Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P05202 (AATM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Synonyms:Got-2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.7 Ref.13

Catalytic activity

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. Ref.9 Ref.13

L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate. Ref.9 Ref.13

Cofactor

Pyridoxal phosphate. Ref.13

Subunit structure

Homodimer. Ref.12 Ref.13

Subcellular location

Mitochondrion matrix. Cell membrane Ref.3 Ref.7.

Tissue specificity

Detected in brain (at protein level). Ref.9

Post-translational modification

Acetylation of Lys-296, Lys-345 and Lys-363 is observed in liver mitochondria from fasted mice but not from fed mice.

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
   DomainTransit peptide
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   PTMAcetylation
Nitration
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process2-oxoglutarate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

aspartate biosynthetic process

Inferred from direct assay PubMed 4193185. Source: MGI

aspartate catabolic process

Inferred from electronic annotation. Source: Ensembl

aspartate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

fatty acid transport

Inferred from electronic annotation. Source: Ensembl

glutamate catabolic process to 2-oxoglutarate

Inferred from direct assay PubMed 4193185. Source: MGI

glutamate catabolic process to aspartate

Inferred from direct assay PubMed 4193185. Source: MGI

glutamate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

oxaloacetate metabolic process

Inferred from direct assay PubMed 4193185. Source: MGI

response to ethanol

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentmitochondrial inner membrane

Inferred from direct assay PubMed 12865426. Source: MGI

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity

Inferred from sequence or structural similarity. 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

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
Chain30 – 430401Aspartate aminotransferase, mitochondrial
PRO_0000001216

Sites

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

Amino acid modifications

Modified residue591N6-acetyllysine Ref.11
Modified residue731N6-acetyllysine; alternate Ref.10 Ref.11
Modified residue731N6-succinyllysine; alternate Ref.10
Modified residue821N6-acetyllysine Ref.11
Modified residue901N6-acetyllysine; alternate Ref.11
Modified residue901N6-succinyllysine; alternate Ref.10
Modified residue961Nitrated tyrosine Ref.8
Modified residue1071N6-acetyllysine; alternate Ref.11
Modified residue1071N6-succinyllysine; alternate Ref.10
Modified residue1221N6-acetyllysine; alternate Ref.11
Modified residue1221N6-succinyllysine; alternate Ref.10
Modified residue1591N6-acetyllysine; alternate Ref.10 Ref.11
Modified residue1591N6-succinyllysine; alternate Ref.10
Modified residue1851N6-acetyllysine; alternate Ref.11
Modified residue1851N6-succinyllysine; alternate Ref.10
Modified residue2271N6-succinyllysine Ref.10
Modified residue2341N6-acetyllysine Ref.11
Modified residue2791N6-(pyridoxal phosphate)lysine; alternate By similarity
Modified residue2791N6-acetyllysine; alternate Ref.11
Modified residue2961N6-acetyllysine; alternate Ref.11
Modified residue2961N6-succinyllysine; alternate Ref.10
Modified residue3021N6-acetyllysine Ref.11
Modified residue3091N6-acetyllysine; alternate Ref.11
Modified residue3091N6-succinyllysine; alternate Ref.10
Modified residue3381N6-acetyllysine; alternate Ref.11
Modified residue3381N6-succinyllysine; alternate Ref.10
Modified residue3451N6-acetyllysine Ref.11
Modified residue3631N6-acetyllysine; alternate Ref.11
Modified residue3631N6-succinyllysine; alternate Ref.10
Modified residue3641N6-acetyllysine Ref.11
Modified residue3871N6-acetyllysine Ref.11
Modified residue3961N6-acetyllysine; alternate Ref.11
Modified residue3961N6-succinyllysine; alternate Ref.10
Modified residue4041N6-acetyllysine; alternate Ref.10 Ref.11
Modified residue4041N6-succinyllysine; alternate Ref.10

Experimental info

Sequence conflict681R → G in BAE39800. Ref.4
Sequence conflict1461Q → E in AAB91426. Ref.3
Sequence conflict1531R → G in BAE39800. Ref.4
Sequence conflict3771Q → K in BAE39800. Ref.4
Sequence conflict4211L → I in BAE39800. Ref.4

Secondary structure

................................................................. 430
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05202 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: D590524CA7FFB885

FASTA43047,411
        10         20         30         40         50         60 
MALLHSSRIL SGMAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA FKRDTNSKKM 

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

       130        140        150        160        170        180 
LKSGRFVTVQ TISGTGALRV GASFLQRFFK FSRDVFLPKP SWGNHTPIFR DAGMQLQGYR 

       190        200        210        220        230        240 
YYDPKTCGFD FSGALEDISK IPEQSVLLLH ACAHNPTGVD PRPEQWKEIA SVVKKKNLFA 

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

       310        320        330        340        350        360 
AKRVESQLKI LIRPLYSNPP LNGARIAATI LTSPDLRKQW LQEVKGMADR IISMRTQLVS 

       370        380        390        400        410        420 
NLKKEGSSHN WQHITDQIGM FCFTGLKPEQ VERLTKEFSV YMTKDGRISV AGVTSGNVGY 

       430 
LAHAIHQVTK 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequence analysis of mRNA for mouse aspartate aminotransferase isoenzymes."
Obaru K., Nomiyama H., Shimada K., Nagashima F., Morino Y.
J. Biol. Chem. 261:16976-16983(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structural organization of the mouse mitochondrial aspartate aminotransferase gene."
Tsuzuki T., Obaru K., Setoyama C., Shimada K.
J. Mol. Biol. 198:21-31(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C3H/He.
Tissue: Liver.
[3]"Mitochondrial aspartate aminotransferase: direction of a single protein with two distinct functions to two subcellular sites does not require alternative splicing of the mRNA."
Bradbury M.W., Berk P.D.
Biochem. J. 345:423-427(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
Strain: FVB.
Tissue: Liver.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: BALB/c, C57BL/6J and NOD.
Tissue: Bone marrow macrophage, Cecum, Dendritic cell and Melanocyte.
[5]"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].
Strain: C57BL/6.
Tissue: Brain and Eye.
[6]Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 60-81; 91-122; 126-139; 171-180; 186-200; 280-296; 310-345; 356-363 AND 397-404, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[7]"Mitochondrial aspartate aminotransferase expressed on the surface of 3T3-L1 adipocytes mediates saturable fatty acid uptake."
Zhou S.-L., Stump D., Kiang C.L., Isola L.M., Berk P.D.
Proc. Soc. Exp. Biol. Med. 208:263-270(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"Endogenously nitrated proteins in mouse brain: links to neurodegenerative disease."
Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C., Bigelow D.J.
Biochemistry 45:8009-8022(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[9]"Mitochondrial aspartate aminotransferase: a third kynurenate-producing enzyme in the mammalian brain."
Guidetti P., Amori L., Sapko M.T., Okuno E., Schwarcz R.
J. Neurochem. 102:103-111(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
[10]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73; LYS-159 AND LYS-404, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-73; LYS-90; LYS-107; LYS-122; LYS-159; LYS-185; LYS-227; LYS-296; LYS-309; LYS-338; LYS-363; LYS-396 AND LYS-404, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
[11]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-59; LYS-73; LYS-82; LYS-90; LYS-107; LYS-122; LYS-159; LYS-185; LYS-234; LYS-279; LYS-296; LYS-302; LYS-309; LYS-338; LYS-345; LYS-363; LYS-364; LYS-387; LYS-396 AND LYS-404, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[12]"Structure, expression, and function of kynurenine aminotransferases in human and rodent brains."
Han Q., Cai T., Tagle D.A., Li J.
Cell. Mol. Life Sci. 67:353-368(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 30-430 IN COMPLEX WITH SYNTHETIC INHIBITOR, SUBUNIT.
[13]"Biochemical and structural characterization of mouse mitochondrial aspartate aminotransferase, a newly identified kynurenine aminotransferase-IV."
Han Q., Robinson H., Cai T., Tagle D.A., Li J.
Biosci. Rep. 31:323-332(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 30-430 IN COMPLEX WITH L-KYNURENINE; OXALOACETATE AND PYRIDOXAL PHOSPHATE, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, COFACTOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02622 mRNA. Translation: AAA37264.1.
X06917 expand/collapse EMBL AC list , X06918, X06919, X06920, X06921, X06922, X06923, X06924, X06925, X06926 Genomic DNA. Translation: CAA30015.1.
M37259 expand/collapse EMBL AC list , M37250, M37251, M37252, M37253, M37254, M37255, M37256, M37258 Genomic DNA. Translation: AAA37265.1. Sequence problems.
U82470 mRNA. Translation: AAB91426.1.
AK136556 mRNA. Translation: BAE23042.1.
AK147953 mRNA. Translation: BAE28248.1.
AK149886 mRNA. Translation: BAE29146.1.
AK149926 mRNA. Translation: BAE29171.1.
AK150194 mRNA. Translation: BAE29370.1.
AK152921 mRNA. Translation: BAE31596.1.
AK155075 mRNA. Translation: BAE33029.1.
AK167767 mRNA. Translation: BAE39800.1.
BC089015 mRNA. Translation: AAH89015.1.
BC089341 mRNA. Translation: AAH89341.1.
PIRS01174.
RefSeqNP_034455.1. NM_010325.2.
UniGeneMm.230169.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HLMX-ray2.50A/B/C/D30-430[»]
3PD6X-ray2.40A/B/C/D30-430[»]
3PDBX-ray2.40A/B/C/D30-430[»]
ProteinModelPortalP05202.
SMRP05202. Positions 30-430.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP05202. 5 interactions.
MINTMINT-1859771.

Chemistry

ChEMBLCHEMBL3647.

PTM databases

PhosphoSiteP05202.

Proteomic databases

PaxDbP05202.
PRIDEP05202.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034097; ENSMUSP00000034097; ENSMUSG00000031672.
GeneID14719.
KEGGmmu:14719.
UCSCuc009mzi.1. mouse.

Organism-specific databases

CTD2806.
MGIMGI:95792. Got2.

Phylogenomic databases

eggNOGCOG1448.
GeneTreeENSGT00390000014081.
HOGENOMHOG000185898.
HOVERGENHBG000951.
InParanoidP05202.
KOK14455.
OMARVGAFTM.
OrthoDBEOG74J980.
PhylomeDBP05202.
TreeFamTF300641.

Gene expression databases

BgeeP05202.
GenevestigatorP05202.

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

EvolutionaryTraceP05202.
NextBio286731.
PROP05202.
SOURCESearch...

Entry information

Entry nameAATM_MOUSE
AccessionPrimary (citable) accession number: P05202
Secondary accession number(s): O09188 expand/collapse secondary AC list , Q3TIP6, Q3UD91, Q5HZH5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: April 16, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot