Cyclin T1

Cyclin T1
Rendering based on PDB 2PK2.
Available structures PDB 2PK2, 3BLH, 3BLQ, 3BLR, 3MI9, 3MIA, 3MY1
Identifiers
Symbols	CCNT1; CCNT; CYCT1; HIVE1
External IDs	OMIM: 143055 MGI: 1328363 HomoloGene: 947 GeneCards: CCNT1 Gene
Gene Ontology Molecular function • DNA binding • protein binding • snRNA binding • protein kinase binding Cellular component • nucleus • nucleoplasm • nucleoplasm • nucleolus Biological process • regulation of cyclin-dependent protein kinase activity • regulation of transcription, DNA-dependent • transcription from RNA polymerase II promoter • transcription elongation from RNA polymerase II promoter • protein phosphorylation • cell cycle • gene expression • viral reproduction • interspecies interaction between organisms • positive regulation of viral transcription • cell division Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	904	12455
Ensembl	ENSG00000129315	ENSMUSG00000011960
UniProt	O60563	Q3V0G4
RefSeq (mRNA)	NM_001240.2	NM_009833.1
RefSeq (protein)	NP_001231.2	NP_033963.1
Location (UCSC)	Chr 12: 49.09 – 49.11 Mb	Chr 15: 98.37 – 98.4 Mb
PubMed search	[1]	[2]

Cyclin-T1 is a protein that in humans is encoded by the CCNT1 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 tightly associates with CDK9 kinase, and was found to be a major subunit of the transcription elongation factor p-TEFb. The kinase complex containing this cyclin and the elongation factor can interact with, and act as a cofactor of human immunodeficiency virus type 1 (HIV-1) Tat protein, and was shown to be both necessary and sufficient for full activation of viral transcription. This cyclin and its kinase partner were also found to be involved in the phosphorylation and regulation of the carboxy-terminal domain (CTD) of the largest RNA polymerase II subunit.^[3]

Interactions

Cyclin T1 has been shown to interact with HEXIM1,^[4] Myc,^[5] Aryl hydrocarbon receptor,^[6] Granulin,^[7] NUFIP1,^[8] CDK9^{[2][4][7][8][9][10][11][12][13]} and Promyelocytic leukemia protein.^[14]

References

1. ^ Wei P, Garber ME, Fang SM, Fischer WH, Jones KA (Mar 1998). "A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA". Cell 92 (4): 451–62. doi:10.1016/S0092-8674(00)80939-3. PMID 9491887. 
2. ^ ^{a b} Peng J, Zhu Y, Milton JT, Price DH (Apr 1998). "Identification of multiple cyclin subunits of human P-TEFb". Genes Dev 12 (5): 755–62. doi:10.1101/gad.12.5.755. PMC 316581. PMID 9499409. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=316581. 
3. ^ "Entrez Gene: CCNT1 cyclin T1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=904. 
4. ^ ^{a b} Michels, Annemieke A; Nguyen Van Trung, Fraldi Alessandro, Labas Valérie, Edwards Mia, Bonnet François, Lania Luigi, Bensaude Olivier (Jul. 2003). "MAQ1 and 7SK RNA interact with CDK9/cyclin T complexes in a transcription-dependent manner". Mol. Cell. Biol. (United States) 23 (14): 4859–69. doi:10.1128/MCB.23.14.4859-4869.2003. ISSN 0270-7306. PMC 162212. PMID 12832472. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=162212. 
5. ^ Kanazawa, Satoshi; Soucek Laura, Evan Gerard, Okamoto Takashi, Peterlin B Matija (Aug. 2003). "c-Myc recruits P-TEFb for transcription, cellular proliferation and apoptosis". Oncogene (England) 22 (36): 5707–11. doi:10.1038/sj.onc.1206800. ISSN 0950-9232. PMID 12944920. 
6. ^ Tian, Yanan; Ke Sui, Chen Min, Sheng Tao (Nov. 2003). "Interactions between the aryl hydrocarbon receptor and P-TEFb. Sequential recruitment of transcription factors and differential phosphorylation of C-terminal domain of RNA polymerase II at cyp1a1 promoter". J. Biol. Chem. (United States) 278 (45): 44041–8. doi:10.1074/jbc.M306443200. ISSN 0021-9258. PMID 12917420. 
7. ^ ^{a b} Hoque, Mainul; Young Tara M, Lee Chee-Gun, Serrero Ginette, Mathews Michael B, Pe'ery Tsafi (Mar. 2003). "The growth factor granulin interacts with cyclin T1 and modulates P-TEFb-dependent transcription". Mol. Cell. Biol. (United States) 23 (5): 1688–702. doi:10.1128/MCB.23.5.1688-1702.2003. ISSN 0270-7306. PMC 151712. PMID 12588988. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=151712. 
8. ^ ^{a b} Cabart, Pavel; Chew Helen K, Murphy Shona (Jul. 2004). "BRCA1 cooperates with NUFIP and P-TEFb to activate transcription by RNA polymerase II". Oncogene (England) 23 (31): 5316–29. doi:10.1038/sj.onc.1207684. ISSN 0950-9232. PMID 15107825. 
9. ^ Young, Tara M; Wang Qi, Pe'ery Tsafi, Mathews Michael B (Sep. 2003). "The human I-mfa domain-containing protein, HIC, interacts with cyclin T1 and modulates P-TEFb-dependent transcription". Mol. Cell. Biol. (United States) 23 (18): 6373–84. doi:10.1128/MCB.23.18.6373-6384.2003. ISSN 0270-7306. PMC 193714. PMID 12944466. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=193714. 
10. ^ Kiernan, R E; Emiliani S, Nakayama K, Castro A, Labbé J C, Lorca T, Nakayama Ki K, Benkirane M (Dec. 2001). "Interaction between cyclin T1 and SCF(SKP2) targets CDK9 for ubiquitination and degradation by the proteasome". Mol. Cell. Biol. (United States) 21 (23): 7956–70. doi:10.1128/MCB.21.23.7956-7970.2001. ISSN 0270-7306. PMC 99964. PMID 11689688. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=99964. 
11. ^ De Falco, G; Bagella L, Claudio P P, De Luca A, Fu Y, Calabretta B, Sala A, Giordano A (Jan. 2000). "Physical interaction between CDK9 and B-Myb results in suppression of B-Myb gene autoregulation". Oncogene (ENGLAND) 19 (3): 373–9. doi:10.1038/sj.onc.1203305. ISSN 0950-9232. PMID 10656684. 
12. ^ Fu, T J; Peng J, Lee G, Price D H, Flores O (Dec. 1999). "Cyclin K functions as a CDK9 regulatory subunit and participates in RNA polymerase II transcription". J. Biol. Chem. (UNITED STATES) 274 (49): 34527–30. doi:10.1074/jbc.274.49.34527. ISSN 0021-9258. PMID 10574912. 
13. ^ 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. 
14. ^ Marcello, Alessandro; Ferrari Aldo, Pellegrini Vittorio, Pegoraro Gianluca, Lusic Marina, Beltram Fabio, Giacca Mauro (May. 2003). "Recruitment of human cyclin T1 to nuclear bodies through direct interaction with the PML protein". EMBO J. (England) 22 (9): 2156–66. doi:10.1093/emboj/cdg205. ISSN 0261-4189. PMC 156077. PMID 12727882. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=156077. 

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. 
• Romano G, Kasten M, De Falco G, et al. (2000). "Regulatory functions of Cdk9 and of cyclin T1 in HIV tat transactivation pathway gene expression.". J. Cell. Biochem. 75 (3): 357–68. doi:10.1002/(SICI)1097-4644(19991201)75:3<357::AID-JCB1>3.0.CO;2-K. PMID 10536359. 
• Cunningham AL, Li S, Juarez J, et al. (2000). "The level of HIV infection of macrophages is determined by interaction of viral and host cell genotypes.". J. Leukoc. Biol. 68 (3): 311–7. PMID 10985245. 
• Marcello A, Zoppé M, Giacca M (2002). "Multiple modes of transcriptional regulation by the HIV-1 Tat transactivator.". IUBMB Life 51 (3): 175–81. doi:10.1080/152165401753544241. PMID 11547919. 
• Huigen MC, Kamp W, Nottet HS (2004). "Multiple effects of HIV-1 trans-activator protein on the pathogenesis of HIV-1 infection.". Eur. J. Clin. Invest. 34 (1): 57–66. doi:10.1111/j.1365-2362.2004.01282.x. PMID 14984439. 
• Rice AP, Herrmann CH (2004). "Regulation of TAK/P-TEFb in CD4+ T lymphocytes and macrophages.". Curr. HIV Res. 1 (4): 395–404. doi:10.2174/1570162033485159. PMID 15049426. 
• Minghetti L, Visentin S, Patrizio M, et al. (2004). "Multiple actions of the human immunodeficiency virus type-1 Tat protein on microglial cell functions.". Neurochem. Res. 29 (5): 965–78. doi:10.1023/B:NERE.0000021241.90133.89. PMID 15139295. 
• Kino T, Pavlakis GN (2004). "Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1.". DNA Cell Biol. 23 (4): 193–205. doi:10.1089/104454904773819789. PMID 15142377. 
• Liou LY, Herrmann CH, Rice AP (2005). "HIV-1 infection and regulation of Tat function in macrophages.". Int. J. Biochem. Cell Biol. 36 (9): 1767–75. doi:10.1016/j.biocel.2004.02.018. PMID 15183343. 
• Pugliese A, Vidotto V, Beltramo T, et al. (2005). "A review of HIV-1 Tat protein biological effects.". Cell Biochem. Funct. 23 (4): 223–7. doi:10.1002/cbf.1147. PMID 15473004. 
• Bannwarth S, Gatignol A (2005). "HIV-1 TAR RNA: the target of molecular interactions between the virus and its host.". Curr. HIV Res. 3 (1): 61–71. doi:10.2174/1570162052772924. PMID 15638724. 
• Gibellini D, Vitone F, Schiavone P, Re MC (2005). "HIV-1 tat protein and cell proliferation and survival: a brief review.". New Microbiol. 28 (2): 95–109. PMID 16035254. 
• Peruzzi F (2006). "The multiple functions of HIV-1 Tat: proliferation versus apoptosis.". Front. Biosci. 11: 708–17. doi:10.2741/1829. PMID 16146763.