P00505 (AATM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	430 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Lipid transport Transport
Cellular component	Cell membrane Membrane Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	2-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: Compara aspartate catabolic process Inferred from direct assay PubMed 2567216. Source: UniProtKB 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 glutamate catabolic process to 2-oxoglutarate Inferred from electronic annotation. Source: Compara glutamate catabolic process to aspartate Inferred from electronic annotation. Source: Compara glutamate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB oxaloacetate metabolic process Inferred from electronic annotation. Source: Compara response to ethanol Inferred from direct assay Ref.6. Source: UniProtKB
Cellular_component	mitochondrial inner membrane Inferred from electronic annotation. Source: Compara mitochondrial matrix Traceable author statement. Source: Reactome plasma membrane Inferred from direct assay Ref.6. Source: UniProtKB
Molecular_function	L-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: EC kynurenine-oxoglutarate transaminase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 29	29	Mitochondrion Ref.5
	Chain	30 – 430	401	Aspartate aminotransferase, mitochondrial		PRO_0000001215
Sites
	Binding site	65	1	Substrate; via amide nitrogen By similarity
	Binding site	162	1	Substrate By similarity
	Binding site	215	1	Substrate By similarity
	Binding site	407	1	Substrate By similarity
Amino acid modifications
	Modified residue	73	1	N6-acetyllysine Ref.7
	Modified residue	90	1	N6-acetyllysine Ref.7
	Modified residue	94	1	N6-acetyllysine By similarity
	Modified residue	159	1	N6-acetyllysine Ref.7
	Modified residue	185	1	N6-acetyllysine By similarity
	Modified residue	234	1	N6-acetyllysine Ref.7
	Modified residue	279	1	N6-(pyridoxal phosphate)lysine By similarity
	Modified residue	296	1	N6-acetyllysine Ref.7
	Modified residue	309	1	N6-succinyllysine By similarity
	Modified residue	345	1	N6-acetyllysine By similarity
	Modified residue	363	1	N6-acetyllysine By similarity
	Modified residue	396	1	N6-acetyllysine Ref.7
	Modified residue	404	1	N6-acetyllysine Ref.7
Natural variations
	Natural variant	2	1	A → S. Corresponds to variant rs11558171 [ dbSNP | Ensembl ].		VAR_055494
	Natural variant	188	1	G → S. Corresponds to variant rs11076256 [ dbSNP | Ensembl ].		VAR_031710
	Natural variant	346	1	V → G. Ref.1 Ref.5 Corresponds to variant rs30842 [ dbSNP | Ensembl ].		VAR_031711
	Natural variant	428	1	V → A. Ref.4 Corresponds to variant rs17849335 [ dbSNP | Ensembl ].		VAR_031712
Experimental info
	Sequence conflict	110 – 111	2	AE → EA AA sequence Ref.5
	Sequence conflict	255	1	D → N AA sequence Ref.5
	Sequence conflict	258	1	A → T in BAD96991. Ref.2
	Sequence conflict	305	1	E → Q AA sequence Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P00505 [UniParc]. Last modified October 5, 2010. Version 3. Checksum: F559567ABF2DB346	FASTA	430	47,518
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY.
[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.
IPI	IPI00018206.
PIR	XNHUDM. A31873.
RefSeq	NP_002071.2. NM_002080.2.
UniGene	Hs.599470.
3D structure databases
ProteinModelPortal	P00505.
SMR	P00505. Positions 30-430.
ModBase	Search...
Protein-protein interaction databases
IntAct	P00505. 3 interactions.
MINT	MINT-1406848.
STRING	9606.ENSP00000245206.
PTM databases
PhosphoSite	P00505.
Polymorphism databases
DMDM	308153643.
2D gel databases
UCD-2DPAGE	P00505.
Proteomic databases
PaxDb	P00505.
PRIDE	P00505.
Protocols and materials databases
DNASU	2806.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000245206; ENSP00000245206; ENSG00000125166.
GeneID	2806.
KEGG	hsa:2806.
UCSC	uc002eof.1. human.
Organism-specific databases
CTD	2806.
GeneCards	GC16M058741.
H-InvDB	HIX0013095.
HGNC	HGNC:4433. GOT2.
HPA	HPA018139.
MIM	138150. gene.
neXtProt	NX_P00505.
PharmGKB	PA28818.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1448.
HOGENOM	HOG000185898.
HOVERGEN	HBG000951.
InParanoid	P00505.
KO	K14455.
OMA	DFTGAIE.
OrthoDB	EOG4RXZ07.
PhylomeDB	P00505.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	P00505.
Bgee	P00505.
CleanEx	HS_GOT2.
Genevestigator	P00505.
GermOnline	ENSG00000125166. Homo sapiens.
Family and domain databases
Gene3D	3.40.640.10. 1 hit.
InterPro	IPR004839. Aminotransferase_I/II. IPR000796. Asp_trans. IPR004838. NHTrfase_class1_PyrdxlP-BS. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
PANTHER	PTHR11879. PTHR11879. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
PRINTS	PR00799. TRANSAMINASE.
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITE	PS00105. AA_TRANSFER_CLASS_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	Got2. human.
DrugBank	DB00128. L-Aspartic Acid. DB00142. L-Glutamic Acid. DB00114. Pyridoxal Phosphate.
GenomeRNAi	2806.
NextBio	11061.
SOURCE	Search...

Entry information

Entry name

AATM_HUMAN

Accession

Primary (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 3, 2013
This is version 147 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.