CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-030542
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Branched-chain-amino-acid aminotransferase 
Protein Synonyms/Alias
  
Gene Name
 BCAT2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
4****MTQKPHKKPGPmethylation[1]
189VGGVGNYKLGGNYGPacetylation[2]
189VGGVGNYKLGGNYGPubiquitination[3, 4, 5]
206LVQQEALKRGCEQVLubiquitination[3, 4, 5, 6]
281VERTITMKQLLRALEacetylation[2]
281VERTITMKQLLRALEubiquitination[3, 6, 7]
313PVHRILYKDRNLHIPubiquitination[6]
334ELILRFQKELKEIQYubiquitination[6]
337LRFQKELKEIQYGIRacetylation[2, 8, 9]
337LRFQKELKEIQYGIRubiquitination[5, 6]
Reference
 [1] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [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] 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]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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] 
Functional Description
  
Sequence Annotation
 MOD_RES 189 189 N6-(pyridoxal phosphate)lysine (By  
Keyword
 Amino-acid biosynthesis; Aminotransferase; Branched-chain amino acid biosynthesis; Complete proteome; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 352 AA 
Protein Sequence
MTQKPHKKPG PGEPLVFGKT FTDHMLMVEW NDKGWGQPRI QPFQNLTLHP ASSSLHYSLQ 60
LFEGMKAFKG KDQQVRLFRP WLNMDRMLRS AMRLCLPSFD KLELLECIRR LIEVDKDWVP 120
DAAGTSLYVR PVLIGNEPSL GVSQPTRALL FVILCPVGAY FPGGSVTPVS LLADPAFIRA 180
WVGGVGNYKL GGNYGPTVLV QQEALKRGCE QVLWLYGPDH QLTEVGTMNI FVYWTHEDGV 240
LELVTPPLNG VILPGVVRQS LLDMAQTWGE FRVVERTITM KQLLRALEEG RVREVFGSGT 300
ACQVCPVHRI LYKDRNLHIP TMENGPELIL RFQKELKEIQ YGIRAHEWMF PV 352 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:Compara.
 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; IEA:UniProtKB-KW.
 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