Cyclin-dependent kinase inhibitor 3 is an enzyme that in humans is encoded by the CDKN3gene.[1][2][3]
The protein encoded by this gene belongs to the dual specificity protein phosphatase family. It was identified as a cyclin-dependent kinase inhibitor, and has been shown to interact with, and dephosphorylate CDK2 kinase, thus prevent the activation of CDK2 kinase. This gene was reported to be deleted, mutated, or overexpressed in several kinds of cancers.[3]
↑ 1.01.1Gyuris J, Golemis E, Chertkov H, Brent R (Dec 1993). "Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2". Cell. 75 (4): 791–803. doi:10.1016/0092-8674(93)90498-F. PMID8242750.
↑Demetrick DJ, Matsumoto S, Hannon GJ, Okamoto K, Xiong Y, Zhang H, Beach DH (May 1995). "Chromosomal mapping of the genes for the human cell cycle proteins cyclin C (CCNC), cyclin E (CCNE), p21 (CDKN1) and KAP (CDKN3)". Cytogenet Cell Genet. 69 (3–4): 190–2. doi:10.1159/000133960. PMID7698009.
↑Yeh, Chau-Ting; Lu Su-Chuan; Chao Chung-Hao; Chao Mei-Ling (May 2003). "Abolishment of the interaction between cyclin-dependent kinase 2 and Cdk-associated protein phosphatase by a truncated KAP mutant". Biochem. Biophys. Res. Commun. United States. 305 (2): 311–4. doi:10.1016/S0006-291X(03)00757-5. ISSN0006-291X. PMID12745075.
↑Harper, J W; Adami G R; Wei N; Keyomarsi K; Elledge S J (Nov 1993). "The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases". Cell. UNITED STATES. 75 (4): 805–16. doi:10.1016/0092-8674(93)90499-G. ISSN0092-8674. PMID8242751.
Harper JW, Adami GR, Wei N, et al. (1993). "The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases". Cell. 75 (4): 805–16. doi:10.1016/0092-8674(93)90499-G. PMID8242751.
Sexl V, Diehl JA, Sherr CJ, et al. (1999). "A rate limiting function of cdc25A for S phase entry inversely correlates with tyrosine dephosphorylation of Cdk2". Oncogene. 18 (3): 573–82. doi:10.1038/sj.onc.1202362. PMID9989807.
Yeh CT, Lu SC, Chen TC, et al. (2000). "Aberrant transcripts of the cyclin-dependent kinase-associated protein phosphatase in hepatocellular carcinoma". Cancer Res. 60 (17): 4697–700. PMID10987270.
Song H, Hanlon N, Brown NR, et al. (2001). "Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2". Mol. Cell. 7 (3): 615–26. doi:10.1016/S1097-2765(01)00208-8. PMID11463386.
Wang H, Iakova P, Wilde M, et al. (2001). "C/EBPalpha arrests cell proliferation through direct inhibition of Cdk2 and Cdk4". Mol. Cell. 8 (4): 817–28. doi:10.1016/S1097-2765(01)00366-5. PMID11684017.
Yeh CT, Lu SC, Chao CH, Chao ML (2003). "Abolishment of the interaction between cyclin-dependent kinase 2 and Cdk-associated protein phosphatase by a truncated KAP mutant". Biochem. Biophys. Res. Commun. 305 (2): 311–4. doi:10.1016/S0006-291X(03)00757-5. PMID12745075.
Chinami M, Yano Y, Yang X, et al. (2005). "Binding of HTm4 to cyclin-dependent kinase (Cdk)-associated phosphatase (KAP).Cdk2.cyclin A complex enhances the phosphatase activity of KAP, dissociates cyclin A, and facilitates KAP dephosphorylation of Cdk2". J. Biol. Chem. 280 (17): 17235–42. doi:10.1074/jbc.M413437200. PMID15671017.
Hsieh MJ, Yao YL, Lai IL, Yang WM (2006). "Transcriptional repression activity of PAX3 is modulated by competition between corepressor KAP1 and heterochromatin protein 1". Biochem. Biophys. Res. Commun. 349 (2): 573–81. doi:10.1016/j.bbrc.2006.08.064. PMID16945326.
Okamoto K, Kitabayashi I, Taya Y (2006). "KAP1 dictates p53 response induced by chemotherapeutic agents via Mdm2 interaction". Biochem. Biophys. Res. Commun. 351 (1): 216–22. doi:10.1016/j.bbrc.2006.10.022. PMID17056014.