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Protein

Aspartate aminotransferase, cytoplasmic

Gene

Got1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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).By similarity

Catalytic activityi

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

Cofactori

Enzyme regulationi

Inhibited by calcium ions.1 Publication

Sites

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

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
  • cellular response to insulin stimulus Source: Ensembl
  • fatty acid homeostasis Source: MGI
  • glutamate catabolic process to 2-oxoglutarate Source: MGI
  • glutamate catabolic process to aspartate Source: MGI
  • glutamate metabolic process Source: UniProtKB
  • glycerol biosynthetic process Source: MGI
  • Notch signaling pathway Source: MGI
  • oxaloacetate metabolic process Source: MGI
  • 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_308431. Gluconeogenesis.
REACT_309077. Amino acid synthesis and interconversion (transamination).
REACT_310863. 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 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:95791. Got1.

Subcellular locationi

GO - Cellular componenti

  • axon terminus Source: Ensembl
  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • extracellular exosome Source: MGI
  • lysosome Source: Ensembl
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 413412Aspartate aminotransferase, cytoplasmicPRO_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.
GenevisibleiP05201. MM.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi199999. 1 interaction.
IntActiP05201. 21 interactions.
MINTiMINT-1869597.
STRINGi10090.ENSMUSP00000026196.

Structurei

3D structure databases

ProteinModelPortaliP05201.
SMRiP05201. Positions 15-412.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1448.
GeneTreeiENSGT00390000014081.
HOGENOMiHOG000185898.
HOVERGENiHBG000951.
InParanoidiP05201.
KOiK14454.
OMAiDSAIWIG.
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

        10         20         30         40         50
MAPPSVFAQV PQAPPVLVFK LTADFRDDPD PRKVNLGVGA YRTDESQPWV
60 70 80 90 100
LPVVRKVEQK IANDNSLNHE YLPILGLAEF RSCASRLVLG DNSLAIRENR
110 120 130 140 150
VGGVQSLGGT GALRIGADFL GRWYNGTDNK NTPIYVSSPT WENHNAVFSA
160 170 180 190 200
AGFKDIRPYC YWDAEKRGLD LQGFLNDLEN APEFSIFVLH ACAHNPTGTD
210 220 230 240 250
PTPEQWKQIA AVMQRRFLFP FFDSAYQGFA SGDLEKDAWA IRYFVSEGFE
260 270 280 290 300
LFCAQSFSKN FGLYNERVGN LTVVGKESDS VLRVLSQMEK IVRITWSNPP
310 320 330 340 350
AQGARIVAAT LSDPELFKEW KGNVKTMADR ILTMRSELRA RLEALKTPGT
360 370 380 390 400
WSHITEQIGM FSFTGLNPKQ VEYLVNEKHI YLLPSGRINM CGLTTKNLDY
410
VATSIHEAVT KIQ
Length:413
Mass (Da):46,248
Last modified:June 28, 2011 - v3
Checksum:i0E37C763155EA6B5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941L → P in AAA37263 (PubMed:3782150).Curated
Sequence conflicti94 – 941L → P in CAA30275 (PubMed:3379636).Curated
Sequence conflicti94 – 941L → P in AAH02057 (PubMed:15489334).Curated
Sequence conflicti291 – 2911I → N in CAA30275 (PubMed:3379636).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP05201.
SMRiP05201. Positions 15-412.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199999. 1 interaction.
IntActiP05201. 21 interactions.
MINTiMINT-1869597.
STRINGi10090.ENSMUSP00000026196.

PTM databases

PhosphoSiteiP05201.

2D gel databases

SWISS-2DPAGEP05201.

Proteomic databases

MaxQBiP05201.
PaxDbiP05201.
PRIDEiP05201.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2805.
MGIiMGI:95791. Got1.

Phylogenomic databases

eggNOGiCOG1448.
GeneTreeiENSGT00390000014081.
HOGENOMiHOG000185898.
HOVERGENiHBG000951.
InParanoidiP05201.
KOiK14454.
OMAiDSAIWIG.
OrthoDBiEOG74J980.
TreeFamiTF314089.

Enzyme and pathway databases

ReactomeiREACT_308431. Gluconeogenesis.
REACT_309077. Amino acid synthesis and interconversion (transamination).
REACT_310863. Methionine salvage pathway.

Miscellaneous databases

NextBioi286727.
PROiP05201.
SOURCEiSearch...

Gene expression databases

BgeeiP05201.
CleanExiMM_GOT1.
GenevisibleiP05201. 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...

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: June 24, 2015
This is version 137 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

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 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.