CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004547
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Aspartate aminotransferase, cytoplasmic 
Protein Synonyms/Alias
 cAspAT; Cysteine aminotransferase, cytoplasmic; Cysteine transaminase, cytoplasmic; cCAT; Glutamate oxaloacetate transaminase 1; Transaminase A 
Gene Name
 GOT1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
33REDPDPRKVNLGVGAubiquitination[1]
56WVLPVVKKVEQKIANubiquitination[1]
60VVKKVEQKIANDNSLubiquitination[2]
97GDDSPALKEKRVGGVubiquitination[1, 2]
99DSPALKEKRVGGVQSubiquitination[1]
130WYNGTNNKNTPVYVSubiquitination[2]
154VFSAAGFKDIRSYRYacetylation[3]
154VFSAAGFKDIRSYRYubiquitination[2]
166YRYWDAEKRGLDLQGubiquitination[1, 4]
276GNLTVVGKEPESILQubiquitination[1, 2]
290QVLSQMEKIVRITWSubiquitination[2]
325EEWTGNVKTMADRILubiquitination[1, 2]
346RARLEALKTPGTWNHubiquitination[2]
378VEYLVNEKHIYLLPSubiquitination[1, 2, 4]
396NVSGLTTKNLDYVATubiquitination[1, 2, 4]
411SIHEAVTKIQ*****ubiquitination[1, 2]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961] 
Functional Description
 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 H(2)S via the action of 3- mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an important synaptic modulator and neuroprotectant in the brain. 
Sequence Annotation
 BINDING 39 39 Aspartate; via amide nitrogen.
 BINDING 141 141 Aspartate.
 BINDING 195 195 Aspartate.
 BINDING 387 387 Aspartate.
 MOD_RES 66 66 Phosphoserine (By similarity).
 MOD_RES 71 71 Phosphotyrosine (By similarity).
 MOD_RES 259 259 N6-(pyridoxal phosphate)lysine (By  
Keyword
 3D-structure; Amino-acid biosynthesis; Aminotransferase; Complete proteome; Cytoplasm; Direct protein sequencing; Phosphoprotein; Polymorphism; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 413 AA 
Protein Sequence
MAPPSVFAEV PQAQPVLVFK LTADFREDPD PRKVNLGVGA YRTDDCHPWV LPVVKKVEQK 60
IANDNSLNHE YLPILGLAEF RSCASRLALG DDSPALKEKR VGGVQSLGGT GALRIGADFL 120
ARWYNGTNNK NTPVYVSSPT WENHNAVFSA AGFKDIRSYR YWDAEKRGLD LQGFLNDLEN 180
APEFSIVVLH ACAHNPTGID PTPEQWKQIA SVMKHRFLFP FFDSAYQGFA SGNLERDAWA 240
IRYFVSEGFE FFCAQSFSKN FGLYNERVGN LTVVGKEPES ILQVLSQMEK IVRITWSNPP 300
AQGARIVAST LSNPELFEEW TGNVKTMADR ILTMRSELRA RLEALKTPGT WNHITDQIGM 360
FSFTGLNPKQ VEYLVNEKHI YLLPSGRINV SGLTTKNLDY VATSIHEAVT KIQ 413 
Gene Ontology
 GO:0043679; C:axon terminus; IEA:Compara.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005764; C:lysosome; IEA:Compara.
 GO:0031406; F:carboxylic acid binding; IEA:Compara.
 GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IDA:UniProtKB.
 GO:0047801; F:L-cysteine:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
 GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:EC.
 GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:Compara.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
 GO:0006532; P:aspartate biosynthetic process; IEA:Compara.
 GO:0006533; P:aspartate catabolic process; IDA:UniProtKB.
 GO:0032869; P:cellular response to insulin stimulus; IEP:UniProtKB.
 GO:0055089; P:fatty acid homeostasis; IEA:Compara.
 GO:0006094; P:gluconeogenesis; TAS:Reactome.
 GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:Compara.
 GO:0019550; P:glutamate catabolic process to aspartate; IEA:Compara.
 GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
 GO:0006114; P:glycerol biosynthetic process; ISS:UniProtKB.
 GO:0019509; P:L-methionine salvage from methylthioadenosine; TAS:Reactome.
 GO:0006107; P:oxaloacetate metabolic process; IEA:Compara.
 GO:0006595; P:polyamine metabolic process; TAS:Reactome.
 GO:0051384; P:response to glucocorticoid stimulus; IEP:UniProtKB. 
Interpro
 IPR004839; Aminotransferase_I/II.
 IPR000796; Asp_trans.
 IPR004838; NHTrfase_class1_PyrdxlP-BS.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1. 
Pfam
 PF00155; Aminotran_1_2 
SMART
  
PROSITE
 PS00105; AA_TRANSFER_CLASS_1 
PRINTS
 PR00799; TRANSAMINASE.