CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005192
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Aspartate aminotransferase, cytoplasmic 
Protein Synonyms/Alias
 Transaminase A 
Gene Name
 AAT2 
Gene Synonyms/Alias
 ASP5; YLR027C; L1746 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
121ISAKFFSKFFPDKLVacetylation[1]
255FVCQSFAKNAGMYGEubiquitination[2]
281QAQNKTIKPAVTSQLubiquitination[2]
290AVTSQLAKIIRSEVSacetylation[1]
290AVTSQLAKIIRSEVSubiquitination[2]
305NPPAYGAKIVAKLLEubiquitination[2]
309YGAKIVAKLLETPELacetylation[1]
417RFYTIEAKL******acetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 Plays a key role in amino acid metabolism. 
Sequence Annotation
 BINDING 38 38 Aspartate; via amide nitrogen.
 BINDING 135 135 Aspartate.
 BINDING 188 188 Aspartate.
 BINDING 387 387 Aspartate.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 255 255 N6-(pyridoxal phosphate)lysine.
 MOD_RES 389 389 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Aminotransferase; Complete proteome; Cytoplasm; Direct protein sequencing; Peroxisome; Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 418 AA 
Protein Sequence
MSATLFNNIE LLPPDALFGI KQRYGQDQRA TKVDLGIGAY RDDNGKPWVL PSVKAAEKLI 60
HNDSSYNHEY LGITGLPSLT SNAAKIIFGT QSDAFQEDRV ISVQSLSGTG ALHISAKFFS 120
KFFPDKLVYL SKPTWANHMA IFENQGLKTA TYPYWANETK SLDLNGFLNA IQKAPEGSIF 180
VLHSCAHNPT GLDPTSEQWV QIVDAIASKN HIALFDTAYQ GFATGDLDKD AYAVRLGVEK 240
LSTVSPVFVC QSFAKNAGMY GERVGCFHLA LTKQAQNKTI KPAVTSQLAK IIRSEVSNPP 300
AYGAKIVAKL LETPELTEQW HKDMVTMSSR ITKMRHALRD HLVKLGTPGN WDHIVNQCGM 360
FSFTGLTPQM VKRLEETHAV YLVASGRASI AGLNQGNVEY VAKAIDEVVR FYTIEAKL 418 
Gene Ontology
 GO:0005829; C:cytosol; IDA:SGD.
 GO:0005777; C:peroxisome; IMP:SGD.
 GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
 GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:EC.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
 GO:0006532; P:aspartate biosynthetic process; IMP:SGD.
 GO:0006536; P:glutamate metabolic process; ISS: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.