Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Aspartate aminotransferase, mitochondrial

Gene

Got2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei65Substrate; via amide nitrogenBy similarity1
Binding sitei162SubstrateBy similarity1
Binding sitei215Substrate1
Binding sitei407Substrate1

GO - Molecular functioni

GO - Biological processi

  • 2-oxoglutarate metabolic process Source: UniProtKB
  • aspartate biosynthetic process Source: MGI
  • aspartate catabolic process Source: MGI
  • aspartate metabolic process Source: UniProtKB
  • fatty acid transport Source: Ensembl
  • glutamate catabolic process to 2-oxoglutarate Source: MGI
  • glutamate catabolic process to aspartate Source: MGI
  • glutamate metabolic process Source: UniProtKB
  • oxaloacetate metabolic process Source: MGI
  • response to ethanol Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi2.6.1.7. 3474.
ReactomeiR-MMU-70263. Gluconeogenesis.
R-MMU-70614. Amino acid synthesis and interconversion (transamination).

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate aminotransferase, mitochondrial (EC:2.6.1.1, EC:2.6.1.7)
Short name:
mAspAT
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 namesi
Name:Got2
Synonyms:Got-2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:95792. Got2.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: Ensembl
  • extracellular exosome Source: MGI
  • mitochondrial inner membrane Source: MGI
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB
  • myelin sheath Source: UniProtKB
  • perikaryon Source: Ensembl
  • plasma membrane Source: MGI
  • protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Mitochondrion

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3647.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 29MitochondrionAdd BLAST29
ChainiPRO_000000121630 – 430Aspartate aminotransferase, mitochondrialAdd BLAST401

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei48PhosphothreonineBy similarity1
Modified residuei59N6-acetyllysineCombined sources1
Modified residuei73N6-acetyllysine; alternateCombined sources1
Modified residuei73N6-succinyllysine; alternateCombined sources1
Modified residuei82N6-acetyllysineCombined sources1
Modified residuei90N6-acetyllysine; alternateCombined sources1
Modified residuei90N6-succinyllysine; alternateCombined sources1
Modified residuei96Nitrated tyrosine; alternateCombined sources1
Modified residuei96Phosphotyrosine; alternateBy similarity1
Modified residuei107N6-acetyllysine; alternateCombined sources1
Modified residuei107N6-succinyllysine; alternateCombined sources1
Modified residuei122N6-acetyllysine; alternateCombined sources1
Modified residuei122N6-succinyllysine; alternateCombined sources1
Modified residuei143PhosphoserineBy similarity1
Modified residuei159N6-acetyllysine; alternateCombined sources1
Modified residuei159N6-succinyllysine; alternateCombined sources1
Modified residuei185N6-acetyllysine; alternateCombined sources1
Modified residuei185N6-succinyllysine; alternateCombined sources1
Modified residuei227N6-succinyllysineCombined sources1
Modified residuei234N6-acetyllysineCombined sources1
Modified residuei279N6-(pyridoxal phosphate)lysine; alternateBy similarity1
Modified residuei279N6-acetyllysine; alternateCombined sources1
Modified residuei296N6-acetyllysine; alternateCombined sources1
Modified residuei296N6-succinyllysine; alternateCombined sources1
Modified residuei302N6-acetyllysineCombined sources1
Modified residuei309N6-acetyllysine; alternateCombined sources1
Modified residuei309N6-succinyllysine; alternateCombined sources1
Modified residuei313Asymmetric dimethylarginineCombined sources1
Modified residuei338N6-acetyllysine; alternateCombined sources1
Modified residuei338N6-succinyllysine; alternateCombined sources1
Modified residuei345N6-acetyllysineCombined sources1
Modified residuei363N6-acetyllysine; alternateCombined sources1
Modified residuei363N6-succinyllysine; alternateCombined sources1
Modified residuei364N6-acetyllysineCombined sources1
Modified residuei387N6-acetyllysineCombined sources1
Modified residuei396N6-acetyllysine; alternateCombined sources1
Modified residuei396N6-succinyllysine; alternateCombined sources1
Modified residuei404N6-acetyllysine; alternateCombined sources1
Modified residuei404N6-succinyllysine; alternateCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Methylation, Nitration, Phosphoprotein

Proteomic databases

EPDiP05202.
MaxQBiP05202.
PaxDbiP05202.
PeptideAtlasiP05202.
PRIDEiP05202.
TopDownProteomicsiP05202.

PTM databases

iPTMnetiP05202.
PhosphoSitePlusiP05202.
SwissPalmiP05202.

Expressioni

Tissue specificityi

Detected in brain (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000031672.
GenevisibleiP05202. MM.

Interactioni

Subunit structurei

Homodimer.2 Publications

GO - Molecular functioni

Protein-protein interaction databases

IntActiP05202. 5 interactors.
MINTiMINT-1859771.
STRINGi10090.ENSMUSP00000034097.

Structurei

Secondary structure

1430
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni32 – 35Combined sources4
Helixi43 – 53Combined sources11
Helixi78 – 89Combined sources12
Helixi103 – 114Combined sources12
Helixi119 – 123Combined sources5
Beta strandi126 – 132Combined sources7
Helixi133 – 148Combined sources16
Beta strandi153 – 160Combined sources8
Helixi165 – 172Combined sources8
Beta strandi175 – 180Combined sources6
Turni184 – 186Combined sources3
Beta strandi187 – 189Combined sources3
Helixi191 – 199Combined sources9
Beta strandi206 – 210Combined sources5
Turni215 – 217Combined sources3
Helixi223 – 235Combined sources13
Beta strandi239 – 245Combined sources7
Turni247 – 251Combined sources5
Helixi254 – 257Combined sources4
Helixi259 – 266Combined sources8
Beta strandi272 – 276Combined sources5
Turni278 – 280Combined sources3
Helixi284 – 286Combined sources3
Beta strandi288 – 294Combined sources7
Helixi298 – 316Combined sources19
Helixi322 – 332Combined sources11
Helixi334 – 364Combined sources31
Helixi373 – 376Combined sources4
Beta strandi379 – 383Combined sources5
Helixi388 – 398Combined sources11
Beta strandi406 – 409Combined sources4
Helixi410 – 412Combined sources3
Turni415 – 417Combined sources3
Helixi418 – 429Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HLMX-ray2.50A/B/C/D30-430[»]
3PD6X-ray2.40A/B/C/D30-430[»]
3PDBX-ray2.40A/B/C/D30-430[»]
ProteinModelPortaliP05202.
SMRiP05202.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05202.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1411. Eukaryota.
COG1448. LUCA.
GeneTreeiENSGT00390000014081.
HOGENOMiHOG000185898.
HOVERGENiHBG000951.
InParanoidiP05202.
KOiK14455.
OMAiWANHAAV.
OrthoDBiEOG091G06G3.
PhylomeDBiP05202.
TreeFamiTF300641.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11879. PTHR11879. 1 hit.
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSiPR00799. TRANSAMINASE.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05202-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLHSSRIL SGMAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA
60 70 80 90 100
FKRDTNSKKM NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK NLDKEYLPIG
110 120 130 140 150
GLAEFCKASA ELALGENNEV LKSGRFVTVQ TISGTGALRV GASFLQRFFK
160 170 180 190 200
FSRDVFLPKP SWGNHTPIFR DAGMQLQGYR YYDPKTCGFD FSGALEDISK
210 220 230 240 250
IPEQSVLLLH ACAHNPTGVD PRPEQWKEIA SVVKKKNLFA FFDMAYQGFA
260 270 280 290 300
SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTVVCKDAEE
310 320 330 340 350
AKRVESQLKI LIRPLYSNPP LNGARIAATI LTSPDLRKQW LQEVKGMADR
360 370 380 390 400
IISMRTQLVS NLKKEGSSHN WQHITDQIGM FCFTGLKPEQ VERLTKEFSV
410 420 430
YMTKDGRISV AGVTSGNVGY LAHAIHQVTK
Length:430
Mass (Da):47,411
Last modified:August 13, 1987 - v1
Checksum:iD590524CA7FFB885
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti68R → G in BAE39800 (PubMed:16141072).Curated1
Sequence conflicti146Q → E in AAB91426 (PubMed:10642497).Curated1
Sequence conflicti153R → G in BAE39800 (PubMed:16141072).Curated1
Sequence conflicti377Q → K in BAE39800 (PubMed:16141072).Curated1
Sequence conflicti421L → I in BAE39800 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02622 mRNA. Translation: AAA37264.1.
X06917
, X06918, X06919, X06920, X06921, X06922, X06923, X06924, X06925, X06926 Genomic DNA. Translation: CAA30015.1.
M37259
, 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.
CCDSiCCDS22568.1.
PIRiS01174.
RefSeqiNP_034455.1. NM_010325.2.
UniGeneiMm.230169.

Genome annotation databases

EnsembliENSMUST00000034097; ENSMUSP00000034097; ENSMUSG00000031672.
GeneIDi14719.
KEGGimmu:14719.
UCSCiuc009mzi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02622 mRNA. Translation: AAA37264.1.
X06917
, X06918, X06919, X06920, X06921, X06922, X06923, X06924, X06925, X06926 Genomic DNA. Translation: CAA30015.1.
M37259
, 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.
CCDSiCCDS22568.1.
PIRiS01174.
RefSeqiNP_034455.1. NM_010325.2.
UniGeneiMm.230169.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HLMX-ray2.50A/B/C/D30-430[»]
3PD6X-ray2.40A/B/C/D30-430[»]
3PDBX-ray2.40A/B/C/D30-430[»]
ProteinModelPortaliP05202.
SMRiP05202.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP05202. 5 interactors.
MINTiMINT-1859771.
STRINGi10090.ENSMUSP00000034097.

Chemistry databases

ChEMBLiCHEMBL3647.

PTM databases

iPTMnetiP05202.
PhosphoSitePlusiP05202.
SwissPalmiP05202.

Proteomic databases

EPDiP05202.
MaxQBiP05202.
PaxDbiP05202.
PeptideAtlasiP05202.
PRIDEiP05202.
TopDownProteomicsiP05202.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034097; ENSMUSP00000034097; ENSMUSG00000031672.
GeneIDi14719.
KEGGimmu:14719.
UCSCiuc009mzi.1. mouse.

Organism-specific databases

CTDi2806.
MGIiMGI:95792. Got2.

Phylogenomic databases

eggNOGiKOG1411. Eukaryota.
COG1448. LUCA.
GeneTreeiENSGT00390000014081.
HOGENOMiHOG000185898.
HOVERGENiHBG000951.
InParanoidiP05202.
KOiK14455.
OMAiWANHAAV.
OrthoDBiEOG091G06G3.
PhylomeDBiP05202.
TreeFamiTF300641.

Enzyme and pathway databases

BRENDAi2.6.1.7. 3474.
ReactomeiR-MMU-70263. Gluconeogenesis.
R-MMU-70614. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

EvolutionaryTraceiP05202.
PROiP05202.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031672.
GenevisibleiP05202. MM.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11879. PTHR11879. 1 hit.
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSiPR00799. TRANSAMINASE.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAATM_MOUSE
AccessioniPrimary (citable) accession number: P05202
Secondary accession number(s): O09188
, Q3TIP6, Q3UD91, Q5HZH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: November 2, 2016
This is version 161 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.