Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on Enzyme Commission mapping
Annotation inferences using phylogenetic trees
Automatic Gene Ontology annotation based on Rhea mapping
Combined Automated Annotation using Multiple IEA Methods
Activating phosphorylation of the Kin28p subunit of yeast TFIIH by Cak1p.
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Cak1 phosphorylates Kin28 Thr162, which stimulates Kin28 CTD kinase activity; Kin28 is a physiological Cak1 substrate.
"Finally, we show that Kin28p is no longer phosphorylated on Thr-162 following inactivation of Cak1p in vivo, that Cak1p can phosphorylate Kin28p on Thr-162 in vitro, and that this phosphorylation stimulates the CTD kinase activity of Kin28p."
A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae.
CAK1 promotes meiosis and spore formation in Saccharomyces cerevisiae in a CDC28-independent fashion.
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Cak1's sole essential mitotic role is Cdc28 Thr169 phosphorylation; in meiosis it acts Cdc28-independently on multiple kinase targets.
"CAK1 encodes a protein kinase in Saccharomyces cerevisiae whose sole essential mitotic role is to activate the Cdc28p cyclin-dependent kinase by phosphorylation of threonine-169 in its activation loop."
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Purified Cak1 does not phosphorylate Smk1 or Ime2 in vitro.
"Neither Ime2-GSTp or Smk1-HAp was phosphorylated under conditions in which CDK2 was phosphorylated in a robust fashion (data not shown)."
Assigning function to yeast proteins by integration of technologies.
Functional organization of the S. cerevisiae phosphorylation network.
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cak1 hypomorphs derepress cryptic initiation from an internal TATA in FLO8.
"Finally, the cak1-DAmP strain, as well as other previously characterized CAK1 mutants (cak1-22, cak1-23, cak1-95) (Espinoza et al., 1998), showed a significant increase of transcription initiation from a cryptic internal TATA site within FLO8 (Figure 6c)."
A global protein kinase and phosphatase interaction network in yeast.
The Cdk-activating kinase (CAK) from budding yeast.
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Cak1 is an active monomer with full activity in E. coli and is not part of TFIIH.
"Unlike CAKs from other organisms, Cak1p is active as a monomer, has full activity when expressed in E. coli, and is not a component of the basal transcription factor, TFIIH."
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cak1-ts cells show a G2 delay with low Cdc28 kinase activity and genetic interaction with CLB2.
"A temperature-sensitive mutation in CAK1 confers a G2 delay accompanied by low Cdc28p protein kinase activity and shows genetic interactions with altered expression of the gene for the major mitotic cyclin, CLB2."
Civ1 (CAK in vivo), a novel Cdk-activating kinase.
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Civ1/Cak1 binds and phosphorylates Cdc28, permitting its activation by cyclin; CIV1 is essential.
"Civ1 binds tightly to and phosphorylates Cdc28, thereby allowing its subsequent activation by the binding of a cyclin."
A cyclin-dependent kinase-activating kinase (CAK) in budding yeast unrelated to vertebrate CAK.
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Cak1 accounts for most yeast CAK activity, is constant through the cell cycle, and is essential.
"Cak1 accounted for most CAK activity in yeast cell lysates, and its activity was constant throughout the cell cycle. The CAK1 gene was essential for cell viability."
Localization and regulation of the cdk-activating kinase (Cak1p) from budding yeast.
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Cak1 is dispersed throughout the cell with most protein in the cytoplasm.
"We have found that Cak1p is dispersed throughout the cell as shown by immunofluorescence; biochemical subcellular fractionation confirmed that most of the Cak1p is found in the cytoplasm."
Fission yeast Csk1 is a CAK-activating kinase (CAKAK).
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Cak1/Civ1 provides CAK activity in budding yeast, whereas other species use a CDK7-cyclin H type CAK.
"Two distinct CAK kinases have been described: in budding yeast Saccharomyces cerevisiae, the Cak1/Civ1 kinase is responsible for CAK activity."
Falcon deep research report for CAK1