Full text data of VARS
VARS
(G7A, VARS2)
[Confidence: low (only semi-automatic identification from reviews)]
Valine--tRNA ligase; 6.1.1.9 (Protein G7a; Valyl-tRNA synthetase; ValRS)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Valine--tRNA ligase; 6.1.1.9 (Protein G7a; Valyl-tRNA synthetase; ValRS)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P26640
ID SYVC_HUMAN Reviewed; 1264 AA.
AC P26640; B0V1N1; Q5JQ90; Q96E77; Q9UQM2;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2000, sequence version 4.
DT 22-JAN-2014, entry version 148.
DE RecName: Full=Valine--tRNA ligase;
DE EC=6.1.1.9;
DE AltName: Full=Protein G7a;
DE AltName: Full=Valyl-tRNA synthetase;
DE Short=ValRS;
GN Name=VARS; Synonyms=G7A, VARS2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1898367;
RA Hsieh H.-L., Campbell R.D.;
RT "Evidence that gene G7a in the human major histocompatibility complex
RT encodes valyl-tRNA synthetase.";
RL Biochem. J. 278:809-816(1991).
RN [2]
RP ERRATUM.
RA Hsieh S.-L., Campbell R.D.;
RL Biochem. J. 281:879-879(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
RA Campbell R.D., Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-17; 123-147; 451-461; 592-606; 619-633; 935-942;
RP 1120-1129 AND 1252-1262, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION
RP AT SER-2, AND MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Dhillon A.S., Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 201-1263.
RX PubMed=8428657; DOI=10.1016/0378-1119(93)90122-J;
RA Vilalta A., Donovan D., Wood L., Vogeli G., Yang D.C.H.;
RT "Cloning, sequencing and expression of a cDNA encoding mammalian
RT valyl-tRNA synthetase.";
RL Gene 123:181-186(1993).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-645, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- CATALYTIC ACTIVITY: ATP + L-valine + tRNA(Val) = AMP + diphosphate
CC + L-valyl-tRNA(Val).
CC -!- ENZYME REGULATION: Can be regulated by protein kinase C-dependent
CC phosphorylation.
CC -!- SUBUNIT: Forms high-molecular-mass aggregates with elongation
CC factor 1.
CC -!- INTERACTION:
CC Q05639:EEF1A2; NbExp=1; IntAct=EBI-355765, EBI-354943;
CC P11171:EPB41; NbExp=1; IntAct=EBI-355765, EBI-1050906;
CC P30480:HLA-B; NbExp=1; IntAct=EBI-355765, EBI-1054175;
CC P19532:TFE3; NbExp=1; IntAct=EBI-355765, EBI-1048957;
CC Q9Y4K3:TRAF6; NbExp=1; IntAct=EBI-355765, EBI-359276;
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC family.
CC -!- SIMILARITY: Contains 1 GST C-terminal domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA41990.1; Type=Frameshift; Positions=620, 640;
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DR EMBL; X59303; CAA41990.1; ALT_FRAME; mRNA.
DR EMBL; AF134726; AAD21819.1; -; Genomic_DNA.
DR EMBL; BA000025; BAB63303.1; -; Genomic_DNA.
DR EMBL; AL671762; CAI18211.1; -; Genomic_DNA.
DR EMBL; AL662899; CAI18211.1; JOINED; Genomic_DNA.
DR EMBL; AL662899; CAI18384.1; -; Genomic_DNA.
DR EMBL; AL671762; CAI18384.1; JOINED; Genomic_DNA.
DR EMBL; AL662834; CAI17732.1; -; Genomic_DNA.
DR EMBL; CR925765; CAQ10624.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03523.1; -; Genomic_DNA.
DR EMBL; BC012808; AAH12808.1; -; mRNA.
DR EMBL; M98326; AAA81332.1; -; mRNA.
DR PIR; S17675; S17675.
DR RefSeq; NP_006286.1; NM_006295.2.
DR UniGene; Hs.520026; -.
DR ProteinModelPortal; P26640; -.
DR SMR; P26640; 43-211, 296-1258.
DR IntAct; P26640; 11.
DR MINT; MINT-1148831; -.
DR STRING; 9606.ENSP00000401121; -.
DR BindingDB; P26640; -.
DR ChEMBL; CHEMBL2612; -.
DR DrugBank; DB00161; L-Valine.
DR PhosphoSite; P26640; -.
DR DMDM; 12644177; -.
DR PaxDb; P26640; -.
DR PRIDE; P26640; -.
DR Ensembl; ENST00000211402; ENSP00000211402; ENSG00000096171.
DR Ensembl; ENST00000375663; ENSP00000364815; ENSG00000204394.
DR Ensembl; ENST00000422694; ENSP00000401121; ENSG00000224264.
DR Ensembl; ENST00000435657; ENSP00000415316; ENSG00000231116.
DR Ensembl; ENST00000457796; ENSP00000403359; ENSG00000226589.
DR GeneID; 7407; -.
DR KEGG; hsa:7407; -.
DR UCSC; uc003nxe.3; human.
DR CTD; 7407; -.
DR GeneCards; GC06M031745; -.
DR GeneCards; GC06Mj31732; -.
DR GeneCards; GC06Mk31727; -.
DR H-InvDB; HIX0005731; -.
DR H-InvDB; HIX0165932; -.
DR H-InvDB; HIX0166155; -.
DR H-InvDB; HIX0166435; -.
DR H-InvDB; HIX0166904; -.
DR H-InvDB; HIX0167447; -.
DR HGNC; HGNC:12651; VARS.
DR HPA; HPA046710; -.
DR MIM; 192150; gene.
DR neXtProt; NX_P26640; -.
DR PharmGKB; PA37275; -.
DR eggNOG; COG0525; -.
DR HOGENOM; HOG000020094; -.
DR HOVERGEN; HBG017878; -.
DR InParanoid; P26640; -.
DR KO; K01873; -.
DR OMA; MAGFINK; -.
DR BRENDA; 6.1.1.9; 2681.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; VARS; human.
DR GeneWiki; VARS; -.
DR GenomeRNAi; 7407; -.
DR NextBio; 28996; -.
DR PRO; PR:P26640; -.
DR ArrayExpress; P26640; -.
DR Bgee; P26640; -.
DR CleanEx; HS_VARS; -.
DR CleanEx; HS_VARS2; -.
DR Genevestigator; P26640; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IDA:UniProtKB.
DR GO; GO:0006450; P:regulation of translational fidelity; IEA:GOC.
DR GO; GO:0006414; P:translational elongation; NAS:UniProtKB.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.50.620; -; 3.
DR Gene3D; 3.90.740.10; -; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd.
DR InterPro; IPR013155; V/L/I-tRNA-synth_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR PANTHER; PTHR11946:SF5; PTHR11946:SF5; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00422; valS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
KW Complete proteome; Direct protein sequencing; Ligase;
KW Nucleotide-binding; Polymorphism; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1264 Valine--tRNA ligase.
FT /FTId=PRO_0000106253.
FT DOMAIN 89 219 GST C-terminal.
FT MOTIF 344 354 "HIGH" region.
FT MOTIF 862 866 "KMSKS" region.
FT BINDING 865 865 ATP (By similarity).
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 645 645 N6-acetyllysine.
FT VARIANT 51 51 P -> R (in dbSNP:rs2607015).
FT /FTId=VAR_052647.
FT VARIANT 51 51 P -> T (in dbSNP:rs2753960).
FT /FTId=VAR_061909.
FT VARIANT 181 181 R -> C (in dbSNP:rs35196751).
FT /FTId=VAR_052648.
FT VARIANT 626 626 P -> S (in dbSNP:rs11531).
FT /FTId=VAR_052649.
FT VARIANT 1008 1008 P -> L (in dbSNP:rs1076827).
FT /FTId=VAR_052650.
FT CONFLICT 51 51 P -> S (in Ref. 1; CAA41990 and 7;
FT AAH12808).
FT CONFLICT 331 331 A -> G (in Ref. 9; AAA81332).
FT CONFLICT 590 590 V -> G (in Ref. 1; CAA41990).
FT CONFLICT 792 792 S -> F (in Ref. 1; CAA41990).
FT CONFLICT 1064 1064 M -> I (in Ref. 9; AAA81332).
FT CONFLICT 1169 1169 Missing (in Ref. 9; AAA81332).
SQ SEQUENCE 1264 AA; 140476 MW; 95CCDDBB3AB148AD CRC64;
MSTLYVSPHP DAFPSLRALI AARYGEAGEG PGWGGAHPRI CLQPPPTSRT PFPPPRLPAL
EQGPGGLWVW GATAVAQLLW PAGLGGPGGS RAAVLVQQWV SYADTELIPA ACGATLPALG
LRSSAQDPQA VLGALGRALS PLEEWLRLHT YLAGEAPTLA DLAAVTALLL PFRYVLDPPA
RRIWNNVTRW FVTCVRQPEF RAVLGEVVLY SGARPLSHQP GPEAPALPKT AAQLKKEAKK
REKLEKFQQK QKIQQQQPPP GEKKPKPEKR EKRDPGVITY DLPTPPGEKK DVSGPMPDSY
SPRYVEAAWY PWWEQQGFFK PEYGRPNVSA ANPRGVFMMC IPPPNVTGSL HLGHALTNAI
QDSLTRWHRM RGETTLWNPG CDHAGIATQV VVEKKLWREQ GLSRHQLGRE AFLQEVWKWK
EEKGDRIYHQ LKKLGSSLDW DRACFTMDPK LSAAVTEAFV RLHEEGIIYR STRLVNWSCT
LNSAISDIEV DKKELTGRTL LSVPGYKEKV EFGVLVSFAY KVQGSDSDEE VVVATTRIET
MLGDVAVAVH PKDTRYQHLK GKNVIHPFLS RSLPIVFDEF VDMDFGTGAV KITPAHDQND
YEVGQRHGLE AISIMDSRGA LINVPPPFLG LPRFEARKAV LVALKERGLF RGIEDNPMVV
PLCNRSKDVV EPLLRPQWYV RCGEMAQAAS AAVTRGDLRI LPEAHQRTWH AWMDNIREWC
ISRQLWWGHR IPAYFVTVSD PAVPPGEDPD GRYWVSGRNE AEAREKAAKE FGVSPDKISL
QQDEDVLDTW FSSGLFPLSI LGWPNQSEDL SVFYPGTLLE TGHDILFFWV ARMVMLGLKL
TGRLPFREVY LHAIVRDAHG RKMSKSLGNV IDPLDVIYGI SLQGLHNQLL NSNLDPSEVE
KAKEGQKADF PAGIPECGTD ALRFGLCAYM SQGRDINLDV NRILGYRHFC NKLWNATKFA
LRGLGKGFVP SPTSQPGGHE SLVDRWIRSR LTEAVRLSNQ GFQAYDFPAV TTAQYSFWLY
ELCDVYLECL KPVLNGVDQV AAECARQTLY TCLDVGLRLL SPFMPFVTEE LFQRLPRRMP
QAPPSLCVTP YPEPSECSWK DPEAEAALEL ALSITRAVRS LRADYNLTRI RPDCFLEVAD
EATGALASAV SGYVQALASA GVVAVLALGA PAPQGCAVAL ASDRCSIHLQ LQGLVDPARE
LGKLQAKRVE AQRQAQRLRE RRAASGYPVK VPLEVQEADE AKLQQTEAEL RKVDEAIALF
QKML
//
ID SYVC_HUMAN Reviewed; 1264 AA.
AC P26640; B0V1N1; Q5JQ90; Q96E77; Q9UQM2;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2000, sequence version 4.
DT 22-JAN-2014, entry version 148.
DE RecName: Full=Valine--tRNA ligase;
DE EC=6.1.1.9;
DE AltName: Full=Protein G7a;
DE AltName: Full=Valyl-tRNA synthetase;
DE Short=ValRS;
GN Name=VARS; Synonyms=G7A, VARS2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1898367;
RA Hsieh H.-L., Campbell R.D.;
RT "Evidence that gene G7a in the human major histocompatibility complex
RT encodes valyl-tRNA synthetase.";
RL Biochem. J. 278:809-816(1991).
RN [2]
RP ERRATUM.
RA Hsieh S.-L., Campbell R.D.;
RL Biochem. J. 281:879-879(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
RA Campbell R.D., Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-17; 123-147; 451-461; 592-606; 619-633; 935-942;
RP 1120-1129 AND 1252-1262, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION
RP AT SER-2, AND MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Dhillon A.S., Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 201-1263.
RX PubMed=8428657; DOI=10.1016/0378-1119(93)90122-J;
RA Vilalta A., Donovan D., Wood L., Vogeli G., Yang D.C.H.;
RT "Cloning, sequencing and expression of a cDNA encoding mammalian
RT valyl-tRNA synthetase.";
RL Gene 123:181-186(1993).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-645, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- CATALYTIC ACTIVITY: ATP + L-valine + tRNA(Val) = AMP + diphosphate
CC + L-valyl-tRNA(Val).
CC -!- ENZYME REGULATION: Can be regulated by protein kinase C-dependent
CC phosphorylation.
CC -!- SUBUNIT: Forms high-molecular-mass aggregates with elongation
CC factor 1.
CC -!- INTERACTION:
CC Q05639:EEF1A2; NbExp=1; IntAct=EBI-355765, EBI-354943;
CC P11171:EPB41; NbExp=1; IntAct=EBI-355765, EBI-1050906;
CC P30480:HLA-B; NbExp=1; IntAct=EBI-355765, EBI-1054175;
CC P19532:TFE3; NbExp=1; IntAct=EBI-355765, EBI-1048957;
CC Q9Y4K3:TRAF6; NbExp=1; IntAct=EBI-355765, EBI-359276;
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC family.
CC -!- SIMILARITY: Contains 1 GST C-terminal domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA41990.1; Type=Frameshift; Positions=620, 640;
CC -----------------------------------------------------------------------
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DR EMBL; X59303; CAA41990.1; ALT_FRAME; mRNA.
DR EMBL; AF134726; AAD21819.1; -; Genomic_DNA.
DR EMBL; BA000025; BAB63303.1; -; Genomic_DNA.
DR EMBL; AL671762; CAI18211.1; -; Genomic_DNA.
DR EMBL; AL662899; CAI18211.1; JOINED; Genomic_DNA.
DR EMBL; AL662899; CAI18384.1; -; Genomic_DNA.
DR EMBL; AL671762; CAI18384.1; JOINED; Genomic_DNA.
DR EMBL; AL662834; CAI17732.1; -; Genomic_DNA.
DR EMBL; CR925765; CAQ10624.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03523.1; -; Genomic_DNA.
DR EMBL; BC012808; AAH12808.1; -; mRNA.
DR EMBL; M98326; AAA81332.1; -; mRNA.
DR PIR; S17675; S17675.
DR RefSeq; NP_006286.1; NM_006295.2.
DR UniGene; Hs.520026; -.
DR ProteinModelPortal; P26640; -.
DR SMR; P26640; 43-211, 296-1258.
DR IntAct; P26640; 11.
DR MINT; MINT-1148831; -.
DR STRING; 9606.ENSP00000401121; -.
DR BindingDB; P26640; -.
DR ChEMBL; CHEMBL2612; -.
DR DrugBank; DB00161; L-Valine.
DR PhosphoSite; P26640; -.
DR DMDM; 12644177; -.
DR PaxDb; P26640; -.
DR PRIDE; P26640; -.
DR Ensembl; ENST00000211402; ENSP00000211402; ENSG00000096171.
DR Ensembl; ENST00000375663; ENSP00000364815; ENSG00000204394.
DR Ensembl; ENST00000422694; ENSP00000401121; ENSG00000224264.
DR Ensembl; ENST00000435657; ENSP00000415316; ENSG00000231116.
DR Ensembl; ENST00000457796; ENSP00000403359; ENSG00000226589.
DR GeneID; 7407; -.
DR KEGG; hsa:7407; -.
DR UCSC; uc003nxe.3; human.
DR CTD; 7407; -.
DR GeneCards; GC06M031745; -.
DR GeneCards; GC06Mj31732; -.
DR GeneCards; GC06Mk31727; -.
DR H-InvDB; HIX0005731; -.
DR H-InvDB; HIX0165932; -.
DR H-InvDB; HIX0166155; -.
DR H-InvDB; HIX0166435; -.
DR H-InvDB; HIX0166904; -.
DR H-InvDB; HIX0167447; -.
DR HGNC; HGNC:12651; VARS.
DR HPA; HPA046710; -.
DR MIM; 192150; gene.
DR neXtProt; NX_P26640; -.
DR PharmGKB; PA37275; -.
DR eggNOG; COG0525; -.
DR HOGENOM; HOG000020094; -.
DR HOVERGEN; HBG017878; -.
DR InParanoid; P26640; -.
DR KO; K01873; -.
DR OMA; MAGFINK; -.
DR BRENDA; 6.1.1.9; 2681.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; VARS; human.
DR GeneWiki; VARS; -.
DR GenomeRNAi; 7407; -.
DR NextBio; 28996; -.
DR PRO; PR:P26640; -.
DR ArrayExpress; P26640; -.
DR Bgee; P26640; -.
DR CleanEx; HS_VARS; -.
DR CleanEx; HS_VARS2; -.
DR Genevestigator; P26640; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IDA:UniProtKB.
DR GO; GO:0006450; P:regulation of translational fidelity; IEA:GOC.
DR GO; GO:0006414; P:translational elongation; NAS:UniProtKB.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.50.620; -; 3.
DR Gene3D; 3.90.740.10; -; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd.
DR InterPro; IPR013155; V/L/I-tRNA-synth_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR PANTHER; PTHR11946:SF5; PTHR11946:SF5; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00422; valS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
KW Complete proteome; Direct protein sequencing; Ligase;
KW Nucleotide-binding; Polymorphism; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1264 Valine--tRNA ligase.
FT /FTId=PRO_0000106253.
FT DOMAIN 89 219 GST C-terminal.
FT MOTIF 344 354 "HIGH" region.
FT MOTIF 862 866 "KMSKS" region.
FT BINDING 865 865 ATP (By similarity).
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 645 645 N6-acetyllysine.
FT VARIANT 51 51 P -> R (in dbSNP:rs2607015).
FT /FTId=VAR_052647.
FT VARIANT 51 51 P -> T (in dbSNP:rs2753960).
FT /FTId=VAR_061909.
FT VARIANT 181 181 R -> C (in dbSNP:rs35196751).
FT /FTId=VAR_052648.
FT VARIANT 626 626 P -> S (in dbSNP:rs11531).
FT /FTId=VAR_052649.
FT VARIANT 1008 1008 P -> L (in dbSNP:rs1076827).
FT /FTId=VAR_052650.
FT CONFLICT 51 51 P -> S (in Ref. 1; CAA41990 and 7;
FT AAH12808).
FT CONFLICT 331 331 A -> G (in Ref. 9; AAA81332).
FT CONFLICT 590 590 V -> G (in Ref. 1; CAA41990).
FT CONFLICT 792 792 S -> F (in Ref. 1; CAA41990).
FT CONFLICT 1064 1064 M -> I (in Ref. 9; AAA81332).
FT CONFLICT 1169 1169 Missing (in Ref. 9; AAA81332).
SQ SEQUENCE 1264 AA; 140476 MW; 95CCDDBB3AB148AD CRC64;
MSTLYVSPHP DAFPSLRALI AARYGEAGEG PGWGGAHPRI CLQPPPTSRT PFPPPRLPAL
EQGPGGLWVW GATAVAQLLW PAGLGGPGGS RAAVLVQQWV SYADTELIPA ACGATLPALG
LRSSAQDPQA VLGALGRALS PLEEWLRLHT YLAGEAPTLA DLAAVTALLL PFRYVLDPPA
RRIWNNVTRW FVTCVRQPEF RAVLGEVVLY SGARPLSHQP GPEAPALPKT AAQLKKEAKK
REKLEKFQQK QKIQQQQPPP GEKKPKPEKR EKRDPGVITY DLPTPPGEKK DVSGPMPDSY
SPRYVEAAWY PWWEQQGFFK PEYGRPNVSA ANPRGVFMMC IPPPNVTGSL HLGHALTNAI
QDSLTRWHRM RGETTLWNPG CDHAGIATQV VVEKKLWREQ GLSRHQLGRE AFLQEVWKWK
EEKGDRIYHQ LKKLGSSLDW DRACFTMDPK LSAAVTEAFV RLHEEGIIYR STRLVNWSCT
LNSAISDIEV DKKELTGRTL LSVPGYKEKV EFGVLVSFAY KVQGSDSDEE VVVATTRIET
MLGDVAVAVH PKDTRYQHLK GKNVIHPFLS RSLPIVFDEF VDMDFGTGAV KITPAHDQND
YEVGQRHGLE AISIMDSRGA LINVPPPFLG LPRFEARKAV LVALKERGLF RGIEDNPMVV
PLCNRSKDVV EPLLRPQWYV RCGEMAQAAS AAVTRGDLRI LPEAHQRTWH AWMDNIREWC
ISRQLWWGHR IPAYFVTVSD PAVPPGEDPD GRYWVSGRNE AEAREKAAKE FGVSPDKISL
QQDEDVLDTW FSSGLFPLSI LGWPNQSEDL SVFYPGTLLE TGHDILFFWV ARMVMLGLKL
TGRLPFREVY LHAIVRDAHG RKMSKSLGNV IDPLDVIYGI SLQGLHNQLL NSNLDPSEVE
KAKEGQKADF PAGIPECGTD ALRFGLCAYM SQGRDINLDV NRILGYRHFC NKLWNATKFA
LRGLGKGFVP SPTSQPGGHE SLVDRWIRSR LTEAVRLSNQ GFQAYDFPAV TTAQYSFWLY
ELCDVYLECL KPVLNGVDQV AAECARQTLY TCLDVGLRLL SPFMPFVTEE LFQRLPRRMP
QAPPSLCVTP YPEPSECSWK DPEAEAALEL ALSITRAVRS LRADYNLTRI RPDCFLEVAD
EATGALASAV SGYVQALASA GVVAVLALGA PAPQGCAVAL ASDRCSIHLQ LQGLVDPARE
LGKLQAKRVE AQRQAQRLRE RRAASGYPVK VPLEVQEADE AKLQQTEAEL RKVDEAIALF
QKML
//
MIM
192150
*RECORD*
*FIELD* NO
192150
*FIELD* TI
*192150 VALYL-tRNA SYNTHETASE; VARS
;;VALYL-tRNA SYNTHETASE 1; VARS1;;
G7A;;
VARS2, FORMERLY
read more*FIELD* TX
CLONING
Hsieh et al. (1991) identified the G7a gene, encoding human valyl-tRNA
synthetase, within the class III region of the major histocompatibility
complex (MHC). Hsieh and Campbell (1991) cloned a VARS cDNA encoding a
deduced 1,265-amino acid protein with a molecular mass of 140,457 Da.
Comparison of the amino acid sequence with those in protein databases
showed 38 to 48% identity to valyl-tRNA of bacteria and yeast.
MAPPING
Hsieh et al. (1991) identified the G7a gene (VARS) in a 680-kb segment
of DNA within the class III region of the MHC on chromosome 6p21.3.
HISTORY
The assignment of another valyl-tRNA synthetase gene, previously
designated VARS1, to chromosome 9 by Walter et al. (1987) was found to
be in error.
*FIELD* RF
1. Hsieh, S.-L.; Campbell, R. D.: Evidence that gene G7a in the human
major histocompatibility complex encodes valyl-tRNA synthetase. Biochem.
J. 278: 809-816, 1991. Note: Erratum: Biochem. J. 281: 879 only,
1992.
2. Hsieh, S.-L.; Kendall, E.; Milner, C.; Cross, S.; Cheng, J.; Khanna,
A.; Olaversen, M.; Campbell, R. D.: Cloning of the human valyl-tRNA
synthetase gene and its location in the major histocompatibility complex
on chromosome 6. (Abstract) Cytogenet. Cell Genet. 58: 1912 only,
1991.
3. Walter, B.; Yen, A.; Wasmuth, J.; Smith, M.: Selection of somatic
cell hybrids containing human chromosome 9 using a temperature sensitive
CHO valyl-t-RNA synthetase mutant. (Abstract) Cytogenet. Cell Genet. 46:
710 only, 1987.
*FIELD* CN
Alan F. Scott - updated: 11/18/1999
*FIELD* CD
Victor A. McKusick: 11/12/1987
*FIELD* ED
carol: 05/02/2006
carol: 5/2/2006
alopez: 11/18/1999
alopez: 7/26/1999
warfield: 3/29/1994
carol: 2/11/1993
carol: 1/15/1993
supermim: 3/16/1992
carol: 2/23/1992
carol: 8/8/1991
*RECORD*
*FIELD* NO
192150
*FIELD* TI
*192150 VALYL-tRNA SYNTHETASE; VARS
;;VALYL-tRNA SYNTHETASE 1; VARS1;;
G7A;;
VARS2, FORMERLY
read more*FIELD* TX
CLONING
Hsieh et al. (1991) identified the G7a gene, encoding human valyl-tRNA
synthetase, within the class III region of the major histocompatibility
complex (MHC). Hsieh and Campbell (1991) cloned a VARS cDNA encoding a
deduced 1,265-amino acid protein with a molecular mass of 140,457 Da.
Comparison of the amino acid sequence with those in protein databases
showed 38 to 48% identity to valyl-tRNA of bacteria and yeast.
MAPPING
Hsieh et al. (1991) identified the G7a gene (VARS) in a 680-kb segment
of DNA within the class III region of the MHC on chromosome 6p21.3.
HISTORY
The assignment of another valyl-tRNA synthetase gene, previously
designated VARS1, to chromosome 9 by Walter et al. (1987) was found to
be in error.
*FIELD* RF
1. Hsieh, S.-L.; Campbell, R. D.: Evidence that gene G7a in the human
major histocompatibility complex encodes valyl-tRNA synthetase. Biochem.
J. 278: 809-816, 1991. Note: Erratum: Biochem. J. 281: 879 only,
1992.
2. Hsieh, S.-L.; Kendall, E.; Milner, C.; Cross, S.; Cheng, J.; Khanna,
A.; Olaversen, M.; Campbell, R. D.: Cloning of the human valyl-tRNA
synthetase gene and its location in the major histocompatibility complex
on chromosome 6. (Abstract) Cytogenet. Cell Genet. 58: 1912 only,
1991.
3. Walter, B.; Yen, A.; Wasmuth, J.; Smith, M.: Selection of somatic
cell hybrids containing human chromosome 9 using a temperature sensitive
CHO valyl-t-RNA synthetase mutant. (Abstract) Cytogenet. Cell Genet. 46:
710 only, 1987.
*FIELD* CN
Alan F. Scott - updated: 11/18/1999
*FIELD* CD
Victor A. McKusick: 11/12/1987
*FIELD* ED
carol: 05/02/2006
carol: 5/2/2006
alopez: 11/18/1999
alopez: 7/26/1999
warfield: 3/29/1994
carol: 2/11/1993
carol: 1/15/1993
supermim: 3/16/1992
carol: 2/23/1992
carol: 8/8/1991