Contents 1 Function 2 Clinical significance 3 As a potential drug target 4 Interactions 5 References 6 Further reading 7 External links


Function[edit] The protein encoded by this gene is a member of the cyclin-dependent protein kinase (CDK) family. CDK8 and cyclin C associate with the mediator complex and regulate transcription by several mechanisms. CDK8 binds to and/or phosphorylates several transcription factors, which can have an activating or inhibitory effect on transcription factor function.[7][8] CDK8 phosphorylates the Notch intracellular domain,[9] SREBP,[10] and STAT1 S727.[11] CDK8 also inhibits transcriptional activation by influencing turnover of subunits in the mediator complex tail module.[12][13] In addition, CDK8 influences binding of RNA polymerase II to the mediator complex.[14][15]


Clinical significance[edit] CDK8 is a colorectal cancer oncogene: the CDK8 gene is amplified in human colorectal tumors, activating β-catenin-mediated transcription that drives colon tumorigenesis.[16] However, CDK8 may not be oncogenic in all cell types, and indeed may act as a tumor suppressor in the notch and EGFR signaling pathways. Specifically, CDK8 promotes turnover of the notch intracellular domain,[9] and inhibits EGFR signaling-driven cell fates in C. elegans.[13] Thus, CDK8 may be an oncogene in cancers driven by Wnt/β-catenin signaling, but could instead be a tumor suppressor gene in cancers driven by notch or EGFR signaling. In addition, CDK8 promotes transcriptional activation mediated by the tumor suppressor protein p53, indicating that it may have an important role in tumor suppression [17] Further research is needed to delineate the effects of CDK8 inhibition in different tissues, so for the time being, drugs targeting CDK8 for cancer treatment remain untested in humans.


As a potential drug target[edit] The natural product cortistatin A is a potent and selective inhibitor of CDK8 and CDK19.[18] Inhibition of CDK8 and CDK19 with cortistatin A suppresses AML cell growth and has anticancer activity in animal models of AML by causing selective and disproportionate up regulation of super-enhancer-associated genes including the cell identity genes CEBPA and IRF8.


Interactions[edit] Cyclin-dependent kinase 8 has been shown to interact with: CCNC,[5][19][20][21][22] CREB binding protein,[21] CRSP3,[19][20] MED1,[19][23] MED12,[19][23] MED14,[20][23] MED16,[19][23] MED17,[19][23] MED21,[19][21][23][24] MED24,[19][23] MED26,[25] MED6,[19][20][23][26] Notch proteins,[9] POLR2A,[21] SMARCB1,[21] STAT1,[11] and SREBP.[10]


References[edit] ^ a b c GRCh38: Ensembl release 89: ENSG00000132964 - Ensembl, May 2017 ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029635 - Ensembl, May 2017 ^ "Human PubMed Reference:".  ^ "Mouse PubMed Reference:".  ^ a b Tassan JP, Jaquenoud M, Léopold P, Schultz SJ, Nigg EA (Sep 1995). "Identification of human cyclin-dependent kinase 8, a putative protein kinase partner for cyclin C". Proceedings of the National Academy of Sciences of the United States of America. 92 (19): 8871–5. doi:10.1073/pnas.92.19.8871. PMC 41069 . PMID 7568034.  ^ "Entrez Gene: CDK8 cyclin-dependent kinase 8".  ^ Nemet J, Jelicic B, Rubelj I, Sopta M (Feb 2014). "The two faces of Cdk8, a positive/negative regulator of transcription". Biochimie. 97: 22–7. doi:10.1016/j.biochi.2013.10.004. PMID 24139904.  ^ Poss ZC, Ebmeier CC, Taatjes DJ. "The mediator complex and transcription regulation". Critical Reviews in Biochemistry and Molecular Biology. 48 (6): 575–608. doi:10.3109/10409238.2013.840259. PMC 3852498 . PMID 24088064.  ^ a b c Fryer CJ, White JB, Jones KA (Nov 2004). "Mastermind recruits CycC:CDK8 to phosphorylate the Notch ICD and coordinate activation with turnover". Molecular Cell. 16 (4): 509–20. doi:10.1016/j.molcel.2004.10.014. PMID 15546612.  ^ a b Zhao X, Feng D, Wang Q, Abdulla A, Xie XJ, Zhou J, Sun Y, Yang ES, Liu LP, Vaitheesvaran B, Bridges L, Kurland IJ, Strich R, Ni JQ, Wang C, Ericsson J, Pessin JE, Ji JY, Yang F (Jul 2012). "Regulation of lipogenesis by cyclin-dependent kinase 8-mediated control of SREBP-1". The Journal of Clinical Investigation. 122 (7): 2417–27. doi:10.1172/JCI61462. PMC 3386818 . PMID 22684109.  ^ a b Bancerek J, Poss ZC, Steinparzer I, Sedlyarov V, Pfaffenwimmer T, Mikulic I, Dölken L, Strobl B, Müller M, Taatjes DJ, Kovarik P (Feb 2013). "CDK8 kinase phosphorylates transcription factor STAT1 to selectively regulate the interferon response". Immunity. 38 (2): 250–62. doi:10.1016/j.immuni.2012.10.017. PMC 3580287 . PMID 23352233.  ^ Gonzalez D, Hamidi N, Del Sol R, Benschop JJ, Nancy T, Li C, Francis L, Tzouros M, Krijgsveld J, Holstege FC, Conlan RS (Feb 2014). "Suppression of Mediator is regulated by Cdk8-dependent Grr1 turnover of the Med3 coactivator". Proceedings of the National Academy of Sciences of the United States of America. 111 (7): 2500–5. doi:10.1073/pnas.1307525111. PMC 3932902 . PMID 24550274.  ^ a b Grants JM, Ying LT, Yoda A, You CC, Okano H, Sawa H, Taubert S (Feb 2016). "The Mediator Kinase Module Restrains Epidermal Growth Factor Receptor Signaling and Represses Vulval Cell Fate Specification in Caenorhabditis elegans". Genetics. 202 (2): 583–99. doi:10.1534/genetics.115.180265. PMID 26715664.  ^ Taatjes DJ, Näär AM, Andel F, Nogales E, Tjian R (Feb 2002). "Structure, function, and activator-induced conformations of the CRSP coactivator". Science. 295 (5557): 1058–62. doi:10.1126/science.1065249. PMID 11834832.  ^ Tsai KL, Sato S, Tomomori-Sato C, Conaway RC, Conaway JW, Asturias FJ (May 2013). "A conserved Mediator-CDK8 kinase module association regulates Mediator-RNA polymerase II interaction". Nature Structural & Molecular Biology. 20 (5): 611–9. doi:10.1038/nsmb.2549. PMC 3648612 . PMID 23563140.  ^ Firestein R, Bass AJ, Kim SY, Dunn IF, Silver SJ, Guney I, Freed E, Ligon AH, Vena N, Ogino S, Chheda MG, Tamayo P, Finn S, Shrestha Y, Boehm JS, Jain S, Bojarski E, Mermel C, Barretina J, Chan JA, Baselga J, Tabernero J, Root DE, Fuchs CS, Loda M, Shivdasani RA, Meyerson M, Hahn WC (Sep 2008). "CDK8 is a colorectal cancer oncogene that regulates beta-catenin activity". Nature. 455 (7212): 547–51. doi:10.1038/nature07179. PMC 2587138 . PMID 18794900.  ^ Donner AJ, Szostek S, Hoover JM, Espinosa JM (Jul 2007). "CDK8 is a stimulus-specific positive coregulator of p53 target genes". Molecular Cell. 27 (1): 121–33. doi:10.1016/j.molcel.2007.05.026. PMC 2936241 . PMID 17612495.  ^ Pelish HE, Liau BB, Nitulescu II, Tangpeerachaikul A, Poss ZC, Da Silva DH, Caruso BT, Arefolov A, Fadeyi O, Christie AL, Du K, Banka D, Schneider EV, Jestel A, Zou G, Si C, Ebmeier CC, Bronson RT, Krivtsov AV, Myers AG, Kohl NE, Kung AL, Armstrong SA, Lemieux ME, Taatjes DJ, Shair MD (Oct 2015). "Mediator kinase inhibition further activates super-enhancer-associated genes in AML". Nature. 526 (7572): 273–6. doi:10.1038/nature14904. PMID 26416749.  ^ a b c d e f g h i Kang YK, Guermah M, Yuan CX, Roeder RG (Mar 2002). "The TRAP/Mediator coactivator complex interacts directly with estrogen receptors alpha and beta through the TRAP220 subunit and directly enhances estrogen receptor function in vitro". Proceedings of the National Academy of Sciences of the United States of America. 99 (5): 2642–7. doi:10.1073/pnas.261715899. PMC 122401 . PMID 11867769.  ^ a b c d Wang G, Cantin GT, Stevens JL, Berk AJ (Jul 2001). "Characterization of mediator complexes from HeLa cell nuclear extract". Molecular and Cellular Biology. 21 (14): 4604–13. doi:10.1128/MCB.21.14.4604-4613.2001. PMC 87123 . PMID 11416138.  ^ a b c d e Cho H, Orphanides G, Sun X, Yang XJ, Ogryzko V, Lees E, Nakatani Y, Reinberg D (Sep 1998). "A human RNA polymerase II complex containing factors that modify chromatin structure". Molecular and Cellular Biology. 18 (9): 5355–63. PMC 109120 . PMID 9710619.  ^ Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D (May 1997). "Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex". Cell. 89 (3): 357–64. doi:10.1016/s0092-8674(00)80216-0. PMID 9150135.  ^ a b c d e f g h Ito M, Yuan CX, Malik S, Gu W, Fondell JD, Yamamura S, Fu ZY, Zhang X, Qin J, Roeder RG (Mar 1999). "Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators". Molecular Cell. 3 (3): 361–70. doi:10.1016/s1097-2765(00)80463-3. PMID 10198638.  ^ Suñé C, Hayashi T, Liu Y, Lane WS, Young RA, Garcia-Blanco MA (Oct 1997). "CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription". Molecular and Cellular Biology. 17 (10): 6029–39. PMC 232452 . PMID 9315662.  ^ Sato S, Tomomori-Sato C, Parmely TJ, Florens L, Zybailov B, Swanson SK, Banks CA, Jin J, Cai Y, Washburn MP, Conaway JW, Conaway RC (Jun 2004). "A set of consensus mammalian mediator subunits identified by multidimensional protein identification technology". Molecular Cell. 14 (5): 685–91. doi:10.1016/j.molcel.2004.05.006. PMID 15175163.  ^ Yang F, DeBeaumont R, Zhou S, Näär AM (Feb 2004). "The activator-recruited cofactor/Mediator coactivator subunit ARC92 is a functionally important target of the VP16 transcriptional activator". Proceedings of the National Academy of Sciences of the United States of America. 101 (8): 2339–44. doi:10.1073/pnas.0308676100. PMC 356952 . PMID 14983011. 


Further reading[edit] Schultz SJ, Nigg EA (Oct 1993). "Identification of 21 novel human protein kinases, including 3 members of a family related to the cell cycle regulator nimA of Aspergillus nidulans". Cell Growth & Differentiation. 4 (10): 821–30. PMID 8274451.  Rickert P, Seghezzi W, Shanahan F, Cho H, Lees E (Jun 1996). "Cyclin C/CDK8 is a novel CTD kinase associated with RNA polymerase II". Oncogene. 12 (12): 2631–40. PMID 8700522.  Cujec TP, Cho H, Maldonado E, Meyer J, Reinberg D, Peterlin BM (Apr 1997). "The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme". Molecular and Cellular Biology. 17 (4): 1817–23. PMC 232028 . PMID 9121429.  Scully R, Anderson SF, Chao DM, Wei W, Ye L, Young RA, Livingston DM, Parvin JD (May 1997). "BRCA1 is a component of the RNA polymerase II holoenzyme". Proceedings of the National Academy of Sciences of the United States of America. 94 (11): 5605–10. doi:10.1073/pnas.94.11.5605. PMC 20825 . PMID 9159119.  Neish AS, Anderson SF, Schlegel BP, Wei W, Parvin JD (Feb 1998). "Factors associated with the mammalian RNA polymerase II holoenzyme". Nucleic Acids Research. 26 (3): 847–53. doi:10.1093/nar/26.3.847. PMC 147327 . PMID 9443979.  Cho H, Orphanides G, Sun X, Yang XJ, Ogryzko V, Lees E, Nakatani Y, Reinberg D (Sep 1998). "A human RNA polymerase II complex containing factors that modify chromatin structure". Molecular and Cellular Biology. 18 (9): 5355–63. PMC 109120 . PMID 9710619.  Sun X, Zhang Y, Cho H, Rickert P, Lees E, Lane W, Reinberg D (Aug 1998). "NAT, a human complex containing Srb polypeptides that functions as a negative regulator of activated transcription". Molecular Cell. 2 (2): 213–22. doi:10.1016/S1097-2765(00)80131-8. PMID 9734358.  Rickert P, Corden JL, Lees E (Jan 1999). "Cyclin C/CDK8 and cyclin H/CDK7/p36 are biochemically distinct CTD kinases". Oncogene. 18 (4): 1093–102. doi:10.1038/sj.onc.1202399. PMID 10023686.  Gu W, Malik S, Ito M, Yuan CX, Fondell JD, Zhang X, Martinez E, Qin J, Roeder RG (Jan 1999). "A novel human SRB/MED-containing cofactor complex, SMCC, involved in transcription regulation". Molecular Cell. 3 (1): 97–108. doi:10.1016/S1097-2765(00)80178-1. PMID 10024883.  Ito M, Yuan CX, Malik S, Gu W, Fondell JD, Yamamura S, Fu ZY, Zhang X, Qin J, Roeder RG (Mar 1999). "Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators". Molecular Cell. 3 (3): 361–70. doi:10.1016/S1097-2765(00)80463-3. PMID 10198638.  Rachez C, Lemon BD, Suldan Z, Bromleigh V, Gamble M, Näär AM, Erdjument-Bromage H, Tempst P, Freedman LP (Apr 1999). "Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex". Nature. 398 (6730): 824–8. doi:10.1038/19783. PMID 10235266.  Akoulitchev S, Chuikov S, Reinberg D (Sep 2000). "TFIIH is negatively regulated by cdk8-containing mediator complexes". Nature. 407 (6800): 102–6. doi:10.1038/35024111. PMID 10993082.  Ramanathan Y, Rajpara SM, Reza SM, Lees E, Shuman S, Mathews MB, Pe'ery T (Apr 2001). "Three RNA polymerase II carboxyl-terminal domain kinases display distinct substrate preferences". The Journal of Biological Chemistry. 276 (14): 10913–20. doi:10.1074/jbc.M010975200. PMID 11278802.  Wang G, Cantin GT, Stevens JL, Berk AJ (Jul 2001). "Characterization of mediator complexes from HeLa cell nuclear extract". Molecular and Cellular Biology. 21 (14): 4604–13. doi:10.1128/MCB.21.14.4604-4613.2001. PMC 87123 . PMID 11416138.  Di Pietro C, Rapisarda A, Bonaiuto C, Lizzio MN, Engel H, Amico V, Scalia M, Amato A, Grzeschik KH, Sichel G, Purrello M (May 1999). "Genomics of the human genes encoding four TAFII subunits of TFIID, the three subunits of TFIIA, as well as CDK8 and SURB7". Somatic Cell and Molecular Genetics. 25 (3): 185–9. doi:10.1023/A:1018897624615. PMID 11441538.  Vogel L, Baratte B, Détivaud L, Azzi L, Leopold P, Meijer L (Apr 2002). "Molecular cloning and characterisation of p15(CDK-BP), a novel CDK-binding protein". Biochimica et Biophysica Acta. 1589 (2): 219–31. doi:10.1016/S0167-4889(02)00175-1. PMID 12007796.  Crowley TE, Kaine EM, Yoshida M, Nandi A, Wolgemuth DJ (Aug 2002). "Reproductive cycle regulation of nuclear import, euchromatic localization, and association with components of Pol II mediator of a mammalian double-bromodomain protein". Molecular Endocrinology. 16 (8): 1727–37. doi:10.1210/me.2001-0353. PMID 12145330.  Sato S, Tomomori-Sato C, Banks CA, Sorokina I, Parmely TJ, Kong SE, Jin J, Cai Y, Lane WS, Brower CS, Conaway RC, Conaway JW (Apr 2003). "Identification of mammalian Mediator subunits with similarities to yeast Mediator subunits Srb5, Srb6, Med11, and Rox3". The Journal of Biological Chemistry. 278 (17): 15123–7. doi:10.1074/jbc.C300054200. PMID 12584197. 


External links[edit] CDK8 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH) CDK8 human gene location in the UCSC Genome Browser. CDK8 human gene details in the UCSC Genome Browser. 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_8&oldid=798050177" Categories: Genes on human chromosome 13Cell cycleProteinsEC 2.7.11


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Cyclin-dependent_kinase_8 - Photos and All Basic Informations

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Protein Data BankGene NomenclatureMouse Genome InformaticsHomoloGeneGeneCardsChromosome 13 (human)ChromosomeChromosome 13 (human)Chromosome 13 (human)Genomic Location For CDK8Genomic Location For CDK8Locus (genetics)Base PairBase PairChromosome 5 (mouse)ChromosomeChromosome 5 (mouse)Genomic Location For CDK8Genomic Location For CDK8Locus (genetics)Base PairBase PairGene ExpressionGene OntologyEntrezEnsemblUniProtPubMedWikidataEnzymeGeneMediator (coactivator)Transcription (genetics)Transcription FactorNotch Signaling PathwaySterol Regulatory Element-binding ProteinSTAT1ProteasomeRNA Polymerase IIOncogeneBeta-cateninTumor Suppressor GeneNotch Signaling PathwayEpidermal Growth Factor ReceptorProteasomeNotch ProteinsEpidermal Growth Factor ReceptorCaenorhabditis ElegansOncogeneWnt Signaling PathwayBeta-cateninTumor Suppressor GeneEpidermal Growth Factor ReceptorTumor SuppressorP53CortistatinsAcute Myeloid LeukemiaSuper-enhancerCEBPAIRF8Protein-protein InteractionCCNC (gene)CREB Binding ProteinCRSP3MED1MED12MED14MED16MED17MED21MED24MED26MED6Notch ProteinsPOLR2ASMARCB1STAT1Sterol Regulatory Element-binding ProteinEnsembl Genome Database ProjectEnsembl Genome Database ProjectDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierPubMed IdentifierPubMed IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed 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 IdentifierDigital Object IdentifierPubMed IdentifierMedical Subject HeadingsUCSC Genome BrowserUCSC Genome BrowserTemplate: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 6Cyclin-dependent Kinase 7Cyclin-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 6Cyclin-dependent Kinase 7CDK9Cyclin-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 13Category: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 About WikipediaAbout The Project, What You Can Do, Where To Find ThingsA List Of Recent Changes In The Wiki [r]List Of All English Wikipedia Pages Containing Links To This Page [j]Recent Changes In Pages Linked From This Page [k]Upload Files [u]A List Of All Special Pages [q]Wikipedia:AboutWikipedia:General Disclaimer



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