondrial glutamate oxaloacetate transaminase (EC
2.6.1.1). In lower animals and plants, many mitochondrial enzymes show
maternal inheritance, indicating that a separate mitochondrial genetic
system is involved in their control. However, family studies showed that
mitochondrial GOT is under the control of nuclear not mitochondrial DNA
(Davidson et al., 1970). GOT2 has substrate and cofactor requirements
very similar to those of cytosolic tyrosine aminotransferase (613018).
Indeed, GOT2 may be responsible for the TAT activity found in
mitochondria (Andersson and Pispa, 1982).
Pol et al. (1988) isolated and sequenced the cDNA of human mitochondrial
aspartate aminotransferase from a human liver cDNA library. Northern
blots showed a single 2.4 kb mRNA band. GOT2 mRNA was detected in
kidney, placenta, stomach, and spleen, as well as in both fetal and
adult liver.
MAPPING
Craig et al. (1978) assigned mitochondrial GOT to chromosome 6 by
somatic cell hybrid studies. The presence of GOT2 was identified by an
anti-GOT-antiserum. The provisional assignment to chromosome 6 was
withdrawn because further study supported assignment to chromosome 16
(Francke and Weitkamp, 1979; Tolley et al., 1980). From combined somatic
cell and family studies, Jeremiah et al. (1982) concluded that the gene
order and map intervals are as follows: pter
PGP:0.25:16qh:0.17:GOT2:0.08:HP qter. From 1 hybrid, 5 subclones were
negative for APRT although positive for GOT2, DIA4 and PGP; APRT is
assigned to 16q12-q22; DIA4 to 16q12-q21; HP to 16q22. That GOT2 is on
16q, not 16p, is supported by the fact that it is 1 of 7 genes that are
on 16 in man and on chromosome 8 in the mouse; others in this group map
to 16q, whereas 16p, which carries the alpha-globin cluster, is
homologous to mouse 11 (Barton et al., 1986).
Pol et al. (1989) used cDNAs corresponding to human liver mitochondrial
aspartate aminotransferase mRNAs as probes to confirm the location of a
gene on chromosome 16, specifically at 16q21. Hybridization was also
observed at 12p13.2-p13.1 and at 2 sites on chromosome 1, 1p33-p32 and
1q25-q31. These may represent pseudogenes.
MOLECULAR GENETICS
Data on gene frequencies of allelic variants were tabulated by
Roychoudhury and Nei (1988).
*FIELD* SA
Chen and Giblett (1971); DeLorenzo and Ruddle (1970); Toyomasu et
al. (1984)
*FIELD* RF
1. Andersson, S. M.; Pispa, J. P.: Purification and properties of
human liver tyrosine aminotransferase. Clin. Chim. Acta 125: 117-123,
1982.
2. Barton, D. E.; Yang-Feng, T. L.; Francke, U.: The human tyrosine
aminotransferase gene mapped to the long arm of chromosome 16 (region
16q22-q24) by somatic cell hybrid analysis and in situ hybridization. Hum.
Genet. 72: 221-224, 1986.
3. Chen, S.-H.; Giblett, E. R.: Genetic variation of soluble glutamic-oxaloacetic
transaminase in man. Am. J. Hum. Genet. 23: 419-424, 1971.
4. Craig, I. W.; Tolley, E.; Bobrow, M.; van Heyningen, V.: Assignment
of a gene necessary for the expression of mitochondrial glutamic-oxaloacetic
transaminase in human-mouse hybrid cells. Cytogenet. Cell Genet. 22:
190-194, 1978.
5. Davidson, R. G.; Cortner, J. A.; Rattazzi, M. C.; Ruddle, F. H.;
Lubs, H. A.: Genetic polymorphisms of human mitochondrial glutamic
oxaloacetic transaminase. Science 169: 391-392, 1970.
6. DeLorenzo, R. J.; Ruddle, F. H.: Glutamate transaminase (GOT)
genetics in mus musculus: linkage, polymorphism, and phenotypes of
the GOT-2 and GOT-1 loci. Biochem. Genet. 4: 259-273, 1970.
7. Francke, U.; Weitkamp, L. R.: Report of the committee on the genetic
constitution of chromosome 6. Cytogenet. Cell Genet. 25: 32-38,
1979.
8. Jeremiah, S. J.; Povey, S.; Burley, M. W.; Kielty, C.; Lee, M.;
Spowart, G.; Corney, G.; Cook, P. J. L.: Mapping studies on human
mitochondrial glutamate oxaloacetate transaminase. Ann. Hum. Genet. 46:
145-152, 1982.
9. Pol, S.; Bousquet-Lemercier, B.; Pave-Preux, M.; Bulle, F.; Passage,
E.; Hanoune, J.; Mattei, M. G.; Barouki, R.: Chromosomal localization
of human aspartate aminotransferase genes by in situ hybridization. Hum.
Genet. 83: 159-164, 1989.
10. 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.
11. Roychoudhury, A. K.; Nei, M.: Human Polymorphic Genes: World
Distribution. New York: Oxford Univ. Press (pub.) 1988.
12. Tolley, E.; van Heyningen, V.; Brown, R.; Bobrow, M.; Craig, I.
W.: Assignment to chromosome 16 of a gene necessary for the expression
of human mitochondrial glutamate oxaloacetate transaminase (aspartate
aminotransferase) (E.C. 2.6.1.1). Biochem. Genet. 18: 947-954, 1980.
13. Toyomasu, T.; Sakakibara, S.; Kagamiyama, H.; Matsumoto, H.:
Genetic polymorphism of mitochondrial glutamate-oxaloacetate transaminase
in Japanese. Hum. Genet. 66: 90-91, 1984.
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
carol: 09/17/2009
pfoster: 2/18/1994
supermim: 3/16/1992
carol: 2/12/1991
carol: 2/4/1991
supermim: 3/20/1990
ddp: 10/27/1989
*RECORD*
*FIELD* NO
138150
*FIELD* TI
*138150 GLUTAMATE OXALOACETATE TRANSAMINASE, MITOCHONDRIAL; GOT2
;;ASPARTATE AMINOTRANSFERASE, MITOCHONDRIAL
read more*FIELD* TX
CLONING
By starch gel electrophoresis, Davidson et al. (1970) demonstrated
polymorphism of mitochondrial glutamate oxaloacetate transaminase (EC
2.6.1.1). In lower animals and plants, many mitochondrial enzymes show
maternal inheritance, indicating that a separate mitochondrial genetic
system is involved in their control. However, family studies showed that
mitochondrial GOT is under the control of nuclear not mitochondrial DNA
(Davidson et al., 1970). GOT2 has substrate and cofactor requirements
very similar to those of cytosolic tyrosine aminotransferase (613018).
Indeed, GOT2 may be responsible for the TAT activity found in
mitochondria (Andersson and Pispa, 1982).
Pol et al. (1988) isolated and sequenced the cDNA of human mitochondrial
aspartate aminotransferase from a human liver cDNA library. Northern
blots showed a single 2.4 kb mRNA band. GOT2 mRNA was detected in
kidney, placenta, stomach, and spleen, as well as in both fetal and
adult liver.
MAPPING
Craig et al. (1978) assigned mitochondrial GOT to chromosome 6 by
somatic cell hybrid studies. The presence of GOT2 was identified by an
anti-GOT-antiserum. The provisional assignment to chromosome 6 was
withdrawn because further study supported assignment to chromosome 16
(Francke and Weitkamp, 1979; Tolley et al., 1980). From combined somatic
cell and family studies, Jeremiah et al. (1982) concluded that the gene
order and map intervals are as follows: pter
PGP:0.25:16qh:0.17:GOT2:0.08:HP qter. From 1 hybrid, 5 subclones were
negative for APRT although positive for GOT2, DIA4 and PGP; APRT is
assigned to 16q12-q22; DIA4 to 16q12-q21; HP to 16q22. That GOT2 is on
16q, not 16p, is supported by the fact that it is 1 of 7 genes that are
on 16 in man and on chromosome 8 in the mouse; others in this group map
to 16q, whereas 16p, which carries the alpha-globin cluster, is
homologous to mouse 11 (Barton et al., 1986).
Pol et al. (1989) used cDNAs corresponding to human liver mitochondrial
aspartate aminotransferase mRNAs as probes to confirm the location of a
gene on chromosome 16, specifically at 16q21. Hybridization was also
observed at 12p13.2-p13.1 and at 2 sites on chromosome 1, 1p33-p32 and
1q25-q31. These may represent pseudogenes.
MOLECULAR GENETICS
Data on gene frequencies of allelic variants were tabulated by
Roychoudhury and Nei (1988).
*FIELD* SA
Chen and Giblett (1971); DeLorenzo and Ruddle (1970); Toyomasu et
al. (1984)
*FIELD* RF
1. Andersson, S. M.; Pispa, J. P.: Purification and properties of
human liver tyrosine aminotransferase. Clin. Chim. Acta 125: 117-123,
1982.
2. Barton, D. E.; Yang-Feng, T. L.; Francke, U.: The human tyrosine
aminotransferase gene mapped to the long arm of chromosome 16 (region
16q22-q24) by somatic cell hybrid analysis and in situ hybridization. Hum.
Genet. 72: 221-224, 1986.
3. Chen, S.-H.; Giblett, E. R.: Genetic variation of soluble glutamic-oxaloacetic
transaminase in man. Am. J. Hum. Genet. 23: 419-424, 1971.
4. Craig, I. W.; Tolley, E.; Bobrow, M.; van Heyningen, V.: Assignment
of a gene necessary for the expression of mitochondrial glutamic-oxaloacetic
transaminase in human-mouse hybrid cells. Cytogenet. Cell Genet. 22:
190-194, 1978.
5. Davidson, R. G.; Cortner, J. A.; Rattazzi, M. C.; Ruddle, F. H.;
Lubs, H. A.: Genetic polymorphisms of human mitochondrial glutamic
oxaloacetic transaminase. Science 169: 391-392, 1970.
6. DeLorenzo, R. J.; Ruddle, F. H.: Glutamate transaminase (GOT)
genetics in mus musculus: linkage, polymorphism, and phenotypes of
the GOT-2 and GOT-1 loci. Biochem. Genet. 4: 259-273, 1970.
7. Francke, U.; Weitkamp, L. R.: Report of the committee on the genetic
constitution of chromosome 6. Cytogenet. Cell Genet. 25: 32-38,
1979.
8. Jeremiah, S. J.; Povey, S.; Burley, M. W.; Kielty, C.; Lee, M.;
Spowart, G.; Corney, G.; Cook, P. J. L.: Mapping studies on human
mitochondrial glutamate oxaloacetate transaminase. Ann. Hum. Genet. 46:
145-152, 1982.
9. Pol, S.; Bousquet-Lemercier, B.; Pave-Preux, M.; Bulle, F.; Passage,
E.; Hanoune, J.; Mattei, M. G.; Barouki, R.: Chromosomal localization
of human aspartate aminotransferase genes by in situ hybridization. Hum.
Genet. 83: 159-164, 1989.
10. 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.
11. Roychoudhury, A. K.; Nei, M.: Human Polymorphic Genes: World
Distribution. New York: Oxford Univ. Press (pub.) 1988.
12. Tolley, E.; van Heyningen, V.; Brown, R.; Bobrow, M.; Craig, I.
W.: Assignment to chromosome 16 of a gene necessary for the expression
of human mitochondrial glutamate oxaloacetate transaminase (aspartate
aminotransferase) (E.C. 2.6.1.1). Biochem. Genet. 18: 947-954, 1980.
13. Toyomasu, T.; Sakakibara, S.; Kagamiyama, H.; Matsumoto, H.:
Genetic polymorphism of mitochondrial glutamate-oxaloacetate transaminase
in Japanese. Hum. Genet. 66: 90-91, 1984.
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
carol: 09/17/2009
pfoster: 2/18/1994
supermim: 3/16/1992
carol: 2/12/1991
carol: 2/4/1991
supermim: 3/20/1990
ddp: 10/27/1989