SYVC_HUMAN
ID SYVC_HUMAN Reviewed; 1264 AA.
AC P26640; B0V1N1; B4DZ61; Q5JQ90; Q96E77; Q9UQM2;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 4.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=Valine--tRNA ligase {ECO:0000305};
DE EC=6.1.1.9 {ECO:0000269|PubMed:8428657};
DE AltName: Full=Protein G7a;
DE AltName: Full=Valyl-tRNA synthetase;
DE Short=ValRS;
GN Name=VARS1 {ECO:0000312|HGNC:HGNC:12651}; Synonyms=G7A, VARS, VARS2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1898367; DOI=10.1042/bj2780809;
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 OF PUBMED:1898367.
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., Campbell R.D.,
RA 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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
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., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., 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., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA 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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
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 AT
RP SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Dhillon A.S., Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 201-1263 (ISOFORM 1), FUNCTION, AND CATALYTIC
RP ACTIVITY.
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 valyl-tRNA
RT synthetase.";
RL Gene 123:181-186(1993).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-645, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
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., Buerckstuemmer T.,
RA 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-527, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [18]
RP INVOLVEMENT IN NDMSCA, AND VARIANTS NDMSCA PHE-885 AND GLN-1058.
RX PubMed=26539891; DOI=10.1016/j.neuron.2015.09.048;
RA Karaca E., Harel T., Pehlivan D., Jhangiani S.N., Gambin T.,
RA Coban Akdemir Z., Gonzaga-Jauregui C., Erdin S., Bayram Y., Campbell I.M.,
RA Hunter J.V., Atik M.M., Van Esch H., Yuan B., Wiszniewski W., Isikay S.,
RA Yesil G., Yuregir O.O., Tug Bozdogan S., Aslan H., Aydin H., Tos T.,
RA Aksoy A., De Vivo D.C., Jain P., Geckinli B.B., Sezer O., Gul D.,
RA Durmaz B., Cogulu O., Ozkinay F., Topcu V., Candan S., Cebi A.H., Ikbal M.,
RA Yilmaz Gulec E., Gezdirici A., Koparir E., Ekici F., Coskun S., Cicek S.,
RA Karaer K., Koparir A., Duz M.B., Kirat E., Fenercioglu E., Ulucan H.,
RA Seven M., Guran T., Elcioglu N., Yildirim M.S., Aktas D., Alikasifoglu M.,
RA Ture M., Yakut T., Overton J.D., Yuksel A., Ozen M., Muzny D.M.,
RA Adams D.R., Boerwinkle E., Chung W.K., Gibbs R.A., Lupski J.R.;
RT "Genes that affect brain structure and function identified by rare variant
RT analyses of mendelian neurologic disease.";
RL Neuron 88:499-513(2015).
CC -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val).
CC {ECO:0000269|PubMed:8428657}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-
CC tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-
CC COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9;
CC Evidence={ECO:0000269|PubMed:8428657};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10705;
CC Evidence={ECO:0000305|PubMed:8428657};
CC -!- ACTIVITY REGULATION: Can be regulated by protein kinase C-dependent
CC phosphorylation.
CC -!- SUBUNIT: Forms high-molecular-mass aggregates with elongation factor 1.
CC -!- INTERACTION:
CC P26640; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-355765, EBI-739580;
CC P26640; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-355765, EBI-1383687;
CC P26640; Q13554-3: CAMK2B; NbExp=3; IntAct=EBI-355765, EBI-11523526;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P26640-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P26640-2; Sequence=VSP_056480, VSP_056481, VSP_056482;
CC -!- DISEASE: Neurodevelopmental disorder with microcephaly, seizures, and
CC cortical atrophy (NDMSCA) [MIM:617802]: An autosomal recessive
CC neurodevelopmental disorder characterized by severe developmental
CC delay, intellectual disability, severe microcephaly, and cortical
CC atrophy. {ECO:0000269|PubMed:26539891}. Note=The disease may be caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA41990.1; Type=Frameshift; Evidence={ECO:0000305};
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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; AK302762; BAG63973.1; -; mRNA.
DR EMBL; AL662834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL671762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR925765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03523.1; -; Genomic_DNA.
DR EMBL; BC012808; AAH12808.1; -; mRNA.
DR EMBL; M98326; AAA81332.1; -; mRNA.
DR CCDS; CCDS34412.1; -. [P26640-1]
DR PIR; S17675; S17675.
DR RefSeq; NP_006286.1; NM_006295.2. [P26640-1]
DR AlphaFoldDB; P26640; -.
DR SMR; P26640; -.
DR BioGRID; 113250; 152.
DR IntAct; P26640; 71.
DR MINT; P26640; -.
DR STRING; 9606.ENSP00000364815; -.
DR BindingDB; P26640; -.
DR ChEMBL; CHEMBL2612; -.
DR DrugBank; DB00161; Valine.
DR GlyGen; P26640; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P26640; -.
DR MetOSite; P26640; -.
DR PhosphoSitePlus; P26640; -.
DR SwissPalm; P26640; -.
DR BioMuta; VARS; -.
DR DMDM; 12644177; -.
DR CPTAC; CPTAC-1642; -.
DR EPD; P26640; -.
DR jPOST; P26640; -.
DR MassIVE; P26640; -.
DR MaxQB; P26640; -.
DR PaxDb; P26640; -.
DR PeptideAtlas; P26640; -.
DR PRIDE; P26640; -.
DR ProteomicsDB; 54358; -. [P26640-1]
DR ProteomicsDB; 5573; -.
DR Antibodypedia; 51277; 188 antibodies from 27 providers.
DR DNASU; 7407; -.
DR Ensembl; ENST00000211402.10; ENSP00000211402.6; ENSG00000096171.14. [P26640-1]
DR Ensembl; ENST00000375663.8; ENSP00000364815.3; ENSG00000204394.13. [P26640-1]
DR Ensembl; ENST00000422694.6; ENSP00000401121.2; ENSG00000224264.9.
DR Ensembl; ENST00000435657.6; ENSP00000415316.2; ENSG00000231116.9.
DR Ensembl; ENST00000457796.6; ENSP00000403359.2; ENSG00000226589.9. [P26640-1]
DR GeneID; 7407; -.
DR KEGG; hsa:7407; -.
DR MANE-Select; ENST00000375663.8; ENSP00000364815.3; NM_006295.3; NP_006286.1.
DR UCSC; uc003nxe.4; human. [P26640-1]
DR CTD; 7407; -.
DR DisGeNET; 7407; -.
DR GeneCards; VARS1; -.
DR HGNC; HGNC:12651; VARS1.
DR HPA; ENSG00000204394; Low tissue specificity.
DR MalaCards; VARS1; -.
DR MIM; 192150; gene.
DR MIM; 617802; phenotype.
DR neXtProt; NX_P26640; -.
DR OpenTargets; ENSG00000204394; -.
DR Orphanet; 420728; Combined oxidative phosphorylation defect type 20.
DR PharmGKB; PA37275; -.
DR VEuPathDB; HostDB:ENSG00000204394; -.
DR eggNOG; KOG0432; Eukaryota.
DR eggNOG; KOG0867; Eukaryota.
DR GeneTree; ENSGT00940000157775; -.
DR HOGENOM; CLU_001493_0_1_1; -.
DR InParanoid; P26640; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 229591at2759; -.
DR PhylomeDB; P26640; -.
DR TreeFam; TF300648; -.
DR BRENDA; 6.1.1.9; 2681.
DR PathwayCommons; P26640; -.
DR Reactome; R-HSA-379716; Cytosolic tRNA aminoacylation.
DR SignaLink; P26640; -.
DR BioGRID-ORCS; 7407; 796 hits in 1053 CRISPR screens.
DR ChiTaRS; VARS; human.
DR GeneWiki; VARS; -.
DR GenomeRNAi; 7407; -.
DR Pharos; P26640; Tchem.
DR PRO; PR:P26640; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P26640; protein.
DR Bgee; ENSG00000096171; Expressed in medulla oblongata and 11 other tissues.
DR ExpressionAtlas; P26640; baseline and differential.
DR Genevisible; P26640; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR Gene3D; 1.10.287.380; -; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 1.
DR HAMAP; MF_02004; Val_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033705; Anticodon_Ia_Val.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR PANTHER; PTHR11946; PTHR11946; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00043; GST_C; 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; Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding;
KW Direct protein sequencing; Disease variant; Epilepsy;
KW Intellectual disability; Ligase; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..1264
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106253"
FT DOMAIN 89..219
FT /note="GST C-terminal"
FT REGION 217..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 344..354
FT /note="'HIGH' region"
FT MOTIF 862..866
FT /note="'KMSKS' region"
FT COMPBIAS 233..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 865
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 645
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..295
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056480"
FT VAR_SEQ 589..592
FT /note="AVKI -> PAQV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056481"
FT VAR_SEQ 593..1264
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056482"
FT VARIANT 51
FT /note="P -> R (in dbSNP:rs2607015)"
FT /id="VAR_052647"
FT VARIANT 51
FT /note="P -> T (in dbSNP:rs2753960)"
FT /id="VAR_061909"
FT VARIANT 181
FT /note="R -> C (in dbSNP:rs35196751)"
FT /id="VAR_052648"
FT VARIANT 626
FT /note="P -> S (in dbSNP:rs11531)"
FT /id="VAR_052649"
FT VARIANT 885
FT /note="L -> F (in NDMSCA; unknown pathological
FT significance; dbSNP:rs1060499734)"
FT /evidence="ECO:0000269|PubMed:26539891"
FT /id="VAR_080602"
FT VARIANT 1008
FT /note="P -> L (in dbSNP:rs1076827)"
FT /id="VAR_052650"
FT VARIANT 1058
FT /note="R -> Q (in NDMSCA; unknown pathological
FT significance; dbSNP:rs769369302)"
FT /evidence="ECO:0000269|PubMed:26539891"
FT /id="VAR_080603"
FT CONFLICT 51
FT /note="P -> S (in Ref. 1; CAA41990 and 7; AAH12808)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="A -> G (in Ref. 10; AAA81332)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="V -> G (in Ref. 1; CAA41990)"
FT /evidence="ECO:0000305"
FT CONFLICT 792
FT /note="S -> F (in Ref. 1; CAA41990)"
FT /evidence="ECO:0000305"
FT CONFLICT 1064
FT /note="M -> I (in Ref. 10; AAA81332)"
FT /evidence="ECO:0000305"
FT CONFLICT 1169
FT /note="Missing (in Ref. 10; AAA81332)"
FT /evidence="ECO:0000305"
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
