![]() In addition, these studies showed that the catalytic subunit, the CDK, must associate with a regulatory subunit, the cyclin, whose protein levels are subject to regulation during the cell cycle (this oscillation lent these regulators their cyclin name). This work established the importance of CDKs in promoting transitions through the cell cycle. ĬDKs were first discovered by genetic and biochemical studies in model organisms such as yeasts and frogs (reviewed in ). To aid nomenclature and analysis of CDKs, proteins belonging to this family have been recently renamed as Cdk1 through to Cdk20. In related kinases such as MAPKs, substrate specificity is conferred by docking sites separated from the catalytic site, whereas CDKs are characterized by dependency on separate protein subunits that provide additional sequences required for enzymatic activity. Based on the sequence of the kinase domain, CDKs belong to the CMGC group of kinases (named for the initials of some members), along with mitogen-activated protein kinases (MAPKs), glycogen synthase kinase-3 beta (Gsk3β), members of the dual-specificity tyrosine-regulated kinase (DYRK) family and CDK-like kinases. Not surprisingly, deregulation of this family of proteins is a hallmark of several diseases, including cancer, and drug-targeted inhibition of specific members has generated very encouraging results in clinical trials.Ĭyclin-dependent kinases (CDKs) are serine/threonine kinases whose activity depends on a regulatory subunit - a cyclin. This review summarizes how, although CDKs are traditionally separated into cell-cycle or transcriptional CDKs, these activities are frequently combined in many family members. Unlike the prototypical Cdc28 kinase of budding yeast, most of these CDKs bind one or a few cyclins, consistent with functional specialization during evolution. The evolutionary expansion of the CDK family in mammals led to the division of CDKs into three cell-cycle-related subfamilies (Cdk1, Cdk4 and Cdk5) and five transcriptional subfamilies (Cdk7, Cdk8, Cdk9, Cdk11 and Cdk20). CDKs play important roles in the control of cell division and modulate transcription in response to several extra- and intracellular cues. You can find data in Pfam in various ways.Cyclin-dependent kinases (CDKs) are protein kinases characterized by needing a separate subunit - a cyclin - that provides domains essential for enzymatic activity. all UniProt and NCBI GI) or different levels of redundancy. Pfam full alignments are available from searching a variety of databases, either to provide different accessions (e.g. The data presented for each entry is based on the UniProt Reference Proteomes but information on individual UniProtKB sequences can still be found by entering the protein accession. A clan is a collection of Pfam entries which are related by similarity of sequence, structure or profile-HMM. Pfam also generates higher-level groupings of related entries, known as clans. The identification of domains that occur within proteins can therefore provide insights into their function. Different combinations of domains give rise to the diverse range of proteins found in nature. Proteins are generally composed of one or more functional regions, commonly termed domains. The Pfam database is a large collection of protein families, each represented by multiple sequence alignments and hidden Markov models (HMMs).
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