Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P26640

- SYVC_HUMAN

UniProt

P26640 - SYVC_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Valine--tRNA ligase

Gene

VARS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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, UP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:12651. VARS.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mitochondrion Source: Ensembl
Complete GO annotation...

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

BgeeiP26640.
CleanExiHS_VARS.
HS_VARS2.
ExpressionAtlasiP26640. baseline and differential.
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. 39 interactions.
IntActiP26640. 11 interactions.
MINTiMINT-1148831.
STRINGi9606.ENSP00000401121.

Structurei

3D structure databases

ProteinModelPortaliP26640.
SMRiP26640. Positions 7-213, 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.
GeneTreeiENSGT00550000074727.
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. 1 hit.
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

        10         20         30         40         50
MSTLYVSPHP DAFPSLRALI AARYGEAGEG PGWGGAHPRI CLQPPPTSRT
60 70 80 90 100
PFPPPRLPAL EQGPGGLWVW GATAVAQLLW PAGLGGPGGS RAAVLVQQWV
110 120 130 140 150
SYADTELIPA ACGATLPALG LRSSAQDPQA VLGALGRALS PLEEWLRLHT
160 170 180 190 200
YLAGEAPTLA DLAAVTALLL PFRYVLDPPA RRIWNNVTRW FVTCVRQPEF
210 220 230 240 250
RAVLGEVVLY SGARPLSHQP GPEAPALPKT AAQLKKEAKK REKLEKFQQK
260 270 280 290 300
QKIQQQQPPP GEKKPKPEKR EKRDPGVITY DLPTPPGEKK DVSGPMPDSY
310 320 330 340 350
SPRYVEAAWY PWWEQQGFFK PEYGRPNVSA ANPRGVFMMC IPPPNVTGSL
360 370 380 390 400
HLGHALTNAI QDSLTRWHRM RGETTLWNPG CDHAGIATQV VVEKKLWREQ
410 420 430 440 450
GLSRHQLGRE AFLQEVWKWK EEKGDRIYHQ LKKLGSSLDW DRACFTMDPK
460 470 480 490 500
LSAAVTEAFV RLHEEGIIYR STRLVNWSCT LNSAISDIEV DKKELTGRTL
510 520 530 540 550
LSVPGYKEKV EFGVLVSFAY KVQGSDSDEE VVVATTRIET MLGDVAVAVH
560 570 580 590 600
PKDTRYQHLK GKNVIHPFLS RSLPIVFDEF VDMDFGTGAV KITPAHDQND
610 620 630 640 650
YEVGQRHGLE AISIMDSRGA LINVPPPFLG LPRFEARKAV LVALKERGLF
660 670 680 690 700
RGIEDNPMVV PLCNRSKDVV EPLLRPQWYV RCGEMAQAAS AAVTRGDLRI
710 720 730 740 750
LPEAHQRTWH AWMDNIREWC ISRQLWWGHR IPAYFVTVSD PAVPPGEDPD
760 770 780 790 800
GRYWVSGRNE AEAREKAAKE FGVSPDKISL QQDEDVLDTW FSSGLFPLSI
810 820 830 840 850
LGWPNQSEDL SVFYPGTLLE TGHDILFFWV ARMVMLGLKL TGRLPFREVY
860 870 880 890 900
LHAIVRDAHG RKMSKSLGNV IDPLDVIYGI SLQGLHNQLL NSNLDPSEVE
910 920 930 940 950
KAKEGQKADF PAGIPECGTD ALRFGLCAYM SQGRDINLDV NRILGYRHFC
960 970 980 990 1000
NKLWNATKFA LRGLGKGFVP SPTSQPGGHE SLVDRWIRSR LTEAVRLSNQ
1010 1020 1030 1040 1050
GFQAYDFPAV TTAQYSFWLY ELCDVYLECL KPVLNGVDQV AAECARQTLY
1060 1070 1080 1090 1100
TCLDVGLRLL SPFMPFVTEE LFQRLPRRMP QAPPSLCVTP YPEPSECSWK
1110 1120 1130 1140 1150
DPEAEAALEL ALSITRAVRS LRADYNLTRI RPDCFLEVAD EATGALASAV
1160 1170 1180 1190 1200
SGYVQALASA GVVAVLALGA PAPQGCAVAL ASDRCSIHLQ LQGLVDPARE
1210 1220 1230 1240 1250
LGKLQAKRVE AQRQAQRLRE RRAASGYPVK VPLEVQEADE AKLQQTEAEL
1260
RKVDEAIALF QKML
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. Curated

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:
EMBLi
GenBanki
DDBJi
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. [P26640-1]
PIRiS17675.
RefSeqiNP_006286.1. NM_006295.2. [P26640-1]
UniGeneiHs.520026.

Genome annotation databases

EnsembliENST00000211402; ENSP00000211402; ENSG00000096171. [P26640-1]
ENST00000375663; ENSP00000364815; ENSG00000204394. [P26640-1]
ENST00000422694; ENSP00000401121; ENSG00000224264.
ENST00000435657; ENSP00000415316; ENSG00000231116.
ENST00000457796; ENSP00000403359; ENSG00000226589. [P26640-1]
GeneIDi7407.
KEGGihsa:7407.
UCSCiuc003nxe.3. human. [P26640-1]

Polymorphism databases

DMDMi12644177.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [P26640-1 ]
PIRi S17675.
RefSeqi NP_006286.1. NM_006295.2. [P26640-1 ]
UniGenei Hs.520026.

3D structure databases

ProteinModelPortali P26640.
SMRi P26640. Positions 7-213, 296-1258.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113250. 39 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 . [P26640-1 ]
ENST00000375663 ; ENSP00000364815 ; ENSG00000204394 . [P26640-1 ]
ENST00000422694 ; ENSP00000401121 ; ENSG00000224264 .
ENST00000435657 ; ENSP00000415316 ; ENSG00000231116 .
ENST00000457796 ; ENSP00000403359 ; ENSG00000226589 . [P26640-1 ]
GeneIDi 7407.
KEGGi hsa:7407.
UCSCi uc003nxe.3. human. [P26640-1 ]

Organism-specific databases

CTDi 7407.
GeneCardsi GC06M031745.
GC06Mi31756.
GC06Mj31732.
GC06Mk31727.
GC06Mm31821.
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.
GeneTreei ENSGT00550000074727.
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

Bgeei P26640.
CleanExi HS_VARS.
HS_VARS2.
ExpressionAtlasi P26640. baseline and differential.
Genevestigatori P26640.

Family and domain databases

Gene3Di 1.10.730.10. 1 hit.
1.20.1050.10. 1 hit.
3.40.50.620. 1 hit.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 158 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