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Protein

Protein VTS1

Gene

VTS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

RNA-binding protein involved in post-transcriptional regulation through transcript degradation of SRE (SMG-recognition elements) bearing mRNAs. May be involved in vacuolar protein transport.2 Publications

GO - Molecular functioni

  • flap-structured DNA binding Source: SGD
  • nucleotide binding Source: UniProtKB-KW
  • RNA binding Source: SGD

GO - Biological processi

  • nuclear-transcribed mRNA catabolic process Source: SGD
  • nuclear-transcribed mRNA poly(A) tail shortening Source: SGD
  • positive regulation of endodeoxyribonuclease activity Source: SGD
  • protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33830-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein VTS1
Alternative name(s):
VTI1-2 suppressor protein 1
Gene namesi
Name:VTS1
Ordered Locus Names:YOR359W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR359W.
SGDiS000005886. VTS1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic mRNA processing body Source: SGD
  • cytosol Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi467 – 4671K → Q: Loss of RNA-binding. 1 Publication
Mutagenesisi498 – 4981A → Q: Loss of RNA-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 523523Protein VTS1PRO_0000081458Add
BLAST

Proteomic databases

MaxQBiQ08831.

PTM databases

iPTMnetiQ08831.

Interactioni

Subunit structurei

Monomer. Binds to RNA.

Protein-protein interaction databases

BioGridi34744. 34 interactions.
DIPiDIP-1279N.
IntActiQ08831. 5 interactions.
MINTiMINT-407159.

Structurei

Secondary structure

1
523
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi444 – 4474Combined sources
Helixi450 – 4534Combined sources
Helixi456 – 4627Combined sources
Helixi466 – 4683Combined sources
Helixi469 – 4724Combined sources
Helixi477 – 4804Combined sources
Helixi485 – 4906Combined sources
Helixi496 – 51419Combined sources
Helixi520 – 5223Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2B6GNMR-A407-523[»]
2D3DX-ray1.60A436-523[»]
2ES6NMR-A373-523[»]
2ESENMR-A373-523[»]
2F8KX-ray2.00A436-523[»]
2FE9NMR-A438-523[»]
ProteinModelPortaliQ08831.
SMRiQ08831. Positions 441-523.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08831.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini451 – 51262SAMAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi74 – 178105Gln-richAdd
BLAST
Compositional biasi374 – 38411His-richAdd
BLAST

Domaini

The SAM domain is essential for RNA-binding.1 Publication

Sequence similaritiesi

Belongs to the VTS1 family.Curated

Phylogenomic databases

HOGENOMiHOG000000803.
InParanoidiQ08831.
OMAiQQNTVMD.
OrthoDBiEOG7M3JBN.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR001660. SAM.
IPR013761. SAM/pointed.
[Graphical view]
PfamiPF07647. SAM_2. 1 hit.
[Graphical view]
SMARTiSM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.

Sequencei

Sequence statusi: Complete.

Q08831-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKHPYEEFPT GSKSPYNMSR GAHPGAVLLS PQSSAINKNN PGSNSGNNQG
60 70 80 90 100
NSSVTANVLS PQSHSMSLND MLDQQSFMLD TAGTRAQPLQ QQQQQQQQQQ
110 120 130 140 150
QASLPSLNIQ TVSSTAAGSA IVSPMMQSPK ALQSTLSSTS MYLDSFQRSP
160 170 180 190 200
NNILGIPSQS GSIPLPQSRQ SQQQSQSQKN DPNMGTNFSQ DINQLCSWIS
210 220 230 240 250
MLNSSQQNTV MDNILSILND DVLKYTKLKI ETLTNTPFIS PPLPAIASPI
260 270 280 290 300
PNRDDTQILN IDSVFSSSPI TNDPENTDNL LYQNWSPQPH SIPISQPIYD
310 320 330 340 350
NITDASQRSK SAEPHVNSSP NLIPVQKQFN NGNSTKYKKL PSENPNYLSH
360 370 380 390 400
SLSSSHSFFQ PKKRSNMGNE YNSHHHHSLH HPLHNTTSYF SNTSRPSGTD
410 420 430 440 450
LNKSNQNVFN NTITHPNAGP TSATSTSTSS NGNTPLSSNS SMNPKSLTDP
460 470 480 490 500
KLLKNIPMWL KSLRLHKYSD ALSGTPWIEL IYLDDETLEK KGVLALGARR
510 520
KLLKAFGIVI DYKERDLIDR SAY
Length:523
Mass (Da):57,557
Last modified:November 1, 1996 - v1
Checksum:i56F55D1A8B4C0EDD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75267 Genomic DNA. Translation: CAA99688.1.
BK006948 Genomic DNA. Translation: DAA11120.1.
PIRiS67271.
RefSeqiNP_015004.3. NM_001183779.3.

Genome annotation databases

EnsemblFungiiYOR359W; YOR359W; YOR359W.
GeneIDi854541.
KEGGisce:YOR359W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75267 Genomic DNA. Translation: CAA99688.1.
BK006948 Genomic DNA. Translation: DAA11120.1.
PIRiS67271.
RefSeqiNP_015004.3. NM_001183779.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2B6GNMR-A407-523[»]
2D3DX-ray1.60A436-523[»]
2ES6NMR-A373-523[»]
2ESENMR-A373-523[»]
2F8KX-ray2.00A436-523[»]
2FE9NMR-A438-523[»]
ProteinModelPortaliQ08831.
SMRiQ08831. Positions 441-523.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34744. 34 interactions.
DIPiDIP-1279N.
IntActiQ08831. 5 interactions.
MINTiMINT-407159.

PTM databases

iPTMnetiQ08831.

Proteomic databases

MaxQBiQ08831.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR359W; YOR359W; YOR359W.
GeneIDi854541.
KEGGisce:YOR359W.

Organism-specific databases

EuPathDBiFungiDB:YOR359W.
SGDiS000005886. VTS1.

Phylogenomic databases

HOGENOMiHOG000000803.
InParanoidiQ08831.
OMAiQQNTVMD.
OrthoDBiEOG7M3JBN.

Enzyme and pathway databases

BioCyciYEAST:G3O-33830-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ08831.
PROiQ08831.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR001660. SAM.
IPR013761. SAM/pointed.
[Graphical view]
PfamiPF07647. SAM_2. 1 hit.
[Graphical view]
SMARTiSM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Genetic interactions with the yeast Q-SNARE VTI1 reveal novel functions for the R-SNARE YKT6."
    Dilcher M., Koehler B., von Mollard G.F.
    J. Biol. Chem. 276:34537-34544(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "The RNA-binding SAM domain of Smaug defines a new family of post-transcriptional regulators."
    Aviv T., Lin Z., Lau S., Rendl L.M., Sicheri F., Smibert C.A.
    Nat. Struct. Biol. 10:614-621(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN, RNA-BINDING, MUTAGENESIS OF LYS-467 AND ALA-498.
  7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiVTS1_YEAST
AccessioniPrimary (citable) accession number: Q08831
Secondary accession number(s): D6W354
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3200 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.