Protein VTS1 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot Q08831 (VTS1_YEAST)

Last modified June 16, 2009. Version 57. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
Protein VTS1
Alternative name(s):
VTI1-2 suppressor protein 1

Gene names

Name:	VTS1
Ordered Locus Names:	YOR359W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	523 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	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. Ref.2 Ref.5
Subunit structure	Monomer. Binds to RNA.
Subcellular location	Cytoplasm. Ref.3
Domain	The SAM domain is essential for RNA-binding. Ref.5
Miscellaneous	Present with 3200 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the VTS1 family. Contains 1 SAM (sterile alpha motif) domain.

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Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cytoplasm
Ligand	Nucleotide-binding RNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	nuclear-transcribed mRNA poly(A) tail shortening Inferred from mutant phenotype. Source: SGD protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasmic mRNA processing body Inferred from direct assay. Source: SGD cytosol Ref.2 Inferred from direct assay. Source: SGD
Molecular function	RNA binding Ref.5 Inferred from direct assay. Source: SGD nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P38758	1	EBI-36342,EBI-24443

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 523

523

Protein VTS1

PRO_0000081458

Regions

Domain

451 – 512

SAM

Compositional bias

74 – 178

105

Gln-rich

Compositional bias

374 – 384

His-rich

Amino acid modifications

Modified residue

135

Phosphothreonine Ref.6

Modified residue

137

Phosphoserine Ref.6

Modified residue

139

Phosphothreonine Ref.6

Modified residue

309

Phosphoserine Ref.6

Modified residue

311

Phosphoserine Ref.6

Modified residue

318

Phosphoserine Ref.6

Modified residue

319

Phosphoserine Ref.6

Experimental info

Mutagenesis

467

K → Q: Loss of RNA-binding. Ref.5

Mutagenesis

498

A → Q: Loss of RNA-binding. Ref.5

Secondary structure

523

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q08831-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 56F55D1A8B4C0EDD
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FASTA

523

57,557

        10         20         30         40         50         60 
MKHPYEEFPT GSKSPYNMSR GAHPGAVLLS PQSSAINKNN PGSNSGNNQG NSSVTANVLS 

        70         80         90        100        110        120 
PQSHSMSLND MLDQQSFMLD TAGTRAQPLQ QQQQQQQQQQ QASLPSLNIQ TVSSTAAGSA 

       130        140        150        160        170        180 
IVSPMMQSPK ALQSTLSSTS MYLDSFQRSP NNILGIPSQS GSIPLPQSRQ SQQQSQSQKN 

       190        200        210        220        230        240 
DPNMGTNFSQ DINQLCSWIS MLNSSQQNTV MDNILSILND DVLKYTKLKI ETLTNTPFIS 

       250        260        270        280        290        300 
PPLPAIASPI PNRDDTQILN IDSVFSSSPI TNDPENTDNL LYQNWSPQPH SIPISQPIYD 

       310        320        330        340        350        360 
NITDASQRSK SAEPHVNSSP NLIPVQKQFN NGNSTKYKKL PSENPNYLSH SLSSSHSFFQ 

       370        380        390        400        410        420 
PKKRSNMGNE YNSHHHHSLH HPLHNTTSYF SNTSRPSGTD LNKSNQNVFN NTITHPNAGP 

       430        440        450        460        470        480 
TSATSTSTSS NGNTPLSSNS SMNPKSLTDP KLLKNIPMWL KSLRLHKYSD ALSGTPWIEL 

       490        500        510        520 
IYLDDETLEK KGVLALGARR KLLKAFGIVI DYKERDLIDR SAY

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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. Kleine K. Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	"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: 11445562] [Abstract] Cited for: FUNCTION.
[3]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"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: 12858164] [Abstract] Cited for: FUNCTION, DOMAIN, RNA-BINDING, MUTAGENESIS OF LYS-467 AND ALA-498.
[6]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135; SER-137; THR-139; SER-309; SER-311; SER-318 AND SER-319, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

Z75267 Genomic DNA. Translation: CAA99688.1.

PIR

S67271.

RefSeq

NP_015004.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2B6G	NMR	-	A	407-523	[»]
2D3D	X-ray	1.60	A	436-523	[»]
2ES6	NMR	-	A	444-523	[»]
2ESE	NMR	-	A	444-523	[»]
2F8K	X-ray	2.00	A	436-523	[»]
2FE9	NMR	-	A	438-523	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:1279N.

IntAct

Q08831. 3 interactions.

Genome annotation databases

Ensembl

YOR359W. Saccharomyces cerevisiae. [Contig view]

GeneID

854541.

GenomeReviews

Gene locus YOR359W in contig Y13140_GR.

KEGG

sce:YOR359W.

NMPDR

fig|4932.3.peg.6123.

Organism-specific databases

CYGD

YOR359w.

SGD

S000005886. VTS1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

Q08831.

OMA

Q08831. QNTVMDN.

Gene expression databases

GermOnline

YOR359W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR001660. SAM.
IPR011510. SAM_2.
IPR013761. SAM_type.
[Graphical view]

Gene3D

G3DSA:1.10.150.50. SAM_type. 1 hit.

Pfam

PF07647. SAM_2. 1 hit.
[Graphical view]

SMART

SM00454. SAM. 1 hit.
[Graphical view]

PROSITE

PS50105. SAM_DOMAIN. False negative.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

976946.

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Entry information

Entry name

VTS1_YEAST

Accession

Primary (citable) accession number: Q08831

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents