Cyclin H

Cyclin H
PDB rendering based on 1jkw.
Available structures PDB 1JKW, 1KXU
Identifiers
Symbols	CCNH; CAK; p34; p37
External IDs	OMIM: 601953 MGI: 1913921 HomoloGene: 946 GeneCards: CCNH Gene
Gene Ontology Molecular function • protein kinase activity • protein binding • DNA-dependent ATPase activity • RNA polymerase II carboxy-terminal domain kinase activity • protein kinase binding Cellular component • nucleus • nucleoplasm • nucleoplasm • holo TFIIH complex • cyclin-dependent protein kinase activating kinase holoenzyme complex Biological process • regulation of cyclin-dependent protein kinase activity • G1 phase of mitotic cell cycle • G1/S transition of mitotic cell cycle • S phase of mitotic cell cycle • G2/M transition of mitotic cell cycle • mitotic cell cycle • nucleotide-excision repair, DNA damage removal • DNA repair • transcription-coupled nucleotide-excision repair • nucleotide-excision repair • regulation of transcription, DNA-dependent • transcription from RNA polymerase I promoter • transcription initiation from RNA polymerase I promoter • transcription elongation from RNA polymerase I promoter • termination of RNA polymerase I transcription • transcription from RNA polymerase II promoter • transcription from RNA polymerase II promoter • transcription initiation from RNA polymerase II promoter • transcription initiation from RNA polymerase II promoter • transcription elongation from RNA polymerase II promoter • transcription elongation from RNA polymerase II promoter • mRNA capping • protein phosphorylation • gene expression • viral reproduction • positive regulation of transcription from RNA polymerase II promoter • positive regulation of viral transcription Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	902	66671
Ensembl	ENSG00000134480	ENSMUSG00000021548
UniProt	P51946	n/a
RefSeq (mRNA)	NM_001199189.1	NM_023243.5
RefSeq (protein)	NP_001186118.1	NP_075732.1
Location (UCSC)	Chr 5: 86.69 – 86.71 Mb	Chr 13: 85.33 – 85.36 Mb
PubMed search	[1]	[2]

Cyclin-H is a protein that in humans is encoded by the CCNH gene.^[1][2]

The protein encoded by this gene belongs to the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle. Cyclins function as regulators of CDK kinases. Different cyclins exhibit distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. This cyclin forms a complex with CDK7 kinase and ring finger protein MAT1. The kinase complex is able to phosphorylate CDK2 and CDC2 kinases, thus functions as a CDK-activating kinase (CAK). This cyclin and its kinase partner are components of TFIIH, as well as RNA polymerase II protein complexes. They participate in two different transcriptional regulation processes, suggesting an important link between basal transcription control and the cell cycle machinery.^[2]

Interactions

Cyclin H has been shown to interact with P53,^[3] Cyclin-dependent kinase 7^[4][5][6] and MNAT1.^[7][8]

References

1. ^ Eki T, Okumura K, Abe M, Kagotani K, Taguchi H, Murakami Y, Pan ZQ, Hanaoka F (Apr 1998). "Mapping of the human genes encoding cyclin H (CCNH) and the CDK-activating kinase (CAK) assembly factor MAT1 (MNAT1) to chromosome bands 5q13.3-q14 and 14q23, respectively". Genomics 47 (1): 115–20. doi:10.1006/geno.1997.5053. PMID 9465303. 
2. ^ ^{a b} "Entrez Gene: CCNH cyclin H". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=902. 
3. ^ Schneider, E; Montenarh M, Wagner P (Nov. 1998). "Regulation of CAK kinase activity by p53". Oncogene (ENGLAND) 17 (21): 2733–41. doi:10.1038/sj.onc.1202504. ISSN 0950-9232. PMID 9840937. 
4. ^ Mäkelä, T P; Tassan J P, Nigg E A, Frutiger S, Hughes G J, Weinberg R A (Sep. 1994). "A cyclin associated with the CDK-activating kinase MO15". Nature (ENGLAND) 371 (6494): 254–7. doi:10.1038/371254a0. ISSN 0028-0836. PMID 8078587. 
5. ^ Yee, A; Nichols M A, Wu L, Hall F L, Kobayashi R, Xiong Y (Dec. 1995). "Molecular cloning of CDK7-associated human MAT1, a cyclin-dependent kinase-activating kinase (CAK) assembly factor". Cancer Res. (UNITED STATES) 55 (24): 6058–62. ISSN 0008-5472. PMID 8521393. 
6. ^ Garber, M E; Mayall T P, Suess E M, Meisenhelder J, Thompson N E, Jones K A (Sep. 2000). "CDK9 autophosphorylation regulates high-affinity binding of the human immunodeficiency virus type 1 tat-P-TEFb complex to TAR RNA". Mol. Cell. Biol. (UNITED STATES) 20 (18): 6958–69. doi:10.1128/MCB.20.18.6958-6969.2000. ISSN 0270-7306. PMC 88771. PMID 10958691. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=88771. 
7. ^ Ewing, Rob M; Chu Peter, Elisma Fred, Li Hongyan, Taylor Paul, Climie Shane, McBroom-Cerajewski Linda, Robinson Mark D, O'Connor Liam, Li Michael, Taylor Rod, Dharsee Moyez, Ho Yuen, Heilbut Adrian, Moore Lynda, Zhang Shudong, Ornatsky Olga, Bukhman Yury V, Ethier Martin, Sheng Yinglun, Vasilescu Julian, Abu-Farha Mohamed, Lambert Jean-Philippe, Duewel Henry S, Stewart Ian I, Kuehl Bonnie, Hogue Kelly, Colwill Karen, Gladwish Katharine, Muskat Brenda, Kinach Robert, Adams Sally-Lin, Moran Michael F, Morin Gregg B, Topaloglou Thodoros, Figeys Daniel (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. (England) 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948. 
8. ^ Talukder, Amjad H; Mishra Sandip K, Mandal Mahitosh, Balasenthil Seetharaman, Mehta Sonal, Sahin Aysegul A, Barnes Christopher J, Kumar Rakesh (Mar. 2003). "MTA1 interacts with MAT1, a cyclin-dependent kinase-activating kinase complex ring finger factor, and regulates estrogen receptor transactivation functions". J. Biol. Chem. (United States) 278 (13): 11676–85. doi:10.1074/jbc.M209570200. ISSN 0021-9258. PMID 12527756. 

Further reading

• Jeang KT (1998). "Tat, Tat-associated kinase, and transcription". J. Biomed. Sci. 5 (1): 24–7. doi:10.1007/BF02253352. PMID 9570510. 
• Yankulov K, Bentley D (1998). "Transcriptional control: Tat cofactors and transcriptional elongation". Curr. Biol. 8 (13): R447–9. doi:10.1016/S0960-9822(98)70289-1. PMID 9651670. 
• Shiekhattar R, Mermelstein F, Fisher RP et al. (1995). "Cdk-activating kinase complex is a component of human transcription factor TFIIH". Nature 374 (6519): 283–7. doi:10.1038/374283a0. PMID 7533895. 
• Darbon JM, Devault A, Taviaux S et al. (1994). "Cloning, expression and subcellular localization of the human homolog of p40MO15 catalytic subunit of cdk-activating kinase". Oncogene 9 (11): 3127–38. PMID 7936635. 
• Feaver WJ, Svejstrup JQ, Henry NL, Kornberg RD (1995). "Relationship of CDK-activating kinase and RNA polymerase II CTD kinase TFIIH/TFIIK". Cell 79 (6): 1103–9. doi:10.1016/0092-8674(94)90040-X. PMID 8001136. 
• Fisher RP, Morgan DO (1994). "A novel cyclin associates with MO15/CDK7 to form the CDK-activating kinase". Cell 78 (4): 713–24. doi:10.1016/0092-8674(94)90535-5. PMID 8069918. 
• Mäkelä TP, Tassan JP, Nigg EA et al. (1994). "A cyclin associated with the CDK-activating kinase MO15". Nature 371 (6494): 254–7. doi:10.1038/371254a0. PMID 8078587. 
• Perez JL, Shen X, Finkernagel S et al. (1994). "Identification and chromosomal mapping of a receptor tyrosine kinase with a putative phospholipid binding sequence in its ectodomain". Oncogene 9 (1): 211–9. PMID 8302582. 
• Tassan JP, Jaquenoud M, Fry AM et al. (1996). "In vitro assembly of a functional human CDK7-cyclin H complex requires MAT1, a novel 36 kDa RING finger protein". EMBO J. 14 (22): 5608–17. PMC 394676. PMID 8521818. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=394676. 
• Adamczewski JP, Rossignol M, Tassan JP et al. (1996). "MAT1, cdk7 and cyclin H form a kinase complex which is UV light-sensitive upon association with TFIIH". EMBO J. 15 (8): 1877–84. PMC 450106. PMID 8617234. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=450106. 
• Blau J, Xiao H, McCracken S et al. (1996). "Three functional classes of transcriptional activation domain". Mol. Cell. Biol. 16 (5): 2044–55. PMC 231191. PMID 8628270. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=231191. 
• Reardon JT, Ge H, Gibbs E et al. (1996). "Isolation and characterization of two human transcription factor IIH (TFIIH)-related complexes: ERCC2/CAK and TFIIH". Proc. Natl. Acad. Sci. U.S.A. 93 (13): 6482–7. doi:10.1073/pnas.93.13.6482. PMC 39049. PMID 8692841. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=39049. 
• Drapkin R, Le Roy G, Cho H et al. (1996). "Human cyclin-dependent kinase-activating kinase exists in three distinct complexes". Proc. Natl. Acad. Sci. U.S.A. 93 (13): 6488–93. doi:10.1073/pnas.93.13.6488. PMC 39050. PMID 8692842. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=39050. 
• Kim KK, Chamberlin HM, Morgan DO, Kim SH (1996). "Three-dimensional structure of human cyclin H, a positive regulator of the CDK-activating kinase". Nat. Struct. Biol. 3 (10): 849–55. doi:10.1038/nsb1096-849. PMID 8836101. 
• Zhou Q, Sharp PA (1996). "Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat". Science 274 (5287): 605–10. doi:10.1126/science.274.5287.605. PMID 8849451. 
• Parada CA, Roeder RG (1996). "Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain". Nature 384 (6607): 375–8. doi:10.1038/384375a0. PMID 8934526. 
• García-Martínez LF, Ivanov D, Gaynor RB (1997). "Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes". J. Biol. Chem. 272 (11): 6951–8. doi:10.1074/jbc.272.11.6951. PMID 9054383. 
• Poterszman A, Andersen G, Busso D et al. (1997). "Expression in Escherichia coli: purification and characterization of cyclin H, a subunit of the human general transcription/DNA repair factor TFIIH". Protein Expr. Purif. 9 (2): 153–8. doi:10.1006/prep.1996.0693. PMID 9056480. 
• Marinoni JC, Roy R, Vermeulen W et al. (1997). "Cloning and characterization of p52, the fifth subunit of the core of the transcription/DNA repair factor TFIIH". EMBO J. 16 (5): 1093–102. doi:10.1093/emboj/16.5.1093. PMC 1169708. PMID 9118947. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1169708. 
• Andersen G, Busso D, Poterszman A et al. (1997). "The structure of cyclin H: common mode of kinase activation and specific features". EMBO J. 16 (5): 958–67. doi:10.1093/emboj/16.5.958. PMC 1169696. PMID 9118957. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1169696.