Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00087
Entry Name
UniProt Accession
Theoretical PI
9.13
Molecular Weight
47411.38
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Aspartate aminotransferase, mitochondrial
Protein Synonyms/Alias
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;
Gene Name
Got2
Gene Synonyms/Alias
Got-2;
Created Date
13-AUG-1987
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
272
Canonical
IEQGINVCLCQSYAK
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Predicted from GPS-Lipid
Functional Description
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.
Sequence Annotation
Binding site: 65 65 Substrate; via amide nitrogen.
Binding site: 162 162 Substrate.
Binding site: 215 215 Substrate.
Binding site: 407 407 Substrate.
Modified residue: 59 59 N6-acetyllysine.
Modified residue: 73 73 N6-acetyllysine; alternate.
Modified residue: 73 73 N6-succinyllysine; alternate.
Modified residue: 82 82 N6-acetyllysine.
Modified residue: 90 90 N6-acetyllysine; alternate.
Modified residue: 90 90 N6-succinyllysine; alternate.
Modified residue: 96 96 Nitrated tyrosine.
Modified residue: 107 107 N6-acetyllysine; alternate.
Modified residue: 107 107 N6-succinyllysine; alternate.
Modified residue: 122 122 N6-acetyllysine; alternate.
Modified residue: 122 122 N6-succinyllysine; alternate.
Modified residue: 159 159 N6-acetyllysine; alternate.
Modified residue: 159 159 N6-succinyllysine; alternate.
Modified residue: 185 185 N6-acetyllysine; alternate.
Modified residue: 185 185 N6-succinyllysine; alternate.
Modified residue: 227 227 N6-succinyllysine.
Modified residue: 234 234 N6-acetyllysine.
Modified residue: 279 279 N6-(pyridoxal phosphate)lysine;alternate.
Modified residue: 279 279 N6-acetyllysine; alternate.
Modified residue: 296 296 N6-acetyllysine; alternate.
Modified residue: 296 296 N6-succinyllysine; alternate.
Modified residue: 302 302 N6-acetyllysine.
Modified residue: 309 309 N6-acetyllysine; alternate.
Modified residue: 309 309 N6-succinyllysine; alternate.
Modified residue: 338 338 N6-acetyllysine; alternate.
Modified residue: 338 338 N6-succinyllysine; alternate.
Modified residue: 345 345 N6-acetyllysine.
Modified residue: 363 363 N6-acetyllysine; alternate.
Modified residue: 363 363 N6-succinyllysine; alternate.
Modified residue: 364 364 N6-acetyllysine.
Modified residue: 387 387 N6-acetyllysine.
Modified residue: 396 396 N6-acetyllysine; alternate.
Modified residue: 396 396 N6-succinyllysine; alternate.
Modified residue: 404 404 N6-acetyllysine; alternate.
Modified residue: 404 404 N6-succinyllysine; alternate.
Protein Length
430 AA.
Protein Sequence
(Canonical)
MALLHSSRIL SGMAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA FKRDTNSKKM  60
NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK NLDKEYLPIG GLAEFCKASA ELALGENNEV  120
LKSGRFVTVQ TISGTGALRV GASFLQRFFK FSRDVFLPKP SWGNHTPIFR DAGMQLQGYR  180
YYDPKTCGFD FSGALEDISK IPEQSVLLLH ACAHNPTGVD PRPEQWKEIA SVVKKKNLFA  240
FFDMAYQGFA SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTVVCKDAEE  300
AKRVESQLKI LIRPLYSNPP LNGARIAATI LTSPDLRKQW LQEVKGMADR IISMRTQLVS  360
NLKKEGSSHN WQHITDQIGM FCFTGLKPEQ VERLTKEFSV YMTKDGRISV AGVTSGNVGY  420
LAHAIHQVTK                                                         430
FASTA
(Canonical)
>LipidDB-10090-00087|P05202
MALLHSSRILSGMAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKM
NLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENNEV
LKSGRFVTVQTISGTGALRVGASFLQRFFKFSRDVFLPKPSWGNHTPIFRDAGMQLQGYR
YYDPKTCGFDFSGALEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIASVVKKKNLFA
FFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTVVCKDAEE
AKRVESQLKILIRPLYSNPPLNGARIAATILTSPDLRKQWLQEVKGMADRIISMRTQLVS
NLKKEGSSHNWQHITDQIGMFCFTGLKPEQVERLTKEFSVYMTKDGRISVAGVTSGNVGY
LAHAIHQVTK
Gene Ontology
GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl
GO:0005743; C:mitochondrial inner membrane; IDA:MGI
GO:0005739; C:mitochondrion; ISS:UniProtKB
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW
GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IEA:UniProtKB-EC
GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; ISS:UniProtKB
GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC
GO:0044822; F:poly(A) RNA binding; IEA:Ensembl
GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro
GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB
GO:0006532; P:aspartate biosynthetic process; IDA:MGI
GO:0006533; P:aspartate catabolic process; IEA:Ensembl
GO:0006531; P:aspartate metabolic process; ISS:UniProtKB
GO:0015908; P:fatty acid transport; IEA:Ensembl
GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IDA:MGI
GO:0019550; P:glutamate catabolic process to aspartate; IDA:MGI
GO:0006536; P:glutamate metabolic process; ISS:UniProtKB
GO:0006107; P:oxaloacetate metabolic process; IDA:MGI
GO:0045471; P:response to ethanol; IEA:Ensembl
Interpro
InterPro; IPR004839; Aminotransferase_I/II
InterPro; IPR000796; Asp_trans
InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS
InterPro; IPR015424; PyrdxlP-dep_Trfase
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1
Pfam
Pfam; PF00155; Aminotran_1_2;
SMART
PROSITE
PROSITE; PS00105; AA_TRANSFER_CLASS_1;
PRINTS
PRINTS; PR00799; TRANSAMINASE;