Q12017 · PLP2_YEAST

Function

function

Essential for cell growth (PubMed:10749875).
Inhibits early G-protein signaling events following pheromone stimulation (PubMed:10749875).
Inhibits the folding activity of the chaperonin-containing T-complex (CCT) CCT2 which leads to inhibition of cytoskeletal actin folding (PubMed:17429077).
Plays a role in cell cycle progression in G1/S phase (PubMed:17429077).

Miscellaneous

Present with 7700 molecules/cell in log phase SD medium.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Molecular Functionactin binding
Molecular FunctionG-protein beta/gamma-subunit complex binding
Biological Processactin cytoskeleton organization
Biological Processcellular response to pheromone
Biological Processnegative regulation of chaperone-mediated protein folding
Biological Processnegative regulation of signal transduction
Biological Processpositive regulation of transcription by RNA polymerase II
Biological Processprotein folding
Biological Processregulation of cell cycle

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phosducin-like protein 2
  • Alternative names
    • Viral IAP-associated factor 1 homolog

Gene names

    • Name
      PLP2
    • Synonyms
      VIAF1
    • Ordered locus names
      YOR281C

Organism names

Accessions

  • Primary accession
    Q12017
  • Secondary accessions
    • D6W2Y0

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Impaired growth, cytoskeletal disruptions caused by actin polarization defects, and abberent nuclear segregation caused by misoriented mitotic spindles (PubMed:17429077).
Cells are enlarged or do not bud, caused by cell cycle arrest in G1/S phase (PubMed:17429077).

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 6 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001637621-286Phosducin-like protein 2
Modified residue35Phosphoserine
Modified residue62Phosphoserine

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Interacts with the G protein beta-gamma subunit complex (STE4-STE18 complex) (PubMed:10749875).
Interacts with CCT2; this interaction leads to inhibition of CCT complex mediated actin folding (PubMed:17429077).

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region96-286Thioredoxin fold

Sequence similarities

Belongs to the phosducin family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    286
  • Mass (Da)
    32,793
  • Last updated
    1996-11-01 v1
  • Checksum
    414A696FFBDBD833
MQNEPMFQVQVDESEDSEWNDILRAKGVIPERAPSPTAKLEEALEEAIAKQHENRLEDKDLSDLEELEDDEDEDFLEAYKIKRLNEIRKLQERSKFGEVFHINKPEYNKEVTLASQGKKYEGAQTNDNGEEDDGGVYVFVHLSLQSKLQSRILSHLFQSAACKFREIKFVEIPANRAIENYPESNCPTLIVYYRGEVIKNMITLLELGGNNSKMEDFEDFMVKVGAVAEGDNRLIMNRDDEESREERKLHYGEKKSIRSGIRGKFNVGIGGNDDGNINDDDDGFFD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF110514
EMBL· GenBank· DDBJ
AAG21890.1
EMBL· GenBank· DDBJ
mRNA
X89633
EMBL· GenBank· DDBJ
CAA61786.1
EMBL· GenBank· DDBJ
Genomic DNA
Z75189
EMBL· GenBank· DDBJ
CAA99507.1
EMBL· GenBank· DDBJ
Genomic DNA
AY558032
EMBL· GenBank· DDBJ
AAS56358.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006948
EMBL· GenBank· DDBJ
DAA11046.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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