Glutamine--tRNA ligase

Details

Name
Glutamine--tRNA ligase
Synonyms
  • 6.1.1.18
  • GlnRS
  • Glutaminyl-tRNA synthetase
Gene Name
QARS
Organism
Humans
Amino acid sequence
>lcl|BSEQ0004400|Glutamine--tRNA ligase
MAALDSLSLFTSLGLSEQKARETLKNSALSAQLREAATQAQQTLGSTIDKATGILLYGLA
SRLRDTRRLSFLVSYIASKKIHTEPQLSAALEYVRSHPLDPIDTVDFERECGVGVIVTPE
QIEEAVEAAINRHRPQLLVERYHFNMGLLMGEARAVLKWADGKMIKNEVDMQVLHLLGPK
LEADLEKKFKVAKARLEETDRRTAKDVVENGETADQTLSLMEQLRGEALKFHKPGENYKT
PGYVVTPHTMNLLKQHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFL
RFDDTNPEKEEAKFFTAICDMVAWLGYTPYKVTYASDYFDQLYAWAVELIRRGLAYVCHQ
RGEELKGHNTLPSPWRDRPMEESLLLFEAMRKGKFSEGEATLRMKLVMEDGKMDPVAYRV
KYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPV
QWEYGRLNLHYAVVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVG
VTVAQTTMEPHLLEACVRDVLNDTAPRAMAVLESLRVIITNFPAAKSLDIQVPNFPADET
KGFHQVPFAPIVFIERTDFKEEPEPGFKRLAWGQPVGLRHTGYVIELQHVVKGPSGCVES
LEVTCRRADAGEKPKAFIHWVSQPLMCEVRLYERLFQHKNPEDPTEVPGGFLSDLNLASL
HVVDAALVDCSVALAKPFDKFQFERLGYFSVDPDSHQGKLVFNRTVTLKEDPGKV
Number of residues
775
Molecular Weight
87797.97
Theoretical pI
7.16
GO Classification
Functions
ATP binding / glutamine-tRNA ligase activity
Processes
brain development / gene expression / glutaminyl-tRNA aminoacylation / tRNA aminoacylation for protein translation
Components
cytoplasm / cytosol / mitochondrial matrix
General Function
Glutamine-trna ligase activity
Specific Function
Plays a critical role in brain development.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0011617|Glutamine--tRNA ligase (QARS)
ATGGCGGCTCTAGACTCCCTGTCGCTCTTCACTAGCCTCGGCCTGAGCGAGCAGAAGGCC
CGCGAGACGCTCAAGAACTCGGCTCTGAGCGCGCAGCTGCGCGAGGCCGCTACTCAGGCT
CAGCAGACCCTGGGTTCCACCATTGACAAAGCTACCGGGATCCTGTTATATGGCTTGGCC
TCCCGACTCAGGGATACCCGGCGTCTCTCCTTCCTTGTAAGCTACATAGCCACTGCCCTT
GAGTATGTGCGGAGTCACCCCTTGGACCCCATCGACACTGTGGACTTCGAGCGGGAATGT
GGCGTGGGTGTCATTGTGACCCCAGAGCAGATTGAGGAGGCTGTGGAGGCTGCTATTAAC
AGGCACCGGCCCCAGCTCCTGGTGGAACGTTACCATTTCAACATGGGGCTGCTGATGGGA
GAGGCTCGGGCTGTGCTGAAGTGGGCAGATGGCAAAATGATCAAGAATGAAGTGGACATG
CAGGTCCTCCACCTTCTGGGCCCCAAGTTGGAGGCTGATCTGGAGAAGAAGTTCAAGGTG
GCAAAAGCTCGGCTAGAAGAAACAGACCGGAGGACGGCAAAGGATGTGGTGGAGAATGGC
GAGACTGCTGACCAGACCCTGTCTCTGATGGAGCAGCTCCGGGGGGAGGCCCTTAAGTTC
CACAAGCCTGGTGAGAACTACAAGACCCCAGGCTATGTGGTCACTCCACACACCATGAAT
CTACTAAAGCAGCACCTGGAGATTACTGGTGGGCAGGTACGTACCCGGTTCCCGCCAGAA
CCCAATGGAATCCTGCATATTGGACATGCCAAAGCCATCAATTTCAACTTTGGCTATGCC
AAGGCCAACAATGGCATCTGTTTTCTGCGTTTTGATGACACCAACCCTGAGAAGGAGGAA
GCAAAGTTCTTCACGGCCATCTGTGACATGGTAGCCTGGCTAGGCTACACACCTTACAAA
GTCACATATGCGTCTGACTATTTTGACCAGCTATATGCGTGGGCTGTGGAGCTCATCCGC
AGGGGTCTGGCTTATGTGTGCCACCAGCGAGGAGAGGAGCTCAAAGGCCATAATACTCTG
CCTTCACCCTGGAGAGACCGTCCCATGGAGGAGTCACTGCTGCTCTTTGAGGCAATGCGC
AAGGGCAAGTTTTCAGAGGGCGAGGCCACACTACGGATGAAGCTGGTGATGGAGGATGGC
AAGATGGACCCTGTAGCCTATCGAGTCAAGTATACACCACACCACCGCACAGGGGACAAA
TGGTGCATCTATCCCACCTACGACTACACACACTGCCTCTGTGACTCCATCGAGCACATC
ACTCACTCACTCTGCACCAAGGAATTCCAGGCCCGACGCTCTTCCTACTTCTGGCTTTGC
AATGCACTGGACGTCTATTGCCCTGTGCAGTGGGAGTATGGCCGCCTCAACCTGCACTAT
GCTGTTGTCTCTAAGAGGAAGATCCTCCAGCTTGTAGCAACTGGTGCTGTGCGGGACTGG
GATGACCCACGGCTCTTTACACTCACGGCCCTGCGACGGCGGGGCTTCCCACCTGAGGCC
ATCAACAACTTCTGTGCCCGGGTGGGAGTGACTGTGGCACAAACCACAATGGAGCCACAT
CTTCTAGAAGCCTGTGTGCGTGATGTGCTGAATGACACAGCCCCACGAGCCATGGCTGTG
CTGGAGTCACTACGGGTCATCATCACCAACTTTCCTGCTGCCAAGTCCTTGGACATCCAG
GTGCCCAACTTCCCAGCTGATGAGACCAAAGGCTTCCATCAGGTTCCCTTTGCACCCATT
GTCTTCATTGAGAGGACTGACTTCAAGGAGGAGCCAGAGCCAGGATTTAAGCGCCTGGCT
TGGGGCCAGCCTGTGGGCCTGAGGCATACAGGCTACGTCATTGAGCTGCAGCATGTTGTC
AAGGGCCCCAGTGGTTGTGTAGAGAGTCTGGAGGTGACCTGCAGACGGGCAGATGCTGGA
GAGAAGCCAAAGGCCTTTATTCACTGGGTGTCACAGCCTTTGATGTGTGAGGTTCGCCTC
TATGAGCGACTATTCCAGCACAAGAACCCTGAAGATCCTACTGAGGTGCCTGGTGGATTT
TTAAGTGACCTGAACCTGGCATCACTACACGTGGTGGATGCAGCATTAGTGGACTGCTCT
GTGGCCCTGGCAAAACCCTTCGACAAGTTCCAGTTTGAGCGTCTTGGATATTTCTCCGTG
GATCCAGACAGCCATCAGGGAAAGCTTGTCTTTAACCGAACTGTCACACTGAAGGAAGAC
CCAGGAAAGGTGTGA
Chromosome Location
3
Locus
3p21.3-p21.1
External Identifiers
ResourceLink
UniProtKB IDP47897
UniProtKB Entry NameSYQ_HUMAN
GenBank Protein ID558586
GenBank Gene IDX76013
GenAtlas IDQARS
HGNC IDHGNC:9751
General References
  1. Lamour V, Quevillon S, Diriong S, N'Guyen VC, Lipinski M, Mirande M: Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme as a case of horizontal gene transfer. Proc Natl Acad Sci U S A. 1994 Aug 30;91(18):8670-4. [Article]
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  4. 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. [Article]
  5. 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. [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. Bienvenut WV, Sumpton D, Martinez A, Lilla S, Espagne C, Meinnel T, Giglione C: Comparative large scale characterization of plant versus mammal proteins reveals similar and idiosyncratic N-alpha-acetylation features. Mol Cell Proteomics. 2012 Jun;11(6):M111.015131. doi: 10.1074/mcp.M111.015131. Epub 2012 Jan 5. [Article]
  10. Van Damme P, Lasa M, Polevoda B, Gazquez C, Elosegui-Artola A, Kim DS, De Juan-Pardo E, Demeyer K, Hole K, Larrea E, Timmerman E, Prieto J, Arnesen T, Sherman F, Gevaert K, Aldabe R: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. Proc Natl Acad Sci U S A. 2012 Jul 31;109(31):12449-54. doi: 10.1073/pnas.1210303109. Epub 2012 Jul 18. [Article]
  11. Zhang X, Ling J, Barcia G, Jing L, Wu J, Barry BJ, Mochida GH, Hill RS, Weimer JM, Stein Q, Poduri A, Partlow JN, Ville D, Dulac O, Yu TW, Lam AT, Servattalab S, Rodriguez J, Boddaert N, Munnich A, Colleaux L, Zon LI, Soll D, Walsh CA, Nabbout R: Mutations in QARS, encoding glutaminyl-tRNA synthetase, cause progressive microcephaly, cerebral-cerebellar atrophy, and intractable seizures. Am J Hum Genet. 2014 Apr 3;94(4):547-58. doi: 10.1016/j.ajhg.2014.03.003. Epub 2014 Mar 20. [Article]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00130L-Glutamineapproved, investigational, nutraceuticalunknownsubstrateDetails