Tyrosine--tRNA ligase, cytoplasmic

Details

Name
Tyrosine--tRNA ligase, cytoplasmic
Synonyms
  • 6.1.1.1
  • Tyrosyl-tRNA synthetase
  • TyrRS
Gene Name
YARS
Organism
Humans
Amino acid sequence
>lcl|BSEQ0036975|Tyrosine--tRNA ligase, cytoplasmic
MGDAPSPEEKLHLITRNLQEVLGEEKLKEILKERELKIYWGTATTGKPHVAYFVPMSKIA
DFLKAGCEVTILFADLHAYLDNMKAPWELLELRVSYYENVIKAMLESIGVPLEKLKFIKG
TDYQLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVD
AQFGGIDQRKIFTFAEKYLPALGYSKRVHLMNPMVPGLTGSKMSSSEEESKIDLLDRKED
VKKKLKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYVDLEKDFA
AEVVHPGDLKNSVEVALNKLLDPIREKFNTPALKKLASAAYPDPSKQKPMAKGPAKNSEP
EEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLV
VVLCNLKPQKMRGVESQGMLLCASIEGINRQVEPLDPPAGSAPGEHVFVKGYEKGQPDEE
LKPKKKVFEKLQADFKISEECIAQWKQTNFMTKLGSISCKSLKGGNIS
Number of residues
528
Molecular Weight
59143.025
Theoretical pI
7.05
GO Classification
Functions
ATP binding / interleukin-8 receptor binding / poly(A) RNA binding / signal transducer activity / tRNA binding / tyrosine-tRNA ligase activity
Processes
apoptotic process / gene expression / signal transduction / tRNA aminoacylation for protein translation / tyrosyl-tRNA aminoacylation
Components
cytoplasm / cytosol / extracellular space / nucleus
General Function
Tyrosine-trna ligase activity
Specific Function
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0010211|Tyrosine--tRNA ligase, cytoplasmic (YARS)
ATGGGGGACGCTCCCAGCCCTGAAGAGAAACTGCACCTTATCACCCGGAACCTGCAGGAG
GTTCTGGGGGAAGAGAAGCTGAAGGAGATACTGAAGGAGCGGGAACTTAAAATTTACTGG
GGAACGGCAACCACGGGCAAACCACATGTGGCTTACTTTGTGCCCATGTCAAAGATTGCA
GACTTCTTAAAGGCAGGGTGTGAGGTAACAATTCTGTTTGCGGACCTCCACGCATACCTG
GATAACATGAAAGCCCCATGGGAACTTCTAGAACTCCGAGTCAGTTACTATGAGAATGTG
ATCAAAGCAATGCTGGAGAGCATTGGTGTGCCCTTGGAGAAGCTCAAGTTCATCAAAGGC
ACTGATTACCAGCTCAGCAAAGAGTACACACTAGATGTGTACAGACTCTCCTCCGTGGTC
ACACAGCACGATTCCAAGAAGGCTGGAGCTGAGGTGGTAAAGCAGGTGGAGCACCCTTTG
CTGAGTGGCCTCTTATACCCCGGACTGCAGGCTTTGGATGAAGAGTATTTAAAAGTAGAT
GCCCAATTTGGAGGCATTGATCAGAGAAAGATTTTCACCTTTGCAGAGAAGTACCTCCCT
GCACTTGGCTATTCAAAACGGGTCCATCTGATGAATCCTATGGTTCCAGGATTAACAGGC
AGCAAAATGAGCTCTTCAGAAGAGGAGTCCAAGATTGATCTCCTTGATCGGAAGGAGGAT
GTGAAGAAAAAACTGAAGAAGGCCTTCTGTGAGCCAGGAAATGTGGAGAACAATGGGGTT
CTGTCCTTCATCAAGCATGTCCTTTTTCCCCTTAAGTCCGAGTTTGTGATCCTACGAGAT
GAGAAATGGGGTGGAAACAAAACCTACACAGCTTACGTGGACCTGGAAAAGGACTTTGCT
GCTGAGGTTGTACATCCTGGAGACCTGAAGAATTCTGTTGAAGTCGCACTGAACAAGTTG
CTGGATCCAATCCGGGAAAAGTTTAATACCCCTGCCCTGAAAAAACTGGCCAGCGCTGCC
TACCCAGATCCCTCAAAGCAGAAGCCAATGGCCAAAGGCCCTGCCAAGAATTCAGAACCA
GAGGAGGTCATCCCATCCCGGCTGGATATCCGTGTGGGGAAAATCATCACTGTGGAGAAG
CACCCAGATGCAGACAGCCTGTATGTAGAGAAGATTGACGTGGGGGAAGCTGAACCACGG
ACTGTGGTGAGCGGCCTGGTACAGTTCGTGCCCAAGGAGGAACTGCAGGACAGGCTGGTA
GTGGTGCTGTGCAACCTGAAACCCCAGAAGATGAGAGGAGTCGAGTCCCAAGGCATGCTT
CTGTGTGCTTCTATAGAAGGGATAAACCGCCAGGTTGAACCTCTGGACCCTCCGGCAGGC
TCTGCTCCTGGTGAGCACGTGTTTGTGAAGGGCTATGAAAAGGGCCAACCAGATGAGGAG
CTCAAGCCCAAGAAGAAAGTCTTCGAGAAGTTGCAGGCTGACTTCAAAATTTCTGAGGAG
TGCATCGCACAGTGGAAGCAAACCAACTTCATGACCAAGCTGGGCTCCATTTCCTGTAAA
TCGCTGAAAGGGGGGAACATTAGCTAG
Chromosome Location
1
Locus
1p35.1
External Identifiers
ResourceLink
UniProtKB IDP54577
UniProtKB Entry NameSYYC_HUMAN
GenBank Protein ID1184699
GenBank Gene IDU40714
GenAtlas IDYARS
HGNC IDHGNC:12840
General References
  1. Ribas de Pouplana L, Frugier M, Quinn CL, Schimmel P: Evidence that two present-day components needed for the genetic code appeared after nucleated cells separated from eubacteria. Proc Natl Acad Sci U S A. 1996 Jan 9;93(1):166-70. [Article]
  2. Kleeman TA, Wei D, Simpson KL, First EA: Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine. J Biol Chem. 1997 May 30;272(22):14420-5. [Article]
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  5. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [Article]
  6. 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. [Article]
  7. 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. [Article]
  8. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  9. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  10. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [Article]
  11. Yang XL, Skene RJ, McRee DE, Schimmel P: Crystal structure of a human aminoacyl-tRNA synthetase cytokine. Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15369-74. Epub 2002 Nov 11. [Article]
  12. Yang XL, Otero FJ, Skene RJ, McRee DE, Schimmel P, Ribas de Pouplana L: Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains. Proc Natl Acad Sci U S A. 2003 Dec 23;100(26):15376-80. Epub 2003 Dec 11. [Article]
  13. Jordanova A, Irobi J, Thomas FP, Van Dijck P, Meerschaert K, Dewil M, Dierick I, Jacobs A, De Vriendt E, Guergueltcheva V, Rao CV, Tournev I, Gondim FA, D'Hooghe M, Van Gerwen V, Callaerts P, Van Den Bosch L, Timmermans JP, Robberecht W, Gettemans J, Thevelein JM, De Jonghe P, Kremensky I, Timmerman V: Disrupted function and axonal distribution of mutant tyrosyl-tRNA synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy. Nat Genet. 2006 Feb;38(2):197-202. Epub 2006 Jan 22. [Article]
  14. Schabhuttl M, Wieland T, Senderek J, Baets J, Timmerman V, De Jonghe P, Reilly MM, Stieglbauer K, Laich E, Windhager R, Erwa W, Trajanoski S, Strom TM, Auer-Grumbach M: Whole-exome sequencing in patients with inherited neuropathies: outcome and challenges. J Neurol. 2014 May;261(5):970-82. doi: 10.1007/s00415-014-7289-8. Epub 2014 Mar 15. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00135Tyrosineapproved, investigational, nutraceuticalunknownDetails
DB03978TyrosinalexperimentalunknownDetails
DB07205N6-ISOPENTENYL-ADENOSINE-5'-MONOPHOSPHATEexperimentalunknownDetails
DB01766Beta-(2-Naphthyl)-AlanineexperimentalunknownDetails
DB08371p-Benzoyl-L-phenylalanineexperimentalunknownDetails
DB086174-(2,2,2-TRIFLUOROETHYL)-L-PHENYLALANINEexperimentalunknownDetails
DB02709ResveratrolinvestigationalunknowninhibitorDetails