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P05201 (AATC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aspartate aminotransferase, cytoplasmic

Short name=cAspAT
EC=2.6.1.1
EC=2.6.1.3
Alternative name(s):
Cysteine aminotransferase, cytoplasmic
Cysteine transaminase, cytoplasmic
Short name=cCAT
Glutamate oxaloacetate transaminase 1
Transaminase A
Gene names
Name:Got1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length413 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

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

Cofactor

Pyridoxal phosphate.

Enzyme regulation

Inhibited by calcium ions. Ref.7

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Tissue specificity

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. Ref.7

Miscellaneous

In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.

Sequence similarities

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

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process2-oxoglutarate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

aspartate biosynthetic process

Inferred from direct assay PubMed 4193185. Source: MGI

aspartate catabolic process

Inferred from electronic annotation. Source: Ensembl

aspartate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to insulin stimulus

Inferred from electronic annotation. Source: Ensembl

fatty acid homeostasis

Inferred from direct assay PubMed 17545671. Source: MGI

glutamate catabolic process to 2-oxoglutarate

Inferred from direct assay PubMed 4193185. Source: MGI

glutamate catabolic process to aspartate

Inferred from direct assay PubMed 4193185. Source: MGI

glutamate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

glycerol biosynthetic process

Inferred from direct assay PubMed 17545671. Source: MGI

oxaloacetate metabolic process

Inferred from direct assay PubMed 4193185. Source: MGI

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaxon terminus

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from direct assay PubMed 4193185. Source: MGI

lysosome

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

L-cysteine:2-oxoglutarate aminotransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

L-phenylalanine:2-oxoglutarate aminotransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

carboxylic acid binding

Inferred from electronic annotation. Source: Ensembl

phosphatidylserine decarboxylase activity

Inferred from direct assay PubMed 3242498. Source: MGI

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 413412Aspartate aminotransferase, cytoplasmic
PRO_0000123880

Sites

Binding site391Aspartate; via amide nitrogen By similarity
Binding site1411Aspartate By similarity
Binding site1951Aspartate By similarity
Binding site3871Aspartate By similarity

Amino acid modifications

Modified residue2591N6-(pyridoxal phosphate)lysine
Modified residue3181N6-succinyllysine Ref.8

Experimental info

Sequence conflict941L → P in AAA37263. Ref.1
Sequence conflict941L → P in CAA30275. Ref.2
Sequence conflict941L → P in AAH02057. Ref.4
Sequence conflict2911I → N in CAA30275. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P05201 [UniParc].

Last modified June 28, 2011. Version 3.
Checksum: 0E37C763155EA6B5

FASTA41346,248
        10         20         30         40         50         60 
MAPPSVFAQV PQAPPVLVFK LTADFRDDPD PRKVNLGVGA YRTDESQPWV LPVVRKVEQK 

        70         80         90        100        110        120 
IANDNSLNHE YLPILGLAEF RSCASRLVLG DNSLAIRENR VGGVQSLGGT GALRIGADFL 

       130        140        150        160        170        180 
GRWYNGTDNK NTPIYVSSPT WENHNAVFSA AGFKDIRPYC YWDAEKRGLD LQGFLNDLEN 

       190        200        210        220        230        240 
APEFSIFVLH ACAHNPTGTD PTPEQWKQIA AVMQRRFLFP FFDSAYQGFA SGDLEKDAWA 

       250        260        270        280        290        300 
IRYFVSEGFE LFCAQSFSKN FGLYNERVGN LTVVGKESDS VLRVLSQMEK IVRITWSNPP 

       310        320        330        340        350        360 
AQGARIVAAT LSDPELFKEW KGNVKTMADR ILTMRSELRA RLEALKTPGT WSHITEQIGM 

       370        380        390        400        410 
FSFTGLNPKQ VEYLVNEKHI YLLPSGRINM CGLTTKNLDY VATSIHEAVT KIQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02623 mRNA. Translation: AAA37263.1.
X07302 expand/collapse EMBL AC list , X07303, X07304, X07305, X07306, X07307, X07308, X07309 Genomic DNA. Translation: CAA30275.1.
AK146445 mRNA. Translation: BAE27177.1.
BC002057 mRNA. Translation: AAH02057.1.
PIRS01076.
RefSeqNP_034454.2. NM_010324.2.
UniGeneMm.19039.

3D structure databases

ProteinModelPortalP05201.
SMRP05201. Positions 15-412.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP05201. 21 interactions.
MINTMINT-1869597.
STRING10090.ENSMUSP00000026196.

PTM databases

PhosphoSiteP05201.

2D gel databases

SWISS-2DPAGEP05201.

Proteomic databases

PaxDbP05201.
PRIDEP05201.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026196; ENSMUSP00000026196; ENSMUSG00000025190.
GeneID14718.
KEGGmmu:14718.
UCSCuc012bmb.1. mouse.

Organism-specific databases

CTD2805.
MGIMGI:95791. Got1.

Phylogenomic databases

eggNOGCOG1448.
GeneTreeENSGT00390000014081.
HOGENOMHOG000185898.
HOVERGENHBG000951.
InParanoidQ3UJH8.
KOK14454.
OMATTKNYLS.
OrthoDBEOG74J980.
TreeFamTF314089.

Gene expression databases

BgeeP05201.
CleanExMM_GOT1.
GenevestigatorP05201.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
InterProIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERPTHR11879. PTHR11879. 1 hit.
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSPR00799. TRANSAMINASE.
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio286727.
PROP05201.
SOURCESearch...

Entry information

Entry nameAATC_MOUSE
AccessionPrimary (citable) accession number: P05201
Secondary accession number(s): Q3UJH8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: June 28, 2011
Last modified: April 16, 2014
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot