PANTHER family review PTHR10828: IBA propagation assessment for cdc25
Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods
DNA damage and replication checkpoints in fission yeast require nuclear exclusion of the Cdc25 phosphatase via 14-3-3 binding.
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14-3-3 (Rad24/Rad25) binding keeps Cdc25 out of the nucleus and is required for DNA damage and replication checkpoint arrest; wild-type Cdc25 localizes to both nucleus and cytoplasm and shuttles between them.
"Nuclear exclusion of wild-type Cdc25 was observed upon overproduction of Rad 24, one of the two fission yeast 14-3-3 proteins, indicating that one function of Rad 24 is to keep Cdc25 out of the nucleus."
Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate.
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Structural study of p13suc1/CKS; does not substantively characterize a Cdc25 interaction, so the Cdc25 protein-binding annotation derived from it is peripheral.
"Cyclin-dependent kinase subunit (CKS) proteins bind to cyclin-dependent kinases and target various proteins to phosphorylation and proteolysis during cell division"
Pyp3 PTPase acts as a mitotic inducer in fission yeast.
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p80cdc25 is the major protein tyrosine phosphatase dephosphorylating Cdc2-Tyr15; Pyp3 cooperates as a second PTPase.
"the actions of the p107wee1 tyrosine kinase and p80cdc25 protein tyrosine phosphatase (PTPase)"
cdc25 is a nuclear protein expressed constitutively throughout the cell cycle in nontransformed mammalian cells.
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Mammalian cdc25 is nuclear during interphase and redistributes to the cytoplasm at nuclear envelope breakdown; this is heterologous evidence relative to S. pombe cdc25.
"cdc25 protein is found essentially localized in the nucleus throughout interphase and during early prophase"
On the slowing of S phase in response to DNA damage in fission yeast.
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The Rad3-Cds1 intra-S DNA damage checkpoint acts through Cdc2, the kinase whose Tyr15 dephosphorylation is controlled by Cdc25.
"a major downstream target of this pathway is the cyclin-dependent kinase, Cdc2"
Inactivation of the Cdc25 phosphatase by the stress-activated Srk1 kinase in fission yeast.
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Srk1 (downstream of Sty1/Spc1) inhibits Cdc25 during the normal cycle and under non-genotoxic stress by phosphorylating it at the Chk1/Cds1 sites, promoting Rad24 (14-3-3) binding and cytoplasmic accumulation.
"Srk1 interacts with and phosphorylates Cdc25 at the same sites phosphorylated by the Chk1 and Cds1 (Chk2) kinases"
ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.
Complementation of the mitotic activator, p80cdc25, by a human protein-tyrosine phosphatase.
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Cdc2-Tyr15 dephosphorylation triggers activation of the Cdc2-cyclin complex, and a human protein tyrosine phosphatase can substitute for p80cdc25.
"dephosphorylation of Tyr15 triggered activation of the pp34-cyclin complex from fission yeast, that a human protein-tyrosine phosphatase can catalyze this event both in vitro and in vivo"
p80cdc25 mitotic inducer is the tyrosine phosphatase that activates p34cdc2 kinase in fission yeast.
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p80cdc25 directly dephosphorylates and activates p34cdc2; the active-site Cys480 is essential for phosphatase activity, defining Cdc25 as a novel PTPase subclass.
"Mutation of the cdc25 Cys480 codon, corresponding to an essential cysteine in the active site of PTPases, abolished the phosphatase activity of GST-cdc25"
Mei4p coordinates the onset of meiosis I by regulating cdc25+ in fission yeast.
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cdc25+ is a key Mei4 target controlling entry into meiosis I; forced Cdc2-Tyr15 dephosphorylation bypasses the mei4 arrest.
"Forced dephosphorylation of Cdc2p on tyrosine-15 thus induced meiosis I in mei4 mutant cells without a delay"
cdc25 M-phase inducer.
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p80cdc25 directly dephosphorylates Cdc2-Tyr15, and its cellular concentration rises as cells approach mitosis, making it rate-limiting for mitotic timing.
"p80cdc25 encodes a phosphate that acts by directly dephosphorylating the Tyr-15 residue of p34cdc2"
Activation of Srk1 by the mitogen-activated protein kinase Sty1/Spc1 precedes its dissociation from the kinase and signals its degradation.
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Stress-activated Srk1 negatively regulates the cell cycle by inhibiting Cdc25; Cdc25 is localized to nucleus and cytosol.
"activation of Srk1 kinase, which negatively regulates cell cycle progression by inhibiting Cdc25"
Multisite phosphoregulation of Cdc25 activity refines the mitotic entrance and exit switches.
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Cdk1 hyperphosphorylates and catalytically activates Cdc25 in a positive feedback loop driving the abrupt G2/M switch; Clp1/Cdc14 reverses this at exit.
"Cdc25 hyperphosphorylation by Cdk1 governs Cdc25 catalytic activation, the precision of mitotic entry, and unvarying cell length"
Meiotic nuclear movements in fission yeast are regulated by the transcription factor Mei4 downstream of a Cds1-dependent replication checkpoint pathway.
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Cdc25 expression (driven by Mei4) activates CDK and is essential for triggering meiotic nuclear divisions, acting downstream of the replication checkpoint.
"Mei4 is also required for the expression of phosphatase Cdc25, which activates cyclin-dependent kinase (CDK), and is thereby essential for triggering meiotic nuclear divisions"
Regulation of p34cdc2 protein kinase during mitosis.
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The cdc25+ gene product activates p34cdc2 to initiate mitosis; mitotic kinase activity also requires cyclin (cdc13).
"the cdc25+ gene product activating the p34cdc2 protein kinase leading to mitotic initiation"
Size-Dependent Expression of the Mitotic Activator Cdc25 Suggests a Mechanism of Size Control in Fission Yeast.
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Cell size in fission yeast is regulated by size-dependent expression of Cdc25: Cdc25 concentration rises as cells grow, triggering division at a threshold.
"cdc25 transcript levels are regulated such that smaller cells express less Cdc25 and larger cells express more Cdc25, creating an increasing concentration of Cdc25 as cells grow and providing a mechanism for cells to trigger cell division when they reach a threshold concentration of Cdc25"
cdc25+ functions as an inducer in the mitotic control of fission yeast.
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cdc25+ is required to initiate mitosis and acts as a dosage-dependent inducer that counteracts the mitotic inhibitor wee1+.
"increased cdc25+ expression causes mitosis to initiate at a reduced cell size. This shows that cdc25+ functions as a dosage-dependent inducer in mitotic control"
Cdc2 tyrosine phosphorylation is required for the DNA damage checkpoint in fission yeast.
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The G2 DNA damage checkpoint depends on inhibitory Cdc2-Tyr15 phosphorylation; irradiation reduces the rate of Cdc2 tyrosine dephosphorylation carried out mainly by Cdc25.
"the rate of Cdc2 tyrosine dephosphorylation is reduced by irradiation. This result implicates regulation of Cdc2 tyrosine dephosphorylation, mainly carried out by the Cdc25 tyrosine phosphatase"
Cdc25 mitotic inducer targeted by chk1 DNA damage checkpoint kinase.
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Cdc25 (not Wee1) is the target of the Chk1 DNA damage checkpoint kinase; Chk1 associates with and phosphorylates Cdc25.
"These findings identify Cdc25, but not Wee1, as a target of the DNA damage checkpoint"
Replication checkpoint requires phosphorylation of the phosphatase Cdc25 by Cds1 or Chk1.
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Chk1 and Cds1 redundantly phosphorylate Cdc25 (including Ser99, Ser192, Ser359) to promote 14-3-3 binding, preventing Cdc25 from activating Cdc2 at the replication checkpoint.
"Phosphorylation of Cdc25 promotes its binding to 14-3-3 proteins, preventing it from activating Cdc2."