Wikipedia

Cyclin K

(Redirected from CCNK)

Cyclin-K is a protein that in humans is encoded by the CCNK gene.[5][6][7]

CCNK
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCCNK, CPR4, Cyclin K, IDDHDF
External IDsOMIM: 603544; MGI: 1276106; HomoloGene: 14748; GeneCards: CCNK; OMA:CCNK - orthologs
Orthologs
SpeciesHumanMouse
Entrez

8812

12454

Ensembl

ENSG00000090061

ENSMUSG00000021258

UniProt

O75909

O88874
Q3U3M5

RefSeq (mRNA)

NM_001099402
NM_003858

NM_009832

RefSeq (protein)

NP_001092872

NP_033962

Location (UCSC)Chr 14: 99.48 – 99.54 MbChr 12: 108.15 – 108.17 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

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The protein encoded by this gene is a member of the transcription cyclin family. These cyclins may regulate transcription through their association with and activation of cyclin-dependent kinases (CDKs) through conformational changes.[8][9] Activation of CDKs through their cyclin partner, creates kinase complexes that will activate target proteins through phosphorylation. Targeted proteins can then ultimately regulate decisions of a cell's progression within the cell cycle to occur. This gene product may be seen to play a dual role in both regulating CDK and RNA polymerase II (RNAP2) activities.[7] Cyclin K only uses RNA recruitment to activate transcription.[10]

Interactions

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Cyclin K has been shown to interact with multiple CDKs including CDK9 and latest CDK12 and CDK13.[6][9] Roles include helping to phosphorylate C-terminal domains of subunits of RNAP2.[11] Cyclin K is most noted for its associated induction of processive elongation.[8] Also, identified with G1 and S phase cyclin activity, however functions are not deeply understood.[5][12]

Cyclin K also interacts with HIV nef protein.[13] In the presence of overexpressed Nef protein, Cyclin k and CDK9 binding is induced, inhibiting the positive elongation factor of other CDK9 binding complexes, resulting in an inhibition of specific HIV-1 gene expression.[9][13] CDK 13 may also be characterized to interact with HIV mRNA splicing, alongside Nef, and the underexpression of Gag and Env related proteins.[12][10]

Cyclin K is indispensable for Leukemia growth. SETD1A, is also known to bind Cyclin K through its FLOS domain.[14] The interaction is shown to be important to DNA damage response genes and for Leukemia proliferation.[10][14]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000090061 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000021258 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b Edwards MC, Wong C, Elledge SJ (July 1998). "Human cyclin K, a novel RNA polymerase II-associated cyclin possessing both carboxy-terminal domain kinase and Cdk-activating kinase activity". Molecular and Cellular Biology. 18 (7): 4291–300. doi:10.1128/MCB.18.7.4291. PMC 109013. PMID 9632813.4291-300&rft.date=1998-07&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC109013#id-name=PMC&rft_id=info:pmid/9632813&rft_id=info:doi/10.1128/MCB.18.7.4291&rft.aulast=Edwards&rft.aufirst=MC&rft.au=Wong, C&rft.au=Elledge, SJ&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC109013&rfr_id=info:sid/en.wikipedia.org:Cyclin K" class="Z3988">
  6. ^ a b Fu TJ, Peng J, Lee G, Price DH, Flores O (December 1999). "Cyclin K functions as a CDK9 regulatory subunit and participates in RNA polymerase II transcription". The Journal of Biological Chemistry. 274 (49): 34527–30. doi:10.1074/jbc.274.49.34527. PMID 10574912.34527-30&rft.date=1999-12&rft_id=info:doi/10.1074/jbc.274.49.34527&rft_id=info:pmid/10574912&rft.aulast=Fu&rft.aufirst=TJ&rft.au=Peng, J&rft.au=Lee, G&rft.au=Price, DH&rft.au=Flores, O&rft_id=https://doi.org/10.1074%2Fjbc.274.49.34527&rfr_id=info:sid/en.wikipedia.org:Cyclin K" class="Z3988">
  7. ^ a b "Entrez Gene: CCNK cyclin K".
  8. ^ a b Baek K, Brown RS, Birrane G, Ladias JA (February 2007). "Crystal structure of human cyclin K, a positive regulator of cyclin-dependent kinase 9". Journal of Molecular Biology. 366 (2): 563–73. doi:10.1016/j.jmb.2006.11.057. PMC 1852425. PMID 17169370.563-73&rft.date=2007-02&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1852425#id-name=PMC&rft_id=info:pmid/17169370&rft_id=info:doi/10.1016/j.jmb.2006.11.057&rft.aulast=Baek&rft.aufirst=K&rft.au=Brown, RS&rft.au=Birrane, G&rft.au=Ladias, JA&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1852425&rfr_id=info:sid/en.wikipedia.org:Cyclin K" class="Z3988">
  9. ^ a b c Greifenberg AK, Hönig D, Pilarova K, Düster R, Bartholomeeusen K, Bösken CA, Anand K, Blazek D, Geyer M (January 2016). "Structural and Functional Analysis of the Cdk13/Cyclin K Complex". Cell Reports. 14 (2): 320–31. doi:10.1016/j.celrep.2015.12.025. hdl:11858/00-001M-0000-0029-567D-5. PMID 26748711.320-31&rft.date=2016-01&rft_id=info:hdl/11858/00-001M-0000-0029-567D-5&rft_id=info:pmid/26748711&rft_id=info:doi/10.1016/j.celrep.2015.12.025&rft.aulast=Greifenberg&rft.aufirst=AK&rft.au=Hönig, D&rft.au=Pilarova, K&rft.au=Düster, R&rft.au=Bartholomeeusen, K&rft.au=Bösken, CA&rft.au=Anand, K&rft.au=Blazek, D&rft.au=Geyer, M&rft_id=https://doi.org/10.1016%2Fj.celrep.2015.12.025&rfr_id=info:sid/en.wikipedia.org:Cyclin K" class="Z3988">
  10. ^ a b c Kohoutek J, Blazek D (April 2012). "Cyclin K goes with Cdk12 and Cdk13". Cell Division. 7: 12. doi:10.1186/1747-1028-7-12. PMC 3348076. PMID 22512864.
  11. ^ Edwards MC, Wong C, Elledge SJ (July 1998). "Human cyclin K, a novel RNA polymerase II-associated cyclin possessing both carboxy-terminal domain kinase and Cdk-activating kinase activity". Molecular and Cellular Biology. 18 (7): 4291–300. doi:10.1128/mcb.18.7.4291. PMC 109013. PMID 9632813.4291-300&rft.date=1998-07&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC109013#id-name=PMC&rft_id=info:pmid/9632813&rft_id=info:doi/10.1128/mcb.18.7.4291&rft.aulast=Edwards&rft.aufirst=MC&rft.au=Wong, C&rft.au=Elledge, SJ&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC109013&rfr_id=info:sid/en.wikipedia.org:Cyclin K" class="Z3988">
  12. ^ a b Berro R, Pedati C, Kehn-Hall K, Wu W, Klase Z, Even Y, Genevière AM, Ammosova T, Nekhai S, Kashanchi F (July 2008). "CDK13, a new potential human immunodeficiency virus type 1 inhibitory factor regulating viral mRNA splicing". Journal of Virology. 82 (14): 7155–66. doi:10.1128/JVI.02543-07. PMC 2446983. PMID 18480452.7155-66&rft.date=2008-07&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2446983#id-name=PMC&rft_id=info:pmid/18480452&rft_id=info:doi/10.1128/JVI.02543-07&rft.aulast=Berro&rft.aufirst=R&rft.au=Pedati, C&rft.au=Kehn-Hall, K&rft.au=Wu, W&rft.au=Klase, Z&rft.au=Even, Y&rft.au=Genevière, AM&rft.au=Ammosova, T&rft.au=Nekhai, S&rft.au=Kashanchi, F&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2446983&rfr_id=info:sid/en.wikipedia.org:Cyclin K" class="Z3988">
  13. ^ a b Khan SZ, Mitra D (July 2011). "Cyclin K inhibits HIV-1 gene expression and replication by interfering with cyclin-dependent kinase 9 (CDK9)-cyclin T1 interaction in Nef-dependent manner". The Journal of Biological Chemistry. 286 (26): 22943–54. doi:10.1074/jbc.M110.201194. PMC 3123062. PMID 21555514.22943-54&rft.date=2011-07&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3123062#id-name=PMC&rft_id=info:pmid/21555514&rft_id=info:doi/10.1074/jbc.M110.201194&rft.aulast=Khan&rft.aufirst=SZ&rft.au=Mitra, D&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3123062&rfr_id=info:sid/en.wikipedia.org:Cyclin K" class="Z3988">
  14. ^ a b Hoshii T, Cifani P, Feng Z, Huang CH, Koche R, Chen CW, Delaney CD, Lowe SW, Kentsis A, Armstrong SA (February 2018). "A Non-catalytic Function of SETD1A Regulates Cyclin K and the DNA Damage Response". Cell. 172 (5): 1007–1021.e17. doi:10.1016/j.cell.2018.01.032. PMC 6052445. PMID 29474905.

Further reading

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  • Lin X, Taube R, Fujinaga K, Peterlin BM (May 2002). "P-TEFb containing cyclin K and Cdk9 can activate transcription via RNA". The Journal of Biological Chemistry. 277 (19): 16873–8. doi:10.1074/jbc.M200117200. PMID 11884399.16873-8&rft.date=2002-05&rft_id=info:doi/10.1074/jbc.M200117200&rft_id=info:pmid/11884399&rft.aulast=Lin&rft.aufirst=X&rft.au=Taube, R&rft.au=Fujinaga, K&rft.au=Peterlin, BM&rft_id=https://doi.org/10.1074%2Fjbc.M200117200&rfr_id=info:sid/en.wikipedia.org:Cyclin K" class="Z3988">
  • Mori T, Anazawa Y, Matsui K, Fukuda S, Nakamura Y, Arakawa H (2002). "Cyclin K as a direct transcriptional target of the p53 tumor suppressor". Neoplasia. 4 (3): 268–74. doi:10.1038/sj.neo.7900235. PMC 1531701. PMID 11988847.268-74&rft.date=2002&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1531701#id-name=PMC&rft_id=info:pmid/11988847&rft_id=info:doi/10.1038/sj.neo.7900235&rft.aulast=Mori&rft.aufirst=T&rft.au=Anazawa, Y&rft.au=Matsui, K&rft.au=Fukuda, S&rft.au=Nakamura, Y&rft.au=Arakawa, H&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1531701&rfr_id=info:sid/en.wikipedia.org:Cyclin K" class="Z3988">
  • Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (August 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.12130-5&rft.date=2004-08&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC514446#id-name=PMC&rft_id=info:pmid/15302935&rft_id=info:doi/10.1073/pnas.0404720101&rft_id=info:bibcode/2004PNAS..10112130B&rft.aulast=Beausoleil&rft.aufirst=SA&rft.au=Jedrychowski, M&rft.au=Schwartz, D&rft.au=Elias, JE&rft.au=Villén, J&rft.au=Li, J&rft.au=Cohn, MA&rft.au=Cantley, LC&rft.au=Gygi, SP&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC514446&rfr_id=info:sid/en.wikipedia.org:Cyclin K" class="Z3988">
  • Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M, Zoghbi HY (May 2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569.801-14&rft.date=2006-05&rft_id=info:doi/10.1016/j.cell.2006.03.032&rft_id=info:pmid/16713569&rft.aulast=Lim&rft.aufirst=J&rft.au=Hao, T&rft.au=Shaw, C&rft.au=Patel, AJ&rft.au=Szabó, G&rft.au=Rual, JF&rft.au=Fisk, CJ&rft.au=Li, N&rft.au=Smolyar, A&rft.au=Hill, DE&rft.au=Barabási, AL&rft.au=Vidal, M&rft.au=Zoghbi, HY&rft_id=https://doi.org/10.1016%2Fj.cell.2006.03.032&rfr_id=info:sid/en.wikipedia.org:Cyclin K" class="Z3988">
  • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (November 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 17081983.635-48&rft.date=2006-11&rft_id=info:doi/10.1016/j.cell.2006.09.026&rft_id=info:pmid/17081983&rft.aulast=Olsen&rft.aufirst=JV&rft.au=Blagoev, B&rft.au=Gnad, F&rft.au=Macek, B&rft.au=Kumar, C&rft.au=Mortensen, P&rft.au=Mann, M&rft_id=https://doi.org/10.1016%2Fj.cell.2006.09.026&rfr_id=info:sid/en.wikipedia.org:Cyclin K" class="Z3988">
  • Baek K, Brown RS, Birrane G, Ladias JA (February 2007). "Crystal structure of human cyclin K, a positive regulator of cyclin-dependent kinase 9". Journal of Molecular Biology. 366 (2): 563–73. doi:10.1016/j.jmb.2006.11.057. PMC 1852425. PMID 17169370.563-73&rft.date=2007-02&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1852425#id-name=PMC&rft_id=info:pmid/17169370&rft_id=info:doi/10.1016/j.jmb.2006.11.057&rft.aulast=Baek&rft.aufirst=K&rft.au=Brown, RS&rft.au=Birrane, G&rft.au=Ladias, JA&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1852425&rfr_id=info:sid/en.wikipedia.org:Cyclin K" class="Z3988">
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