Got2

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

Miscellaneous

In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.

Catalytic activityⁱ

2-oxoglutarate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
L-aspartate
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
L-glutamate
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
oxaloacetate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
EC:2.6.1.1
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
2-oxoglutarate
zoom
+
L-aspartate
zoom
=
L-glutamate
zoom
+
oxaloacetate
zoom
2-oxoglutarate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
L-kynurenine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
4-(2-aminophenyl)-2,4-dioxobutanoate
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
L-glutamate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
EC:2.6.1.7
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
2-oxoglutarate
zoom
+
L-kynurenine
zoom
=
4-(2-aminophenyl)-2,4-dioxobutanoate
zoom
+
L-glutamate
zoom

Cofactorⁱ

pyridoxal 5'-phosphate1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	65	Substrate; via amide nitrogenBy similarity	1
Binding siteⁱ	162	SubstrateBy similarity	1
Binding siteⁱ	215	Substrate	1
Binding siteⁱ	407	Substrate	1

GO - Molecular functionⁱ

amino acid binding Source: MGI
carboxylic acid binding Source: MGI
enzyme binding Source: MGI
kynurenine-oxoglutarate transaminase activity Source: UniProtKB-EC
L-aspartate:2-oxoglutarate aminotransferase activity
Source: MGI
Inferred from direct assayⁱ
phospholipid binding Source: MGI
protein homodimerization activity Source: MGI
pyridoxal phosphate binding Source: MGI

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

2-oxoglutarate metabolic process Source: UniProtKB
aspartate biosynthetic process
Source: MGI
Inferred from direct assayⁱ
- 4193185
aspartate catabolic process Source: MGI
aspartate metabolic process Source: UniProtKB
cellular amino acid metabolic process Source: MGI
dicarboxylic acid metabolic process Source: MGI
fatty acid transport Source: Ensembl
female pregnancy Source: Ensembl
glutamate catabolic process to 2-oxoglutarate
Source: MGI
Inferred from direct assayⁱ
- 4193185
glutamate catabolic process to aspartate
Source: MGI
Inferred from direct assayⁱ
- 4193185
glutamate metabolic process Source: UniProtKB
lactation Source: Ensembl
oxaloacetate metabolic process
Source: MGI
Inferred from direct assayⁱ
- 4193185
response to ethanol Source: MGI
response to insulin Source: Ensembl
response to morphine Source: Ensembl
response to muscle activity Source: Ensembl

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Aminotransferase, Transferase
Biological process	Lipid transport, Transport
Ligand	Pyridoxal phosphate

Enzyme and pathway databases

BRENDAⁱ	2.6.1.7 3474
Reactomeⁱ	R-MMU-389661 Glyoxylate metabolism and glycine degradation R-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
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 8

Organism-specific databases

MGIⁱ	MGI:95792 Got2

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Cell membrane, Membrane, Mitochondrion

Pathology & Biotechⁱ

Chemistry databases

ChEMBLⁱ	CHEMBL3647

ChEMBLⁱ

CHEMBL3647

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transit peptideⁱ	1 – 29	MitochondrionAdd BLAST		29
ChainⁱPRO_0000001216	30 – 430	Aspartate aminotransferase, mitochondrialAdd BLAST		401

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	48	PhosphothreonineBy similarity	1
Modified residueⁱ	59	N6-acetyllysineCombined sources	1
Modified residueⁱ	73	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	73	N6-succinyllysine; alternateCombined sources	1
Modified residueⁱ	82	N6-acetyllysineCombined sources	1
Modified residueⁱ	90	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	90	N6-succinyllysine; alternateCombined sources	1
Modified residueⁱ	96	Nitrated tyrosine; alternateCombined sources	1
Modified residueⁱ	96	Phosphotyrosine; alternateBy similarity	1
Modified residueⁱ	107	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	107	N6-succinyllysine; alternateCombined sources	1
Modified residueⁱ	122	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	122	N6-succinyllysine; alternateCombined sources	1
Modified residueⁱ	143	PhosphoserineBy similarity	1
Modified residueⁱ	159	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	159	N6-succinyllysine; alternateCombined sources	1
Modified residueⁱ	185	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	185	N6-succinyllysine; alternateCombined sources	1
Modified residueⁱ	227	N6-succinyllysineCombined sources	1
Modified residueⁱ	234	N6-acetyllysineCombined sources	1
Modified residueⁱ	279	N6-(pyridoxal phosphate)lysine; alternateBy similarity	1
Modified residueⁱ	279	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	296	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	296	N6-succinyllysine; alternateCombined sources	1
Modified residueⁱ	302	N6-acetyllysineCombined sources	1
Modified residueⁱ	309	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	309	N6-succinyllysine; alternateCombined sources	1
Modified residueⁱ	313	Asymmetric dimethylarginineCombined sources	1
Modified residueⁱ	338	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	338	N6-succinyllysine; alternateCombined sources	1
Modified residueⁱ	345	N6-acetyllysineCombined sources	1
Modified residueⁱ	363	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	363	N6-succinyllysine; alternateCombined sources	1
Modified residueⁱ	364	N6-acetyllysineCombined sources	1
Modified residueⁱ	387	N6-acetyllysineCombined sources	1
Modified residueⁱ	396	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	396	N6-succinyllysine; alternateCombined sources	1
Modified residueⁱ	404	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	404	N6-succinyllysine; alternateCombined sources	1

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

EPDⁱ	P05202
jPOSTⁱ	P05202
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P05202
PaxDbⁱ	P05202
PeptideAtlas More...PeptideAtlasⁱ	P05202
PRIDEⁱ	P05202
TopDownProteomicsⁱ	P05202

PTM databases

iPTMnetⁱ	P05202
PhosphoSitePlusⁱ	P05202
SwissPalmⁱ	P05202

Expressionⁱ

Tissue specificityⁱ

Detected in brain (at protein level).1 Publication

Gene expression databases

Bgeeⁱ	ENSMUSG00000031672 Expressed in 114 organ(s), highest expression level in heart
Genevisibleⁱ	P05202 MM

Interactionⁱ

Subunit structureⁱ

Homodimer.2 Publications

GO - Molecular functionⁱ

enzyme binding Source: MGI
protein homodimerization activity Source: MGI

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

IntActⁱ	P05202, 8 interactors
Molecular INTeraction database More...MINTⁱ	P05202
STRINGⁱ	10090.ENSMUSP00000034097

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Turnⁱ	32 – 35	Combined sources	4
Helixⁱ	43 – 53	Combined sources	11
Helixⁱ	78 – 89	Combined sources	12
Helixⁱ	103 – 114	Combined sources	12
Helixⁱ	119 – 123	Combined sources	5
Beta strandⁱ	126 – 132	Combined sources	7
Helixⁱ	133 – 148	Combined sources	16
Beta strandⁱ	153 – 160	Combined sources	8
Helixⁱ	165 – 172	Combined sources	8
Beta strandⁱ	175 – 180	Combined sources	6
Turnⁱ	184 – 186	Combined sources	3
Beta strandⁱ	187 – 189	Combined sources	3
Helixⁱ	191 – 199	Combined sources	9
Beta strandⁱ	206 – 210	Combined sources	5
Turnⁱ	215 – 217	Combined sources	3
Helixⁱ	223 – 235	Combined sources	13
Beta strandⁱ	239 – 245	Combined sources	7
Turnⁱ	247 – 251	Combined sources	5
Helixⁱ	254 – 257	Combined sources	4
Helixⁱ	259 – 266	Combined sources	8
Beta strandⁱ	272 – 276	Combined sources	5
Turnⁱ	278 – 280	Combined sources	3
Helixⁱ	284 – 286	Combined sources	3
Beta strandⁱ	288 – 294	Combined sources	7
Helixⁱ	298 – 316	Combined sources	19
Helixⁱ	322 – 332	Combined sources	11
Helixⁱ	334 – 364	Combined sources	31
Helixⁱ	373 – 376	Combined sources	4
Beta strandⁱ	379 – 383	Combined sources	5
Helixⁱ	388 – 398	Combined sources	11
Beta strandⁱ	406 – 409	Combined sources	4
Helixⁱ	410 – 412	Combined sources	3
Turnⁱ	415 – 417	Combined sources	3
Helixⁱ	418 – 429	Combined sources	12

Show more details

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	3HLM	X-ray	2.50	A/B/C/D	30-430	[»]
	3PD6	X-ray	2.40	A/B/C/D	30-430	[»]
	3PDB	X-ray	2.40	A/B/C/D	30-430	[»]
ProteinModelPortalⁱ	P05202
SMRⁱ	P05202
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P05202

Family & Domainsⁱ

Sequence similaritiesⁱ

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

Keywords - Domainⁱ

Transit peptide

Phylogenomic databases

eggNOGⁱ	KOG1411 Eukaryota COG1448 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000014081
HOGENOMⁱ	HOG000185898
HOVERGENⁱ	HBG000951
InParanoidⁱ	P05202
KEGG Orthology (KO) More...KOⁱ	K14455
OMAⁱ	RDTNPKK
Database of Orthologous Groups More...OrthoDBⁱ	1104596at2759
PhylomeDBⁱ	P05202
TreeFamⁱ	TF300641

Family and domain databases

Gene3Dⁱ	3.40.640.10, 1 hit 3.90.1150.10, 1 hit
InterProⁱ	View protein in InterPro IPR004839 Aminotransferase_I/II IPR000796 Asp_trans IPR004838 NHTrfase_class1_PyrdxlP-BS IPR015424 PyrdxlP-dep_Trfase IPR015422 PyrdxlP-dep_Trfase_dom1 IPR015421 PyrdxlP-dep_Trfase_major
PANTHERⁱ	PTHR11879 PTHR11879, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00155 Aminotran_1_2, 1 hit
PRINTSⁱ	PR00799 TRANSAMINASE
SUPFAMⁱ	SSF53383 SSF53383, 1 hit
PROSITEⁱ	View protein in PROSITE PS00105 AA_TRANSFER_CLASS_1, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P05202-1 [UniParc]FASTA Add 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 key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	68	R → G in BAE39800 (PubMed:16141072).Curated	1
Sequence conflictⁱ	146	Q → E in AAB91426 (PubMed:10642497).Curated	1
Sequence conflictⁱ	153	R → G in BAE39800 (PubMed:16141072).Curated	1
Sequence conflictⁱ	377	Q → K in BAE39800 (PubMed:16141072).Curated	1
Sequence conflictⁱ	421	L → I in BAE39800 (PubMed:16141072).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J02622 mRNA Translation: AAA37264.1 X06917 X06926 Genomic DNA Translation: CAA30015.1 M37259 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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS22568.1
PIRⁱ	S01174
NCBI Reference Sequences More...RefSeqⁱ	NP_034455.1, NM_010325.2
UniGeneⁱ	Mm.230169

Genome annotation databases

Ensemblⁱ	ENSMUST00000034097; ENSMUSP00000034097; ENSMUSG00000031672
GeneIDⁱ	14719
KEGGⁱ	mmu:14719
UCSC genome browser More...UCSCⁱ	uc009mzi.1 mouse

Protein	Similar proteins		Species	Score	Length	Source
P05202	Aspartate aminotransferase, mitochondrial	)	HUMAN		430	UniRef90_P00505
Aspartate aminotransferase, mitochondrial		RAT		430
Aspartate aminotransferase		PANTR		430
Aspartate aminotransferase		GORGO		430
Aspartate aminotransferase		AILME		430
+139

Protein	Similar proteins		Species	Score	Length	Source
P05202	Aspartate aminotransferase, mitochondrial	)	HUMAN		430	UniRef50_P00505
Aspartate aminotransferase		NEOSC		430
Aspartate aminotransferase		FELCA		430
Aspartate aminotransferase		BALAS		430
Aspartate aminotransferase		SHEEP		430
+293

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J02622 mRNA Translation: AAA37264.1 X06917 X06926 Genomic DNA Translation: CAA30015.1 M37259 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
CCDSⁱ	CCDS22568.1
PIRⁱ	S01174
RefSeqⁱ	NP_034455.1, NM_010325.2
UniGeneⁱ	Mm.230169

3D structure databases

Select the link destinations: PDBeⁱ RCSB PDBⁱ PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	3HLM	X-ray	2.50	A/B/C/D	30-430	[»]
	3PD6	X-ray	2.40	A/B/C/D	30-430	[»]
	3PDB	X-ray	2.40	A/B/C/D	30-430	[»]
ProteinModelPortalⁱ	P05202
SMRⁱ	P05202
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

IntActⁱ	P05202, 8 interactors
MINTⁱ	P05202
STRINGⁱ	10090.ENSMUSP00000034097

Chemistry databases

ChEMBLⁱ	CHEMBL3647

ChEMBLⁱ

CHEMBL3647

PTM databases

iPTMnetⁱ	P05202
PhosphoSitePlusⁱ	P05202
SwissPalmⁱ	P05202

Proteomic databases

EPDⁱ	P05202
jPOSTⁱ	P05202
MaxQBⁱ	P05202
PaxDbⁱ	P05202
PeptideAtlasⁱ	P05202
PRIDEⁱ	P05202
TopDownProteomicsⁱ	P05202

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSMUST00000034097; ENSMUSP00000034097; ENSMUSG00000031672
GeneIDⁱ	14719
KEGGⁱ	mmu:14719
UCSCⁱ	uc009mzi.1 mouse

Organism-specific databases

CTDⁱ	2806
MGIⁱ	MGI:95792 Got2

Phylogenomic databases

eggNOGⁱ	KOG1411 Eukaryota COG1448 LUCA
GeneTreeⁱ	ENSGT00390000014081
HOGENOMⁱ	HOG000185898
HOVERGENⁱ	HBG000951
InParanoidⁱ	P05202
KOⁱ	K14455
OMAⁱ	RDTNPKK
OrthoDBⁱ	1104596at2759
PhylomeDBⁱ	P05202
TreeFamⁱ	TF300641

Enzyme and pathway databases

BRENDAⁱ	2.6.1.7 3474
Reactomeⁱ	R-MMU-389661 Glyoxylate metabolism and glycine degradation R-MMU-70263 Gluconeogenesis R-MMU-70614 Amino acid synthesis and interconversion (transamination)

Miscellaneous databases

EvolutionaryTraceⁱ	P05202
Protein Ontology More...PROⁱ	PR:P05202
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000031672 Expressed in 114 organ(s), highest expression level in heart
Genevisibleⁱ	P05202 MM

Family and domain databases

Gene3Dⁱ	3.40.640.10, 1 hit 3.90.1150.10, 1 hit
InterProⁱ	View protein in InterPro IPR004839 Aminotransferase_I/II IPR000796 Asp_trans IPR004838 NHTrfase_class1_PyrdxlP-BS IPR015424 PyrdxlP-dep_Trfase IPR015422 PyrdxlP-dep_Trfase_dom1 IPR015421 PyrdxlP-dep_Trfase_major
PANTHERⁱ	PTHR11879 PTHR11879, 1 hit
Pfamⁱ	View protein in Pfam PF00155 Aminotran_1_2, 1 hit
PRINTSⁱ	PR00799 TRANSAMINASE
SUPFAMⁱ	SSF53383 SSF53383, 1 hit
PROSITEⁱ	View protein in PROSITE PS00105 AA_TRANSFER_CLASS_1, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	AATM_MOUSE
Accessionⁱ	P05202Primary (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:	January 16, 2019
	This is version 175 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

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

Documents

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P05202 (AATM_MOUSE)

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Aspartate aminotransferase, mitochondrial

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Plasma membrane

Mitochondrion

Mitochondrion

Plasma Membrane

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ