CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008878
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Branched-chain-amino-acid aminotransferase, cytosolic 
Protein Synonyms/Alias
 BCAT(c); Protein ECA39 
Gene Name
 BCAT1 
Gene Synonyms/Alias
 BCT1; ECA39 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
2******MKDCSNGCSubiquitination[1]
19CTGEGGSKEVVGTFKubiquitination[1, 2]
28VVGTFKAKDLIVTPAubiquitination[1, 3]
107AFRGVDNKIRLFQPNubiquitination[1]
215PKYVRAWKGGTGDCKubiquitination[1]
305AHQWGEFKVSERYLTubiquitination[1, 4]
360PTMENGPKLASRILSubiquitination[1, 2, 3]
368LASRILSKLTDIQYGubiquitination[1, 2, 5]
Reference
 [1] 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]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional Description
 Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. 
Sequence Annotation
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 222 222 N6-(pyridoxal phosphate)lysine (By  
Keyword
 3D-structure; Acetylation; Alternative splicing; Amino-acid biosynthesis; Aminotransferase; Branched-chain amino acid biosynthesis; Complete proteome; Cytoplasm; Polymorphism; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 386 AA 
Protein Sequence
MKDCSNGCSA ECTGEGGSKE VVGTFKAKDL IVTPATILKE KPDPNNLVFG TVFTDHMLTV 60
EWSSEFGWEK PHIKPLQNLS LHPGSSALHY AVELFEGLKA FRGVDNKIRL FQPNLNMDRM 120
YRSAVRATLP VFDKEELLEC IQQLVKLDQE WVPYSTSASL YIRPTFIGTE PSLGVKKPTK 180
ALLFVLLSPV GPYFSSGTFN PVSLWANPKY VRAWKGGTGD CKMGGNYGSS LFAQCEAVDN 240
GCQQVLWLYG EDHQITEVGT MNLFLYWINE DGEEELATPP LDGIILPGVT RRCILDLAHQ 300
WGEFKVSERY LTMDDLTTAL EGNRVREMFG SGTACVVCPV SDILYKGETI HIPTMENGPK 360
LASRILSKLT DIQYGREESD WTIVLS 386 
Gene Ontology
 GO:0005829; C:cytosol; 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:0008283; P:cell proliferation; TAS:ProtInc.
 GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
 GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:ProtInc. 
Interpro
 IPR001544; Aminotrans_IV.
 IPR018300; Aminotrans_IV_CS.
 IPR005786; B_amino_transII. 
Pfam
 PF01063; Aminotran_4 
SMART
  
PROSITE
 PS00770; AA_TRANSFER_CLASS_4 
PRINTS