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Protein

Syntaxin PEP12

Gene

PEP12

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

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

GO - Molecular functioni

  • SNAP receptor activity Source: SGD
  • SNARE binding Source: GO_Central

GO - Biological processi

  • CVT pathway Source: SGD
  • Golgi to vacuole transport Source: SGD
  • macroautophagy Source: SGD
  • vacuole inheritance Source: SGD
  • vesicle docking Source: GO_Central
  • vesicle fusion Source: GO_Central
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-33582-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Syntaxin PEP12
Alternative name(s):
Carboxypeptidase Y-deficient protein 12
Vacuolar protein sorting-associated protein 6
Vacuolar protein-targeting protein 13
Gene namesi
Name:PEP12
Synonyms:VPS6, VPT13
Ordered Locus Names:YOR036W
ORF Names:OR26.29
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR036W.
SGDiS000005562. PEP12.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 268268CytoplasmicSequence analysisAdd
BLAST
Transmembranei269 – 28820Helical; Anchor for type IV membrane proteinSequence analysisAdd
BLAST

GO - Cellular componenti

  • endosome Source: SGD
  • Golgi apparatus Source: SGD
  • integral component of membrane Source: GO_Central
  • SNARE complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi271 – 2711L → D: Increases ubiquitination by TUL1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 288288Syntaxin PEP12PRO_0000210271Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21PhosphoserineCombined sources
Modified residuei23 – 231PhosphoserineCombined sources

Post-translational modificationi

Ubiquitinated.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP32854.

PTM databases

iPTMnetiP32854.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
YKT6P360152EBI-13098,EBI-26982

GO - Molecular functioni

  • SNAP receptor activity Source: SGD
  • SNARE binding Source: GO_Central

Protein-protein interaction databases

BioGridi34438. 106 interactions.
DIPiDIP-2021N.
IntActiP32854. 14 interactions.
MINTiMINT-389382.

Structurei

3D structure databases

ProteinModelPortaliP32854.
SMRiP32854. Positions 198-282.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini195 – 25763t-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the syntaxin family.Curated
Contains 1 t-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00450000040239.
HOGENOMiHOG000000782.
InParanoidiP32854.
KOiK08488.
OMAiGTEFRAS.
OrthoDBiEOG7SV15X.

Family and domain databases

InterProiIPR006012. Syntaxin/epimorphin_CS.
IPR006011. Syntaxin_N.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF05739. SNARE. 1 hit.
[Graphical view]
SMARTiSM00503. SynN. 1 hit.
SM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMiSSF47661. SSF47661. 1 hit.
PROSITEiPS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32854-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEDEFFGGD NEAVWNGSRF SDSPEFQTLK EEVAAELFEI NGQISTLQQF
60 70 80 90 100
TATLKSFIDR GDVSAKVVER INKRSVAKIE EIGGLIKKVN TSVKKMDAIE
110 120 130 140 150
EASLDKTQII AREKLVRDVS YSFQEFQGIQ RQFTQVMKQV NERAKESLEA
160 170 180 190 200
SEMANDAALL DEEQRQNSSK STRIPGSQIV IERDPINNEE FAYQQNLIEQ
210 220 230 240 250
RDQEISNIER GITELNEVFK DLGSVVQQQG VLVDNIEANI YTTSDNTQLA
260 270 280
SDELRKAMRY QKRTSRWRVY LLIVLLVMLL FIFLIMKL
Length:288
Mass (Da):33,006
Last modified:October 1, 1996 - v2
Checksum:iD9F5711339DA1CDA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131A → G in AAB38370 (PubMed:8730101).Curated
Sequence conflicti89 – 891V → I in AAB38370 (PubMed:8730101).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90395 Genomic DNA. Translation: AAB38370.1.
X87331 Genomic DNA. Translation: CAA60755.1.
Z74944 Genomic DNA. Translation: CAA99226.1.
BK006948 Genomic DNA. Translation: DAA10819.1.
PIRiS62175.
RefSeqiNP_014679.1. NM_001183455.1.

Genome annotation databases

EnsemblFungiiYOR036W; YOR036W; YOR036W.
GeneIDi854201.
KEGGisce:YOR036W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90395 Genomic DNA. Translation: AAB38370.1.
X87331 Genomic DNA. Translation: CAA60755.1.
Z74944 Genomic DNA. Translation: CAA99226.1.
BK006948 Genomic DNA. Translation: DAA10819.1.
PIRiS62175.
RefSeqiNP_014679.1. NM_001183455.1.

3D structure databases

ProteinModelPortaliP32854.
SMRiP32854. Positions 198-282.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34438. 106 interactions.
DIPiDIP-2021N.
IntActiP32854. 14 interactions.
MINTiMINT-389382.

PTM databases

iPTMnetiP32854.

Proteomic databases

MaxQBiP32854.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR036W; YOR036W; YOR036W.
GeneIDi854201.
KEGGisce:YOR036W.

Organism-specific databases

EuPathDBiFungiDB:YOR036W.
SGDiS000005562. PEP12.

Phylogenomic databases

GeneTreeiENSGT00450000040239.
HOGENOMiHOG000000782.
InParanoidiP32854.
KOiK08488.
OMAiGTEFRAS.
OrthoDBiEOG7SV15X.

Enzyme and pathway databases

BioCyciYEAST:G3O-33582-MONOMER.

Miscellaneous databases

PROiP32854.

Family and domain databases

InterProiIPR006012. Syntaxin/epimorphin_CS.
IPR006011. Syntaxin_N.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF05739. SNARE. 1 hit.
[Graphical view]
SMARTiSM00503. SynN. 1 hit.
SM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMiSSF47661. SSF47661. 1 hit.
PROSITEiPS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , 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.
  3. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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 nameiPEP12_YEAST
AccessioniPrimary (citable) accession number: P32854
Secondary accession number(s): D6W2A3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. 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.