Cyclin K

PDB rendering based on 2i53.

Available structures
PDB	2i53

Identifiers

Symbols

CCNK; CPR4; MGC9113

External IDs

OMIM: 603544 HomoloGene: 14748 GeneCards: CCNK Gene

Gene Ontology
Molecular function	• protein binding • protein kinase binding
Biological process	• regulation of cyclin-dependent protein kinase activity • regulation of transcription, DNA-dependent • transcription from RNA polymerase II promoter • cell cycle • mitosis • cell division
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

n/a

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 14:
99.95 – 99.98 Mb

Chr 12:
109.42 – 109.44 Mb

PubMed search

[1]

[2]

Cyclin-K is a protein that in humans is encoded by the CCNK gene.^[1]^[2]^[3]

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 (CDK) that phosphorylate the C-terminal domain (CTD) of the large subunit of RNA polymerase II. This gene product may play a dual role in regulating CDK and RNA polymerase II activities.^[3]

Interactions

Cyclin K has been shown to interact with CDK9.^[2]

References

^ Edwards MC, Wong C, Elledge SJ (Jul 1998). "Human Cyclin K, a Novel RNA Polymerase II-Associated Cyclin Possessing Both Carboxy-Terminal Domain Kinase and Cdk-Activating Kinase Activity". Mol Cell Biol 18 (7): 4291–300. PMC 109013. PMID 9632813. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=109013.
^ ^a ^b Fu TJ, Peng J, Lee G, Price DH, Flores O (Feb 2000). "Cyclin K functions as a CDK9 regulatory subunit and participates in RNA polymerase II transcription". J Biol Chem 274 (49): 34527–30. doi:10.1074/jbc.274.49.34527. PMID 10574912.
^ ^a ^b "Entrez Gene: CCNK cyclin K". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8812.

Lin X, Taube R, Fujinaga K, Peterlin BM (2002). "P-TEFb containing cyclin K and Cdk9 can activate transcription via RNA". J. Biol. Chem. 277 (19): 16873–8. doi:10.1074/jbc.M200117200. PMID 11884399.
Mori T, Anazawa Y, Matsui K et al. (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1531701.
Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Beausoleil SA, Jedrychowski M, Schwartz D et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=514446.
Gerhard DS, Wagner L, Feingold EA et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
Rual JF, Venkatesan K, Hao T et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Lim J, Hao T, Shaw C et al. (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 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.
Baek K, Brown RS, Birrane G, Ladias JA (2007). "Crystal Structure of Human Cyclin K, a Positive Regulator of Cyclin-dependent Kinase 9". J. Mol. Biol. 366 (2): 563–73. doi:10.1016/j.jmb.2006.11.057. PMC 1852425. PMID 17169370. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1852425.

PDB gallery

2i53: Crystal structure of Cyclin K

Cyclin K

Interactions

References

Further reading