We have updated our privacy policy. If you have any question, contact us at privacy@scicrunch.org. Dismiss and don't show again

Searching across hundreds of databases

Our searching services are busy right now. Your search will reload in five seconds.

Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

KAP: a dual specificity phosphatase that interacts with cyclin-dependent kinases.

The cyclin-dependent kinases are key cell cycle regulators whose activation is required for passage from one cell cycle phase to the next. In mammalian cells, CDK2 has been implicated in control of the G1 and S phases. We have used a two-hybrid protein interaction screen to identify cDNAs encoding proteins that can interact with CDK2. Among those identified was a protein (KAP), which contained the HCXX-XXGR motif characteristic of protein tyrosine phosphatases. KAP showed phosphatase activity toward substrates containing either phosphotyrosine or phosphoserine residues. Since KAP is not significantly similar to known phosphatases beyond the catalytic core motif, it represents an additional class of dual specificity phosphatase. KAP interacted with cdc2 and CDK2 in yeast. In mammalian cells, KAP also associated with cdc2 and CDK2 but showed a preference for cdc2. The ability of KAP to bind multiple cyclin-dependent kinases suggests that it may play a role in cell cycle regulation.

Pubmed ID: 8127873 RIS Download

Mesh terms: Amino Acid Sequence | Base Sequence | CDC2 Protein Kinase | CDC2-CDC28 Kinases | Cell Cycle Proteins | Cyclin-Dependent Kinase 2 | Cyclin-Dependent Kinase Inhibitor Proteins | Cyclin-Dependent Kinases | DNA, Complementary | Dual-Specificity Phosphatases | Escherichia coli | G1 Phase | HeLa Cells | Humans | Molecular Sequence Data | Phosphoric Monoester Hydrolases | Phosphorylation | Protein Kinases | Protein Tyrosine Phosphatases | Protein-Serine-Threonine Kinases | Recombinant Fusion Proteins | S Phase | Substrate Specificity

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.

We have not found any resources mentioned in this publication.