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P26640 (SYVC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Valine--tRNA ligase

EC=6.1.1.9
Alternative name(s):
Protein G7a
Valyl-tRNA synthetase
Short name=ValRS
Gene names
Name:VARS
Synonyms:G7A, VARS2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1264 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val). HAMAP-Rule MF_02004

Enzyme regulation

Can be regulated by protein kinase C-dependent phosphorylation. HAMAP-Rule MF_02004

Subunit structure

Forms high-molecular-mass aggregates with elongation factor 1.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Contains 1 GST C-terminal domain.

Sequence caution

The sequence CAA41990.1 differs from that shown. Reason: Frameshift at positions 620 and 640.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 12641263Valine--tRNA ligase HAMAP-Rule MF_02004
PRO_0000106253

Regions

Domain89 – 219131GST C-terminal
Motif344 – 35411"HIGH" region HAMAP-Rule MF_02004
Motif862 – 8665"KMSKS" region HAMAP-Rule MF_02004

Sites

Binding site8651ATP By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.8 Ref.12 Ref.13
Modified residue6451N6-acetyllysine Ref.10

Natural variations

Natural variant511P → R.
Corresponds to variant rs2607015 [ dbSNP | Ensembl ].
VAR_052647
Natural variant511P → T.
Corresponds to variant rs2753960 [ dbSNP | Ensembl ].
VAR_061909
Natural variant1811R → C.
Corresponds to variant rs35196751 [ dbSNP | Ensembl ].
VAR_052648
Natural variant6261P → S.
Corresponds to variant rs11531 [ dbSNP | Ensembl ].
VAR_052649
Natural variant10081P → L.
Corresponds to variant rs1076827 [ dbSNP | Ensembl ].
VAR_052650

Experimental info

Sequence conflict511P → S in CAA41990. Ref.1
Sequence conflict511P → S in AAH12808. Ref.7
Sequence conflict3311A → G in AAA81332. Ref.9
Sequence conflict5901V → G in CAA41990. Ref.1
Sequence conflict7921S → F in CAA41990. Ref.1
Sequence conflict10641M → I in AAA81332. Ref.9
Sequence conflict11691Missing in AAA81332. Ref.9

Sequences

Sequence LengthMass (Da)Tools
P26640 [UniParc].

Last modified December 1, 2000. Version 4.
Checksum: 95CCDDBB3AB148AD

FASTA1,264140,476
        10         20         30         40         50         60 
MSTLYVSPHP DAFPSLRALI AARYGEAGEG PGWGGAHPRI CLQPPPTSRT PFPPPRLPAL 

        70         80         90        100        110        120 
EQGPGGLWVW GATAVAQLLW PAGLGGPGGS RAAVLVQQWV SYADTELIPA ACGATLPALG 

       130        140        150        160        170        180 
LRSSAQDPQA VLGALGRALS PLEEWLRLHT YLAGEAPTLA DLAAVTALLL PFRYVLDPPA 

       190        200        210        220        230        240 
RRIWNNVTRW FVTCVRQPEF RAVLGEVVLY SGARPLSHQP GPEAPALPKT AAQLKKEAKK 

       250        260        270        280        290        300 
REKLEKFQQK QKIQQQQPPP GEKKPKPEKR EKRDPGVITY DLPTPPGEKK DVSGPMPDSY 

       310        320        330        340        350        360 
SPRYVEAAWY PWWEQQGFFK PEYGRPNVSA ANPRGVFMMC IPPPNVTGSL HLGHALTNAI 

       370        380        390        400        410        420 
QDSLTRWHRM RGETTLWNPG CDHAGIATQV VVEKKLWREQ GLSRHQLGRE AFLQEVWKWK 

       430        440        450        460        470        480 
EEKGDRIYHQ LKKLGSSLDW DRACFTMDPK LSAAVTEAFV RLHEEGIIYR STRLVNWSCT 

       490        500        510        520        530        540 
LNSAISDIEV DKKELTGRTL LSVPGYKEKV EFGVLVSFAY KVQGSDSDEE VVVATTRIET 

       550        560        570        580        590        600 
MLGDVAVAVH PKDTRYQHLK GKNVIHPFLS RSLPIVFDEF VDMDFGTGAV KITPAHDQND 

       610        620        630        640        650        660 
YEVGQRHGLE AISIMDSRGA LINVPPPFLG LPRFEARKAV LVALKERGLF RGIEDNPMVV 

       670        680        690        700        710        720 
PLCNRSKDVV EPLLRPQWYV RCGEMAQAAS AAVTRGDLRI LPEAHQRTWH AWMDNIREWC 

       730        740        750        760        770        780 
ISRQLWWGHR IPAYFVTVSD PAVPPGEDPD GRYWVSGRNE AEAREKAAKE FGVSPDKISL 

       790        800        810        820        830        840 
QQDEDVLDTW FSSGLFPLSI LGWPNQSEDL SVFYPGTLLE TGHDILFFWV ARMVMLGLKL 

       850        860        870        880        890        900 
TGRLPFREVY LHAIVRDAHG RKMSKSLGNV IDPLDVIYGI SLQGLHNQLL NSNLDPSEVE 

       910        920        930        940        950        960 
KAKEGQKADF PAGIPECGTD ALRFGLCAYM SQGRDINLDV NRILGYRHFC NKLWNATKFA 

       970        980        990       1000       1010       1020 
LRGLGKGFVP SPTSQPGGHE SLVDRWIRSR LTEAVRLSNQ GFQAYDFPAV TTAQYSFWLY 

      1030       1040       1050       1060       1070       1080 
ELCDVYLECL KPVLNGVDQV AAECARQTLY TCLDVGLRLL SPFMPFVTEE LFQRLPRRMP 

      1090       1100       1110       1120       1130       1140 
QAPPSLCVTP YPEPSECSWK DPEAEAALEL ALSITRAVRS LRADYNLTRI RPDCFLEVAD 

      1150       1160       1170       1180       1190       1200 
EATGALASAV SGYVQALASA GVVAVLALGA PAPQGCAVAL ASDRCSIHLQ LQGLVDPARE 

      1210       1220       1230       1240       1250       1260 
LGKLQAKRVE AQRQAQRLRE RRAASGYPVK VPLEVQEADE AKLQQTEAEL RKVDEAIALF 


QKML 

« Hide

References

« Hide 'large scale' references
[1]"Evidence that gene G7a in the human major histocompatibility complex encodes valyl-tRNA synthetase."
Hsieh H.-L., Campbell R.D.
Biochem. J. 278:809-816(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Erratum
Hsieh S.-L., Campbell R.D.
Biochem. J. 281:879-879(1992)
[3]"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
Shiina S., Tamiya G., Oka A., Inoko H.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Muscle.
[8]Bienvenut W.V., Dhillon A.S., Kolch W.
Submitted (FEB-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-17; 123-147; 451-461; 592-606; 619-633; 935-942; 1120-1129 AND 1252-1262, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hepatoma.
[9]"Cloning, sequencing and expression of a cDNA encoding mammalian valyl-tRNA synthetase."
Vilalta A., Donovan D., Wood L., Vogeli G., Yang D.C.H.
Gene 123:181-186(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 201-1263.
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-645, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59303 mRNA. Translation: CAA41990.1. Frameshift.
AF134726 Genomic DNA. Translation: AAD21819.1.
BA000025 Genomic DNA. Translation: BAB63303.1.
AL671762, AL662899 Genomic DNA. Translation: CAI18211.1.
AL662899, AL671762 Genomic DNA. Translation: CAI18384.1.
AL662834 Genomic DNA. Translation: CAI17732.1.
CR925765 Genomic DNA. Translation: CAQ10624.1.
CH471081 Genomic DNA. Translation: EAX03523.1.
BC012808 mRNA. Translation: AAH12808.1.
M98326 mRNA. Translation: AAA81332.1.
PIRS17675.
RefSeqNP_006286.1. NM_006295.2.
UniGeneHs.520026.

3D structure databases

ProteinModelPortalP26640.
SMRP26640. Positions 4-211, 296-1258.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113250. 32 interactions.
IntActP26640. 11 interactions.
MINTMINT-1148831.
STRING9606.ENSP00000401121.

Chemistry

BindingDBP26640.
ChEMBLCHEMBL2612.
DrugBankDB00161. L-Valine.

PTM databases

PhosphoSiteP26640.

Polymorphism databases

DMDM12644177.

Proteomic databases

PaxDbP26640.
PRIDEP26640.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000211402; ENSP00000211402; ENSG00000096171.
ENST00000375663; ENSP00000364815; ENSG00000204394.
ENST00000422694; ENSP00000401121; ENSG00000224264.
ENST00000435657; ENSP00000415316; ENSG00000231116.
ENST00000457796; ENSP00000403359; ENSG00000226589.
GeneID7407.
KEGGhsa:7407.
UCSCuc003nxe.3. human.

Organism-specific databases

CTD7407.
GeneCardsGC06M031745.
GC06Mj31732.
GC06Mk31727.
H-InvDBHIX0005731.
HIX0165932.
HIX0166155.
HIX0166435.
HIX0166904.
HIX0167447.
HGNCHGNC:12651. VARS.
HPAHPA046710.
MIM192150. gene.
neXtProtNX_P26640.
PharmGKBPA37275.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0525.
HOGENOMHOG000020094.
HOVERGENHBG017878.
InParanoidP26640.
KOK01873.
OMAMAGFINK.
PhylomeDBP26640.
TreeFamTF300648.

Enzyme and pathway databases

BRENDA6.1.1.9. 2681.
ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressP26640.
BgeeP26640.
CleanExHS_VARS.
HS_VARS2.
GenevestigatorP26640.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
1.20.1050.10. 1 hit.
3.40.50.620. 3 hits.
3.90.740.10. 1 hit.
HAMAPMF_02004. Val_tRNA_synth_type1.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
IPR002303. Valyl-tRNA_ligase.
[Graphical view]
PANTHERPTHR11946:SF5. PTHR11946:SF5. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSPR00986. TRNASYNTHVAL.
SUPFAMSSF47323. SSF47323. 1 hit.
SSF47616. SSF47616. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00422. valS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
PS50405. GST_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSVARS. human.
GeneWikiVARS.
GenomeRNAi7407.
NextBio28996.
PROP26640.
SOURCESearch...

Entry information

Entry nameSYVC_HUMAN
AccessionPrimary (citable) accession number: P26640
Secondary accession number(s): B0V1N1 expand/collapse secondary AC list , Q5JQ90, Q96E77, Q9UQM2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: December 1, 2000
Last modified: April 16, 2014
This is version 151 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries