Protein VTS1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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Q08831 (VTS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 80. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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 (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	523 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.3 Ref.6
Subunit structure	Monomer. Binds to RNA.
Subcellular location	Cytoplasm Ref.4.
Domain	The SAM domain is essential for RNA-binding. Ref.6
Miscellaneous	Present with 3200 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the VTS1 family. Contains 1 SAM (sterile alpha motif) domain.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cytoplasm
Ligand	Nucleotide-binding RNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	nuclear-transcribed mRNA poly(A) tail shortening Inferred from mutant phenotype. Source: SGD positive regulation of endodeoxyribonuclease activity Inferred from direct assay. Source: SGD protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasmic mRNA processing body Inferred from direct assay. Source: SGD cytosol Inferred from direct assay Ref.3. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	RNA binding Inferred from direct assay Ref.6. Source: SGD flap-structured DNA binding Inferred from direct assay. Source: SGD nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
YHR009C	P38758	1	EBI-36342,EBI-24443

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.7

Modified residue

137

Phosphoserine Ref.7

Modified residue

139

Phosphothreonine Ref.7

Modified residue

309

Phosphoserine Ref.7

Modified residue

311

Phosphoserine Ref.7

Modified residue

318

Phosphoserine Ref.7

Modified residue

319

Phosphoserine Ref.7

Experimental info

Mutagenesis

467

K → Q: Loss of RNA-binding. Ref.6

Mutagenesis

498

A → Q: Loss of RNA-binding. Ref.6

Secondary structure

523

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q08831 [UniParc].

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

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

« Hide

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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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: 11445562] [Abstract] Cited for: FUNCTION.
[4]	"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].
[5]	"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].
[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: 12858164] [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: 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z75267 Genomic DNA. Translation: CAA99688.1.
BK006948 Genomic DNA. Translation: DAA11120.1.

PIR

S67271.

RefSeq

NP_015004.1. NM_001183779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q08831.

SMR

Q08831. Positions 441-523.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1279N.

IntAct

Q08831. 4 interactions.

MINT

MINT-407159.

STRING

Q08831.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YOR359W; YOR359W; YOR359W.

GeneID

854541.

KEGG

sce:YOR359W.

NMPDR

fig|4932.3.peg.6123.

Organism-specific databases

CYGD

YOR359w.

SGD

S000005886. VTS1.

Phylogenomic databases

eggNOG

fuNOG06728.

GeneTree

EFGT00050000002930.

HOGENOM

HBG202932.

OMA

QQNTVMD.

OrthoDB

EOG4VX5FS.

Gene expression databases

ArrayExpress

Q08831.

Genevestigator

Q08831.

GermOnline

YOR359W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
[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]

SUPFAM

SSF47769. SAM_homology. 1 hit.

PROSITE

PS50105. SAM_DOMAIN. False negative.
[Graphical view]

ProtoNet

Search...

Other

NextBio

976946.

Entry information

Entry name

VTS1_YEAST

Accession

Primary (citable) accession number: Q08831
Secondary accession number(s): D6W354

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

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

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents