CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-043610
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Lysine--tRNA ligase 
Protein Synonyms/Alias
  
Gene Name
 KARS 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
106VDPNQYYKIRSQAIHubiquitination[1, 2]
155HLTDITLKVAGRIHAubiquitination[2, 3]
169AKRASGGKLIFYDLRacetylation[4]
192MANSRNYKSEEEFIHacetylation[5]
203EFIHINNKLRRGDIIacetylation[3]
203EFIHINNKLRRGDIIubiquitination[2, 3]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 256 AA 
Protein Sequence
MLTQAAVRLV RGSLRKTSWA EWGHRELRLG QLAPFTAPHK DKSFSDQRSE LKRRLKAEKK 60
VAEKEAKQKE LSEKQLSQAT AAATNHTTDN GVGPEEESVD PNQYYKIRSQ AIHQLKVNGE 120
DPYPHKFHVD ISLTDFIQKY SHLQPGDHLT DITLKVAGRI HAKRASGGKL IFYDLRGEGV 180
KLQVMANSRN YKSEEEFIHI NNKLRRGDII GVQGNPGKTK KGELSIIPYE ITLLSPCLHM 240
LPHLHFGLKD KETRYR 256 
Gene Ontology
 GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IEA:Compara.
 GO:0016597; F:amino acid binding; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:Compara.
 GO:0004824; F:lysine-tRNA ligase activity; IEA:Compara.
 GO:0000049; F:tRNA binding; IEA:Compara.
 GO:0015966; P:diadenosine tetraphosphate biosynthetic process; IEA:Compara.
 GO:0006430; P:lysyl-tRNA aminoacylation; IEA:Compara. 
Interpro
 IPR018150; aa-tRNA-synt_II-like.
 IPR002313; Lys-tRNA-ligase_II.
 IPR012340; NA-bd_OB-fold.
 IPR004365; NA-bd_OB_tRNA-helicase. 
Pfam
 PF01336; tRNA_anti 
SMART
  
PROSITE
  
PRINTS