CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008164
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cysteine--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
 Cysteinyl-tRNA synthetase; CysRS 
Gene Name
 CARS 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
295PEAVGDQKALQEGEGubiquitination[1]
482DITGQFEKWGEEEAEubiquitination[1]
503DKKTAIHKALCDNVDacetylation[2]
Reference
 [1] 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]
 [2] 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] 
Functional Description
  
Sequence Annotation
 MOTIF 57 67 "HIGH" region.
 MOTIF 406 410 "KMSKS" region.
 METAL 55 55 Zinc (By similarity).
 METAL 348 348 Zinc (By similarity).
 METAL 373 373 Zinc (By similarity).
 METAL 377 377 Zinc (By similarity).
 BINDING 409 409 ATP (By similarity).
 MOD_RES 307 307 Phosphoserine (By similarity).
 MOD_RES 503 503 N6-acetyllysine.
 MOD_RES 746 746 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding; Chromosomal rearrangement; Complete proteome; Cytoplasm; Ligase; Metal-binding; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Proto-oncogene; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 748 AA 
Protein Sequence
MADSSGQQGK GRRVQPQWSP PAGTQPCRLH LYNSLTRNKE VFIPQDGKKV TWYCCGPTVY 60
DASHMGHARS YISFDILRRV LKDYFKFDVF YCMNITDIDD KIIKRARQNH LFEQYREKRP 120
EAAQLLEDVQ AALKPFSVKL NETTDPDKKQ MLERIQHAVQ LATEPLEKAV QSRLTGEEVN 180
SCVEVLLEEA KDLLSDWLDS TLGCDVTDNS IFSKLPKFWE GDFHRDMEAL NVLPPDVLTR 240
VSEYVPEIVN FVQKIVDNGY GYVSNGSVYF DTAKFASSEK HSYGKLVPEA VGDQKALQEG 300
EGDLSISADR LSEKRSPNDF ALWKASKPGE PSWPCPWGKG RPGWHIECSA MAGTLLGASM 360
DIHGGGFDLR FPHHDNELAQ SEAYFENDCW VRYFLHTGHL TIAGCKMSKS LKNFITIKDA 420
LKKHSARQLR LAFLMHSWKD TLDYSSNTME SALQYEKFLN EFFLNVKDIL RAPVDITGQF 480
EKWGEEEAEL NKNFYDKKTA IHKALCDNVD TRTVMEEMRA LVSQCNLYMA ARKAVRKRPN 540
QALLENIALY LTHMLKIFGA VEEDSSLGFP VGGPGTSLSL EATVMPYLQV LSEFREGVRK 600
IAREQKVPEI LQLSDALRDN ILPELGVRFE DHEGLPTVVK LVDRNTLLKE REEKRRVEEE 660
KRKKKEEAAR RKQEQEAAKL AKMKIPPSEM FLSETDKYSK FDENGLPTHD MEGKELSKGQ 720
AKKLKKLFEA QEKLYKEYLQ MAQNGSFQ 748 
Gene Ontology
 GO:0005737; C:cytoplasm; NAS:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0004817; F:cysteine-tRNA ligase activity; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0000049; F:tRNA binding; IDA:UniProtKB.
 GO:0006423; P:cysteinyl-tRNA aminoacylation; IDA:UniProtKB. 
Interpro
 IPR015803; Cys-tRNA-ligase.
 IPR024909; Cys-tRNA/MSH_ligase.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR009080; tRNAsynth_1a_anticodon-bd. 
Pfam
 PF01406; tRNA-synt_1e 
SMART
  
PROSITE
 PS00178; AA_TRNA_LIGASE_I 
PRINTS
 PR00983; TRNASYNTHCYS.