Cyclin-dependent kinase 3: Difference between revisions

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Latest revision as of 17:59, 30 August 2017

Lua error in Module:Redirect at line 65: could not parse redirect on page "CDK3".

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

↑ 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.
↑ ^2.0 ^2.1 "Entrez Gene: CDK3 cyclin-dependent kinase 3".

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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.

External links

CDK3+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
CDK3 human gene location in the UCSC Genome Browser.
CDK3 human gene details in the UCSC Genome Browser.

This EC 2.7 enzyme-related article is a stub. You can help Wikipedia by expanding it.

[pmid1639063-1] 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.

[entrez-2] 2.0 ^2.1 "Entrez Gene: CDK3 cyclin-dependent kinase 3".

[1]

[2]

@@ Line 1: / Line 1: @@
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+{{Redirect|CDK3|the IATA airport code|Dorset/Kawagama Lake (South) Water Aerodrome}}
--->{{PBB_Controls
+{{Infobox_gene}}
-| update_page = yes
+'''Cell division protein kinase 3''' is an [[enzyme]] that in humans is encoded by the ''CDK3'' [[gene]].<ref name="pmid1639063">{{cite journal | vauthors = Meyerson M, Enders GH, Wu CL, Su LK, Gorka C, Nelson C, Harlow E, Tsai LH | title = A family of human cdc2-related protein kinases | journal = EMBO J | volume = 11 | issue = 8 | pages = 2909–17 |date=Aug 1992 | pmid = 1639063 | pmc = 556772 | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CDK3 cyclin-dependent kinase 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1018| accessdate = }}</ref>
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-{{GNF_Protein_box
- | image =
- | image_source =
- | PDB =
- | Name = Cyclin-dependent kinase 3
- | HGNCid = 1772
- | Symbol = CDK3
- | AltSymbols =;
- | OMIM = 123828
- | ECnumber =
- | Homologene = 74387
- | MGIid =
- | GeneAtlas_image1 = PBB_GE_CDK3_207188_at_tn.png
-  | GeneAtlas_image2 = PBB_GE_CDK3_gnf1h09546_at_tn.png
- | Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004693 |text = cyclin-dependent protein kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
- | Component =
- | Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007067 |text = mitosis}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0051301 |text = cell division}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 1018
-    | Hs_Ensembl = ENSG00000108504
-    | Hs_RefseqProtein = NP_001249
-    | Hs_RefseqmRNA = NM_001258
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 17
-    | Hs_GenLoc_start = 71486907
-    | Hs_GenLoc_end = 71513673
-    | Hs_Uniprot = Q00526
-    | Mm_EntrezGene =
-    | Mm_Ensembl =
-    | Mm_RefseqmRNA =
-    | Mm_RefseqProtein =
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-    | Mm_GenLoc_chr =
-    | Mm_GenLoc_start =
-    | Mm_GenLoc_end =
-    | Mm_Uniprot =
-  }}
-}}
-{{CMG}}
+== 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]].<ref name="entrez"/>
-'''Cyclin-dependent kinase 3''', also known as '''CDK3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CDK3 cyclin-dependent kinase 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1018| accessdate = }}</ref>
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
-{{PBB_Summary
-| section_title =
-| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: CDK3 cyclin-dependent kinase 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1018| accessdate = }}</ref>
-}}
 ==References==
 {{reflist}}
 ==Further reading==
-{{refbegin | 2}}
+{{refbegin|35em}}
-{{PBB_Further_reading
+*{{cite journal  | vauthors=Bullrich F, MacLachlan TK, Sang N |title=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. |journal=Cancer Res. |volume=55 |issue= 6 |pages= 1199–205 |year= 1995 |pmid= 7882308 |doi=  |display-authors=etal}}
-| citations =
+*{{cite journal  | vauthors=Gyuris J, Golemis E, Chertkov H, Brent R |title=Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2. |journal=Cell |volume=75 |issue= 4 |pages= 791–803 |year= 1993 |pmid= 8242750 |doi=10.1016/0092-8674(93)90498-F  }}
-*{{cite journal  | author=Meyerson M, Enders GH, Wu CL, ''et al.'' |title=A family of human cdc2-related protein kinases. |journal=EMBO J. |volume=11 |issue= 8 |pages= 2909-17 |year= 1992 |pmid= 1639063 |doi=  }}
+*{{cite journal  | vauthors=Sasaguri T, Ishida A, Kosaka C |title=Phorbol ester inhibits the phosphorylation of the retinoblastoma protein without suppressing cyclin D-associated kinase in vascular smooth muscle cells. |journal=J. Biol. Chem. |volume=271 |issue= 14 |pages= 8345–51 |year= 1996 |pmid= 8626531 |doi=10.1074/jbc.271.14.8345  |display-authors=etal}}
-*{{cite journal  | author=Bullrich F, MacLachlan TK, Sang N, ''et al.'' |title=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. |journal=Cancer Res. |volume=55 |issue= 6 |pages= 1199-205 |year= 1995 |pmid= 7882308 |doi=  }}
+*{{cite journal  | vauthors=Meikrantz W, Schlegel R |title=Suppression of apoptosis by dominant negative mutants of cyclin-dependent protein kinases. |journal=J. Biol. Chem. |volume=271 |issue= 17 |pages= 10205–9 |year= 1996 |pmid= 8626584 |doi=10.1074/jbc.271.17.10205  }}
-*{{cite journal  | author=Gyuris J, Golemis E, Chertkov H, Brent R |title=Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2. |journal=Cell |volume=75 |issue= 4 |pages= 791-803 |year= 1993 |pmid= 8242750 |doi=  }}
+*{{cite journal  | vauthors=Hofmann F, Livingston DM |title=Differential effects of cdk2 and cdk3 on the control of pRb and E2F function during G1 exit. |journal=Genes Dev. |volume=10 |issue= 7 |pages= 851–61 |year= 1996 |pmid= 8846921 |doi=10.1101/gad.10.7.851  }}
-*{{cite journal  | author=Sasaguri T, Ishida A, Kosaka C, ''et al.'' |title=Phorbol ester inhibits the phosphorylation of the retinoblastoma protein without suppressing cyclin D-associated kinase in vascular smooth muscle cells. |journal=J. Biol. Chem. |volume=271 |issue= 14 |pages= 8345-51 |year= 1996 |pmid= 8626531 |doi=  }}
+*{{cite journal  | vauthors=Lamphere L, Fiore F, Xu X |title=Interaction between Cdc37 and Cdk4 in human cells. |journal=Oncogene |volume=14 |issue= 16 |pages= 1999–2004 |year= 1997 |pmid= 9150368 |doi= 10.1038/sj.onc.1201036 |display-authors=etal}}
-*{{cite journal  | author=Meikrantz W, Schlegel R |title=Suppression of apoptosis by dominant negative mutants of cyclin-dependent protein kinases. |journal=J. Biol. Chem. |volume=271 |issue= 17 |pages= 10205-9 |year= 1996 |pmid= 8626584 |doi=  }}
+*{{cite journal  | vauthors=Braun K, Hölzl G, Soucek T |title=Investigation of the cell cycle regulation of cdk3-associated kinase activity and the role of cdk3 in proliferation and transformation. |journal=Oncogene |volume=17 |issue= 17 |pages= 2259–69 |year= 1998 |pmid= 9811456 |doi= 10.1038/sj.onc.1202145 |display-authors=etal}}
-*{{cite journal  | author=Hofmann F, Livingston DM |title=Differential effects of cdk2 and cdk3 on the control of pRb and E2F function during G1 exit. |journal=Genes Dev. |volume=10 |issue= 7 |pages= 851-61 |year= 1996 |pmid= 8846921 |doi=  }}
+*{{cite journal  | vauthors=Yamochi T, Semba K, Tsuji K |title=ik3-1/Cables is a substrate for cyclin-dependent kinase 3 (cdk 3). |journal=Eur. J. Biochem. |volume=268 |issue= 23 |pages= 6076–82 |year= 2002 |pmid= 11733001 |doi=10.1046/j.0014-2956.2001.02555.x  |display-authors=etal}}
-*{{cite journal  | author=Lamphere L, Fiore F, Xu X, ''et al.'' |title=Interaction between Cdc37 and Cdk4 in human cells. |journal=Oncogene |volume=14 |issue= 16 |pages= 1999-2004 |year= 1997 |pmid= 9150368 |doi= 10.1038/sj.onc.1201036 }}
+*{{cite journal  | vauthors=Sato H, Nishimoto I, Matsuoka M |title=ik3-2, a relative to ik3-1/cables, is associated with cdk3, cdk5, and c-abl. |journal=Biochim. Biophys. Acta |volume=1574 |issue= 2 |pages= 157–63 |year= 2002 |pmid= 11955625 |doi=10.1016/S0167-4781(01)00367-0  }}
-*{{cite journal  | author=Braun K, Hölzl G, Soucek T, ''et al.'' |title=Investigation of the cell cycle regulation of cdk3-associated kinase activity and the role of cdk3 in proliferation and transformation. |journal=Oncogene |volume=17 |issue= 17 |pages= 2259-69 |year= 1998 |pmid= 9811456 |doi= 10.1038/sj.onc.1202145 }}
+*{{cite journal  | vauthors=Schang LM, Bantly A, Schaffer PA |title=Explant-induced reactivation of herpes simplex virus occurs in neurons expressing nuclear cdk2 and cdk4 |journal=J. Virol. |volume=76 |issue= 15 |pages= 7724–35 |year= 2002 |pmid= 12097586 |doi=10.1128/JVI.76.15.7724-7735.2002  | pmc=136347  }}
-*{{cite journal  | author=Yamochi T, Semba K, Tsuji K, ''et al.'' |title=ik3-1/Cables is a substrate for cyclin-dependent kinase 3 (cdk 3). |journal=Eur. J. Biochem. |volume=268 |issue= 23 |pages= 6076-82 |year= 2002 |pmid= 11733001 |doi=  }}
+*{{cite journal  | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
-*{{cite journal  | author=Sato H, Nishimoto I, Matsuoka M |title=ik3-2, a relative to ik3-1/cables, is associated with cdk3, cdk5, and c-abl. |journal=Biochim. Biophys. Acta |volume=1574 |issue= 2 |pages= 157-63 |year= 2002 |pmid= 11955625 |doi=  }}
+*{{cite journal  | vauthors=Ren S, Rollins BJ |title=Cyclin C/cdk3 promotes Rb-dependent G0 exit |journal=Cell |volume=117 |issue= 2 |pages= 239–51 |year= 2004 |pmid= 15084261 |doi=10.1016/S0092-8674(04)00300-9  }}
-*{{cite journal  | author=Schang LM, Bantly A, Schaffer PA |title=Explant-induced reactivation of herpes simplex virus occurs in neurons expressing nuclear cdk2 and cdk4. |journal=J. Virol. |volume=76 |issue= 15 |pages= 7724-35 |year= 2002 |pmid= 12097586 |doi=  }}
+*{{cite journal  | vauthors=Zhang Y, Wolf-Yadlin A, Ross PL |title=Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules |journal=Mol. Cell. Proteomics |volume=4 |issue= 9 |pages= 1240–50 |year= 2005 |pmid= 15951569 |doi= 10.1074/mcp.M500089-MCP200 |display-authors=etal}}
-*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
+*{{cite journal  | vauthors=Beausoleil SA, Villén J, Gerber SA |title=A probability-based approach for high-throughput protein phosphorylation analysis and site localization |journal=Nat. Biotechnol. |volume=24 |issue= 10 |pages= 1285–92 |year= 2006 |pmid= 16964243 |doi= 10.1038/nbt1240 |display-authors=etal}}
-*{{cite journal  | author=Ren S, Rollins BJ |title=Cyclin C/cdk3 promotes Rb-dependent G0 exit. |journal=Cell |volume=117 |issue= 2 |pages= 239-51 |year= 2004 |pmid= 15084261 |doi=  }}
+*{{cite journal  | vauthors=Olsen JV, Blagoev B, Gnad F |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks |journal=Cell |volume=127 |issue= 3 |pages= 635–48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 |display-authors=etal}}
-*{{cite journal  | author=Zhang Y, Wolf-Yadlin A, Ross PL, ''et al.'' |title=Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. |journal=Mol. Cell Proteomics |volume=4 |issue= 9 |pages= 1240-50 |year= 2005 |pmid= 15951569 |doi= 10.1074/mcp.M500089-MCP200 }}
+*{{cite journal  | vauthors=Wissing J, Jänsch L, Nimtz M |title=Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry |journal=Mol. Cell. Proteomics |volume=6 |issue= 3 |pages= 537–47 |year= 2007 |pmid= 17192257 |doi= 10.1074/mcp.T600062-MCP200 |display-authors=etal}}
-*{{cite journal  | author=Beausoleil SA, Villén J, Gerber SA, ''et al.'' |title=A probability-based approach for high-throughput protein phosphorylation analysis and site localization. |journal=Nat. Biotechnol. |volume=24 |issue= 10 |pages= 1285-92 |year= 2006 |pmid= 16964243 |doi= 10.1038/nbt1240 }}
-*{{cite journal  | author=Olsen JV, Blagoev B, Gnad F, ''et al.'' |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. |journal=Cell |volume=127 |issue= 3 |pages= 635-48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 }}
-*{{cite journal  | author=Wissing J, Jänsch L, Nimtz M, ''et al.'' |title=Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. |journal=Mol. Cell Proteomics |volume=6 |issue= 3 |pages= 537-47 |year= 2007 |pmid= 17192257 |doi= 10.1074/mcp.T600062-MCP200 }}
-}}
 {{refend}}
 ==External links==
 * {{MeshName|CDK3+protein,+human}}
+* {{UCSC genome browser|CDK3}}
+* {{UCSC gene details|CDK3}}
-{{Enzyme-stub}}
 {{Cell cycle proteins}}
+{{Serine/threonine-specific protein kinases}}
+{{Enzymes}}
+{{Portal bar|Molecular and Cellular Biology|border=no}}
+{{DEFAULTSORT:Cyclin-dependent kinase 03}}
 [[Category:Cell cycle]]
+[[Category:Proteins]]
+[[Category:EC 2.7.11]]
-{{WH}}
+{{2.7-enzyme-stub}}
-{{WS}}

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

Cyclin-dependent kinase 3: Difference between revisions

Latest revision as of 17:59, 30 August 2017

Contents

Function

References

Further reading

External links

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