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P05201

- AATC_MOUSE

UniProt

P05201 - AATC_MOUSE

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Protein
Aspartate aminotransferase, cytoplasmic
Gene
Got1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis. Using L-cysteine as substrate, regulates levels of mercaptopyruvate, an important source of hydrogen sulfide. Mercaptopyruvate is converted into H2S via the action of 3-mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an important synaptic modulator and neuroprotectant in the brain By similarity.

Catalytic activityi

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
L-cysteine + 2-oxoglutarate = mercaptopyruvate + L-glutamate.

Cofactori

Pyridoxal phosphate.

Enzyme regulationi

Inhibited by calcium ions.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391Aspartate; via amide nitrogen By similarity
Binding sitei141 – 1411Aspartate By similarity
Binding sitei195 – 1951Aspartate By similarity
Binding sitei387 – 3871Aspartate By similarity

GO - Molecular functioni

  1. L-aspartate:2-oxoglutarate aminotransferase activity Source: UniProtKB
  2. L-cysteine:2-oxoglutarate aminotransferase activity Source: UniProtKB
  3. L-phenylalanine:2-oxoglutarate aminotransferase activity Source: UniProtKB-EC
  4. carboxylic acid binding Source: Ensembl
  5. phosphatidylserine decarboxylase activity Source: MGI
  6. 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. cellular response to insulin stimulus Source: Ensembl
  6. fatty acid homeostasis Source: MGI
  7. glutamate catabolic process to 2-oxoglutarate Source: MGI
  8. glutamate catabolic process to aspartate Source: MGI
  9. glutamate metabolic process Source: UniProtKB
  10. glycerol biosynthetic process Source: MGI
  11. oxaloacetate metabolic process Source: MGI
  12. response to glucocorticoid Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiREACT_199099. Methionine salvage pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate aminotransferase, cytoplasmic (EC:2.6.1.1, EC:2.6.1.3)
Short name:
cAspAT
Alternative name(s):
Cysteine aminotransferase, cytoplasmic
Cysteine transaminase, cytoplasmic
Short name:
cCAT
Glutamate oxaloacetate transaminase 1
Transaminase A
Gene namesi
Name:Got1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:95791. Got1.

Subcellular locationi

GO - Cellular componenti

  1. axon terminus Source: Ensembl
  2. cytosol Source: MGI
  3. lysosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 413412Aspartate aminotransferase, cytoplasmic
PRO_0000123880Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei259 – 2591N6-(pyridoxal phosphate)lysine
Modified residuei318 – 3181N6-succinyllysine1 Publication

Proteomic databases

MaxQBiP05201.
PaxDbiP05201.
PRIDEiP05201.

2D gel databases

SWISS-2DPAGEP05201.

PTM databases

PhosphoSiteiP05201.

Expressioni

Tissue specificityi

Expressed in neurons of the retina. Localizes to the inner and outer plexiform layers, the inner and outer nuclear layer and the outer segments of photoreceptors.1 Publication

Gene expression databases

BgeeiP05201.
CleanExiMM_GOT1.
GenevestigatoriP05201.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

IntActiP05201. 21 interactions.
MINTiMINT-1869597.
STRINGi10090.ENSMUSP00000026196.

Structurei

3D structure databases

ProteinModelPortaliP05201.
SMRiP05201. Positions 15-412.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1448.
GeneTreeiENSGT00390000014081.
HOGENOMiHOG000185898.
HOVERGENiHBG000951.
InParanoidiQ3UJH8.
KOiK14454.
OMAiCMAGLNH.
OrthoDBiEOG74J980.
TreeFamiTF314089.

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.

P05201-1 [UniParc]FASTAAdd to Basket

« Hide

MAPPSVFAQV PQAPPVLVFK LTADFRDDPD PRKVNLGVGA YRTDESQPWV    50
LPVVRKVEQK IANDNSLNHE YLPILGLAEF RSCASRLVLG DNSLAIRENR 100
VGGVQSLGGT GALRIGADFL GRWYNGTDNK NTPIYVSSPT WENHNAVFSA 150
AGFKDIRPYC YWDAEKRGLD LQGFLNDLEN APEFSIFVLH ACAHNPTGTD 200
PTPEQWKQIA AVMQRRFLFP FFDSAYQGFA SGDLEKDAWA IRYFVSEGFE 250
LFCAQSFSKN FGLYNERVGN LTVVGKESDS VLRVLSQMEK IVRITWSNPP 300
AQGARIVAAT LSDPELFKEW KGNVKTMADR ILTMRSELRA RLEALKTPGT 350
WSHITEQIGM FSFTGLNPKQ VEYLVNEKHI YLLPSGRINM CGLTTKNLDY 400
VATSIHEAVT KIQ 413
Length:413
Mass (Da):46,248
Last modified:June 28, 2011 - v3
Checksum:i0E37C763155EA6B5
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941L → P in AAA37263. 1 Publication
Sequence conflicti94 – 941L → P in CAA30275. 1 Publication
Sequence conflicti94 – 941L → P in AAH02057. 1 Publication
Sequence conflicti291 – 2911I → N in CAA30275. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02623 mRNA. Translation: AAA37263.1.
X07302
, X07303, X07304, X07305, X07306, X07307, X07308, X07309 Genomic DNA. Translation: CAA30275.1.
AK146445 mRNA. Translation: BAE27177.1.
BC002057 mRNA. Translation: AAH02057.1.
CCDSiCCDS29832.1.
PIRiS01076.
RefSeqiNP_034454.2. NM_010324.2.
UniGeneiMm.19039.

Genome annotation databases

EnsembliENSMUST00000026196; ENSMUSP00000026196; ENSMUSG00000025190.
GeneIDi14718.
KEGGimmu:14718.
UCSCiuc012bmb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02623 mRNA. Translation: AAA37263.1 .
X07302
, X07303 , X07304 , X07305 , X07306 , X07307 , X07308 , X07309 Genomic DNA. Translation: CAA30275.1 .
AK146445 mRNA. Translation: BAE27177.1 .
BC002057 mRNA. Translation: AAH02057.1 .
CCDSi CCDS29832.1.
PIRi S01076.
RefSeqi NP_034454.2. NM_010324.2.
UniGenei Mm.19039.

3D structure databases

ProteinModelPortali P05201.
SMRi P05201. Positions 15-412.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P05201. 21 interactions.
MINTi MINT-1869597.
STRINGi 10090.ENSMUSP00000026196.

PTM databases

PhosphoSitei P05201.

2D gel databases

SWISS-2DPAGE P05201.

Proteomic databases

MaxQBi P05201.
PaxDbi P05201.
PRIDEi P05201.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000026196 ; ENSMUSP00000026196 ; ENSMUSG00000025190 .
GeneIDi 14718.
KEGGi mmu:14718.
UCSCi uc012bmb.1. mouse.

Organism-specific databases

CTDi 2805.
MGIi MGI:95791. Got1.

Phylogenomic databases

eggNOGi COG1448.
GeneTreei ENSGT00390000014081.
HOGENOMi HOG000185898.
HOVERGENi HBG000951.
InParanoidi Q3UJH8.
KOi K14454.
OMAi CMAGLNH.
OrthoDBi EOG74J980.
TreeFami TF314089.

Enzyme and pathway databases

Reactomei REACT_199099. Methionine salvage pathway.

Miscellaneous databases

NextBioi 286727.
PROi P05201.
SOURCEi Search...

Gene expression databases

Bgeei P05201.
CleanExi MM_GOT1.
Genevestigatori P05201.

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].
    Tissue: Liver.
  2. "Structural organization of the mouse aspartate aminotransferase isoenzyme genes. Introns antedate the divergence of cytosolic and mitochondrial isoenzyme genes."
    Obaru K., Tsuzuki T., Setoyama C., Shimada K.
    J. Mol. Biol. 200:13-22(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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: C57BL/6J.
    Tissue: Heart.
  4. "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/6J.
    Tissue: Mammary gland.
  5. Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-55; 61-81; 87-97; 101-166; 208-236; 260-276; 306-318 AND 347-411, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  6. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  7. "Hydrogen sulfide protects the retina from light-induced degeneration by the modulation of Ca2+ influx."
    Mikami Y., Shibuya N., Kimura Y., Nagahara N., Yamada M., Kimura H.
    J. Biol. Chem. 286:39379-39386(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, ENZYME REGULATION.
  8. "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: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-318, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiAATC_MOUSE
AccessioniPrimary (citable) accession number: P05201
Secondary accession number(s): Q3UJH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: June 28, 2011
Last modified: September 3, 2014
This is version 128 of the entry and version 3 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi