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Identification
HMDB Protein ID HMDBP09253
Secondary Accession Numbers
  • 15081
  • HMDBP10704
Name Cysteine--tRNA ligase, cytoplasmic
Synonyms
  1. SubName: Putative uncharacterized protein DKFZp686F1612
  2. SubName: cDNA FLJ54741, highly similar to Homo sapiens cysteinyl-tRNA synthetase (CARS), transcript variant 3, mRNA
  3. CysRS
  4. Cysteine--tRNA ligase
  5. Cysteinyl-tRNA synthetase
Gene Name CARS
Protein Type Enzyme
Biological Properties
General Function Involved in nucleotide binding
Specific Function Not Available
Pathways
  • Aminoacyl-tRNA biosynthesis
  • Beta-mercaptolactate-cysteine disulfiduria
  • Cysteine Metabolism
  • Cystinosis, ocular nonnephropathic
Reactions
Adenosine triphosphate + L-Cysteine + tRNA(Cys) → Adenosine monophosphate + Pyrophosphate + L-cysteinyl-tRNA(Cys) details
Adenosine triphosphate + L-Cysteine + tRNA(Cys) → Adenosine monophosphate + Pyrophosphate + L-Cysteinyl-tRNA(Cys) details
GO Classification
Biological Process
cysteinyl-tRNA aminoacylation
Cellular Component
cytosol
cytoplasm
Component
cell part
intracellular part
cytoplasm
Function
cysteine-trna ligase activity
binding
nucleotide binding
catalytic activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
ligase activity
ligase activity, forming carbon-oxygen bonds
ligase activity, forming aminoacyl-trna and related compounds
aminoacyl-trna ligase activity
Molecular Function
metal ion binding
ATP binding
cysteine-tRNA ligase activity
protein homodimerization activity
tRNA binding
Process
rna metabolic process
ncrna metabolic process
trna metabolic process
trna aminoacylation
trna aminoacylation for protein translation
macromolecule biosynthetic process
cellular macromolecule biosynthetic process
translation
cysteinyl-trna aminoacylation
metabolic process
macromolecule metabolic process
cellular macromolecule metabolic process
biosynthetic process
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 11
Locus 11p15.5
SNPs DKFZp686F1612
Gene Sequence
>2496 bp
ATGGCAGATTCCTCCGGGCAGCAGGCTCCTGACTACAGGTCCATTCTGAGCATTAGTGAC
GAGGCAGCCAGGGCACAAGCCCTGAACGAGCACCTCAGCACGCGTAGCTATGTCCAGGGG
TACTCACTGTCCCAGGCAGACGTGGACGCGTTCAGGCAGCTCTCGGCCCCGCCCGCTGAC
CCCCAGCTCTTCCACGTGGCTCGGTGGTTCAGGCACATAGAAGCGCTCCTGGGTAGCCCC
TGTGGCAAAGGCCAGCCCTGCAGGCTCCAAGCAAGCAAAGGCCGGCGTGTGCAGCCCCAG
TGGTCCCCTCCTGCTGGGACCCAGCCATGCAGACTCCACCTTTACAACAGCCTCACCAGG
AACAAGGAAGTGTTCATACCTCAAGATGGGAAAAAGGTGACGTGGTATTGCTGTGGGCCA
ACCGTCTATGACGCATCTCACATGGGGCACGCCAGGTCCTACATCTCTTTTGATATCTTG
AGAAGAGTGTTGAAGGATTACTTCAAATTTGATGTCTTTTATTGCATGAACATTACGGAT
ATTGATGACAAGATCATCAAGAGGGCCCGGCAGAACCACCTGTTCGAGCAGTATCGGGAG
AAGAGGCCTGAAGCGGCACAGCTCTTGGAGGATGTTCAGGCCGCCCTGAAGCCATTTTCA
GTAAAATTAAATGAGACCACGGATCCCGATAAAAAGCAGATGCTCGAACGGATTCAGCAC
GCAGTGCAGCTTGCCACAGAGCCACTTGAGAAAGCTGTGCAGTCCAGACTCACGGGAGAG
GAAGTCAACAGCTGTGTGGAGGTGTTGCTGGAAGAAGCCAAGGATTTGCTCTCTGACTGG
CTGGATTCTACACTTGGCTGTGATGTCACTGACAATTCCATCTTCTCCAAGCTGCCCAAG
TTCTGGGAGGGGGACTTCCACAGAGACATGGAAGCTCTGAATGTTCTCCCTCCAGATGTC
TTAACCCGGGTTAGTGAGTATGTGCCAGAAATTGTGAACTTTGTCCAGAAGATTGTGGAC
AACGGTTACGGCTATGTCTCCAATGGGTCTGTCTACTTTGATACAGCGAAGTTTGCTTCT
AGCGAGAAGCACTCCTATGGGAAGCTGGTGCCTGAGGCCGTTGGAGATCAGAAAGCCCTT
CAAGAAGGGGAAGGTGACCTGAGCATCTCTGCAGACCGCCTGAGTGAGAAGCGCTCTCCC
AACGACTTTGCCTTATGGAAGGCCTCTAAGCCCGGAGAACCGTCCTGGCCGTGCCCTTGG
GGAAAGGGTCGTCCGGGCTGGCATATCGAGTGCTCGGCCATGGCAGGCACCCTCCTAGGG
GCTTCGATGGACATTCACGGAGGTGGGTTCGACCTCCGGTTCCCCCACCATGACAATGAG
CTGGCACAGTCGGAGGCCTACTTTGAAAACGACTGCTGGGTCAGGTACTTCCTGCACACA
GGCCACCTGACCATTGCAGGCTGCAAAATGTCAAAGTCACTAAAAAACTTCATCACCATT
AAAGATGCCTTGAAAAAGCACTCAGCACGGCAGTTGCGGCTGGCCTTCCTCATGCACTCG
TGGAAGGACACCCTGGACTACTCCAGCAACACCATGGAGTCAGCGCTTCAATATGAGAAG
TTCTTGAATGAGTTTTTCTTAAATGTGAAAGATATCCTTCGCGCTCCTGTTGACATCACT
GGTCAGTTTGAGAAGTGGGGAGAAGAAGAAGCAGAACTGAATAAGAACTTTTATGACAAG
AAGACAGCAATTCACAAAGCCCTCTGTGACAATGTTGACACCCGCACCGTCATGGAAGAG
ATGCGGGCCTTGGTCAGTCAGTGCAACCTCTATATGGCAGCCCGGAAAGCCGTGAGGAAG
AGGCCCAACCAGGCTCTGCTGGAGAACATCGCCCTGTACCTCACCCATATGCTGAAGATC
TTTGGGGCCGTAGAAGAGGACAGCTCCCTGGGATTCCCGGTCGGAGGGCCTGGAACCAGC
CTCAGTCTCGAGGCCACAGTCATGCCCTACCTTCAGGTGTTATCAGAATTCCGAGAAGGA
GTGCGGAAGATTGCCCGAGAGCAAAAAGTCCCTGAGATTCTGCAGCTCAGCGATGCCCTG
CGGGACAACATCCTGCCCGAGCTTGGGGTGCGGTTTGAAGACCACGAAGGACTGCCCACA
GTGGTGAAACTGGTAGACAGAAACACCTTATTAAAAGAGAGAGAAGAAAAGAGACGGGTT
GAAGAGGAGAAGAGGAAGAAGAAAGAGGAGGCGGCCCGGAGGAAACAGGAACAAGAAGCA
GCAAAGCTGGCCAAGATGAAGATTCCCCCCAGTGAGATGTTCTTGTCAGAAACCGACAAA
TACTCCAAGTTTGATGAAAATGGTCTGCCCACACATGACATGGAGGGCAAAGAGCTCAGC
AAAGGGCAAGCCAAGAAGCTGAAGAAGCTCTTCGAGGCTCAGGAGAAGCTCTACAAGGAA
TATCTGCAGATGGCCCAGAATGGAAGCTTCCAGTGA
Protein Properties
Number of Residues 831
Molecular Weight 94636.8
Theoretical pI 6.833
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Cysteinyl-tRNA synthetase, isoform CRA_e
MADSSGQQAPDYRSILSISDEAARAQALNEHLSTRSYVQGYSLSQADVDAFRQLSAPPAD
PQLFHVARWFRHIEALLGSPCGKGQPCRLQASKGRRVQPQWSPPAGTQPCRLHLYNSLTR
NKEVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLKDYFKFDVFYCMNITD
IDDKIIKRARQNHLFEQYREKRPEAAQLLEDVQAALKPFSVKLNETTDPDKKQMLERIQH
AVQLATEPLEKAVQSRLTGEEVNSCVEVLLEEAKDLLSDWLDSTLGCDVTDNSIFSKLPK
FWEGDFHRDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYVSNGSVYFDTAKFAS
SEKHSYGKLVPEAVGDQKALQEGEGDLSISADRLSEKRSPNDFALWKASKPGEPSWPCPW
GKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHT
GHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTMESALQYEK
FLNEFFLNVKDILRAPVDITGQFEKWGEEEAELNKNFYDKKTAIHKALCDNVDTRTVMEE
MRALVSQCNLYMAARKAVRKRPNQALLENIALYLTHMLKIFGAVEEDSSLGFPVGGPGTS
LSLEATVMPYLQVLSEFREGVRKIAREQKVPEILQLSDALRDNILPELGVRFEDHEGLPT
VVKLVDRNTLLKEREEKRRVEEEKRKKKEEAARRKQEQEAAKLAKMKIPPSEMFLSETDK
YSKFDENGLPTHDMEGKELSKGQAKKLKKLFEAQEKLYKEYLQMAQNGSFQ
GenBank ID Protein 194380236
UniProtKB/Swiss-Prot ID P49589
UniProtKB/Swiss-Prot Entry Name Q5HYE4_HUMAN
PDB IDs Not Available
GenBank Gene ID AK302644
GeneCard ID DKFZp686F1612
GenAtlas ID DKFZp686F1612
HGNC ID HGNC:1493
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed:15592455 ]
  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  4. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  5. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  6. Cools J, Wlodarska I, Somers R, Mentens N, Pedeutour F, Maes B, De Wolf-Peeters C, Pauwels P, Hagemeijer A, Marynen P: Identification of novel fusion partners of ALK, the anaplastic lymphoma kinase, in anaplastic large-cell lymphoma and inflammatory myofibroblastic tumor. Genes Chromosomes Cancer. 2002 Aug;34(4):354-62. [PubMed:12112524 ]
  7. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [PubMed:20068231 ]
  8. Cruzen ME, Arfin SM: Nucleotide and deduced amino acid sequence of human cysteinyl-tRNA synthetase. DNA Seq. 1994;4(4):243-8. [PubMed:7987009 ]
  9. Davidson E, Caffarella J, Vitseva O, Hou YM, King MP: Isolation of two cDNAs encoding functional human cytoplasmic cysteinyl-tRNA synthetase. Biol Chem. 2001 Mar;382(3):399-406. [PubMed:11347887 ]