P42656 · RAD24_SCHPO

Function

function

Acts in cell cycle and stress checkpoint signaling by sequestering signal transducers regulated by the checkpoints (PubMed:11818066, PubMed:15629716, PubMed:8036497).
Required for the DNA damage checkpoint that ensures that DNA damage is repaired before mitosis is attempted (PubMed:8036497).
During environmental stress, sequesters srk1-phosphorylated cdc25 in the cytoplasm to delay the G2/M transition (PubMed:15629716).
Sequesters byr2 in the cytoplasm to prevent its translocation to the plasma membrane (PubMed:12242289).
Sequesters ran1/pat1-phosphorylated mei2 from its non-coding RNA activators (including meiRNA), to prevent meiotic induction in vegetative cells and to regulate meiosis I (PubMed:11818066).

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 Componentcell division site
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentmitotic actomyosin contractile ring, distal actin filament layer
Cellular Componentmitotic spindle
Cellular Componentmitotic spindle midzone
Cellular Componentmitotic spindle pole body
Cellular Componentnucleus
Molecular Functionprotein sequestering activity
Biological Processcellular response to heat
Biological Processmeiotic cell cycle
Biological Processmitotic cytokinesis checkpoint signaling
Biological Processmitotic DNA replication checkpoint signaling
Biological Processmitotic G2 DNA damage checkpoint signaling
Biological Processnegative regulation of induction of conjugation with cellular fusion
Biological Processprotein localization
Biological Processsignal transduction

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Checkpoint signal transducer rad24

Gene names

    • Name
      rad24
    • ORF names
      SPAC8E11.02c

Organism names

Accessions

  • Primary accession
    P42656
  • Secondary accessions
    • O42704
    • O42879

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00000587171-270Checkpoint signal transducer rad24
Modified residue34Phosphoserine
Modified residue66Phosphoserine

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Homodimer (PubMed:12242289).
Binds preferentially to mei2 phosphorylated by ran1/pat1 (PubMed:11818066).
Binds preferentially to cdc25 phosphorylated by srk1 during G2; the interaction is increased during osmotic stress (PubMed:15629716).
Interacts with byr2 (PubMed:12242289).
Interacts with rad25 (PubMed:12242289).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY P42656clp1 Q9P7H13EBI-704791, EBI-704737

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region242-270Disordered

Sequence similarities

Belongs to the 14-3-3 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    270
  • Mass (Da)
    30,082
  • Last updated
    1998-07-15 v2
  • Checksum
    1401DD425A1A872F
MSTTSREDAVYLAKLAEQAERYEGMVENMKSVASTDQELTVEERNLLSVAYKNVIGARRASWRIVSSIEQKEESKGNTAQVELIKEYRQKIEQELDTICQDILTVLEKHLIPNAASAESKVFYYKMKGDYYRYLAEFAVGEKRQHSADQSLEGYKAASEIATAELAPTHPIRLGLALNFSVFYYEILNSPDRACYLAKQAFDEAISELDSLSEESYKDSTLIMQLLRDNLTLWTSDAEYSAAAAGGNTEGAQENAPSNAPEGEAEPKADA

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict219in Ref. 2; BAA24800
Sequence conflict264in Ref. 1; CAA55795
Sequence conflict269-270in Ref. 1; CAA55795

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X79206
EMBL· GenBank· DDBJ
CAA55795.1
EMBL· GenBank· DDBJ
Genomic DNA
AB010899
EMBL· GenBank· DDBJ
BAA24800.1
EMBL· GenBank· DDBJ
mRNA
AB008545
EMBL· GenBank· DDBJ
BAA28672.1
EMBL· GenBank· DDBJ
Genomic DNA
CU329670
EMBL· GenBank· DDBJ
CAA17023.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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