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Protein

Phosducin-like protein 2

Gene

PLP2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Essential for cell growth. Inhibits early G-protein signaling events following pheromone stimulation.1 Publication

GO - Molecular functioni

  • actin binding Source: SGD
  • G-protein beta/gamma-subunit complex binding Source: SGD

GO - Biological processi

  • negative regulation of signal transduction Source: UniProtKB-KW
  • positive regulation of transcription from RNA polymerase II promoter by pheromones Source: SGD
  • protein folding Source: SGD
  • queuosine biosynthetic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Signal transduction inhibitor

Keywords - Biological processi

Pheromone response

Enzyme and pathway databases

BioCyciYEAST:G3O-33768-MONOMER.
ReactomeiR-SCE-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosducin-like protein 2
Alternative name(s):
Viral IAP-associated factor 1 homolog
Gene namesi
Name:PLP2Imported
Synonyms:VIAF1Imported
Ordered Locus Names:YOR281C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR281C.
SGDiS000005807. PLP2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 286286Phosducin-like protein 2PRO_0000163762Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351PhosphoserineCombined sources
Modified residuei62 – 621PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12017.

PTM databases

iPTMnetiQ12017.

Interactioni

Subunit structurei

Interacts with the G protein beta-gamma subunit complex (STE4-STE18 complex).1 Publication

GO - Molecular functioni

  • actin binding Source: SGD
  • G-protein beta/gamma-subunit complex binding Source: SGD

Protein-protein interaction databases

BioGridi34669. 28 interactions.
DIPiDIP-5004N.
IntActiQ12017. 11 interactions.
MINTiMINT-513281.

Structurei

3D structure databases

ProteinModelPortaliQ12017.
SMRiQ12017. Positions 95-227.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni96 – 286191Thioredoxin foldBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the phosducin family.Curated

Phylogenomic databases

GeneTreeiENSGT00530000062970.
HOGENOMiHOG000184445.
InParanoidiQ12017.
OMAiSGQDYVK.
OrthoDBiEOG73Z34Z.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.

Sequencei

Sequence statusi: Complete.

Q12017-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQNEPMFQVQ VDESEDSEWN DILRAKGVIP ERAPSPTAKL EEALEEAIAK
60 70 80 90 100
QHENRLEDKD LSDLEELEDD EDEDFLEAYK IKRLNEIRKL QERSKFGEVF
110 120 130 140 150
HINKPEYNKE VTLASQGKKY EGAQTNDNGE EDDGGVYVFV HLSLQSKLQS
160 170 180 190 200
RILSHLFQSA ACKFREIKFV EIPANRAIEN YPESNCPTLI VYYRGEVIKN
210 220 230 240 250
MITLLELGGN NSKMEDFEDF MVKVGAVAEG DNRLIMNRDD EESREERKLH
260 270 280
YGEKKSIRSG IRGKFNVGIG GNDDGNINDD DDGFFD
Length:286
Mass (Da):32,793
Last modified:November 1, 1996 - v1
Checksum:i414A696FFBDBD833
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF110514 mRNA. Translation: AAG21890.1.
X89633 Genomic DNA. Translation: CAA61786.1.
Z75189 Genomic DNA. Translation: CAA99507.1.
AY558032 Genomic DNA. Translation: AAS56358.1.
BK006948 Genomic DNA. Translation: DAA11046.1.
PIRiS67183.
RefSeqiNP_014924.3. NM_001183700.3.

Genome annotation databases

EnsemblFungiiYOR281C; YOR281C; YOR281C.
GeneIDi854456.
KEGGisce:YOR281C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF110514 mRNA. Translation: AAG21890.1.
X89633 Genomic DNA. Translation: CAA61786.1.
Z75189 Genomic DNA. Translation: CAA99507.1.
AY558032 Genomic DNA. Translation: AAS56358.1.
BK006948 Genomic DNA. Translation: DAA11046.1.
PIRiS67183.
RefSeqiNP_014924.3. NM_001183700.3.

3D structure databases

ProteinModelPortaliQ12017.
SMRiQ12017. Positions 95-227.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34669. 28 interactions.
DIPiDIP-5004N.
IntActiQ12017. 11 interactions.
MINTiMINT-513281.

PTM databases

iPTMnetiQ12017.

Proteomic databases

MaxQBiQ12017.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR281C; YOR281C; YOR281C.
GeneIDi854456.
KEGGisce:YOR281C.

Organism-specific databases

EuPathDBiFungiDB:YOR281C.
SGDiS000005807. PLP2.

Phylogenomic databases

GeneTreeiENSGT00530000062970.
HOGENOMiHOG000184445.
InParanoidiQ12017.
OMAiSGQDYVK.
OrthoDBiEOG73Z34Z.

Enzyme and pathway databases

BioCyciYEAST:G3O-33768-MONOMER.
ReactomeiR-SCE-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Miscellaneous databases

PROiQ12017.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "VIAF, a conserved inhibitor of apoptosis (IAP)-interacting factor that modulates caspase activation."
    Wilkinson J.C., Richter B.W.M., Wilkinson A.S., Burstein E., Rumble J.M., Balliu B., Duckett C.S.
    J. Biol. Chem. 279:51091-51099(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "DNA sequence analysis of the VPH1-SNF2 region on chromosome XV of Saccharomyces cerevisiae."
    Cheret G., Bernardi A., Sor F.J.
    Yeast 12:1059-1064(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "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.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE.
  6. "Functional analysis of Plp1 and Plp2, two homologues of phosducin in yeast."
    Flanary P.L., DiBello P.R., Estrada P., Dohlman H.G.
    J. Biol. Chem. 275:18462-18469(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH THE STE4-STE18 COMPLEX.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  10. "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-35 AND SER-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  11. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-35 AND SER-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPLP2_YEAST
AccessioniPrimary (citable) accession number: Q12017
Secondary accession number(s): D6W2Y0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 126 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 7700 molecules/cell in log phase SD medium.1 Publication

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.