Cyclin-dependent kinase 3

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
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View/Edit Human

Cell division protein kinase 3 is an enzyme that in humans is encoded by the CDK3 gene.[1][2]

Function

CDK3 complements cdc28 mutants of Saccharomyces cerevisiae suggesting that it may be involved in cell cycle control. CDK3 can phosphorylate histone H1 and interacts with an unknown type of cyclin.[2]

References

  1. Meyerson M, Enders GH, Wu CL, Su LK, Gorka C, Nelson C, Harlow E, Tsai LH (Aug 1992). "A family of human cdc2-related protein kinases". EMBO J. 11 (8): 2909–17. PMC 556772. PMID 1639063.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  2. 2.0 2.1 "Entrez Gene: CDK3 cyclin-dependent kinase 3".<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>

Further reading

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  • Bullrich F, MacLachlan TK, Sang N, et al. (1995). "Chromosomal mapping of members of the cdc2 family of protein kinases, cdk3, cdk6, PISSLRE, and PITALRE, and a cdk inhibitor, p27Kip1, to regions involved in human cancer". Cancer Res. 55 (6): 1199–205. PMID 7882308.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • Gyuris J, Golemis E, Chertkov H, Brent R (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. PMID 8242750.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • Sasaguri T, Ishida A, Kosaka C, et al. (1996). "Phorbol ester inhibits the phosphorylation of the retinoblastoma protein without suppressing cyclin D-associated kinase in vascular smooth muscle cells". J. Biol. Chem. 271 (14): 8345–51. doi:10.1074/jbc.271.14.8345. PMID 8626531.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • Meikrantz W, Schlegel R (1996). "Suppression of apoptosis by dominant negative mutants of cyclin-dependent protein kinases". J. Biol. Chem. 271 (17): 10205–9. doi:10.1074/jbc.271.17.10205. PMID 8626584.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • Hofmann F, Livingston DM (1996). "Differential effects of cdk2 and cdk3 on the control of pRb and E2F function during G1 exit". Genes Dev. 10 (7): 851–61. doi:10.1101/gad.10.7.851. PMID 8846921.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • Lamphere L, Fiore F, Xu X, et al. (1997). "Interaction between Cdc37 and Cdk4 in human cells". Oncogene. 14 (16): 1999–2004. doi:10.1038/sj.onc.1201036. PMID 9150368.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • Braun K, Hölzl G, Soucek T, et al. (1998). "Investigation of the cell cycle regulation of cdk3-associated kinase activity and the role of cdk3 in proliferation and transformation". Oncogene. 17 (17): 2259–69. doi:10.1038/sj.onc.1202145. PMID 9811456.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • Yamochi T, Semba K, Tsuji K, et al. (2002). "ik3-1/Cables is a substrate for cyclin-dependent kinase 3 (cdk 3)". Eur. J. Biochem. 268 (23): 6076–82. doi:10.1046/j.0014-2956.2001.02555.x. PMID 11733001.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • Sato H, Nishimoto I, Matsuoka M (2002). "ik3-2, a relative to ik3-1/cables, is associated with cdk3, cdk5, and c-abl". Biochim. Biophys. Acta. 1574 (2): 157–63. doi:10.1016/S0167-4781(01)00367-0. PMID 11955625.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • Schang LM, Bantly A, Schaffer PA (2002). "Explant-induced reactivation of herpes simplex virus occurs in neurons expressing nuclear cdk2 and cdk4". J. Virol. 76 (15): 7724–35. doi:10.1128/JVI.76.15.7724-7735.2002. PMC 136347. PMID 12097586.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • Ren S, Rollins BJ (2004). "Cyclin C/cdk3 promotes Rb-dependent G0 exit". Cell. 117 (2): 239–51. doi:10.1016/S0092-8674(04)00300-9. PMID 15084261.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • Zhang Y, Wolf-Yadlin A, Ross PL, et al. (2005). "Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules". Mol. Cell. Proteomics. 4 (9): 1240–50. doi:10.1074/mcp.M500089-MCP200. PMID 15951569.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • Beausoleil SA, Villén J, Gerber SA, et al. (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • Wissing J, Jänsch L, Nimtz M, et al. (2007). "Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry". Mol. Cell. Proteomics. 6 (3): 537–47. doi:10.1074/mcp.T600062-MCP200. PMID 17192257.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>

External links