CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-037006
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Aspartate aminotransferase 
Protein Synonyms/Alias
  
Gene Name
 GOT2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
73AYRDDNGKPYVLPSVacetylation[1, 2]
116SRDVFLPKPTWGNHTacetylation[1, 2]
142GYRYYDPKTCGFDFTacetylation[2]
184DPRPEQWKEIATVVKacetylation[2]
191KEIATVVKKRNLFAFacetylation[1]
253GAFTMVCKDADEAKRacetylation[2]
253GAFTMVCKDADEAKRubiquitination[3]
295LNTPDLRKQWLQEVKubiquitination[3]
320TQLVSNLKKEGSTHNacetylation[2]
320TQLVSNLKKEGSTHNubiquitination[3]
353EQVERLIKEFSIYMTacetylation[1, 2]
353EQVERLIKEFSIYMTubiquitination[4]
361EFSIYMTKDGRISVAacetylation[1]
Reference
 [1] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [2] 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]
 [3] 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]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473] 
Functional Description
  
Sequence Annotation
  
Keyword
 Aminotransferase; Complete proteome; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 387 AA 
Protein Sequence
MALLHSGRVL PGIAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA FKRDTNSKKM 60
NLGVGAYRDD NGKPYVLPSV RKFVTVQTIS GTGALRIGAS FLQRFFKFSR DVFLPKPTWG 120
NHTPIFRDAG MQLQGYRYYD PKTCGFDFTG AVEDISKIPE QSVLLLHACA HNPTGVDPRP 180
EQWKEIATVV KKRNLFAFFD MAYQGFASGD GDKDAWAVRH FIEQGINVCL CQSYAKNMGL 240
YGERVGAFTM VCKDADEAKR VESQLKILIR PMYSNPPLNG ARIAAAILNT PDLRKQWLQE 300
VKVMADRIIG MRTQLVSNLK KEGSTHNWQH ITDQIGMFCF TGLKPEQVER LIKEFSIYMT 360
KDGRISVAGV TSSNVGYLAH AIHQVTK 387 
Gene Ontology
 GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:EC.
 GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:EC.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0009058; P:biosynthetic process; IEA:InterPro.
 GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro. 
Interpro
 IPR004839; Aminotransferase_I/II.
 IPR000796; Asp_trans.
 IPR004838; NHTrfase_class1_PyrdxlP-BS.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1.
 IPR015422; PyrdxlP-dep_Trfase_major_sub2. 
Pfam
 PF00155; Aminotran_1_2 
SMART
  
PROSITE
 PS00105; AA_TRANSFER_CLASS_1 
PRINTS
 PR00799; TRANSAMINASE.