Skip Header

Contribute Send feedback
Read comments (?) or add your own

P32854 (PEP12_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Syntaxin PEP12
Alternative name(s):
Carboxypeptidase Y-deficient protein 12
Vacuolar protein sorting-associated protein 6
Vacuolar protein-targeting protein 13
Gene names
Name:PEP12
Synonyms:VPS6, VPT13
Ordered Locus Names:YOR036W
ORF Names:OR26.29
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length288 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in the sorting and targeting of vacuolar proteases.

Subcellular location

Membrane; Single-pass type IV membrane protein Potential.

Post-translational modification

Ubiquitinated. Ref.4

Sequence similarities

Belongs to the syntaxin family.

Contains 1 t-SNARE coiled-coil homology domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

YKT6P360152EBI-13098,EBI-26982

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 288288Syntaxin PEP12
PRO_0000210271

Regions

Topological domain1 – 268268Cytoplasmic Potential
Transmembrane269 – 28820Helical; Anchor for type IV membrane protein; Potential
Domain195 – 25763t-SNARE coiled-coil homology

Amino acid modifications

Modified residue21Phosphoserine Ref.5 Ref.6
Modified residue231Phosphoserine Ref.6

Experimental info

Mutagenesis2711L → D: Increases ubiquitination by TUL1. Ref.4
Sequence conflict131A → G in AAB38370. Ref.1
Sequence conflict891V → I in AAB38370. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P32854 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: D9F5711339DA1CDA

FASTA28833,006
        10         20         30         40         50         60 
MSEDEFFGGD NEAVWNGSRF SDSPEFQTLK EEVAAELFEI NGQISTLQQF TATLKSFIDR 

        70         80         90        100        110        120 
GDVSAKVVER INKRSVAKIE EIGGLIKKVN TSVKKMDAIE EASLDKTQII AREKLVRDVS 

       130        140        150        160        170        180 
YSFQEFQGIQ RQFTQVMKQV NERAKESLEA SEMANDAALL DEEQRQNSSK STRIPGSQIV 

       190        200        210        220        230        240 
IERDPINNEE FAYQQNLIEQ RDQEISNIER GITELNEVFK DLGSVVQQQG VLVDNIEANI 

       250        260        270        280 
YTTSDNTQLA SDELRKAMRY QKRTSRWRVY LLIVLLVMLL FIFLIMKL 

« Hide

References

« Hide 'large scale' references
[1]"Novel syntaxin homologue, Pep12p, required for the sorting of lumenal hydrolases to the lysosome-like vacuole in yeast."
Becherer K.A., Rieder S.E., Emr S.D., Jones E.W.
Mol. Biol. Cell 7:579-594(1996) [PubMed: 8730101] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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. expand/collapse author list , 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: 9169874] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies."
Reggiori F., Pelham H.R.B.
Nat. Cell Biol. 4:117-123(2002) [PubMed: 11788821] [Abstract]
Cited for: UBIQUITINATION BY TUL1, MUTAGENESIS OF LEU-271.
[5]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY.
Strain: ADR376.
[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 SER-2 AND SER-23, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M90395 Genomic DNA. Translation: AAB38370.1.
X87331 Genomic DNA. Translation: CAA60755.1.
Z74944 Genomic DNA. Translation: CAA99226.1.
BK006948 Genomic DNA. Translation: DAA10819.1.
PIRS62175.
RefSeqNP_014679.1. NM_001183455.1.

3D structure databases

ProteinModelPortalP32854.
SMRP32854. Positions 200-265.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2021N.
IntActP32854. 13 interactions.
MINTMINT-389382.
STRINGP32854.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR036W; YOR036W; YOR036W.
GeneID854201.
KEGGsce:YOR036W.
NMPDRfig|4932.3.peg.5779.

Organism-specific databases

CYGDYOR036w.
SGDS000005562. PEP12.

Phylogenomic databases

eggNOGfuNOG12527.
GeneTreeEFGT00050000002424.
HOGENOMHBG202813.
OMAASEMAND.
OrthoDBEOG4ZKNWR.

Gene expression databases

ArrayExpressP32854.
GenevestigatorP32854.
GermOnlineYOR036W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR006012. Syntaxin/epimorphin_CS.
IPR006011. Syntaxin_N.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]
KOK08488.
PfamPF05739. SNARE. 1 hit.
[Graphical view]
SMARTSM00503. SynN. 1 hit.
SM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMSSF47661. t-snare. 1 hit.
PROSITEPS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio976038.

Entry information

Entry namePEP12_YEAST
AccessionPrimary (citable) accession number: P32854
Secondary accession number(s): D6W2A3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: December 14, 2011
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

SIMILARITY comments

Index of protein domains and families