CCNT1_HUMAN
ID CCNT1_HUMAN Reviewed; 726 AA.
AC O60563; A9XU13; E7EX76; O60581;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Cyclin-T1;
DE Short=CycT1;
DE Short=Cyclin-T;
GN Name=CCNT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION).
RC TISSUE=T-cell lymphoma;
RX PubMed=9491887; DOI=10.1016/s0092-8674(00)80939-3;
RA Wei P., Garber M.E., Fang S.-M., Fischer W.H., Jones K.A.;
RT "A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat
RT and mediates its high-affinity, loop-specific binding to TAR RNA.";
RL Cell 92:451-462(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Mammary cancer;
RX PubMed=9499409; DOI=10.1101/gad.12.5.755;
RA Peng J.-M., Zhu Y., Milton J.T., Price D.H.;
RT "Identification of multiple cyclin subunits of human P-TEFb.";
RL Genes Dev. 12:755-762(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Wu X., Liu Q., Guo D.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP IDENTIFICATION IN A COMPLEX WITH HTATSF1; CDK9; RNA POL II; SUPT5H AND NCL.
RX PubMed=10393184; DOI=10.1093/emboj/18.13.3688;
RA Parada C.A., Roeder R.G.;
RT "A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-
RT 1 transcription.";
RL EMBO J. 18:3688-3701(1999).
RN [6]
RP INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION), AND FUNCTION (MICROBIAL
RP INFECTION).
RX PubMed=10329125; DOI=10.1006/jmbi.1999.2663;
RA Ivanov D., Kwak Y.T., Nee E., Guo J., Garcia-Martinez L.F., Gaynor R.B.;
RT "Cyclin T1 domains involved in complex formation with Tat and TAR RNA are
RT critical for tat-activation.";
RL J. Mol. Biol. 288:41-56(1999).
RN [7]
RP MUTAGENESIS OF CYS-261, FUNCTION (MICROBIAL INFECTION), AND INTERACTION
RP WITH HIV-1 TAT (MICROBIAL INFECTION).
RX PubMed=10329126; DOI=10.1006/jmbi.1999.2664;
RA Kwak Y.T., Ivanov D., Guo J., Nee E., Gaynor R.B.;
RT "Role of the human and murine cyclin T proteins in regulating HIV-1 Tat-
RT activation.";
RL J. Mol. Biol. 288:57-69(1999).
RN [8]
RP INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION), AND ROLE OF CYS-261.
RX PubMed=9832504; DOI=10.1101/gad.12.22.3512;
RA Garber M.E., Wei P., KewalRamani V.N., Mayall T.P., Herrmann C.H.,
RA Rice A.P., Littman D.R., Jones K.A.;
RT "The interaction between HIV-1 Tat and human cyclin T1 requires zinc and a
RT critical cysteine residue that is not conserved in the murine CycT1
RT protein.";
RL Genes Dev. 12:3512-3527(1998).
RN [9]
RP INTERACTION WITH HIV-1 TAT; HIV-2 TAT AND SIV TAT (MICROBIAL INFECTION).
RX PubMed=10364329; DOI=10.1128/jvi.73.7.5777-5786.1999;
RA Bieniasz P.D., Grdina T.A., Bogerd H.P., Cullen B.R.;
RT "Analysis of the effect of natural sequence variation in Tat and in cyclin
RT T on the formation and RNA binding properties of Tat-cyclin T complexes.";
RL J. Virol. 73:5777-5786(1999).
RN [10]
RP INTERACTION WITH HTATSF1.
RX PubMed=10913173; DOI=10.1128/mcb.20.16.5897-5907.2000;
RA Fong Y.W., Zhou Q.;
RT "Relief of two built-In autoinhibitory mechanisms in P-TEFb is required for
RT assembly of a multicomponent transcription elongation complex at the human
RT immunodeficiency virus type 1 promoter.";
RL Mol. Cell. Biol. 20:5897-5907(2000).
RN [11]
RP INTERACTION WITH AFF4.
RX PubMed=12065898; DOI=10.1007/bf02256070;
RA Estable M.C., Naghavi M.H., Kato H., Xiao H., Qin J., Vahlne A.,
RA Roeder R.G.;
RT "MCEF, the newest member of the AF4 family of transcription factors
RT involved in leukemia, is a positive transcription elongation factor-b-
RT associated protein.";
RL J. Biomed. Sci. 9:234-245(2002).
RN [12]
RP INTERACTION WITH MDFIC, AND SUBCELLULAR LOCATION.
RX PubMed=12944466; DOI=10.1128/mcb.23.18.6373-6384.2003;
RA Young T.M., Wang Q., Pe'ery T., Mathews M.B.;
RT "The human I-mfa domain-containing protein, HIC, interacts with cyclin T1
RT and modulates P-TEFb-dependent transcription.";
RL Mol. Cell. Biol. 23:6373-6384(2003).
RN [13]
RP CHARACTERIZATION.
RX PubMed=14972556; DOI=10.1016/j.virol.2003.10.003;
RA Das C., Edgcomb S.P., Peteranderl R., Chen L., Frankel A.D.;
RT "Evidence for conformational flexibility in the Tat-TAR recognition motif
RT of cyclin T1.";
RL Virology 318:306-317(2004).
RN [14]
RP FUNCTION, AND INTERACTION WITH BRD4.
RX PubMed=16109376; DOI=10.1016/j.molcel.2005.06.027;
RA Jang M.K., Mochizuki K., Zhou M., Jeong H.S., Brady J.N., Ozato K.;
RT "The bromodomain protein Brd4 is a positive regulatory component of P-TEFb
RT and stimulates RNA polymerase II-dependent transcription.";
RL Mol. Cell 19:523-534(2005).
RN [15]
RP FUNCTION, AND INTERACTION WITH BRD4.
RX PubMed=16109377; DOI=10.1016/j.molcel.2005.06.029;
RA Yang Z., Yik J.H., Chen R., He N., Jang M.K., Ozato K., Zhou Q.;
RT "Recruitment of P-TEFb for stimulation of transcriptional elongation by the
RT bromodomain protein Brd4.";
RL Mol. Cell 19:535-545(2005).
RN [16]
RP IDENTIFICATION IN THE 7SK SNRNP COMPLEX.
RX PubMed=17643375; DOI=10.1016/j.molcel.2007.06.027;
RA Jeronimo C., Forget D., Bouchard A., Li Q., Chua G., Poitras C.,
RA Therien C., Bergeron D., Bourassa S., Greenblatt J., Chabot B.,
RA Poirier G.G., Hughes T.R., Blanchette M., Price D.H., Coulombe B.;
RT "Systematic analysis of the protein interaction network for the human
RT transcription machinery reveals the identity of the 7SK capping enzyme.";
RL Mol. Cell 27:262-274(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495 AND SER-577, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117 AND SER-340, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-390, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP INTERACTION WITH BRD4 AND JMJD6.
RX PubMed=24360279; DOI=10.1016/j.cell.2013.10.056;
RA Liu W., Ma Q., Wong K., Li W., Ohgi K., Zhang J., Aggarwal A.,
RA Rosenfeld M.G.;
RT "Brd4 and JMJD6-associated anti-pause enhancers in regulation of
RT transcriptional pause release.";
RL Cell 155:1581-1595(2013).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340; SER-388; SER-564 AND
RP SER-577, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [24]
RP INTERACTION WITH TBX21.
RX PubMed=27292648; DOI=10.1016/j.celrep.2016.05.054;
RA Hertweck A., Evans C.M., Eskandarpour M., Lau J.C., Oleinika K.,
RA Jackson I., Kelly A., Ambrose J., Adamson P., Cousins D.J., Lavender P.,
RA Calder V.L., Lord G.M., Jenner R.G.;
RT "T-bet activates Th1 genes through mediator and the super elongation
RT complex.";
RL Cell Rep. 15:2756-2770(2016).
RN [25]
RP INTERACTION WITH HSF1.
RX PubMed=27189267; DOI=10.1038/srep26294;
RA Pan X.Y., Zhao W., Zeng X.Y., Lin J., Li M.M., Shen X.T., Liu S.W.;
RT "Heat shock factor 1 mediates latent HIV reactivation.";
RL Sci. Rep. 6:26294-26294(2016).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-342; LYS-415 AND LYS-481, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [27]
RP VARIANT CYS-541.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
CC -!- FUNCTION: Regulatory subunit of the cyclin-dependent kinase pair
CC (CDK9/cyclin-T1) complex, also called positive transcription elongation
CC factor B (P-TEFb), which is proposed to facilitate the transition from
CC abortive to productive elongation by phosphorylating the CTD (C-
CC terminal domain) of the large subunit of RNA polymerase II (RNA Pol
CC II). {ECO:0000269|PubMed:16109376, ECO:0000269|PubMed:16109377}.
CC -!- FUNCTION: (Microbial infection) In case of HIV or SIV infections, binds
CC to the transactivation domain of the viral nuclear transcriptional
CC activator, Tat, thereby increasing Tat's affinity for the
CC transactivating response RNA element (TAR RNA). Serves as an essential
CC cofactor for Tat, by promoting RNA Pol II activation, allowing
CC transcription of viral genes. {ECO:0000269|PubMed:10329125,
CC ECO:0000269|PubMed:10329126}.
CC -!- SUBUNIT: Cyclin-T1 is the predominant cyclin that associates with CDK9
CC to form a heterodimer called P-TEFb. P-TEFb forms a complex with
CC AFF4/AF5Q31. Component of a complex which is at least composed of
CC HTATSF1/Tat-SF1, P-TEFb complex, RNA pol II, SUPT5H, and NCL/nucleolin
CC (PubMed:10393184). Component of the 7SK snRNP complex at least composed
CC of P-TEFb (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2,
CC BCDIN3, SART3 proteins and 7SK and U6 snRNAs (PubMed:17643375).
CC Interacts with BRD4, targets chromatin binding (PubMed:16109376,
CC PubMed:16109377, PubMed:24360279). Interacts with JMJD6
CC (PubMed:24360279). Interacts with MDFIC (PubMed:12944466). Interacts
CC with HSF1 (PubMed:27189267). Interacts with HTATSF1 (PubMed:10913173).
CC Interacts with AFF4 (PubMed:12065898). Interacts with TBX21
CC (PubMed:27292648). {ECO:0000269|PubMed:10393184,
CC ECO:0000269|PubMed:10913173, ECO:0000269|PubMed:12065898,
CC ECO:0000269|PubMed:12944466, ECO:0000269|PubMed:16109376,
CC ECO:0000269|PubMed:16109377, ECO:0000269|PubMed:17643375,
CC ECO:0000269|PubMed:24360279, ECO:0000269|PubMed:27189267,
CC ECO:0000269|PubMed:27292648}.
CC -!- SUBUNIT: (Microbial infection) Interacts with the transactivation
CC region of HIV-1, HIV-2 and SIV Tat. {ECO:0000269|PubMed:10329125,
CC ECO:0000269|PubMed:10329126, ECO:0000269|PubMed:10364329,
CC ECO:0000269|PubMed:9491887, ECO:0000269|PubMed:9832504}.
CC -!- INTERACTION:
CC O60563; Q9UHB7: AFF4; NbExp=6; IntAct=EBI-2479671, EBI-395282;
CC O60563; O60885-1: BRD4; NbExp=6; IntAct=EBI-2479671, EBI-9345088;
CC O60563; P50750: CDK9; NbExp=26; IntAct=EBI-2479671, EBI-1383449;
CC O60563; O94992: HEXIM1; NbExp=10; IntAct=EBI-2479671, EBI-2832510;
CC O60563; P04608: tat; Xeno; NbExp=9; IntAct=EBI-2479671, EBI-6164389;
CC O60563; P04610: tat; Xeno; NbExp=2; IntAct=EBI-2479671, EBI-7845069;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12944466}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60563-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60563-2; Sequence=VSP_054569, VSP_054570;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- MISCELLANEOUS: Interaction between Tat and cyclin-T1 requires zinc.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.
CC {ECO:0000305}.
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DR EMBL; AF045161; AAC39638.1; -; mRNA.
DR EMBL; AF048730; AAC39664.1; -; mRNA.
DR EMBL; EF688064; ABV58572.1; -; mRNA.
DR EMBL; AC079951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS61109.1; -. [O60563-2]
DR CCDS; CCDS8766.1; -. [O60563-1]
DR RefSeq; NP_001231.2; NM_001240.3. [O60563-1]
DR RefSeq; NP_001264771.1; NM_001277842.1. [O60563-2]
DR PDB; 2PK2; X-ray; 2.67 A; A/B/C/D=1-281.
DR PDB; 3BLH; X-ray; 2.48 A; B=2-259.
DR PDB; 3BLQ; X-ray; 2.90 A; B=2-259.
DR PDB; 3BLR; X-ray; 2.80 A; B=2-259.
DR PDB; 3LQ5; X-ray; 3.00 A; B=2-259.
DR PDB; 3MI9; X-ray; 2.10 A; B=1-266.
DR PDB; 3MIA; X-ray; 3.00 A; B=1-266.
DR PDB; 3MY1; X-ray; 2.80 A; B=2-259.
DR PDB; 3TN8; X-ray; 2.95 A; B=2-259.
DR PDB; 3TNH; X-ray; 3.20 A; B=1-259.
DR PDB; 3TNI; X-ray; 3.23 A; B=1-259.
DR PDB; 4BCF; X-ray; 3.01 A; B=2-259.
DR PDB; 4BCG; X-ray; 3.08 A; B=2-259.
DR PDB; 4BCH; X-ray; 2.96 A; B=2-259.
DR PDB; 4BCI; X-ray; 3.10 A; B=2-259.
DR PDB; 4BCJ; X-ray; 3.16 A; B=2-259.
DR PDB; 4EC8; X-ray; 3.60 A; B=2-259.
DR PDB; 4EC9; X-ray; 3.21 A; B=2-259.
DR PDB; 4IMY; X-ray; 2.94 A; B/D/F=1-264.
DR PDB; 4OGR; X-ray; 3.00 A; B/F/K=1-264.
DR PDB; 4OR5; X-ray; 2.90 A; B/G=1-266.
DR PDB; 5L1Z; X-ray; 5.90 A; B=1-264.
DR PDB; 6CYT; X-ray; 3.50 A; B=1-264.
DR PDB; 6GZH; X-ray; 3.17 A; B=1-726.
DR PDB; 6W9E; X-ray; 3.10 A; B=1-259.
DR PDB; 6Z45; X-ray; 3.37 A; B=2-259.
DR PDB; 7NWK; X-ray; 2.81 A; B=2-259.
DR PDBsum; 2PK2; -.
DR PDBsum; 3BLH; -.
DR PDBsum; 3BLQ; -.
DR PDBsum; 3BLR; -.
DR PDBsum; 3LQ5; -.
DR PDBsum; 3MI9; -.
DR PDBsum; 3MIA; -.
DR PDBsum; 3MY1; -.
DR PDBsum; 3TN8; -.
DR PDBsum; 3TNH; -.
DR PDBsum; 3TNI; -.
DR PDBsum; 4BCF; -.
DR PDBsum; 4BCG; -.
DR PDBsum; 4BCH; -.
DR PDBsum; 4BCI; -.
DR PDBsum; 4BCJ; -.
DR PDBsum; 4EC8; -.
DR PDBsum; 4EC9; -.
DR PDBsum; 4IMY; -.
DR PDBsum; 4OGR; -.
DR PDBsum; 4OR5; -.
DR PDBsum; 5L1Z; -.
DR PDBsum; 6CYT; -.
DR PDBsum; 6GZH; -.
DR PDBsum; 6W9E; -.
DR PDBsum; 6Z45; -.
DR PDBsum; 7NWK; -.
DR AlphaFoldDB; O60563; -.
DR SMR; O60563; -.
DR BioGRID; 107343; 217.
DR ComplexPortal; CPX-222; Positive transcription elongation factor B, CDK9-cyclinT1 complex.
DR CORUM; O60563; -.
DR DIP; DIP-29891N; -.
DR IntAct; O60563; 101.
DR MINT; O60563; -.
DR STRING; 9606.ENSP00000261900; -.
DR BindingDB; O60563; -.
DR ChEMBL; CHEMBL2108; -.
DR iPTMnet; O60563; -.
DR PhosphoSitePlus; O60563; -.
DR BioMuta; CCNT1; -.
DR EPD; O60563; -.
DR jPOST; O60563; -.
DR MassIVE; O60563; -.
DR MaxQB; O60563; -.
DR PaxDb; O60563; -.
DR PeptideAtlas; O60563; -.
DR PRIDE; O60563; -.
DR ProteomicsDB; 2517; -.
DR ProteomicsDB; 49468; -. [O60563-1]
DR ABCD; O60563; 6 sequenced antibodies.
DR Antibodypedia; 1442; 300 antibodies from 38 providers.
DR DNASU; 904; -.
DR Ensembl; ENST00000261900.8; ENSP00000261900.3; ENSG00000129315.11. [O60563-1]
DR Ensembl; ENST00000417344.2; ENSP00000399845.2; ENSG00000129315.11. [O60563-2]
DR Ensembl; ENST00000618666.4; ENSP00000481035.1; ENSG00000129315.11. [O60563-2]
DR GeneID; 904; -.
DR KEGG; hsa:904; -.
DR MANE-Select; ENST00000261900.8; ENSP00000261900.3; NM_001240.4; NP_001231.2.
DR UCSC; uc001rsd.5; human. [O60563-1]
DR CTD; 904; -.
DR DisGeNET; 904; -.
DR GeneCards; CCNT1; -.
DR HGNC; HGNC:1599; CCNT1.
DR HPA; ENSG00000129315; Low tissue specificity.
DR MIM; 143055; gene.
DR neXtProt; NX_O60563; -.
DR OpenTargets; ENSG00000129315; -.
DR PharmGKB; PA26163; -.
DR VEuPathDB; HostDB:ENSG00000129315; -.
DR eggNOG; KOG0834; Eukaryota.
DR GeneTree; ENSGT00940000159544; -.
DR HOGENOM; CLU_022000_4_2_1; -.
DR InParanoid; O60563; -.
DR OMA; PSMFEYR; -.
DR OrthoDB; 1437076at2759; -.
DR PhylomeDB; O60563; -.
DR TreeFam; TF101014; -.
DR PathwayCommons; O60563; -.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
DR Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
DR Reactome; R-HSA-167238; Pausing and recovery of Tat-mediated HIV elongation.
DR Reactome; R-HSA-167243; Tat-mediated HIV elongation arrest and recovery.
DR Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
DR Reactome; R-HSA-167287; HIV elongation arrest and recovery.
DR Reactome; R-HSA-167290; Pausing and recovery of HIV elongation.
DR Reactome; R-HSA-176034; Interactions of Tat with host cellular proteins.
DR Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR SignaLink; O60563; -.
DR SIGNOR; O60563; -.
DR BioGRID-ORCS; 904; 34 hits in 1094 CRISPR screens.
DR ChiTaRS; CCNT1; human.
DR EvolutionaryTrace; O60563; -.
DR GeneWiki; Cyclin_T1; -.
DR GenomeRNAi; 904; -.
DR Pharos; O60563; Tchem.
DR PRO; PR:O60563; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O60563; protein.
DR Bgee; ENSG00000129315; Expressed in sperm and 193 other tissues.
DR ExpressionAtlas; O60563; baseline and differential.
DR Genevisible; O60563; HS.
DR GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070691; C:P-TEFb complex; IDA:FlyBase.
DR GO; GO:0097322; F:7SK snRNA binding; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IBA:GO_Central.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0070063; F:RNA polymerase binding; IPI:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1903655; P:phosphorylation of RNA polymerase II C-terminal domain serine 2 residues involved in positive regulation of transcription elongation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:1903654; P:phosphorylation of RNA polymerase II C-terminal domain serine 5 residues involved in positive regulation of transcription elongation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; IDA:ComplexPortal.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR CDD; cd00043; CYCLIN; 1.
DR DisProt; DP01462; -.
DR InterPro; IPR028863; CCNT1.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR043198; Cyclin/Ssn8.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10026; PTHR10026; 1.
DR PANTHER; PTHR10026:SF42; PTHR10026:SF42; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Coiled coil; Cyclin; Direct protein sequencing; Host-virus interaction;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..726
FT /note="Cyclin-T1"
FT /id="PRO_0000080491"
FT REGION 360..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 384..425
FT /evidence="ECO:0000255"
FT MOTIF 253..270
FT /note="Nuclear localization signal, and interaction with
FT Tat-TAR RNA"
FT /evidence="ECO:0000255"
FT COMPBIAS 487..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..530
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..726
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 261
FT /note="Essential for interacting with HIV-1 Tat"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 390
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 577
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 342
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 415
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 481
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 181..184
FT /note="SLHL -> RTDT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_054569"
FT VAR_SEQ 185..726
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_054570"
FT VARIANT 362
FT /note="H -> R (in dbSNP:rs17123261)"
FT /id="VAR_053054"
FT VARIANT 541
FT /note="R -> C (in dbSNP:rs201951577)"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_069400"
FT MUTAGEN 261
FT /note="C->Y: Loss of HIV-1 Tat transactivation."
FT /evidence="ECO:0000269|PubMed:10329126"
FT CONFLICT 77
FT /note="Q -> R (in Ref. 2; AAC39664)"
FT /evidence="ECO:0000305"
FT TURN 8..12
FT /evidence="ECO:0007829|PDB:3MI9"
FT HELIX 16..20
FT /evidence="ECO:0007829|PDB:3MI9"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:3MI9"
FT HELIX 31..52
FT /evidence="ECO:0007829|PDB:3MI9"
FT HELIX 56..69
FT /evidence="ECO:0007829|PDB:3MI9"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:3MI9"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:3MI9"
FT HELIX 80..94
FT /evidence="ECO:0007829|PDB:3MI9"
FT HELIX 101..112
FT /evidence="ECO:0007829|PDB:3MI9"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:3MI9"
FT HELIX 124..143
FT /evidence="ECO:0007829|PDB:3MI9"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:3MI9"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:3MI9"
FT HELIX 168..184
FT /evidence="ECO:0007829|PDB:3MI9"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:3MI9"
FT HELIX 193..207
FT /evidence="ECO:0007829|PDB:3MI9"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:2PK2"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:3MI9"
FT HELIX 231..246
FT /evidence="ECO:0007829|PDB:3MI9"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:3MI9"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:3BLH"
FT TURN 258..262
FT /evidence="ECO:0007829|PDB:2PK2"
SQ SEQUENCE 726 AA; 80685 MW; 4637EFB2DDEDFE13 CRC64;
MEGERKNNNK RWYFTREQLE NSPSRRFGVD PDKELSYRQQ AANLLQDMGQ RLNVSQLTIN
TAIVYMHRFY MIQSFTQFPG NSVAPAALFL AAKVEEQPKK LEHVIKVAHT CLHPQESLPD
TRSEAYLQQV QDLVILESII LQTLGFELTI DHPHTHVVKC TQLVRASKDL AQTSYFMATN
SLHLTTFSLQ YTPPVVACVC IHLACKWSNW EIPVSTDGKH WWEYVDATVT LELLDELTHE
FLQILEKTPN RLKRIWNWRA CEAAKKTKAD DRGTDEKTSE QTILNMISQS SSDTTIAGLM
SMSTSTTSAV PSLPVSEESS SNLTSVEMLP GKRWLSSQPS FKLEPTQGHR TSENLALTGV
DHSLPQDGSN AFISQKQNSK SVPSAKVSLK EYRAKHAEEL AAQKRQLENM EANVKSQYAY
AAQNLLSHHD SHSSVILKMP IEGSENPERP FLEKADKTAL KMRIPVAGGD KAASSKPEEI
KMRIKVHAAA DKHNSVEDSV TKSREHKEKH KTHPSNHHHH HNHHSHKHSH SQLPVGTGNK
RPGDPKHSSQ TSNLAHKTYS LSSSFSSSSS TRKRGPSEET GGAVFDHPAK IAKSTKSSSL
NFSFPSLPTM GQMPGHSSDT SGLSFSQPSC KTRVPHSKLD KGPTGANGHN TTQTIDYQDT
VNMLHSLLSA QGVQPTQPTA FEFVRPYSDY LNPRSGGISS RSGNTDKPRP PPLPSEPPPP
LPPLPK
