ID SYVC_HUMAN Reviewed; 1264 AA. AC P26640; B0V1N1; Q5JQ90; Q96E77; Q9UQM2; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 4. DT 11-JUL-2012, entry version 133. 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 MEDLINE=91378943; 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 MEDLINE=22935763; 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 MEDLINE=93154582; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-300, AND MASS RP SPECTROMETRY. RC TISSUE=Lung carcinoma; RX PubMed=18083107; DOI=10.1016/j.cell.2007.11.025; RA Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., RA Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., RA Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., RA Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., RA Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; RT "Global survey of phosphotyrosine signaling identifies oncogenic RT kinases in lung cancer."; RL Cell 131:1190-1203(2007). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-420; LYS-423 AND LYS-645, RP AND MASS SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., RA 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 [12] 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). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 IPI; IPI00000873; -. DR PIR; S17675; S17675. DR RefSeq; NP_006286.1; NM_006295.2. DR UniGene; Hs.520026; -. DR ProteinModelPortal; P26640; -. DR SMR; P26640; 2-211, 295-1260. DR IntAct; P26640; 7. DR MINT; MINT-1148831; -. DR STRING; P26640; -. DR PhosphoSite; P26640; -. DR DMDM; 12644177; -. DR PRIDE; P26640; -. DR Ensembl; ENST00000211402; ENSP00000211402; ENSG00000096171. DR Ensembl; ENST00000375663; ENSP00000364815; ENSG00000204394. DR Ensembl; ENST00000457796; ENSP00000403359; ENSG00000226589. DR GeneID; 7407; -. DR KEGG; hsa:7407; -. DR UCSC; uc003nxe.3; human. DR CTD; 7407; -. DR GeneCards; GC06M031745; -. 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 MIM; 192150; gene. DR neXtProt; NX_P26640; -. DR PharmGKB; PA37275; -. DR eggNOG; COG0525; -. DR GeneTree; ENSGT00550000074727; -. DR HOGENOM; HOG000020094; -. DR HOVERGEN; HBG017878; -. DR InParanoid; P26640; -. DR KO; K01873; -. DR OMA; SIMDSRG; -. DR OrthoDB; EOG4QZ7K3; -. DR BRENDA; 6.1.1.9; 2681. DR Reactome; REACT_71; Gene Expression. DR DrugBank; DB00161; L-Valine. DR NextBio; 28996; -. DR Bgee; P26640; -. DR CleanEx; HS_VARS; -. DR CleanEx; HS_VARS2; -. DR Genevestigator; P26640; -. DR GermOnline; ENSG00000204394; Homo sapiens. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IEA:Compara. 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; G3DSA:3.90.740.10; G3DSA:3.90.740.10; 1. DR Gene3D; G3DSA:1.20.1050.10; GST_C_like; 1. DR Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 3. 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; IPR017933; Glutathione_S_Trfase/Cl_chnl_C. 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_synthetase. DR PANTHER; PTHR11946:SF5; tRNA-synt_val; 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; SSF47616; GST_C_like; 1. DR SUPFAM; SSF47323; tRNAsyn_1a_bind; 1. DR SUPFAM; SSF50677; ValRS_IleRS_edit; 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; Phosphoprotein; Polymorphism; KW Protein biosynthesis; 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 300 300 Phosphotyrosine. FT MOD_RES 420 420 N6-acetyllysine. FT MOD_RES 423 423 N6-acetyllysine. 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 //