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P05202

- AATM_MOUSE

UniProt

P05202 - AATM_MOUSE

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Protein

Aspartate aminotransferase, mitochondrial

Gene

Got2

Organism
Mus musculus (Mouse)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei65 – 651Substrate; via amide nitrogenBy similarity
Binding sitei162 – 1621SubstrateBy similarity
Binding sitei215 – 2151Substrate
Binding sitei407 – 4071Substrate

GO - Molecular functioni

  1. kynurenine-oxoglutarate transaminase activity Source: UniProtKB-EC
  2. L-aspartate:2-oxoglutarate aminotransferase activity Source: UniProtKB
  3. L-phenylalanine:2-oxoglutarate aminotransferase activity Source: UniProtKB-EC
  4. poly(A) RNA binding Source: Ensembl
  5. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. 2-oxoglutarate metabolic process Source: UniProtKB
  2. aspartate biosynthetic process Source: MGI
  3. aspartate catabolic process Source: Ensembl
  4. aspartate metabolic process Source: UniProtKB
  5. fatty acid transport Source: Ensembl
  6. glutamate catabolic process to 2-oxoglutarate Source: MGI
  7. glutamate catabolic process to aspartate Source: MGI
  8. glutamate metabolic process Source: UniProtKB
  9. oxaloacetate metabolic process Source: MGI
  10. response to ethanol Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiREACT_239550. Amino acid synthesis and interconversion (transamination).
REACT_263230. Gluconeogenesis.

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
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:95792. Got2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. mitochondrial inner membrane Source: MGI
  3. mitochondrion Source: UniProtKB
  4. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2929MitochondrionAdd
BLAST
Chaini30 – 430401Aspartate aminotransferase, mitochondrialPRO_0000001216Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591N6-acetyllysine1 Publication
Modified residuei73 – 731N6-acetyllysine; alternate2 Publications
Modified residuei73 – 731N6-succinyllysine; alternate1 Publication
Modified residuei82 – 821N6-acetyllysine1 Publication
Modified residuei90 – 901N6-acetyllysine; alternate1 Publication
Modified residuei90 – 901N6-succinyllysine; alternate1 Publication
Modified residuei96 – 961Nitrated tyrosine1 Publication
Modified residuei107 – 1071N6-acetyllysine; alternate1 Publication
Modified residuei107 – 1071N6-succinyllysine; alternate1 Publication
Modified residuei122 – 1221N6-acetyllysine; alternate1 Publication
Modified residuei122 – 1221N6-succinyllysine; alternate1 Publication
Modified residuei159 – 1591N6-acetyllysine; alternate2 Publications
Modified residuei159 – 1591N6-succinyllysine; alternate1 Publication
Modified residuei185 – 1851N6-acetyllysine; alternate1 Publication
Modified residuei185 – 1851N6-succinyllysine; alternate1 Publication
Modified residuei227 – 2271N6-succinyllysine1 Publication
Modified residuei234 – 2341N6-acetyllysine1 Publication
Modified residuei279 – 2791N6-(pyridoxal phosphate)lysine; alternateBy similarity
Modified residuei279 – 2791N6-acetyllysine; alternate1 Publication
Modified residuei296 – 2961N6-acetyllysine; alternate1 Publication
Modified residuei296 – 2961N6-succinyllysine; alternate1 Publication
Modified residuei302 – 3021N6-acetyllysine1 Publication
Modified residuei309 – 3091N6-acetyllysine; alternate1 Publication
Modified residuei309 – 3091N6-succinyllysine; alternate1 Publication
Modified residuei338 – 3381N6-acetyllysine; alternate1 Publication
Modified residuei338 – 3381N6-succinyllysine; alternate1 Publication
Modified residuei345 – 3451N6-acetyllysine1 Publication
Modified residuei363 – 3631N6-acetyllysine; alternate1 Publication
Modified residuei363 – 3631N6-succinyllysine; alternate1 Publication
Modified residuei364 – 3641N6-acetyllysine1 Publication
Modified residuei387 – 3871N6-acetyllysine1 Publication
Modified residuei396 – 3961N6-acetyllysine; alternate1 Publication
Modified residuei396 – 3961N6-succinyllysine; alternate1 Publication
Modified residuei404 – 4041N6-acetyllysine; alternate2 Publications
Modified residuei404 – 4041N6-succinyllysine; alternate1 Publication

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.2 Publications

Keywords - PTMi

Acetylation, Nitration

Proteomic databases

MaxQBiP05202.
PaxDbiP05202.
PRIDEiP05202.

PTM databases

PhosphoSiteiP05202.

Expressioni

Tissue specificityi

Detected in brain (at protein level).1 Publication

Gene expression databases

BgeeiP05202.
GenevestigatoriP05202.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

IntActiP05202. 5 interactions.
MINTiMINT-1859771.

Structurei

Secondary structure

1
430
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni32 – 354Combined sources
Helixi43 – 5311Combined sources
Helixi78 – 8912Combined sources
Helixi103 – 11412Combined sources
Helixi119 – 1235Combined sources
Beta strandi126 – 1327Combined sources
Helixi133 – 14816Combined sources
Beta strandi153 – 1608Combined sources
Helixi165 – 1728Combined sources
Beta strandi175 – 1806Combined sources
Turni184 – 1863Combined sources
Beta strandi187 – 1893Combined sources
Helixi191 – 1999Combined sources
Beta strandi206 – 2105Combined sources
Turni215 – 2173Combined sources
Helixi223 – 23513Combined sources
Beta strandi239 – 2457Combined sources
Turni247 – 2515Combined sources
Helixi254 – 2574Combined sources
Helixi259 – 2668Combined sources
Beta strandi272 – 2765Combined sources
Turni278 – 2803Combined sources
Helixi284 – 2863Combined sources
Beta strandi288 – 2947Combined sources
Helixi298 – 31619Combined sources
Helixi322 – 33211Combined sources
Helixi334 – 36431Combined sources
Helixi373 – 3764Combined sources
Beta strandi379 – 3835Combined sources
Helixi388 – 39811Combined sources
Beta strandi406 – 4094Combined sources
Helixi410 – 4123Combined sources
Turni415 – 4173Combined sources
Helixi418 – 42912Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 30-430.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05202.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1448.
GeneTreeiENSGT00390000014081.
HOGENOMiHOG000185898.
HOVERGENiHBG000951.
InParanoidiP05202.
KOiK14455.
OMAiRVGAFTM.
OrthoDBiEOG74J980.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681R → G in BAE39800. (PubMed:16141072)Curated
Sequence conflicti146 – 1461Q → E in AAB91426. (PubMed:10642497)Curated
Sequence conflicti153 – 1531R → G in BAE39800. (PubMed:16141072)Curated
Sequence conflicti377 – 3771Q → K in BAE39800. (PubMed:16141072)Curated
Sequence conflicti421 – 4211L → I in BAE39800. (PubMed:16141072)Curated

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 .
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
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. Positions 30-430.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P05202. 5 interactions.
MINTi MINT-1859771.

Chemistry

ChEMBLi CHEMBL3647.

PTM databases

PhosphoSitei P05202.

Proteomic databases

MaxQBi P05202.
PaxDbi P05202.
PRIDEi P05202.

Protocols and materials databases

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 COG1448.
GeneTreei ENSGT00390000014081.
HOGENOMi HOG000185898.
HOVERGENi HBG000951.
InParanoidi P05202.
KOi K14455.
OMAi RVGAFTM.
OrthoDBi EOG74J980.
PhylomeDBi P05202.
TreeFami TF300641.

Enzyme and pathway databases

Reactomei REACT_239550. Amino acid synthesis and interconversion (transamination).
REACT_263230. Gluconeogenesis.

Miscellaneous databases

EvolutionaryTracei P05202.
NextBioi 286731.
PROi P05202.
SOURCEi Search...

Gene expression databases

Bgeei P05202.
Genevestigatori P05202.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
InterProi IPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view ]
PANTHERi PTHR11879. PTHR11879. 1 hit.
Pfami PF00155. Aminotran_1_2. 1 hit.
[Graphical view ]
PRINTSi PR00799. TRANSAMINASE.
SUPFAMi SSF53383. SSF53383. 1 hit.
PROSITEi PS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

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 26, 2014
This is version 142 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

External Data

Dasty 3