CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000444
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Branched-chain-amino-acid aminotransferase, mitochondrial 
Protein Synonyms/Alias
 BCAT(m); Placental protein 18; PP18 
Gene Name
 BCAT2 
Gene Synonyms/Alias
 BCATM; BCT2; ECA40 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
44LQLEMTQKPHKKPGPacetylation[1]
229VGGVGNYKLGGNYGPubiquitination[2]
246LVQQEALKRGCEQVLubiquitination[2]
321VERTITMKQLLRALEacetylation[1]
321VERTITMKQLLRALEubiquitination[3, 4]
353PVHRILYKDRNLHIPubiquitination[2]
374ELILRFQKELKEIQYubiquitination[2]
377LRFQKELKEIQYGIRacetylation[1]
377LRFQKELKEIQYGIRubiquitination[2]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] 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]
 [3] 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]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids. 
Sequence Annotation
 BINDING 168 168 Substrate.
 MOD_RES 229 229 N6-(pyridoxal phosphate)lysine.
 MOD_RES 321 321 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Amino-acid biosynthesis; Aminotransferase; Branched-chain amino acid biosynthesis; Complete proteome; Cytoplasm; Mitochondrion; Polymorphism; Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 392 AA 
Protein Sequence
MAAAALGQIW ARKLLSVPWL LCGPRRYASS SFKAADLQLE MTQKPHKKPG PGEPLVFGKT 60
FTDHMLMVEW NDKGWGQPRI QPFQNLTLHP ASSSLHYSLQ LFEGMKAFKG KDQQVRLFRP 120
WLNMDRMLRS AMRLCLPSFD KLELLECIRR LIEVDKDWVP DAAGTSLYVR PVLIGNEPSL 180
GVSQPTRALL FVILCPVGAY FPGGSVTPVS LLADPAFIRA WVGGVGNYKL GGNYGPTVLV 240
QQEALKRGCE QVLWLYGPDH QLTEVGTMNI FVYWTHEDGV LELVTPPLNG VILPGVVRQS 300
LLDMAQTWGE FRVVERTITM KQLLRALEEG RVREVFGSGT ACQVCPVHRI LYKDRNLHIP 360
TMENGPELIL RFQKELKEIQ YGIRAHEWMF PV 392 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0004084; F:branched-chain-amino-acid transaminase activity; EXP:Reactome.
 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; TAS:ProtInc.
 GO:0009083; P:branched-chain amino acid catabolic process; TAS:Reactome.
 GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
 GO:0006550; P:isoleucine catabolic process; IEA:Compara.
 GO:0006551; P:leucine metabolic process; IEA:Compara.
 GO:0010817; P:regulation of hormone levels; IEA:Compara.
 GO:0006573; P:valine metabolic process; IEA:Compara. 
Interpro
 IPR001544; Aminotrans_IV.
 IPR018300; Aminotrans_IV_CS.
 IPR005786; B_amino_transII. 
Pfam
 PF01063; Aminotran_4 
SMART
  
PROSITE
 PS00770; AA_TRANSFER_CLASS_4 
PRINTS