CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007042
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Branched-chain-amino-acid aminotransferase, mitochondrial 
Protein Synonyms/Alias
 BCAT; Protein ECA39; Protein TWT1 
Gene Name
 BAT1 
Gene Synonyms/Alias
 ECA39; TWT1; YHR208W 
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
113ITMFRPDKNMARMNKacetylation[1]
141ELIKLTGKLIEQDKHacetylation[1]
147GKLIEQDKHLVPQGNacetylation[1]
197PYYKTGFKAVRLEATacetylation[1]
218WPGGVGDKKLGANYAacetylation[1]
299VLTLARDKLDPQEWDacetylation[1]
322TEVATRAKQGELLEAubiquitination[2]
387VNYGNWSKTVADLN*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] Identification, analysis, and prediction of protein ubiquitination sites.
 Radivojac P, Vacic V, Haynes C, Cocklin RR, Mohan A, Heyen JW, Goebl MG, Iakoucheva LM.
 Proteins. 2010 Feb 1;78(2):365-80. [PMID: 19722269
Functional Description
 Involved in the biosynthesis of the branched chain amino acids leucine, isoleucine, and valine. Catalyzes the formation of methionine from 2-keto-4-methylthiobutyrate (KMTB) in the methionine salvage pathway primarily using branched chain amino acids (leucine, isoleucine, and valine) as the amino donors. Appears to be involved in the regulation of the transition from G1 to S phase in the cell cycle. High copy suppressor of a temperature-sensitive mutation in the ABC transporter, ATM1. 
Sequence Annotation
 MOD_RES 219 219 N6-(pyridoxal phosphate)lysine (By
 MOD_RES 315 315 Phosphothreonine.  
Keyword
 Amino-acid biosynthesis; Aminotransferase; Branched-chain amino acid biosynthesis; Complete proteome; Mitochondrion; Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 393 AA 
Protein Sequence
MLQRHSLKLG KFSIRTLATG APLDASKLKI TRNPNPSKPR PNEELVFGQT FTDHMLTIPW 60
SAKEGWGTPH IKPYGNLSLD PSACVFHYAF ELFEGLKAYR TPQNTITMFR PDKNMARMNK 120
SAARICLPTF ESEELIKLTG KLIEQDKHLV PQGNGYSLYI RPTMIGTSKG LGVGTPSEAL 180
LYVITSPVGP YYKTGFKAVR LEATDYATRA WPGGVGDKKL GANYAPCILP QLQAAKRGYQ 240
QNLWLFGPEK NITEVGTMNV FFVFLNKVTG KKELVTAPLD GTILEGVTRD SVLTLARDKL 300
DPQEWDINER YYTITEVATR AKQGELLEAF GSGTAAVVSP IKEIGWNNED IHVPLLPGEQ 360
CGALTKQVAQ WIADIQYGRV NYGNWSKTVA DLN 393 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IDA:SGD.
 GO:0004084; F:branched-chain-amino-acid transaminase activity; IDA:SGD.
 GO:0052656; F:L-isoleucine transaminase activity; IEA:EC.
 GO:0052654; F:L-leucine transaminase activity; IEA:EC.
 GO:0052655; F:L-valine transaminase activity; IEA:EC.
 GO:0009082; P:branched-chain amino acid biosynthetic process; IMP:SGD.
 GO:0009083; P:branched-chain amino acid catabolic process; IMP:SGD.
 GO:0034644; P:cellular response to UV; IMP:MGI.
 GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
 GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0031571; P:mitotic G1 DNA damage checkpoint; IMP:MGI.
 GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway. 
Interpro
 IPR001544; Aminotrans_IV.
 IPR018300; Aminotrans_IV_CS.
 IPR005786; B_amino_transII. 
Pfam
 PF01063; Aminotran_4 
SMART
  
PROSITE
 PS00770; AA_TRANSFER_CLASS_4 
PRINTS