Contents 1 Structure 2 Function 2.1 Cell cycle 2.2 Cellular development 2.3 DNA protection 2.4 Metabolic homeostasis 2.5 Centrosome stability 3 Mechanisms of regulation 4 Clinical relevance 4.1 Cancer 4.2 Medulloblastoma 4.3 As a drug target 4.4 Interactions 5 See also 6 References 7 Further reading 8 External links


Structure[edit] The CDK6 gene is conserved in eukaryotes, including the budding yeast and the nematode Caenorhabditis elegans.[11] The CDK6 gene is located on chromosome 7 in humans. The gene spans 231,706 base pairs and encodes a 326 amino acid protein with a kinase function.[6] The gene is overexpressed in cancers like lymphoma, leukemia, medulloblastoma and melanoma associated with chromosomal rearrangements.[6] The CDK6 protein contains a catalytic core composed of a serine/threonine domain.[12] This protein also contains an ATP-binding pocket, inhibitory and activating phosphorylation sites, a PSTAIRE-like cyclin-binding domain and an activating T-loop motif.[10] After binding the Cyclin in the PSTAIRE helix, the protein changes its conformational structure to expose the phosphorylation motif.[10] The protein can be found in the cytoplasm and the nucleus, however most of the active complexes are found in the nucleus of proliferating cells.[10]


Function[edit] Cell cycle[edit] In 1994, Matthew Meyerson and Ed Harlow investigated the product of a close analogous gene of CDK4.[7] This gene, identified as PLSTIRE was translated into a protein that interacted with the cyclins CD1, CD2 and CD3 (same as CDK4), but that was different from CDK4; the protein was then renamed CDK6 for simplicity.[7] In mammalian cells, cell cycle is activated by CDK6 in the early G1 phase[13] through interactions with cyclins D1, D2 and D3.[7] There are many changes in gene expression that are regulated through this enzyme.[14] After the complex is formed, the C-CDK6 enzymatic complex phosphorylates the protein pRb.[15] After its phosphorylation, pRb releases its binding partner E2F, a transcriptional activator, which in turn activates DNA replication.[16] The CDK6 complex ensures a point of switch to commit to division responding to external signals, like mitogens and growth factors.[17] CDK6 is involved in a positive feedback loop that activates transcription factors through a reaction cascade.[18] Importantly, these C-CDK complexes act as a kinase, phosphorylating and inactivating the protein of Rb and p-Rb related “pocket proteins” p107 and p130.[19] While doing this, the CDK6 in conjunction with CDK4, act as a switch signal that first appears in G1,[7] directing the cell towards S phase of the cell cycle.[14] CDK6 is important for the control of G1 to S phase transition.[7] However, in recent years, new evidence proved that the presence of CDK6 is not essential for proliferation in every cell type,[20] the cell cycle has a complex circuitry of regulation and the role of CDK6 might be more important in certain cell types than in others, where CDK4 or CDK2 can act as protein kinases compensating its role.[20][21] Cellular development[edit] In mutant Knockout mice of CDK6, the hematopoietic function is impaired, regardless of otherwise organism normal development.[20] This might hint additional roles of CDK6 in the development of blood components.[20] There are additional functions of CDK6 not associated with its kinase activity.[22] For example, CDK6 is involved in the differentiation of T cells, acting as an inhibitor of differentiation.[22] Even though CDK6 and CDK4 share 71% amino acid identity, this role in differentiation is unique to CDK6.[22] CDK6 has also been found to be important in the development of other cell lines, for example, CDK6 has a role in the alteration of the morphology of astrocytes[23] and in the development of other stem cells.[10][16] DNA protection[edit] CDK6 differs from CDK4 in other important roles.[24] For example, CDK6 plays a role in the accumulation of the apoptosis proteins p53 and p130, this accumulation keeps cells from entering cell division if there is DNA damage, activating pro- apoptotic pathways.[24] Metabolic homeostasis[edit] Studies in the metabolic control of cells have revealed yet another role of CDK6.[25] This new role is associated with the balance of the oxidative and non-oxidative branches of the pentose pathway in cells.[25] This pathway is a known route altered in cancer cells, when there is an aberrant overexpression of CDK6 and CDK4.[25] The overepression of these proteins provides the cancer cells with a new hallmark capability of cancer; the deregulation of the cell metabolism.[25] Centrosome stability[edit] In 2013 researches discovered yet another role of CDK6.[26] There is evidence that CDK6 associates with the centrosome and controls organized division and cell cycle phases in neuron production.[26] When the CDK6 gene is mutated in these developing lines, the centrosomes are not properly divided, this could lead to division problems such as aneuploidy, which in turns leads to health issues like primary microcephaly.[26]


Mechanisms of regulation[edit] CDK6 is positively regulated primarily by its union to the D cyclins D1,D2 and D3. If this subunit of the complex is not available, CDK6 is not active or available to phosphorylate the pRb substrate.[9] An additional positive activator needed by CDK6 is the phosphorylation in a conserved threonine residue located in 177 position, this phosphorylation is done by the cdk-activating kinases, CAK.[27] Additionally, CDK6 can be phosphorylated and activated by the Kaposi's sarcoma-associated herpes virus, stimulating the CDK6 over activation and uncontrolled cell proliferation.[28] CDK6 is negatively regulated by binding to certain inhibitors that can be classified in two groups;[29] CKIs or CIP/KIP family members like the protein p21[16] and p27 act blocking and inhibiting the assembled C-CDKs binding complex enzymes[27] in their catalytic domain.[30] Furthermore, inhibitors of the INK4 family members like p15, p16, p18 and p19 inhibit the monomer of CDK6, preventing the complex formation.[19][31]


Clinical relevance[edit] CDK6 is a protein kinase activating cell proliferation, it is involved in an important point of restriction in the cell cycle.[18] For this reason, CDK6 and other regulators of the G1 phase of the cell cycle are known to be unbalanced in more than 80-90% of tumors.[9] In cervical cancer cells, CDK6 function has been shown to be altered indirectly by the p16 inhibitor.[31] CDK6 is also overexpressed in tumors that exhibit drug resistance, for example glioma malignancies exhibit resistance to chemotherapy using temozolomide (TMZ) when they have a mutation overexpressing CDK6.[32] Likewise, the overexpression of CDK6 is also associated with resistance to hormone therapy using the anti oestrogen Fluvestrant in breast cancer.[33] Cancer[edit] Loss of normal cell cycle control is the first step to developing different hallmarks of cancer; alterations of CDK6 can directly or indirectly affect the following hallmarks; disregulated cell cellular energetics, sustaining of proliferative signaling, evading growth suppressors and inducing angiogenesis,[9] for example, deregulation of CDK6 has been shown to be important in lymphoid malignancies by increasing angiogenesis, a hallmark of cancer.[19] These features are reached through upregulation of CDK6 due to chromosome alterations or epigenetic dysregulations.[9] Additionally, CDK6 might be altered through genomic instability, a mechanism of downregulation of tumor suppressor genes; this represents another evolving hallmark of cancer.[34] Medulloblastoma[edit] Medulloblastoma is the most common cause of brain cancer in children.[35] About a third of these cancers have upregulated CDK6, representing a marker for poor prognosis for this disease.[35] Since it is so common for these cells to have alterations in CDK6, researchers are seeking for ways to downregulate CDK6 expression acting specifically in those cell lines. The MicroRNA (miR) -124 has successfully controlled cancer progression in an in-vitro setting for medulloblastoma and glioblastoma cells.[35] Furthermore, researchers have found that it successfully reduces the growth of xenograft tumors in rat models.[35] As a drug target[edit] Further information: CDK inhibitor Palbociclib and Ribociclib are FDA approved inhibitors of CDK4 and CDK6. Ribociclib is approved in combination with letrozole for treatment of breast cancer in patients with an hormone receptor positive, HER2 negative advanced metastatic breast cancer.[36] A phase three clinical trial found that Ribocyclib administered in combination with letrozole increased the likelihood of progression free survival to 63% in the first 18 months of therapy versus 42% for letrozole alone.[37] Subsequent analysis demonstrated that patients treated with Ribociclib and letrozole showed a median progression-free survival of 25.3 months.[36] Inhibitors of CDK6 have shown the disadvantage of having low specificity for CDK6 over other CDKs, and as a consequence they might act inhibiting other CDKs that are crucial in other tissues and at other points of cell cycle.[38] The compound PD-0332991, is currently under more than 20 clinical trials acting either as single agent or as coadjuvant of other therapies in clinical trial phase I-III showing promising results in the control of breast cancer in-vitro.[39] The direct targeting of CDK6 and CDK4 should be used with caution in the treatment of cancer, because these enzymes are important for the cell cycle of normal cells as well.[35] Furthermore, small molecules targeting these proteins might increase drug resistance events.[35] However, these kinases have been shown to be useful as coadjuvants in breast cancer chemotherapy.[40] Another indirect mechanism for the control of CDK6 expression, is the use of a mutated D-cyclin that binds with high affinity to CDK6, but does not induce its kinase activity.[40] this mechanism was studied in the development of mammary tumorigenesis in rat cells, however, the clinical effects have not yet been shown in human patients.[40] A Interactions[edit] Cyclin-dependent kinase 6 interacts with: CDKN2C,[41][42][43] Cyclin D1,[44][45] Cyclin D3,[44][46] P16,[47][48][49] PPM1B,[50] and PPP2CA.[50]


See also[edit] Cell cycle, Mitosis, CDK, CDK4, Hallmarks of cancer Genecards Uniprot NCI


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Further reading[edit] Adams MD, Kerlavage AR, Fleischmann RD, Fuldner RA, Bult CJ, Lee NH, Kirkness EF, Weinstock KG, Gocayne JD, White O (Sep 1995). "Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence" (PDF). Nature. 377 (6547 Suppl): 3–174. PMID 7566098.  Aprelikova O, Xiong Y, Liu ET (Aug 1995). "Both p16 and p21 families of cyclin-dependent kinase (CDK) inhibitors block the phosphorylation of cyclin-dependent kinases by the CDK-activating kinase". The Journal of Biological Chemistry. 270 (31): 18195–7. doi:10.1074/jbc.270.31.18195. PMID 7629134.  Lucas JJ, Szepesi A, Modiano JF, Domenico J, Gelfand EW (Jun 1995). "Regulation of synthesis and activity of the PLSTIRE protein (cyclin-dependent kinase 6 (cdk6)), a major cyclin D-associated cdk4 homologue in normal human T lymphocytes". Journal of Immunology. 154 (12): 6275–84. PMID 7759865.  Bullrich F, MacLachlan TK, Sang N, Druck T, Veronese ML, Allen SL, Chiorazzi N, Koff A, Heubner K, Croce CM (Mar 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 Research. 55 (6): 1199–205. PMID 7882308.  Guan KL, Jenkins CW, Li Y, Nichols MA, Wu X, O'Keefe CL, Matera AG, Xiong Y (Dec 1994). "Growth suppression by p18, a p16INK4/MTS1- and p14INK4B/MTS2-related CDK6 inhibitor, correlates with wild-type pRb function". Genes & Development. 8 (24): 2939–52. doi:10.1101/gad.8.24.2939. PMID 8001816.  Meyerson M, Harlow E (Mar 1994). "Identification of G1 kinase activity for cdk6, a novel cyclin D partner". Molecular and Cellular Biology. 14 (3): 2077–86. PMC 358568 . PMID 8114739.  Fåhraeus R, Paramio JM, Ball KL, Laín S, Lane DP (Jan 1996). "Inhibition of pRb phosphorylation and cell-cycle progression by a 20-residue peptide derived from p16CDKN2/INK4A". Current Biology. 6 (1): 84–91. doi:10.1016/S0960-9822(02)00425-6. PMID 8805225.  Bonaldo MF, Lennon G, Soares MB (Sep 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.  Lamphere L, Fiore F, Xu X, Brizuela L, Keezer S, Sardet C, Draetta GF, Gyuris J (Apr 1997). "Interaction between Cdc37 and Cdk4 in human cells". Oncogene. 14 (16): 1999–2004. doi:10.1038/sj.onc.1201036. PMID 9150368.  Nagasawa M, Melamed I, Kupfer A, Gelfand EW, Lucas JJ (Jun 1997). "Rapid nuclear translocation and increased activity of cyclin-dependent kinase 6 after T cell activation". Journal of Immunology. 158 (11): 5146–54. PMID 9164930.  Ezhevsky SA, Nagahara H, Vocero-Akbani AM, Gius DR, Wei MC, Dowdy SF (Sep 1997). "Hypo-phosphorylation of the retinoblastoma protein (pRb) by cyclin D:Cdk4/6 complexes results in active pRb". Proceedings of the National Academy of Sciences of the United States of America. 94 (20): 10699–704. doi:10.1073/pnas.94.20.10699. PMC 23451 . PMID 9380698.  Fåhraeus R, Laín S, Ball KL, Lane DP (Feb 1998). "Characterization of the cyclin-dependent kinase inhibitory domain of the INK4 family as a model for a synthetic tumour suppressor molecule". Oncogene. 16 (5): 587–96. doi:10.1038/sj.onc.1201580. PMID 9482104.  Gonzales AJ, Goldsworthy TL, Fox TR (Jun 1998). "Chemical transformation of mouse liver cells results in altered cyclin D-CDK protein complexes". Carcinogenesis. 19 (6): 1093–102. doi:10.1093/carcin/19.6.1093. PMID 9667749.  Russo AA, Tong L, Lee JO, Jeffrey PD, Pavletich NP (Sep 1998). "Structural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4a". Nature. 395 (6699): 237–43. doi:10.1038/26155. PMID 9751050.  Brotherton DH, Dhanaraj V, Wick S, Brizuela L, Domaille PJ, Volyanik E, Xu X, Parisini E, Smith BO, Archer SJ, Serrano M, Brenner SL, Blundell TL, Laue ED (Sep 1998). "Crystal structure of the complex of the cyclin D-dependent kinase Cdk6 bound to the cell-cycle inhibitor p19INK4d". Nature. 395 (6699): 244–50. doi:10.1038/26164. PMID 9751051.  Jiang W, Wells NJ, Hunter T (May 1999). "Multistep regulation of DNA replication by Cdk phosphorylation of HsCdc6". Proceedings of the National Academy of Sciences of the United States of America. 96 (11): 6193–8. doi:10.1073/pnas.96.11.6193. PMC 26858 . PMID 10339564.  Yarbrough WG, Buckmire RA, Bessho M, Liu ET (Sep 1999). "Biologic and biochemical analyses of p16(INK4a) mutations from primary tumors". Journal of the National Cancer Institute. 91 (18): 1569–74. doi:10.1093/jnci/91.18.1569. PMID 10491434.  Harbour JW, Luo RX, Dei Santi A, Postigo AA, Dean DC (Sep 1999). 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External links[edit] Cyclin-Dependent Kinase 6 at the US National Library of Medicine Medical Subject Headings (MeSH) CDK6 human gene location in the UCSC Genome Browser. CDK6 human gene details in the UCSC Genome Browser. v t e PDB gallery 1bi7: MECHANISM OF G1 CYCLIN DEPENDENT KINASE INHIBITION FROM THE STRUCTURE OF THE CDK6-P16INK4A TUMOR SUPPRESSOR COMPLEX  1bi8: MECHANISM OF G1 CYCLIN DEPENDENT KINASE INHIBITION FROM THE STRUCTURES CDK6-P19INK4D INHIBITOR COMPLEX  1blx: P19INK4D/CDK6 COMPLEX  1g3n: STRUCTURE OF A P18(INK4C)-CDK6-K-CYCLIN TERNARY COMPLEX  1jow: Crystal structure of a complex of human CDK6 and a viral cyclin  1xo2: Crystal structure of a human cyclin-dependent kinase 6 complex with a flavonol inhibitor, fisetin  2euf: X-ray structure of human CDK6-Vcyclin in complex with the inhibitor PD0332991  2f2c: X-ray structure of human CDK6-Vcyclinwith the inhibitor aminopurvalanol  v t e Cell cycle proteins Cyclin A (A1, A2) B (B1, B2, B3) D (D1, D2, D3) E (E1, E2) CDK 1 2 3 4 5 6 7 8 9 10 CDK-activating kinase CDK inhibitor INK4a/ARF (p14arf/p16, p15, p18, p19) cip/kip (p21, p27, p57) P53 p63 p73 family p53 p63 p73 Other Cdc2 Cdc25 Cdc42 Cellular apoptosis susceptibility protein E2F Maturation promoting factor Wee Cullin (CUL7) Phases and checkpoints Interphase G1 phase S phase G2 phase M phase Mitosis (Preprophase Prophase Prometaphase Metaphase Anaphase Telophase) Cytokinesis Cell cycle checkpoints Restriction point Spindle checkpoint Postreplication checkpoint Other cellular phases Apoptosis G0 phase Meiosis v t e Kinases: Serine/threonine-specific protein kinases (EC 2.7.11-12) Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20) Non-specific serine/threonine protein kinases (EC 2.7.11.1) LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B AKT1 AKT2 AKT3 Ataxia telangiectasia mutated Mammalian target of rapamycin EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1 Pyruvate dehydrogenase kinase (EC 2.7.11.2) PDK1 PDK2 PDK3 Dephospho-(reductase kinase) kinase (EC 2.7.11.3) AMP-activated protein kinase α PRKAA1 PRKAA2 β PRKAB1 PRKAB2 γ PRKAG1 PRKAG2 PRKAG3 3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4) BCKDK BCKDHA BCKDHB (isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5) IDH2 IDH3A IDH3B IDH3G (tyrosine 3-monooxygenase) kinase (EC 2.7.11.6) STK4 Myosin-heavy-chain kinase (EC 2.7.11.7) Aurora kinase Aurora A kinase Aurora B kinase Fas-activated serine/threonine kinase (EC 2.7.11.8) FASTK STK10 Goodpasture-antigen-binding protein kinase (EC 2.7.11.9) - IκB kinase (EC 2.7.11.10) CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP cAMP-dependent protein kinase (EC 2.7.11.11) Protein kinase A PRKACG PRKACB PRKACA PRKY cGMP-dependent protein kinase (EC 2.7.11.12) Protein kinase G PRKG1 Protein kinase C (EC 2.7.11.13) Protein kinase C Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3 Rhodopsin kinase (EC 2.7.11.14) Rhodopsin kinase Beta adrenergic receptor kinase (EC 2.7.11.15) Beta adrenergic receptor kinase Beta adrenergic receptor kinase-2 G-protein coupled receptor kinases (EC 2.7.11.16) GRK4 GRK5 GRK6 Ca2+/calmodulin-dependent (EC 2.7.11.17) BRSK2 CAMK1 CAMK2A CAMK2B CAMK2D CAMK2G CAMK4 MLCK CASK CHEK1 CHEK2 DAPK1 DAPK2 DAPK3 STK11 MAPKAPK2 MAPKAPK3 MAPKAPK5 MARK1 MARK2 MARK3 MARK4 MELK MKNK1 MKNK2 NUAK1 NUAK2 OBSCN PASK PHKG1 PHKG2 PIM1 PIM2 PKD1 PRKD2 PRKD3 PSKH1 SNF1LK2 KIAA0999 STK40 SNF1LK SNRK SPEG TSSK2 Kalirin TRIB1 TRIB2 TRIB3 TRIO Titin DCLK1 Myosin light-chain kinase (EC 2.7.11.18) MYLK MYLK2 MYLK3 MYLK4 Phosphorylase kinase (EC 2.7.11.19) PHKA1 PHKA2 PHKB PHKG1 PHKG2 Elongation factor 2 kinase (EC 2.7.11.20) EEF2K STK19 Polo kinase (EC 2.7.11.21) PLK1 PLK2 PLK3 PLK4 Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30) Polo kinase (EC 2.7.11.21) PLK1 PLK2 PLK3 PLK4 Cyclin-dependent kinase (EC 2.7.11.22) CDK1 CDK2 CDKL2 CDK3 CDK4 CDK5 CDKL5 CDK6 CDK7 CDK8 CDK9 CDK10 CDK12 CDC2L5 PCTK1 PCTK2 PCTK3 PFTK1 CDC2L1 (RNA-polymerase)-subunit kinase (EC 2.7.11.23) RPS6KA5 RPS6KA4 P70S6 kinase P70-S6 Kinase 1 RPS6KB2 RPS6KA2 RPS6KA3 RPS6KA1 RPS6KC1 Mitogen-activated protein kinase (EC 2.7.11.24) Extracellular signal-regulated MAPK1 MAPK3 MAPK4 MAPK6 MAPK7 MAPK12 MAPK15 C-Jun N-terminal MAPK8 MAPK9 MAPK10 P38 mitogen-activated protein MAPK11 MAPK13 MAPK14 MAP3K (EC 2.7.11.25) MAP kinase kinase kinases MAP3K1 MAP3K2 MAP3K3 MAP3K4 MAP3K5 MAP3K6 MAP3K7 MAP3K8 RAFs ARAF BRAF KSR1 KSR2 MLKs MAP3K12 MAP3K13 MAP3K9 MAP3K10 MAP3K11 MAP3K7 ZAK CDC7 MAP3K14 Tau-protein kinase (EC 2.7.11.26) TPK1 TTK GSK-3 (acetyl-CoA carboxylase) kinase (EC 2.7.11.27) - Tropomyosin kinase (EC 2.7.11.28) - Low-density-lipoprotein receptor kinase (EC 2.7.11.29) - Receptor protein serine/threonine kinase (EC 2.7.11.30) Bone morphogenetic protein receptors BMPR1 BMPR1A BMPR1B BMPR2 ACVR1 ACVR1B ACVR1C ACVR2A ACVR2B ACVRL1 Anti-Müllerian hormone receptor Dual-specificity kinases (EC 2.7.12) MAP2K MAP2K1 MAP2K2 MAP2K3 MAP2K4 MAP2K5 MAP2K6 MAP2K7 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 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) Molecular and Cellular Biology portal Retrieved from "https://en.wikipedia.org/w/index.php?title=Cyclin-dependent_kinase_6&oldid=807945492" Categories: Genes on human chromosome 7Cell cycleProteinsEC 2.7.11


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Cyclin-dependent_kinase_6 - Photos and All Basic Informations

Cyclin-dependent_kinase_6 More Links

Protein Data BankGene NomenclatureMendelian Inheritance In ManMouse Genome InformaticsHomoloGeneGeneCardsChromosome 7 (human)ChromosomeChromosome 7 (human)Chromosome 7 (human)Genomic Location For CDK6Genomic Location For CDK6Locus (genetics)Base PairBase PairChromosome 5 (mouse)ChromosomeChromosome 5 (mouse)Genomic Location For CDK6Genomic Location For CDK6Locus (genetics)Base PairBase PairGene ExpressionGene OntologyEntrezEnsemblUniProtPubMedWikidataEnzymeGeneCyclinsCyclin DCyclin-dependent Kinase Inhibitor ProteinCyclin-dependent KinaseCDK4Cell CycleRestriction PointRetinoblastoma ProteinCancerGeneEukaryoteBudding YeastNematodeCaenorhabditis ElegansLymphomaLeukemiaMedulloblastomaMelanomaAnalogousE2FMitogensGrowth FactorsCDK2Knockout MiceAstrocytesApoptosisP53CentrosomeAneuploidyMicrocephalyKaposi's Sarcoma-associated Herpes VirusMonomerDrug ResistanceGliomaChemotherapyTemozolomideHormone TherapyBreast CancerHallmarks Of CancerAngiogenesisTumor Suppressor GeneMicroRNAMedulloblastomaGlioblastomaPatient Derived Tumor XenograftsCDK InhibitorPalbociclibRibociclibCDK4RibociclibLetrozoleHormone ReceptorHER2Clinical TrialTumorigenesisProtein-protein InteractionCDKN2CCyclin D1Cyclin D3P16 (gene)PPM1BPPP2CACell CycleMitosisCyclin-dependent KinaseCDK4Hallmarks Of CancerEnsembl Genome Database ProjectEnsembl Genome Database ProjectPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierPubMed IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierMedical Subject HeadingsUCSC Genome BrowserUCSC Genome BrowserTemplate:PDB GalleryTemplate Talk:PDB Gallery1bi7: MECHANISM OF G1 CYCLIN DEPENDENT KINASE INHIBITION FROM THE STRUCTURE OF THE CDK6-P16INK4A TUMOR SUPPRESSOR COMPLEX1bi8: MECHANISM OF G1 CYCLIN DEPENDENT KINASE INHIBITION FROM THE STRUCTURES CDK6-P19INK4D INHIBITOR COMPLEX1blx: P19INK4D/CDK6 COMPLEX1g3n: STRUCTURE OF A P18(INK4C)-CDK6-K-CYCLIN TERNARY COMPLEX1jow: Crystal Structure Of A Complex Of Human CDK6 And A Viral Cyclin1xo2: Crystal Structure Of A Human Cyclin-dependent Kinase 6 Complex With A Flavonol Inhibitor, Fisetin2euf: X-ray Structure Of Human CDK6-Vcyclin In Complex With The Inhibitor PD03329912f2c: X-ray Structure Of Human CDK6-Vcyclinwith The Inhibitor AminopurvalanolTemplate:Cell Cycle ProteinsTemplate Talk:Cell Cycle ProteinsCell CycleProteinCyclinCyclin ACyclin A1Cyclin A2Cyclin BCyclin B1Cyclin B2Cyclin DCyclin D1Cyclin D2Cyclin D3Cyclin ECyclin E1Cyclin E2Cyclin-dependent KinaseCyclin-dependent Kinase 1Cyclin-dependent Kinase 2Cyclin-dependent Kinase 3Cyclin-dependent Kinase 4Cyclin-dependent Kinase 5Cyclin-dependent Kinase 7Cyclin-dependent Kinase 8Cyclin-dependent Kinase 9Cyclin-dependent Kinase 10CDK-activating KinaseCyclin-dependent Kinase Inhibitor ProteinCell CycleP14arfP16CDKN2BCDKN2CCDKN2DCell CycleP21CDKN1BCyclin-dependent Kinase Inhibitor 1CP53 P63 P73 FamilyP53TP63P73Cdk1Cdc25CDC42Cellular Apoptosis Susceptibility ProteinE2FMaturation Promoting FactorWee1CullinCUL7InterphaseG1 PhaseS PhaseG2 PhaseCell DivisionMitosisPreprophaseProphasePrometaphaseMetaphaseAnaphaseTelophaseCytokinesisCell Cycle CheckpointRestriction PointSpindle CheckpointPostreplication CheckpointApoptosisG0 PhaseMeiosisTemplate:Serine/threonine-specific Protein KinasesTemplate Talk:Serine/threonine-specific Protein KinasesKinaseSerine/threonine-specific Protein KinaseEnzyme Commission NumberSerine/threonine-specific Protein KinaseNon-specific Serine/threonine Protein KinaseLATS1LATS2MAST1MAST2STK38STK38LCIT (gene)ROCK1SGKSGK2SGK3AKTAKT1AKT2AKT3Ataxia Telangiectasia MutatedMammalian Target Of RapamycinEIF-2 KinaseProtein Kinase REIF2AK1EIF2AK3EIF2AK4Wee1Wee1-like Protein KinasePyruvate Dehydrogenase KinasePyruvate Dehydrogenase Lipoamide Kinase Isozyme 1PDK2PDK3Dephospho-(reductase Kinase) KinaseAMP-activated Protein KinaseProtein Kinase, AMP-activated, Alpha 1PRKAA2PRKAB1PRKAB2PRKAG1PRKAG2PRKAG33-methyl-2-oxobutanoate Dehydrogenase (acetyl-transferring) KinaseBCKDKBCKDHABCKDHB(isocitrate Dehydrogenase (NADP+)) KinaseIDH2IDH3AIDH3BIDH3G(tyrosine 3-monooxygenase) KinaseSTK4Myosin-heavy-chain KinaseAurora KinaseAurora A KinaseAurora B KinaseFas-activated Serine/threonine KinaseFASTKSTK10Goodpasture-antigen-binding Protein KinaseIκB KinaseCHUKIKK2TANK-binding Kinase 1IKBKEIKBKGIKBKAPProtein Kinase AProtein Kinase APRKACGPRKACBPRKACAPRKYCGMP-dependent Protein KinaseCGMP-dependent Protein KinasePRKG1Protein Kinase CProtein Kinase CProtein Kinase C Zeta TypePKC AlphaPRKCB1PRKCDPRKCEPRKCHPRKCGPRKCIPRKCQProtein Kinase N1PKN2PKN3 (gene)Rhodopsin KinaseRhodopsin KinaseBeta Adrenergic Receptor KinaseBeta Adrenergic Receptor KinaseBeta Adrenergic Receptor Kinase-2G Protein-coupled Receptor KinaseGRK4GRK5GRK6Ca2+/calmodulin-dependent Protein KinaseBRSK2CAMK1CAMK2ACAMK2BCAMK2DCAMK2GCAMK4Myosin Light-chain KinaseCASKCHEK1CHEK2DAPK1DAPK2DAPK3STK11MAPKAPK2MAPKAPK3MAPKAPK5MARK1MARK2MARK3MARK4MELKMKNK1MKNK2NUAK1NUAK2OBSCNPASKPHKG1PHKG2PIM1PIM2 (gene)Protein Kinase D1PRKD2PRKD3PSKH1SNF1LK2KIAA0999STK40SNF1LKSNRKSPEGTSSK2KalirinTRIB1TRIB2TRIB3TRIO (gene)TitinDCLK1Myosin Light-chain KinaseMYLKMYLK2MYLK3MYLK4Phosphorylase KinasePhosphorylase Kinase, Alpha 1PHKA2PHKBPHKG1PHKG2Elongation Factor 2 KinaseEEF2KSTK19Polo KinasePLK1PLK2PLK3PLK4Serine/threonine-specific Protein KinasePolo KinasePLK1PLK2PLK3PLK4Cyclin-dependent KinaseCdk1Cyclin-dependent Kinase 2CDKL2Cyclin-dependent Kinase 3Cyclin-dependent Kinase 4Cyclin-dependent Kinase 5CDKL5Cyclin-dependent Kinase 7Cyclin-dependent Kinase 8CDK9Cyclin-dependent Kinase 10CDK12CDC2L5PCTK1PCTK2PCTK3PFTK1CDC2L1(RNA-polymerase)-subunit KinaseRPS6KA5RPS6KA4P70S6 KinaseP70-S6 Kinase 1RPS6KB2RPS6KA2RPS6KA3RPS6KA1RPS6KC1Mitogen-activated Protein KinaseExtracellular Signal-regulated KinasesMAPK1MAPK3MAPK4MAPK6MAPK7MAPK12MAPK15C-Jun N-terminal KinasesMAPK8Mitogen-activated Protein Kinase 9MAPK10P38 Mitogen-activated Protein KinasesMAPK11MAPK13MAPK14MAP Kinase Kinase KinaseMAP Kinase Kinase KinaseMAP3K1MAP3K2MAP3K3MAP3K4ASK1MAP3K7MAP3K8C-RafARAFBRAF (gene)KSR1KSR2MAP3K12MAP3K13MAP3K9MAP3K10MAP3K11MAP3K7ZAKCell Division Cycle 7-related Protein KinaseMAP3K14Tau-protein KinaseTPK1TTK (gene)GSK-3(acetyl-CoA Carboxylase) KinaseTropomyosin KinaseLow-density-lipoprotein Receptor KinaseReceptor Protein Serine/threonine KinaseBone Morphogenetic Protein ReceptorsBone Morphogenetic Protein Receptor, Type 1BMPR1ABMPR1BBMPR2ACVR1ACVR1BACVR1CACVR2AACVR2BACVRL1Anti-Müllerian Hormone ReceptorDual-specificity KinaseMitogen-activated Protein Kinase KinaseMAP2K1MAP2K2MAP2K3MAP2K4MAP2K5MAP2K6MAP2K7Template:EnzymesTemplate Talk:EnzymesEnzymeActive SiteBinding SiteCatalytic TriadOxyanion HoleEnzyme PromiscuityCatalytically Perfect EnzymeCoenzymeCofactor (biochemistry)Enzyme CatalysisAllosteric RegulationCooperativityEnzyme InhibitorEnzyme Commission NumberEnzyme SuperfamilyEnzyme FamilyList Of EnzymesEnzyme KineticsEadie–Hofstee DiagramHanes–Woolf PlotLineweaver–Burk PlotMichaelis–Menten KineticsOxidoreductaseList Of EC Numbers (EC 1)TransferaseList Of EC Numbers (EC 2)HydrolaseList Of EC Numbers (EC 3)LyaseList Of EC Numbers (EC 4)IsomeraseList Of EC Numbers (EC 5)LigaseList Of EC Numbers (EC 6)Portal:Molecular And Cellular BiologyHelp:CategoryCategory:Genes On Human Chromosome 7Category:Cell CycleCategory:ProteinsCategory:EC 2.7.11Discussion About Edits From This IP Address [n]A List Of Edits Made From This IP Address [y]View The Content Page [c]Discussion About The Content Page [t]Edit This Page [e]Visit The Main Page [z]Guides To Browsing WikipediaFeatured Content – The Best Of WikipediaFind Background Information On Current EventsLoad A Random Article [x]Guidance On How To Use And Edit WikipediaFind Out 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