VARS

Protein-coding gene in the species Homo sapiens
VARS1
Identifiers
AliasesVARS1, VARS, NDMSCA, valyl-tRNA synthetase 1, G7A, VARS2, valyl-tRNA synthetase
External IDsOMIM: 192150; MGI: 90675; HomoloGene: 4587; GeneCards: VARS1; OMA:VARS1 - orthologs
Gene location (Human)
Chromosome 6 (human)
Chr.Chromosome 6 (human)[1]
Chromosome 6 (human)
Genomic location for VARS1
Genomic location for VARS1
Band6p21.33Start31,777,518 bp[1]
End31,795,752 bp[1]
Gene location (Mouse)
Chromosome 17 (mouse)
Chr.Chromosome 17 (mouse)[2]
Chromosome 17 (mouse)
Genomic location for VARS1
Genomic location for VARS1
Band17 B1|17 18.54 cMStart35,219,963 bp[2]
End35,235,298 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right testis

  • left testis

  • islet of Langerhans

  • pituitary gland

  • ganglionic eminence

  • appendix

  • anterior pituitary

  • stromal cell of endometrium

  • gastrocnemius muscle

  • muscle tissue
Top expressed in
  • spermatid

  • ventricular zone

  • tail of embryo

  • seminiferous tubule

  • epiblast

  • yolk sac

  • spermatocyte

  • lip

  • tibiofemoral joint

  • otic vesicle
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • aminoacyl-tRNA ligase activity
  • nucleotide binding
  • ligase activity
  • protein binding
  • ATP binding
  • aminoacyl-tRNA editing activity
  • valine-tRNA ligase activity
Cellular component
  • cytoplasm
  • cytosol
Biological process
  • tRNA aminoacylation for protein translation
  • protein biosynthesis
  • valyl-tRNA aminoacylation
  • aminoacyl-tRNA metabolism involved in translational fidelity
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

7407

22321

Ensembl
ENSG00000226589
ENSG00000096171
ENSG00000231945
ENSG00000227686
ENSG00000204394

ENSG00000224264
ENSG00000231116

ENSMUSG00000007029

UniProt

P26640

Q9Z1Q9

RefSeq (mRNA)

NM_006295

NM_011690

RefSeq (protein)

NP_006286
NP_006286.1

NP_035820

Location (UCSC)Chr 6: 31.78 – 31.8 MbChr 17: 35.22 – 35.24 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Valyl-tRNA synthetase is an enzyme that in humans is encoded by the VARS gene.[5][6]

Function

Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. The protein encoded by this gene belongs to class I aminoacyl-tRNA synthetase family and is located in the class III region of the major histocompatibility complex.[6]

See also

References

  1. ^ a b c ENSG00000096171, ENSG00000231945, ENSG00000227686, ENSG00000204394, ENSG00000224264, ENSG00000231116 GRCh38: Ensembl release 89: ENSG00000226589, ENSG00000096171, ENSG00000231945, ENSG00000227686, ENSG00000204394, ENSG00000224264, ENSG00000231116 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000007029 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Bonnefond L, Fender A, Rudinger-Thirion J, Giegé R, Florentz C, Sissler M (March 2005). "Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS". Biochemistry. 44 (12): 4805–16. doi:10.1021/bi047527z. PMID 15779907.
  6. ^ a b "Entrez Gene: VARS valyl-tRNA synthetase".

Further reading

  • Hsieh SL, Campbell RD (September 1991). "Evidence that gene G7a in the human major histocompatibility complex encodes valyl-tRNA synthetase". The Biochemical Journal. 278 (3): 809–16. doi:10.1042/bj2780809. PMC 1151418. PMID 1898367.
  • Sargent CA, Dunham I, Campbell RD (August 1989). "Identification of multiple HTF-island associated genes in the human major histocompatibility complex class III region". The EMBO Journal. 8 (8): 2305–12. doi:10.1002/j.1460-2075.1989.tb08357.x. PMC 401163. PMID 2477242.
  • Bec G, Kerjan P, Zha XD, Waller JP (December 1989). "Valyl-tRNA synthetase from rabbit liver. I. Purification as a heterotypic complex in association with elongation factor 1". The Journal of Biological Chemistry. 264 (35): 21131–7. doi:10.1016/S0021-9258(19)30056-0. PMID 2556394.
  • Wolfson AD, Orlovsky AF, Gladilin KL (October 1988). "Mammalian valyl-tRNA synthetase forms a complex with the first elongation factor". FEBS Letters. 238 (2): 262–4. Bibcode:1988FEBSL.238..262M. doi:10.1016/0014-5793(88)80492-7. PMID 3169261. S2CID 45934458.
  • Bec G, Kerjan P, Waller JP (January 1994). "Reconstitution in vitro of the valyl-tRNA synthetase-elongation factor (EF) 1 beta gamma delta complex. Essential roles of the NH2-terminal extension of valyl-tRNA synthetase and of the EF-1 delta subunit in complex formation". The Journal of Biological Chemistry. 269 (3): 2086–92. doi:10.1016/S0021-9258(17)42139-9. PMID 8294461.
  • Vilalta A, Donovan D, Wood L, Vogeli G, Yang DC (January 1993). "Cloning, sequencing and expression of a cDNA encoding mammalian valyl-tRNA synthetase". Gene. 123 (2): 181–6. doi:10.1016/0378-1119(93)90122-J. PMID 8428657.
  • Motorin Y (May 1996). "Two human valyl-tRNA synthetase-encoding cDNA sequences deposited in GenBank display extensive differences". Gene. 170 (2): 289–91. doi:10.1016/0378-1119(96)84699-3. PMID 8666263.
  • Xie T, Rowen L, Aguado B, Ahearn ME, Madan A, Qin S, Campbell RD, Hood L (December 2003). "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse". Genome Research. 13 (12): 2621–36. doi:10.1101/gr.1736803. PMC 403804. PMID 14656967.
  • Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S, Hopf C, Huhse B, Mangano R, Michon AM, Schirle M, Schlegl J, Schwab M, Stein MA, Bauer A, Casari G, Drewes G, Gavin AC, Jackson DB, Joberty G, Neubauer G, Rick J, Kuster B, Superti-Furga G (February 2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nature Cell Biology. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Jiang S, Wolfe CL, Warrington JA, Norcum MT (November 2005). "Three-dimensional reconstruction of the valyl-tRNA synthetase/elongation factor-1H complex and localization of the delta subunit". FEBS Letters. 579 (27): 6049–54. Bibcode:2005FEBSL.579.6049J. doi:10.1016/j.febslet.2005.09.062. PMID 16229838. S2CID 83645345.
  • Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
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