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P26640

- SYVC_HUMAN

UniProt

P26640 - SYVC_HUMAN

Protein

Valine--tRNA ligase

Gene

VARS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 4 (01 Dec 2000)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Enzyme regulationi

    Can be regulated by protein kinase C-dependent phosphorylation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei865 – 8651ATPBy similarity

    GO - Molecular functioni

    1. aminoacyl-tRNA editing activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. valine-tRNA ligase activity Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. tRNA aminoacylation for protein translation Source: Reactome
    3. valyl-tRNA aminoacylation Source: InterPro

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi6.1.1.9. 2681.
    ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Valine--tRNA ligase (EC:6.1.1.9)
    Alternative name(s):
    Protein G7a
    Valyl-tRNA synthetase
    Short name:
    ValRS
    Gene namesi
    Name:VARS
    Synonyms:G7A, VARS2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:12651. VARS.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. mitochondrion Source: Ensembl

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37275.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 12641263Valine--tRNA ligasePRO_0000106253Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine3 Publications
    Modified residuei645 – 6451N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP26640.
    PaxDbiP26640.
    PRIDEiP26640.

    PTM databases

    PhosphoSiteiP26640.

    Expressioni

    Gene expression databases

    ArrayExpressiP26640.
    BgeeiP26640.
    CleanExiHS_VARS.
    HS_VARS2.
    GenevestigatoriP26640.

    Organism-specific databases

    HPAiHPA046710.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EEF1A2Q056391EBI-355765,EBI-354943
    EPB41P111711EBI-355765,EBI-1050906
    HLA-BP304801EBI-355765,EBI-1054175
    TFE3P195321EBI-355765,EBI-1048957
    TRAF6Q9Y4K31EBI-355765,EBI-359276

    Protein-protein interaction databases

    BioGridi113250. 33 interactions.
    IntActiP26640. 11 interactions.
    MINTiMINT-1148831.
    STRINGi9606.ENSP00000401121.

    Structurei

    3D structure databases

    ProteinModelPortaliP26640.
    SMRiP26640. Positions 1-206, 296-1258.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini89 – 219131GST C-terminalAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi344 – 35411"HIGH" regionAdd
    BLAST
    Motifi862 – 8665"KMSKS" region

    Sequence similaritiesi

    Contains 1 GST C-terminal domain.Curated

    Phylogenomic databases

    eggNOGiCOG0525.
    HOGENOMiHOG000020094.
    HOVERGENiHBG017878.
    InParanoidiP26640.
    KOiK01873.
    OMAiTEEHDCG.
    PhylomeDBiP26640.
    TreeFamiTF300648.

    Family and domain databases

    Gene3Di1.10.730.10. 1 hit.
    1.20.1050.10. 1 hit.
    3.40.50.620. 3 hits.
    3.90.740.10. 1 hit.
    HAMAPiMF_02004. Val_tRNA_synth_type1.
    InterProiIPR001412. 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]
    PfamiPF08264. Anticodon_1. 1 hit.
    PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    PF00133. tRNA-synt_1. 1 hit.
    [Graphical view]
    PRINTSiPR00986. TRNASYNTHVAL.
    SUPFAMiSSF47323. SSF47323. 1 hit.
    SSF47616. SSF47616. 1 hit.
    SSF50677. SSF50677. 1 hit.
    TIGRFAMsiTIGR00422. valS. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    PS50405. GST_CTER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P26640-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSTLYVSPHP DAFPSLRALI AARYGEAGEG PGWGGAHPRI CLQPPPTSRT     50
    PFPPPRLPAL EQGPGGLWVW GATAVAQLLW PAGLGGPGGS RAAVLVQQWV 100
    SYADTELIPA ACGATLPALG LRSSAQDPQA VLGALGRALS PLEEWLRLHT 150
    YLAGEAPTLA DLAAVTALLL PFRYVLDPPA RRIWNNVTRW FVTCVRQPEF 200
    RAVLGEVVLY SGARPLSHQP GPEAPALPKT AAQLKKEAKK REKLEKFQQK 250
    QKIQQQQPPP GEKKPKPEKR EKRDPGVITY DLPTPPGEKK DVSGPMPDSY 300
    SPRYVEAAWY PWWEQQGFFK PEYGRPNVSA ANPRGVFMMC IPPPNVTGSL 350
    HLGHALTNAI QDSLTRWHRM RGETTLWNPG CDHAGIATQV VVEKKLWREQ 400
    GLSRHQLGRE AFLQEVWKWK EEKGDRIYHQ LKKLGSSLDW DRACFTMDPK 450
    LSAAVTEAFV RLHEEGIIYR STRLVNWSCT LNSAISDIEV DKKELTGRTL 500
    LSVPGYKEKV EFGVLVSFAY KVQGSDSDEE VVVATTRIET MLGDVAVAVH 550
    PKDTRYQHLK GKNVIHPFLS RSLPIVFDEF VDMDFGTGAV KITPAHDQND 600
    YEVGQRHGLE AISIMDSRGA LINVPPPFLG LPRFEARKAV LVALKERGLF 650
    RGIEDNPMVV PLCNRSKDVV EPLLRPQWYV RCGEMAQAAS AAVTRGDLRI 700
    LPEAHQRTWH AWMDNIREWC ISRQLWWGHR IPAYFVTVSD PAVPPGEDPD 750
    GRYWVSGRNE AEAREKAAKE FGVSPDKISL QQDEDVLDTW FSSGLFPLSI 800
    LGWPNQSEDL SVFYPGTLLE TGHDILFFWV ARMVMLGLKL TGRLPFREVY 850
    LHAIVRDAHG RKMSKSLGNV IDPLDVIYGI SLQGLHNQLL NSNLDPSEVE 900
    KAKEGQKADF PAGIPECGTD ALRFGLCAYM SQGRDINLDV NRILGYRHFC 950
    NKLWNATKFA LRGLGKGFVP SPTSQPGGHE SLVDRWIRSR LTEAVRLSNQ 1000
    GFQAYDFPAV TTAQYSFWLY ELCDVYLECL KPVLNGVDQV AAECARQTLY 1050
    TCLDVGLRLL SPFMPFVTEE LFQRLPRRMP QAPPSLCVTP YPEPSECSWK 1100
    DPEAEAALEL ALSITRAVRS LRADYNLTRI RPDCFLEVAD EATGALASAV 1150
    SGYVQALASA GVVAVLALGA PAPQGCAVAL ASDRCSIHLQ LQGLVDPARE 1200
    LGKLQAKRVE AQRQAQRLRE RRAASGYPVK VPLEVQEADE AKLQQTEAEL 1250
    RKVDEAIALF QKML 1264
    Length:1,264
    Mass (Da):140,476
    Last modified:December 1, 2000 - v4
    Checksum:i95CCDDBB3AB148AD
    GO
    Isoform 2 (identifier: P26640-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-295: Missing.
         589-592: AVKI → PAQV
         593-1264: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:297
    Mass (Da):33,795
    Checksum:i67A51E4BB45D4A57
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti51 – 511P → S in CAA41990. (PubMed:1898367)Curated
    Sequence conflicti51 – 511P → S in AAH12808. 1 PublicationCurated
    Sequence conflicti331 – 3311A → G in AAA81332. (PubMed:8428657)Curated
    Sequence conflicti590 – 5901V → G in CAA41990. (PubMed:1898367)Curated
    Sequence conflicti792 – 7921S → F in CAA41990. (PubMed:1898367)Curated
    Sequence conflicti1064 – 10641M → I in AAA81332. (PubMed:8428657)Curated
    Sequence conflicti1169 – 11691Missing in AAA81332. (PubMed:8428657)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti51 – 511P → R.
    Corresponds to variant rs2607015 [ dbSNP | Ensembl ].
    VAR_052647
    Natural varianti51 – 511P → T.
    Corresponds to variant rs2753960 [ dbSNP | Ensembl ].
    VAR_061909
    Natural varianti181 – 1811R → C.
    Corresponds to variant rs35196751 [ dbSNP | Ensembl ].
    VAR_052648
    Natural varianti626 – 6261P → S.
    Corresponds to variant rs11531 [ dbSNP | Ensembl ].
    VAR_052649
    Natural varianti1008 – 10081P → L.
    Corresponds to variant rs1076827 [ dbSNP | Ensembl ].
    VAR_052650

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 295295Missing in isoform 2. 1 PublicationVSP_056480Add
    BLAST
    Alternative sequencei589 – 5924AVKI → PAQV in isoform 2. 1 PublicationVSP_056481
    Alternative sequencei593 – 1264672Missing in isoform 2. 1 PublicationVSP_056482Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59303 mRNA. Translation: CAA41990.1. Frameshift.
    AF134726 Genomic DNA. Translation: AAD21819.1.
    BA000025 Genomic DNA. Translation: BAB63303.1.
    AK302762 mRNA. Translation: BAG63973.1.
    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.
    CCDSiCCDS34412.1.
    PIRiS17675.
    RefSeqiNP_006286.1. NM_006295.2.
    UniGeneiHs.520026.

    Genome annotation databases

    EnsembliENST00000211402; ENSP00000211402; ENSG00000096171.
    ENST00000375663; ENSP00000364815; ENSG00000204394.
    ENST00000422694; ENSP00000401121; ENSG00000224264.
    ENST00000435657; ENSP00000415316; ENSG00000231116.
    ENST00000444930; ENSP00000398317; ENSG00000204394.
    ENST00000457796; ENSP00000403359; ENSG00000226589.
    GeneIDi7407.
    KEGGihsa:7407.
    UCSCiuc003nxe.3. human.

    Polymorphism databases

    DMDMi12644177.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59303 mRNA. Translation: CAA41990.1 . Frameshift.
    AF134726 Genomic DNA. Translation: AAD21819.1 .
    BA000025 Genomic DNA. Translation: BAB63303.1 .
    AK302762 mRNA. Translation: BAG63973.1 .
    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 .
    CCDSi CCDS34412.1.
    PIRi S17675.
    RefSeqi NP_006286.1. NM_006295.2.
    UniGenei Hs.520026.

    3D structure databases

    ProteinModelPortali P26640.
    SMRi P26640. Positions 1-206, 296-1258.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113250. 33 interactions.
    IntActi P26640. 11 interactions.
    MINTi MINT-1148831.
    STRINGi 9606.ENSP00000401121.

    Chemistry

    BindingDBi P26640.
    ChEMBLi CHEMBL2612.
    DrugBanki DB00161. L-Valine.

    PTM databases

    PhosphoSitei P26640.

    Polymorphism databases

    DMDMi 12644177.

    Proteomic databases

    MaxQBi P26640.
    PaxDbi P26640.
    PRIDEi P26640.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000211402 ; ENSP00000211402 ; ENSG00000096171 .
    ENST00000375663 ; ENSP00000364815 ; ENSG00000204394 .
    ENST00000422694 ; ENSP00000401121 ; ENSG00000224264 .
    ENST00000435657 ; ENSP00000415316 ; ENSG00000231116 .
    ENST00000444930 ; ENSP00000398317 ; ENSG00000204394 .
    ENST00000457796 ; ENSP00000403359 ; ENSG00000226589 .
    GeneIDi 7407.
    KEGGi hsa:7407.
    UCSCi uc003nxe.3. human.

    Organism-specific databases

    CTDi 7407.
    GeneCardsi GC06M031745.
    GC06Mj31732.
    GC06Mk31727.
    H-InvDB HIX0005731.
    HIX0165932.
    HIX0166155.
    HIX0166435.
    HIX0166904.
    HIX0167447.
    HGNCi HGNC:12651. VARS.
    HPAi HPA046710.
    MIMi 192150. gene.
    neXtProti NX_P26640.
    PharmGKBi PA37275.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0525.
    HOGENOMi HOG000020094.
    HOVERGENi HBG017878.
    InParanoidi P26640.
    KOi K01873.
    OMAi TEEHDCG.
    PhylomeDBi P26640.
    TreeFami TF300648.

    Enzyme and pathway databases

    BRENDAi 6.1.1.9. 2681.
    Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

    Miscellaneous databases

    ChiTaRSi VARS. human.
    GeneWikii VARS.
    GenomeRNAii 7407.
    NextBioi 28996.
    PROi P26640.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P26640.
    Bgeei P26640.
    CleanExi HS_VARS.
    HS_VARS2.
    Genevestigatori P26640.

    Family and domain databases

    Gene3Di 1.10.730.10. 1 hit.
    1.20.1050.10. 1 hit.
    3.40.50.620. 3 hits.
    3.90.740.10. 1 hit.
    HAMAPi MF_02004. Val_tRNA_synth_type1.
    InterProi IPR001412. 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 ]
    Pfami PF08264. Anticodon_1. 1 hit.
    PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    PF00133. tRNA-synt_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00986. TRNASYNTHVAL.
    SUPFAMi SSF47323. SSF47323. 1 hit.
    SSF47616. SSF47616. 1 hit.
    SSF50677. SSF50677. 1 hit.
    TIGRFAMsi TIGR00422. valS. 1 hit.
    PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
    PS50405. GST_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] (ISOFORM 1).
    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. "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].
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Testis.
    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.
      , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 1).
      Tissue: Muscle.
    9. 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.
    10. "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 (ISOFORM 1).
    11. "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].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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].
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSYVC_HUMAN
    AccessioniPrimary (citable) accession number: P26640
    Secondary accession number(s): B0V1N1
    , B4DZ61, Q5JQ90, Q96E77, Q9UQM2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 156 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3