The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The requested protein is correctly identified. CAK1 (synonym CIV1; ordered locus YFL029C; UniProt P43568) in Saccharomyces cerevisiae S288c encodes Cak1, an essential, atypical, monomeric serine/threonine protein kinase. Independent biochemical purifications identified a 42–44-kDa protein whose peptides matched YFL029C, and recombinant Cak1 reproduced CDK-activating kinase activity. Its kinase-domain architecture and catalytic activity agree with the supplied CMGC/protein-kinase domain annotations. This report excludes similarly named CAK1 proteins from Candida, filamentous fungi, plants, and other organisms. (espinoza1998theactivationof pages 72-76, kaldis1996thecdkactivatingkinase pages 2-4, espinoza1996acyclindependentkinaseactivating pages 3-3)
Cak1’s primary function is to phosphorylate the activation-loop—or T-loop—threonine of selected cyclin-dependent kinases. Its best-established physiological targets are the cell-cycle CDK Cdc28 at Thr169 and the transcriptional CDKs Kin28, Bur1 at Thr240, and Ctk1 at Thr338. Thus, Cak1 is upstream of both cell-cycle progression and several RNA-polymerase-II transcription modules. (kaldis1999thecdkactivatingkinase pages 1-2, espinoza1998cak1isrequired pages 1-1, yao2002activationofthe pages 7-8, ostapenko2005phosphorylationbycak1 pages 1-2)
| Feature/target | Precise finding | Biological consequence | Evidence type/strength | Key publication and year |
|---|---|---|---|---|
| Identity and kinase family | CAK1/CIV1/YFL029C encodes an essential, atypical ~42–44-kDa CDK-activating Ser/Thr kinase; peptides from purified CAK matched YFL029C. The protein lacks the canonical kinase GxGxxG nucleotide-binding motif. | Establishes that UniProt P43568 is the budding-yeast CAK rather than a similarly named protein from another organism. | Very strong: independent purification, peptide sequencing, recombinant activity, genetics (espinoza1998theactivationof pages 72-76, kaldis1996thecdkactivatingkinase pages 2-4, espinoza1996acyclindependentkinaseactivating pages 3-3) | Kaldis, Sutton & Solomon, 1996; Espinoza et al., 1996 |
| Oligomeric state | Purified and recombinant Cak1 is catalytically active as a single-polypeptide, apparently monomeric kinase, without a required cyclin partner. | Distinguishes fungal Cak1 from metazoan Cdk7–cyclin H–MAT1 CAK. | Strong: gel filtration, purification, recombinant expression, and immunoprecipitated activity (kaldis1996thecdkactivatingkinase pages 2-4, espinoza1996acyclindependentkinaseactivating pages 3-3, kaldis1998humanandyeast pages 1-2) | Kaldis, Sutton & Solomon, 1996; Espinoza et al., 1996 |
| Cdc28/Cdk1—Thr169 | Cak1 directly phosphorylates the Cdc28 activation-loop residue Thr169; conditional cak1 loss reduces Thr169 phosphorylation and Cdc28 activity. Cak1 preferentially recognizes free/monomeric CDK substrate, with phosphorylation normally preceding cyclin binding. | Enables Cdc28–cyclin activity and therefore G1/S and G2/M cell-cycle progression; loss of CAK1 is lethal. | Very strong: recombinant kinase assays, nonphosphorylatable-site evidence, conditional mutants, immunodepletion, and cellular kinase assays (kaldis1999thecdkactivatingkinase pages 1-2, kaldis1998humanandyeast pages 1-2, kaldis1996thecdkactivatingkinase pages 8-9) | Kaldis et al., 1998; Ross, Kaldis & Solomon, 2000 |
| Kin28—T-loop/T162 context | Cak1 is required for Kin28 T-loop phosphorylation and activation in vivo; the relevant activation-loop context is represented experimentally by Kin28-T162A. Pho85 and Srb10 activity was not similarly Cak1-dependent. | Activates the TFIIH-associated transcriptional CDK Kin28, linking Cak1 to RNA polymerase II transcription initiation. | Strong: conditional cak1 mutants, Kin28 phosphorylation/activity measurements, genetic interactions, and heterologous coexpression; exact direct site assignment is less extensively documented here than Cdc28 Thr169 (espinoza1998cak1isrequired pages 1-1, yao2002activationofthe pages 1-2) | Espinoza et al., 1998 |
| Bur1—Thr240 | Cak1-dependent phosphorylation of the Bur1 T-loop residue Thr240 stimulates Bur1–Bur2 RNA polymerase II CTD kinase activity. Bur1-T240A and Bur1 purified from cak1 cells show similarly severe loss of detectable in-vitro activity, although T240A cells remain viable. | Promotes transcription elongation-associated Bur1–Bur2 signaling; phosphorylation is important for maximal catalytic activity but is not absolutely required for Bur1’s essential cellular function. | Strong: recombinant stimulation, site-directed mutants, kinase assays, and in-vivo genetic/biochemical dependence (yao2002activationofthe pages 1-1, yao2002activationofthe pages 7-8) | Yao & Prelich, 2002 |
| Ctk1—Thr338 | Cak1 directly phosphorylates the Ctk1 T-loop residue Thr338. Ctk1-T338A or Ctk1 isolated from cak1 cells has little or no detectable in-vitro CTD kinase activity; the mutation does not prevent Ctk2/Ctk3-complex association. | Supports RNA polymerase II CTD Ser2 phosphorylation, transcriptional elongation/3′ processing, and adaptation during diauxic shift or low-temperature growth. | Very strong: direct recombinant phosphorylation, phosphatase and two-dimensional-gel analysis, site mutant, conditional cak1 dependence, rescue, and functional transcription assays (ostapenko2005phosphorylationbycak1 pages 3-4, ostapenko2005phosphorylationbycak1 pages 1-2, ostapenko2005phosphorylationbycak1 pages 4-5) | Ostapenko & Solomon, 2005 |
| Cellular localization | Cak1 has been reported as predominantly cytoplasmic. This is compatible with phosphorylation of monomeric Cdc28 before cyclin assembly, but localization is less comprehensively documented in the retrieved evidence than substrate biochemistry. | Places a major pool of CAK activity in the cytoplasm; it does not exclude transient interactions or access to transcriptional CDKs associated with nuclear functions. | Moderate/limited: older localization study and review-level synthesis; interpret more cautiously than the direct substrate assignments (kaldis1999thecdkactivatingkinase pages 1-2) | Kaldis et al., 1998; Kaldis, 1999 |
| Essentiality and quantitative phenotype | Immunodepletion removes >97% of extract CAK activity. CAK1-null spores form terminal microcolonies of approximately 8–12 cells, with heterogeneous budding morphologies. | Demonstrates that Cak1 supplies the dominant CAK activity and is indispensable for sustained vegetative proliferation. | Very strong: immunodepletion and null-spore phenotype (espinoza1998theactivationof pages 72-76, espinoza1996acyclindependentkinaseactivating pages 3-3) | Espinoza et al., 1996 |
Table: Evidence summary for the verified S. cerevisiae Cak1 protein, emphasizing direct CDK substrates, activation-loop sites, biological outcomes, and confidence. Localization is explicitly separated as less strongly documented than the biochemical substrate assignments.
Two independent discovery studies in 1996 converged on the same protein. Purified yeast CAK activity contained a 43–44-kDa polypeptide, peptide sequences matched YFL029C, and the predicted molecular mass was approximately 42.2 kDa. Recombinant protein expressed in bacteria was catalytically active, while immunodepletion removed more than 97% of detectable CAK activity from yeast lysate. These observations establish YFL029C/CAK1/CIV1—not a similarly named gene from another species—as the principal budding-yeast CAK. [Kaldis, Sutton & Solomon, August 1996, Cell, DOI/URL: https://doi.org/10.1016/S0092-8674(00)80129-4; Espinoza et al., 20 September 1996, Science, DOI/URL: https://doi.org/10.1126/science.273.5282.1714]. (kaldis1996thecdkactivatingkinase pages 2-4, espinoza1996acyclindependentkinaseactivating pages 3-3)
Cak1 belongs to the protein-kinase superfamily but is exceptionally divergent. It has only approximately 20–25% sequence identity to conventional Cdk7-type CAKs, lacks the canonical subdomain-I GxGxxG glycine-rich nucleotide-binding motif, and substitutes several otherwise highly conserved kinase residues. Nevertheless, ATP-dependent phosphorylation assays and recombinant activity establish it as a genuine protein kinase. Its activity as an apparently monomeric single polypeptide agrees with the supplied kinase-like and protein-kinase domain calls, while distinguishing it from metazoan Cdk7–cyclin H–MAT1 CAK. (kaldis1996thecdkactivatingkinase pages 2-4, kaldis1999thecdkactivatingkinase pages 1-2, espinoza1996acyclindependentkinaseactivating pages 3-3)
The reaction is the standard protein-kinase phosphotransfer:
ATP + CDK T-loop threonine → ADP + phospho-CDK T-loop threonine.
Radiolabeled γ-³²P-ATP experiments showed direct incorporation of phosphate into CDK substrates. Cak1 phosphorylated kinase-dead CDK2, excluding substrate autophosphorylation, but failed to phosphorylate CDK2-T160A or T160E activation-site mutants. Equivalent genetic and biochemical evidence identifies Cdc28 Thr169 as the physiological budding-yeast site. Phosphorylation rearranges/stabilizes the CDK activation segment and permits high catalytic activity after cyclin association. (kaldis1996thecdkactivatingkinase pages 2-4, kaldis1999thecdkactivatingkinase pages 1-2, espinoza1996acyclindependentkinaseactivating pages 3-3, kaldis1998humanandyeast pages 1-2)
Cak1 is not a broadly indiscriminate kinase. Its defining specificity is for activation-loop threonines in selected CDKs, with an experimentally demonstrated preference for free or monomeric CDKs. In comparative assays, yeast Cak1 preferentially phosphorylated monomeric CDKs, whereas human Cdk7-containing CAK favored cyclin-bound complexes. Cak1 can phosphorylate Cdc28 without cyclin, although robust downstream Cdc28 activity requires cyclin such as Clb2. This supports a maturation pathway in which Cak1 phosphorylation commonly precedes cyclin binding. [Kaldis et al., September 1998, Molecular Biology of the Cell, DOI/URL: https://doi.org/10.1091/mbc.9.9.2545]. (kaldis1998humanandyeast pages 1-2, espinoza1998theactivationof pages 72-76)
Cak1 is itself active without an associated cyclin. Gel filtration, biochemical purification, immunoprecipitation, and bacterial expression all support an active monomer rather than a conventional CDK–cyclin complex. This is a central functional distinction: Cak1 activates CDKs but is not regulated like an ordinary cyclin-dependent kinase. (kaldis1996thecdkactivatingkinase pages 2-4, espinoza1996acyclindependentkinaseactivating pages 3-3)
The dominant cell-cycle substrate is Cdc28, the principal CDK that drives budding-yeast cell-cycle transitions. Cak1 directly phosphorylates Thr169 in the Cdc28 T-loop. Conditional cak1 mutants lose Thr169 phosphorylation, CAK activity, and Cdc28 kinase activity, while purified or recombinant Cak1 phosphorylates and activates Cdc28 in vitro. This activating modification is required for normal Cdc28 activity and viability. (kaldis1999thecdkactivatingkinase pages 1-2, kaldis1998humanandyeast pages 1-2, kaldis1996thecdkactivatingkinase pages 8-9)
Because Cdc28 acts with different cyclins across the cycle, Cak1 lies upstream of both G1/S and G2/M progression rather than acting as a phase-specific cyclin signal. Conditional mutants arrest heterogeneously, including predominant G2/M arrest and a substantial G1 fraction; in one analysis approximately 35% arrested in G1. The delayed arrest—about 5–7 hours after temperature shift despite faster Cak1 inactivation—is consistent with persistence of previously phosphorylated Cdc28 and dilution or turnover over subsequent divisions. (kaldis1996thecdkactivatingkinase pages 8-9)
A later study also reported a phosphorylation-independent genetic role: elevated Cak1 could suppress phenotypes of certain Cdc28 C-terminal mutants even when Cak1 catalytic activity was compromised. This suggests a possible physical or chaperone-like contribution to Cdc28 maturation, but it is subsidiary to—and less firmly established than—the essential Thr169-phosphorylation mechanism. [Kim et al., 15 November 2009, Gene, DOI/URL: https://doi.org/10.1016/j.gene.2009.07.016]. (kim2009aphosphorylationindependentrole pages 1-3)
Cak1 also activates Kin28, the budding-yeast Cdk7-related kinase associated with TFIIH. Conditional cak1 mutations reduce Kin28 phosphorylation and activity in vivo; coexpression of Cak1 with Kin28 and its regulatory partners Ccl1 and Tfb3 produces active, phosphorylated Kin28. The relevant T-loop context has been tested through a Kin28-T162A allele. Genetic interactions between CAK1 and KIN28 further support physiological coupling. In contrast, Pho85 and Srb10 activities were not detectably dependent on Cak1, demonstrating selectivity among yeast CDKs. [Espinoza et al., November 1998, Molecular and Cellular Biology, DOI/URL: https://doi.org/10.1128/MCB.18.11.6365]. (espinoza1998cak1isrequired pages 1-1, yao2002activationofthe pages 1-2)
Through Kin28, Cak1 contributes indirectly to RNA polymerase II transcription initiation and promoter-associated CTD phosphorylation. Cak1 itself is not a TFIIH subunit and lacks the direct RNA-polymerase-II CTD kinase activity characteristic of Cdk7-containing metazoan CAK. (kaldis1998humanandyeast pages 1-2)
Cak1 phosphorylates the activation-loop residue Thr240 of Bur1, the catalytic component of the Bur1–Bur2 transcriptional CDK complex. Recombinant Cak1 stimulates Bur1–Bur2-associated CTD kinase activity. Bur1-T240 substitution and isolation of Bur1 from a cak1 mutant each cause a comparable loss of detectable in-vitro activity, supporting a direct activation mechanism. [Yao & Prelich, October 2002, Molecular and Cellular Biology, DOI/URL: https://doi.org/10.1128/MCB.22.19.6750-6758.2002]. (yao2002activationofthe pages 1-1, yao2002activationofthe pages 7-8)
The phenotype is nuanced: Bur1-T240A and T240E strains remain viable and grow relatively well, whereas deletion of BUR1 or mutation of its catalytic Asp213 is lethal. T-loop phosphorylation is therefore important for maximal Bur1 catalytic output but is not absolutely required for every essential in-vivo Bur1 function; residual activity, cellular cofactors, or pathway compensation may explain this difference. (yao2002activationofthe pages 7-8)
Cak1 directly phosphorylates Ctk1 Thr338, the conserved T-loop residue of the CTDK-I catalytic subunit. Wild-type Ctk1 efficiently phosphorylates an RNA-polymerase-II CTD peptide, whereas Ctk1-T338A has near-background activity comparable to a catalytic mutant. Ctk1 from cak1 cells is unphosphorylated and inactive in vitro; reintroduction of CAK1 restores activity, and recombinant Cak1 directly phosphorylates wild-type Ctk1 but not Ctk1-T338A. Kin28 and Bur1 mutants do not abolish Ctk1 activity, arguing against their serving as obligatory intermediates. [Ostapenko & Solomon, May 2005, Molecular and Cellular Biology, DOI/URL: https://doi.org/10.1128/MCB.25.10.3906-3913.2005]. (ostapenko2005phosphorylationbycak1 pages 3-4, ostapenko2005phosphorylationbycak1 pages 1-2, ostapenko2005phosphorylationbycak1 pages 4-5)
Ctk1-T338A still assembles with Ctk2/Ctk3, so its catalytic defect is not simply loss of the kinase complex. Functionally, Cak1-dependent Ctk1 activation supports RNA polymerase II CTD Ser2 phosphorylation, transcriptional elongation and 3′-end processing. The defect is condition-sensitive: T338A cells grow nearly normally at 30°C but poorly at 17°C, fail to produce the normal rise in CTD Ser2 phosphorylation during the diauxic shift, enter stationary phase inefficiently, and show impaired activation of genes including CTT1 and SPI1. (ostapenko2005phosphorylationbycak1 pages 1-2, ostapenko2005phosphorylationbycak1 pages 4-5, ostapenko2005phosphorylationbycak1 pages 2-3)
Older localization work and subsequent authoritative synthesis describe Cak1 as predominantly cytoplasmic. This fits its preference for phosphorylation of monomeric Cdc28 before cyclin assembly. However, the retrieved localization evidence is less detailed than the substrate biochemistry, and cytoplasmic enrichment should not be interpreted as strict nuclear exclusion: Cak1 functionally activates Kin28, Bur1, and Ctk1, whose principal actions occur in nuclear transcription. Transient substrate encounters, shuttling, or phosphorylation before assembly into nuclear complexes remain compatible with the evidence. (kaldis1999thecdkactivatingkinase pages 1-2)
Cak1 abundance and measured CAK activity are broadly constant through G1, S phase, and mitosis. Thus, Cak1 is best understood as a constitutive CDK-maturation enzyme rather than an oscillatory cell-cycle switch. Cell-cycle timing is generated mainly downstream through cyclin availability, inhibitory phosphorylation, phosphatases, localization, and substrate access. (espinoza1998theactivationof pages 72-76)
Cak1 represents a distinct monomeric CAK solution found principally among fungi and some plant lineages. Its lack of the conventional glycine-rich loop and unusual conserved-residue substitutions show that canonical motif inspection alone can underestimate kinase function. Active bacterial recombinant protein demonstrates that neither a cyclin nor a eukaryote-specific activating modification is obligatorily required for basal catalysis. The strongest structural-functional inference is therefore that Cak1 has evolved a noncanonical ATP-binding pocket while retaining the bilobal protein-kinase fold represented by the supplied PF00069/IPR000719 annotations. (kaldis1996thecdkactivatingkinase pages 2-4, kaldis1999thecdkactivatingkinase pages 1-2)
Its preference for unbound CDKs is biologically coherent: Cak1 acts as a CDK-maturation kinase, installing the activating phosphate before or during assembly of cell-cycle and transcription complexes. This division of labor contrasts with metazoan Cdk7, which is itself a cyclin-associated CDK and participates directly in TFIIH. (kaldis1998humanandyeast pages 1-2)
Cak1 is used principally as a mechanistic tool rather than as an industrial enzyme or approved therapeutic target. Conditional cak1 alleles, activation-loop mutants, and recombinant Cak1 assays allow investigators to separate CDK activation from cyclin binding and to perturb several CDK modules from one upstream node. This has been especially useful for distinguishing direct T-loop regulation from secondary effects on cell-cycle progression or transcription. (espinoza1998cak1isrequired pages 1-1, yao2002activationofthe pages 7-8, ostapenko2005phosphorylationbycak1 pages 4-5)
The unusual fungal-type ATP pocket and absence of a close human equivalent have also motivated the expert proposal that Cak1-like kinases could provide fungal-selective inhibitor targets. This remains a target-discovery concept, not a demonstrated clinical or agricultural implementation for S. cerevisiae Cak1. Any inhibitor program would need to establish conservation in the pathogen of interest, cellular target engagement, selectivity, and whether the pathogen’s CAK1 ortholog is essential under infection conditions.
A targeted search of 2023–2024 literature did not identify a primary study that materially revises the core functional annotation of S288c Cak1/P43568. Recent papers mentioning “Cak1” frequently concern orthologs in other fungi, broad kinase screens, cell-cycle reviews, or high-throughput yeast interaction resources. Those sources were not used to transfer organism-specific phenotypes onto P43568. Accordingly, the most precise evidence remains the foundational 1996–2005 biochemical and genetic literature rather than a newer omics association.
This absence of recent revision is itself informative: the direct assignments—Cdc28 Thr169, Kin28 activation, Bur1 Thr240, and Ctk1 Thr338—are mature mechanistic conclusions. The major remaining uncertainties concern quantitative in-vivo flux through each substrate, dynamic compartmentalization, complete structural characterization of substrate recognition, and whether non-CDK substrates exist.
High-confidence primary annotation: Cak1 is an essential, monomeric CDK-activating serine/threonine kinase that transfers phosphate from ATP to activation-loop threonines of selected CDKs, most importantly Cdc28 Thr169. (kaldis1996thecdkactivatingkinase pages 2-4, kaldis1999thecdkactivatingkinase pages 1-2, kaldis1998humanandyeast pages 1-2)
High-confidence pathway annotation: It activates the core Cdc28 cell-cycle engine and the transcriptional CDKs Kin28, Bur1, and Ctk1, thereby influencing cell-cycle transitions, RNA polymerase II initiation/elongation, CTD Ser2 phosphorylation, and transcriptional adaptation to nutrient depletion. (espinoza1998cak1isrequired pages 1-1, yao2002activationofthe pages 7-8, ostapenko2005phosphorylationbycak1 pages 1-2, ostapenko2005phosphorylationbycak1 pages 4-5)
Moderate-confidence localization annotation: A major Cak1 pool is cytoplasmic, but this should not be represented as exclusive localization because its direct physiological substrate set includes nuclear transcriptional kinases. (kaldis1999thecdkactivatingkinase pages 1-2)
Not supported: Cak1 should not be annotated as a TFIIH CTD kinase, a transporter, a structural protein, or a conventional cyclin-dependent kinase requiring its own cyclin. It is upstream of those CDK complexes and has no demonstrated direct RNA-polymerase-II CTD kinase activity. (espinoza1996acyclindependentkinaseactivating pages 3-3, kaldis1998humanandyeast pages 1-2)
References
(espinoza1998theactivationof pages 72-76): FH Espinoza. The activation of cyclin-dependent kinases in saccharomyces cerevisiae. Unknown journal, 1998.
(kaldis1996thecdkactivatingkinase pages 2-4): Philipp Kaldis, Ann Sutton, and Mark J Solomon. The cdk-activating kinase (cak) from budding yeast. Cell, 86:553-564, Aug 1996. URL: https://doi.org/10.1016/s0092-8674(00)80129-4, doi:10.1016/s0092-8674(00)80129-4. This article has 344 citations and is from a highest quality peer-reviewed journal.
(espinoza1996acyclindependentkinaseactivating pages 3-3): F. Hernan Espinoza, Alison Farrell, Hediye Erdjument-Bromage, Paul Tempst, and David O. Morgan. A cyclin-dependent kinase-activating kinase (cak) in budding yeast unrelated to vertebrate cak. Science, 273:1714-1717, Sep 1996. URL: https://doi.org/10.1126/science.273.5282.1714, doi:10.1126/science.273.5282.1714. This article has 246 citations and is from a highest quality peer-reviewed journal.
(kaldis1999thecdkactivatingkinase pages 1-2): P. Kaldis. The cdk-activating kinase (cak): from yeast to mammals. Cellular and Molecular Life Sciences CMLS, 55:284-296, Feb 1999. URL: https://doi.org/10.1007/s000180050290, doi:10.1007/s000180050290. This article has 389 citations.
(espinoza1998cak1isrequired pages 1-1): F. Hernán Espinoza, Alison Farrell, Jamison L. Nourse, Holly M. Chamberlin, Opher Gileadi, and David O. Morgan. Cak1 is required for kin28 phosphorylation and activation in vivo. Molecular and Cellular Biology, 18:6365-6373, Nov 1998. URL: https://doi.org/10.1128/mcb.18.11.6365, doi:10.1128/mcb.18.11.6365. This article has 100 citations and is from a domain leading peer-reviewed journal.
(yao2002activationofthe pages 7-8): Sheng Yao and Gregory Prelich. Activation of the bur1-bur2 cyclin-dependent kinase complex by cak1. Molecular and Cellular Biology, 22:6750-6758, Oct 2002. URL: https://doi.org/10.1128/mcb.22.19.6750-6758.2002, doi:10.1128/mcb.22.19.6750-6758.2002. This article has 65 citations and is from a domain leading peer-reviewed journal.
(ostapenko2005phosphorylationbycak1 pages 1-2): Denis Ostapenko and Mark J. Solomon. Phosphorylation by cak1 regulates the c-terminal domain kinase ctk1 in saccharomyces cerevisiae. Molecular and Cellular Biology, 25:3906-3913, May 2005. URL: https://doi.org/10.1128/mcb.25.10.3906-3913.2005, doi:10.1128/mcb.25.10.3906-3913.2005. This article has 37 citations and is from a domain leading peer-reviewed journal.
(kaldis1998humanandyeast pages 1-2): Philipp Kaldis, Alicia A. Russo, Hubert S. Chou, Nikola P. Pavletich, and Mark J. Solomon. Human and yeast cdk-activating kinases (caks) display distinct substrate specificities. Molecular biology of the cell, 9 9:2545-60, Sep 1998. URL: https://doi.org/10.1091/mbc.9.9.2545, doi:10.1091/mbc.9.9.2545. This article has 159 citations and is from a domain leading peer-reviewed journal.
(kaldis1996thecdkactivatingkinase pages 8-9): Philipp Kaldis, Ann Sutton, and Mark J Solomon. The cdk-activating kinase (cak) from budding yeast. Cell, 86:553-564, Aug 1996. URL: https://doi.org/10.1016/s0092-8674(00)80129-4, doi:10.1016/s0092-8674(00)80129-4. This article has 344 citations and is from a highest quality peer-reviewed journal.
(yao2002activationofthe pages 1-2): Sheng Yao and Gregory Prelich. Activation of the bur1-bur2 cyclin-dependent kinase complex by cak1. Molecular and Cellular Biology, 22:6750-6758, Oct 2002. URL: https://doi.org/10.1128/mcb.22.19.6750-6758.2002, doi:10.1128/mcb.22.19.6750-6758.2002. This article has 65 citations and is from a domain leading peer-reviewed journal.
(yao2002activationofthe pages 1-1): Sheng Yao and Gregory Prelich. Activation of the bur1-bur2 cyclin-dependent kinase complex by cak1. Molecular and Cellular Biology, 22:6750-6758, Oct 2002. URL: https://doi.org/10.1128/mcb.22.19.6750-6758.2002, doi:10.1128/mcb.22.19.6750-6758.2002. This article has 65 citations and is from a domain leading peer-reviewed journal.
(ostapenko2005phosphorylationbycak1 pages 3-4): Denis Ostapenko and Mark J. Solomon. Phosphorylation by cak1 regulates the c-terminal domain kinase ctk1 in saccharomyces cerevisiae. Molecular and Cellular Biology, 25:3906-3913, May 2005. URL: https://doi.org/10.1128/mcb.25.10.3906-3913.2005, doi:10.1128/mcb.25.10.3906-3913.2005. This article has 37 citations and is from a domain leading peer-reviewed journal.
(ostapenko2005phosphorylationbycak1 pages 4-5): Denis Ostapenko and Mark J. Solomon. Phosphorylation by cak1 regulates the c-terminal domain kinase ctk1 in saccharomyces cerevisiae. Molecular and Cellular Biology, 25:3906-3913, May 2005. URL: https://doi.org/10.1128/mcb.25.10.3906-3913.2005, doi:10.1128/mcb.25.10.3906-3913.2005. This article has 37 citations and is from a domain leading peer-reviewed journal.
(kim2009aphosphorylationindependentrole pages 1-3): Su-Hwa Kim, Keerthi Gadiparthi, Stephen J. Kron, and Ana A. Kitazono. A phosphorylation-independent role for the yeast cyclin-dependent kinase activating kinase cak1. Gene, 447 2:97-105, Nov 2009. URL: https://doi.org/10.1016/j.gene.2009.07.016, doi:10.1016/j.gene.2009.07.016. This article has 3 citations and is from a peer-reviewed journal.
(ostapenko2005phosphorylationbycak1 pages 2-3): Denis Ostapenko and Mark J. Solomon. Phosphorylation by cak1 regulates the c-terminal domain kinase ctk1 in saccharomyces cerevisiae. Molecular and Cellular Biology, 25:3906-3913, May 2005. URL: https://doi.org/10.1128/mcb.25.10.3906-3913.2005, doi:10.1128/mcb.25.10.3906-3913.2005. This article has 37 citations and is from a domain leading peer-reviewed journal.