CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002236
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
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
33RDDPDPRKVNLGVGAubiquitination[1]
60VVRKVEQKIANDNSLubiquitination[1]
130WYNGTDNKNTPIYVSubiquitination[1]
166YCYWDAEKRGLDLQGubiquitination[1]
276GNLTVVGKESDSVLRubiquitination[1]
290RVLSQMEKIVRITWSacetylation[2, 3, 4]
290RVLSQMEKIVRITWSubiquitination[1]
318LSDPELFKEWKGNVKacetylation[5, 6]
318LSDPELFKEWKGNVKsuccinylation[6]
318LSDPELFKEWKGNVKubiquitination[1]
321PELFKEWKGNVKTMAubiquitination[1]
378VEYLVNEKHIYLLPSacetylation[3]
378VEYLVNEKHIYLLPSubiquitination[1]
396NMCGLTTKNLDYVATacetylation[3]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [4] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [6] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
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 (By similarity). 
Sequence Annotation
 BINDING 39 39 Aspartate; via amide nitrogen (By
 BINDING 141 141 Aspartate (By similarity).
 BINDING 195 195 Aspartate (By similarity).
 BINDING 387 387 Aspartate (By similarity).
 MOD_RES 66 66 Phosphoserine.
 MOD_RES 71 71 Phosphotyrosine.
 MOD_RES 259 259 N6-(pyridoxal phosphate)lysine.  
Keyword
 Amino-acid biosynthesis; Aminotransferase; Complete proteome; Cytoplasm; Direct protein sequencing; Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 413 AA 
Protein Sequence
MAPPSVFAQV PQAPPVLVFK LTADFRDDPD PRKVNLGVGA YRTDESQPWV LPVVRKVEQK 60
IANDNSLNHE YLPILGLAEF RSCASRLVLG DNSLAIRENR VGGVQSLGGT GALRIGADFL 120
GRWYNGTDNK NTPIYVSSPT WENHNAVFSA AGFKDIRPYC YWDAEKRGLD LQGFLNDLEN 180
APEFSIFVLH ACAHNPTGTD PTPEQWKQIA AVMQRRFLFP FFDSAYQGFA SGDLEKDAWA 240
IRYFVSEGFE LFCAQSFSKN FGLYNERVGN LTVVGKESDS VLRVLSQMEK IVRITWSNPP 300
AQGARIVAAT LSDPELFKEW KGNVKTMADR ILTMRSELRA RLEALKTPGT WSHITEQIGM 360
FSFTGLNPKQ VEYLVNEKHI YLLPSGRINM CGLTTKNLDY VATSIHEAVT KIQ 413 
Gene Ontology
 GO:0043679; C:axon terminus; IEA:Compara.
 GO:0005829; C:cytosol; IDA:MGI.
 GO:0005764; C:lysosome; IEA:Compara.
 GO:0031406; F:carboxylic acid binding; IEA:Compara.
 GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; ISS: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; IDA:MGI.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0006532; P:aspartate biosynthetic process; IDA:MGI.
 GO:0006533; P:aspartate catabolic process; IEA:Compara.
 GO:0032869; P:cellular response to insulin stimulus; IEA:Compara.
 GO:0055089; P:fatty acid homeostasis; IDA:MGI.
 GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IDA:MGI.
 GO:0019550; P:glutamate catabolic process to aspartate; IDA:MGI.
 GO:0006114; P:glycerol biosynthetic process; IDA:MGI.
 GO:0006107; P:oxaloacetate metabolic process; IDA:MGI.
 GO:0051384; P:response to glucocorticoid stimulus; IEA:Compara. 
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.