Misplaced Pages

CCNK
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2I53, 4CXA, 4NST, 4UN0, 5EFQ, 5ACB
Identifiers
Aliases	CCNK, CPR4, Cyclin K, IDDHDF
External IDs	OMIM: 603544; MGI: 1276106; HomoloGene: 14748; GeneCards: CCNK; OMA:CCNK - orthologs
Gene location (Human) Chr. Chromosome 14 (human) Band 14q32.2 Start 99,481,169 bp End 99,535,044 bp
Gene location (Mouse) Chr. Chromosome 12 (mouse) Band 12 F1|12 59.23 cM Start 108,145,838 bp End 108,169,618 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in skin of arm cardiac muscle tissue of right atrium myocardium of left ventricle mucosa of ileum amniotic fluid monocyte tibialis anterior muscle parotid gland pancreatic ductal cell bone marrow cells Top expressed in zygote muscle of thigh tail of embryo genital tubercle interventricular septum seminiferous tubule ventricular zone spermatid spermatocyte neural layer of retina More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding protein kinase binding RNA polymerase II CTD heptapeptide repeat kinase activity cyclin-dependent protein serine/threonine kinase activity cyclin-dependent protein serine/threonine kinase regulator activity protein serine/threonine kinase activity cyclin-dependent protein serine/threonine kinase activator activity Cellular component cyclin K-CDK12 complex nucleus cyclin K-CDK13 complex nucleoplasm cyclin-dependent protein kinase holoenzyme complex cyclin/CDK positive transcription elongation factor complex Biological process positive regulation of cyclin-dependent protein serine/threonine kinase activity transcription elongation from RNA polymerase II promoter regulation of cyclin-dependent protein serine/threonine kinase activity positive regulation of phosphorylation of RNA polymerase II C-terminal domain serine 2 residues regulation of transcription, DNA-templated cellular response to DNA damage stimulus transcription by RNA polymerase II negative regulation by host of viral genome replication positive regulation of transcription by RNA polymerase II cell division cell cycle protein phosphorylation transcription, DNA-templated snRNA transcription by RNA polymerase II positive regulation of phosphorylation of RNA polymerase II C-terminal domain regulation of transcription by RNA polymerase II positive regulation of DNA-templated transcription, elongation Sources:Amigo / QuickGO
Orthologs Species Human Mouse 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 Mb Chr 12: 108.15 – 108.17 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Cyclin-K is a protein that in humans is encoded by the CCNK gene.

Function

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. 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. Cyclin K only uses RNA recruitment to activate transcription.

Interactions

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

Cyclin K also interacts with HIV nef protein. 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. CDK 13 may also be characterized to interact with HIV mRNA splicing, alongside Nef, and the underexpression of Gag and Env related proteins.

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

References

1. ^ GRCh38: Ensembl release 89: ENSG00000090061 – Ensembl, May 2017
2. ^ 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. ^ 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.
6. ^ 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.
7. ^ "Entrez Gene: CCNK cyclin K".
8. ^ 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.
9. ^ 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.
10. ^ 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.
12. ^ 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.
13. ^ 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.
14. ^ 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

• 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.
• 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.
• 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.
• 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.
• 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.
• 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.

External links

• Overview of all the structural information available in the PDB for UniProt: O75909 (Cyclin-K) at the PDBe-KB.

This article on a gene on human chromosome 14 is a stub. You can help Misplaced Pages by expanding it.

• v
• t
• e

• Genes on human chromosome 14
• Human chromosome 14 gene stubs