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P00505 (AATM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aspartate aminotransferase, mitochondrial

Short name=mAspAT
EC=2.6.1.1
EC=2.6.1.7
Alternative name(s):
Fatty acid-binding protein
Short name=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
Short name=FABPpm
Transaminase A
Gene names
Name:GOT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. Facilitates cellular uptake of long-chain free fatty acids. Ref.6

Catalytic activity

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.

L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.

Cofactor

Pyridoxal phosphate.

Subunit structure

Homodimer.

Subcellular location

Mitochondrion matrix. Cell membrane. Note: Exposure to alcohol promotes translocation to the cell membrane. Ref.6

Induction

Up-regulated by long-time exposure to alcohol. Ref.6

Miscellaneous

In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
   Biological processLipid transport
Transport
   Cellular componentCell membrane
Membrane
Mitochondrion
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   PTMAcetylation
Nitration
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process2-oxoglutarate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

4-hydroxyproline catabolic process

Traceable author statement PubMed 21998747. Source: BHF-UCL

aspartate biosynthetic process

Inferred from electronic annotation. Source: Ensembl

aspartate catabolic process

Inferred from direct assay PubMed 2567216. Source: UniProtKB

aspartate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

carbohydrate metabolic process

Traceable author statement. Source: Reactome

cellular amino acid biosynthetic process

Traceable author statement. Source: Reactome

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

fatty acid transport

Inferred from expression pattern Ref.6. Source: UniProtKB

gluconeogenesis

Traceable author statement. Source: Reactome

glucose metabolic process

Traceable author statement. Source: Reactome

glutamate catabolic process to 2-oxoglutarate

Inferred from electronic annotation. Source: Ensembl

glutamate catabolic process to aspartate

Inferred from electronic annotation. Source: Ensembl

glutamate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

oxaloacetate metabolic process

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from direct assay Ref.6. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentextracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

mitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrion

Inferred from direct assay Ref.6. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity

Inferred from direct assay PubMed 2182221PubMed 2567216PubMed 2731362. Source: UniProtKB

L-phenylalanine:2-oxoglutarate aminotransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

kynurenine-oxoglutarate transaminase activity

Inferred from electronic annotation. Source: UniProtKB-EC

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2929Mitochondrion Ref.5
Chain30 – 430401Aspartate aminotransferase, mitochondrial
PRO_0000001215

Sites

Binding site651Substrate; via amide nitrogen By similarity
Binding site1621Substrate By similarity
Binding site2151Substrate By similarity
Binding site4071Substrate By similarity

Amino acid modifications

Modified residue591N6-acetyllysine By similarity
Modified residue731N6-acetyllysine; alternate Ref.7
Modified residue731N6-succinyllysine; alternate By similarity
Modified residue821N6-acetyllysine By similarity
Modified residue901N6-acetyllysine; alternate Ref.7
Modified residue901N6-succinyllysine; alternate By similarity
Modified residue961Nitrated tyrosine By similarity
Modified residue1071N6-acetyllysine; alternate By similarity
Modified residue1071N6-succinyllysine; alternate By similarity
Modified residue1221N6-acetyllysine; alternate By similarity
Modified residue1221N6-succinyllysine; alternate By similarity
Modified residue1591N6-acetyllysine; alternate Ref.7
Modified residue1591N6-succinyllysine; alternate By similarity
Modified residue1851N6-acetyllysine; alternate By similarity
Modified residue1851N6-succinyllysine; alternate By similarity
Modified residue2271N6-succinyllysine By similarity
Modified residue2341N6-acetyllysine Ref.7
Modified residue2791N6-(pyridoxal phosphate)lysine; alternate By similarity
Modified residue2791N6-acetyllysine; alternate By similarity
Modified residue2961N6-acetyllysine; alternate Ref.7
Modified residue2961N6-succinyllysine; alternate By similarity
Modified residue3021N6-acetyllysine By similarity
Modified residue3091N6-acetyllysine; alternate By similarity
Modified residue3091N6-succinyllysine; alternate By similarity
Modified residue3381N6-acetyllysine; alternate By similarity
Modified residue3381N6-succinyllysine; alternate By similarity
Modified residue3451N6-acetyllysine By similarity
Modified residue3631N6-acetyllysine; alternate By similarity
Modified residue3631N6-succinyllysine; alternate By similarity
Modified residue3641N6-acetyllysine By similarity
Modified residue3871N6-acetyllysine By similarity
Modified residue3961N6-acetyllysine; alternate Ref.7
Modified residue3961N6-succinyllysine; alternate By similarity
Modified residue4041N6-acetyllysine; alternate Ref.7
Modified residue4041N6-succinyllysine; alternate By similarity

Natural variations

Natural variant21A → S.
Corresponds to variant rs11558171 [ dbSNP | Ensembl ].
VAR_055494
Natural variant1881G → S.
Corresponds to variant rs11076256 [ dbSNP | Ensembl ].
VAR_031710
Natural variant3461V → G. Ref.1 Ref.5
Corresponds to variant rs30842 [ dbSNP | Ensembl ].
VAR_031711
Natural variant4281V → A. Ref.4
Corresponds to variant rs17849335 [ dbSNP | Ensembl ].
VAR_031712

Experimental info

Sequence conflict110 – 1112AE → EA AA sequence Ref.5
Sequence conflict2551D → N AA sequence Ref.5
Sequence conflict2581A → T in BAD96991. Ref.2
Sequence conflict3051E → Q AA sequence Ref.5

Sequences

Sequence LengthMass (Da)Tools
P00505 [UniParc].

Last modified October 5, 2010. Version 3.
Checksum: F559567ABF2DB346

FASTA43047,518
        10         20         30         40         50         60 
MALLHSGRVL PGIAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA FKRDTNSKKM 

        70         80         90        100        110        120 
NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK NLDKEYLPIG GLAEFCKASA ELALGENSEV 

       130        140        150        160        170        180 
LKSGRFVTVQ TISGTGALRI GASFLQRFFK FSRDVFLPKP TWGNHTPIFR DAGMQLQGYR 

       190        200        210        220        230        240 
YYDPKTCGFD FTGAVEDISK IPEQSVLLLH ACAHNPTGVD PRPEQWKEIA TVVKKRNLFA 

       250        260        270        280        290        300 
FFDMAYQGFA SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTMVCKDADE 

       310        320        330        340        350        360 
AKRVESQLKI LIRPMYSNPP LNGARIAAAI LNTPDLRKQW LQEVKVMADR IIGMRTQLVS 

       370        380        390        400        410        420 
NLKKEGSTHN WQHITDQIGM FCFTGLKPEQ VERLIKEFSI YMTKDGRISV AGVTSSNVGY 

       430 
LAHAIHQVTK 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence and tissue distribution of the human mitochondrial aspartate aminotransferase mRNA."
Pol S., Bousquet-Lemercier B., Pave-Preux M., Pawlak A., Nalpas B., Berthelot P., Hanoune J., Barouki R.
Biochem. Biophys. Res. Commun. 157:1309-1315(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-346.
[2]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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Gastric mucosa.
[3]"The sequence and analysis of duplication-rich human chromosome 16."
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. expand/collapse author list , 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.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-428.
Tissue: Muscle.
[5]"The primary structure of mitochondrial aspartate aminotransferase from human heart."
Martini F., Angelaccio S., Barra D., Pascarella S., Maras B., Doonan S., Bossa F.
Biochim. Biophys. Acta 832:46-51(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 30-430, VARIANT GLY-346.
[6]"Ethanol up-regulates fatty acid uptake and plasma membrane expression and export of mitochondrial aspartate aminotransferase in HepG2 cells."
Zhou S.L., Gordon R.E., Bradbury M., Stump D., Kiang C.L., Berk P.D.
Hepatology 27:1064-1074(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION, SUBCELLULAR LOCATION.
[7]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73; LYS-90; LYS-159; LYS-234; LYS-296; LYS-396 AND LYS-404, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M22632 mRNA. Translation: AAA35568.1.
AK223271 mRNA. Translation: BAD96991.1.
BC000525 mRNA. Translation: AAH00525.1.
PIRXNHUDM. A31873.
RefSeqNP_001273149.1. NM_001286220.1.
NP_002071.2. NM_002080.3.
UniGeneHs.599470.

3D structure databases

ProteinModelPortalP00505.
SMRP00505. Positions 30-430.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109068. 13 interactions.
IntActP00505. 7 interactions.
MINTMINT-1406848.
STRING9606.ENSP00000245206.

Chemistry

DrugBankDB00128. L-Aspartic Acid.
DB00142. L-Glutamic Acid.
DB00114. Pyridoxal Phosphate.

PTM databases

PhosphoSiteP00505.

Polymorphism databases

DMDM308153643.

2D gel databases

UCD-2DPAGEP00505.

Proteomic databases

PaxDbP00505.
PRIDEP00505.

Protocols and materials databases

DNASU2806.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000245206; ENSP00000245206; ENSG00000125166.
GeneID2806.
KEGGhsa:2806.
UCSCuc002eof.1. human.

Organism-specific databases

CTD2806.
GeneCardsGC16M058741.
H-InvDBHIX0013095.
HGNCHGNC:4433. GOT2.
HPAHPA018139.
MIM138150. gene.
neXtProtNX_P00505.
PharmGKBPA28818.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1448.
HOGENOMHOG000185898.
HOVERGENHBG000951.
InParanoidP00505.
KOK14455.
OMARVGAFTM.
OrthoDBEOG74J980.
PhylomeDBP00505.
TreeFamTF300641.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP00505.
BgeeP00505.
CleanExHS_GOT2.
GenevestigatorP00505.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
InterProIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERPTHR11879. PTHR11879. 1 hit.
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSPR00799. TRANSAMINASE.
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGot2. human.
GeneWikiGOT2.
GenomeRNAi2806.
NextBio11061.
PROP00505.
SOURCESearch...

Entry information

Entry nameAATM_HUMAN
AccessionPrimary (citable) accession number: P00505
Secondary accession number(s): Q53FL3, Q9BWA3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 5, 2010
Last modified: April 16, 2014
This is version 155 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM