CCNT1_MOUSE
ID CCNT1_MOUSE Reviewed; 724 AA.
AC Q9QWV9; Q3V0G4; Q9Z0U7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Cyclin-T1;
DE Short=CycT1;
DE Short=Cyclin-T;
GN Name=Ccnt1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=9843510; DOI=10.1093/emboj/17.23.7056;
RA Bieniasz P.D., Grdina T.A., Bogerd H.P., Cullen B.R.;
RT "Recruitment of a protein complex containing Tat and cyclin T1 to TAR
RT governs the species specificity of HIV-1 Tat.";
RL EMBO J. 17:7056-7065(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF TYR-261.
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF ARG-256; TYR-261; GLN-262;
RP MET-265 AND ASN-277.
RC TISSUE=Spleen;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS.
RC TISSUE=Fibroblast;
RX PubMed=9990016; DOI=10.1073/pnas.96.4.1285;
RA Fujinaga K., Taube R., Wimmer J., Cujec T.P., Peterlin B.M.;
RT "Interactions between human cyclin T, Tat, and the transactivation response
RT element (TAR) are disrupted by a cysteine to tyrosine substitution found in
RT mouse cyclin T.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1285-1290(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH TBX21 AND CDK9.
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).
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).
CC -!- SUBUNIT: Cyclin-T1 is the predominant cyclin that associates with CDK9
CC to form a heterodimer called P-TEFb (PubMed:27292648). P-TEFb forms a
CC complex with AFF4/AF5Q31. Component of a complex which is at least
CC composed of HTATSF1/Tat-SF1, P-TEFb complex, RNA pol II, SUPT5H, and
CC NCL/nucleolin. Component of the 7SK snRNP complex at least composed of
CC P-TEFb (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2, BCDIN3,
CC SART3 proteins and 7SK and U6 snRNAs. Interacts with BRD4, targets
CC chromatin binding. Interacts with JMJD6. Interacts with MDFIC.
CC Interacts with HSF1. Interacts with HTATSF1. Interacts with AFF4 (By
CC similarity). Interacts with TBX21 (PubMed:27292648).
CC {ECO:0000250|UniProtKB:O60563, ECO:0000269|PubMed:27292648}.
CC -!- INTERACTION:
CC Q9QWV9; Q91Y44: Brdt; NbExp=2; IntAct=EBI-2655009, EBI-6260929;
CC Q9QWV9; P28574: Max; NbExp=2; IntAct=EBI-2655009, EBI-1183003;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.
CC {ECO:0000305}.
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DR EMBL; AF095640; AAD13656.1; -; mRNA.
DR EMBL; AF109179; AAD19654.1; -; mRNA.
DR EMBL; AF087662; AAD17798.1; -; mRNA.
DR EMBL; AF113951; AAD17205.1; -; mRNA.
DR EMBL; AK133168; BAE21540.1; -; mRNA.
DR EMBL; AC138221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC131685; AAI31686.1; -; mRNA.
DR CCDS; CCDS27797.1; -.
DR RefSeq; NP_033963.1; NM_009833.1.
DR AlphaFoldDB; Q9QWV9; -.
DR SMR; Q9QWV9; -.
DR BioGRID; 198559; 5.
DR ComplexPortal; CPX-230; Positive transcription elongation factor B, CDK9-cyclinT1 complex.
DR CORUM; Q9QWV9; -.
DR IntAct; Q9QWV9; 6.
DR MINT; Q9QWV9; -.
DR STRING; 10090.ENSMUSP00000126874; -.
DR iPTMnet; Q9QWV9; -.
DR PhosphoSitePlus; Q9QWV9; -.
DR EPD; Q9QWV9; -.
DR MaxQB; Q9QWV9; -.
DR PaxDb; Q9QWV9; -.
DR PeptideAtlas; Q9QWV9; -.
DR PRIDE; Q9QWV9; -.
DR ProteomicsDB; 281342; -.
DR Antibodypedia; 1442; 300 antibodies from 38 providers.
DR DNASU; 12455; -.
DR Ensembl; ENSMUST00000012104; ENSMUSP00000012104; ENSMUSG00000011960.
DR Ensembl; ENSMUST00000169707; ENSMUSP00000126874; ENSMUSG00000011960.
DR GeneID; 12455; -.
DR KEGG; mmu:12455; -.
DR UCSC; uc007xmv.1; mouse.
DR CTD; 904; -.
DR MGI; MGI:1328363; Ccnt1.
DR VEuPathDB; HostDB:ENSMUSG00000011960; -.
DR eggNOG; KOG0834; Eukaryota.
DR GeneTree; ENSGT00940000159544; -.
DR HOGENOM; CLU_012994_1_0_1; -.
DR InParanoid; Q9QWV9; -.
DR OMA; PSMFEYR; -.
DR OrthoDB; 1437076at2759; -.
DR PhylomeDB; Q9QWV9; -.
DR TreeFam; TF101014; -.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR BioGRID-ORCS; 12455; 17 hits in 75 CRISPR screens.
DR ChiTaRS; Ccnt1; mouse.
DR PRO; PR:Q9QWV9; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9QWV9; protein.
DR Bgee; ENSMUSG00000011960; Expressed in rostral migratory stream and 251 other tissues.
DR ExpressionAtlas; Q9QWV9; baseline and differential.
DR Genevisible; Q9QWV9; MM.
DR GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0070691; C:P-TEFb complex; ISO:MGI.
DR GO; GO:0097322; F:7SK snRNA binding; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IDA:MGI.
DR GO; GO:0070063; F:RNA polymerase binding; ISO:MGI.
DR GO; GO:0017069; F:snRNA binding; IDA:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1900364; P:negative regulation of mRNA polyadenylation; ISO:MGI.
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; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
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:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00043; CYCLIN; 1.
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 Acetylation; Cell cycle; Cell division; Coiled coil; Cyclin;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..724
FT /note="Cyclin-T1"
FT /id="PRO_0000080493"
FT REGION 483..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..724
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"
FT /evidence="ECO:0000255"
FT COMPBIAS 483..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..529
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..724
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT MOD_RES 390
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT CROSSLNK 342
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT CROSSLNK 415
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT CROSSLNK 480
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT MUTAGEN 256
FT /note="R->W: No effect."
FT /evidence="ECO:0000269|PubMed:10329126"
FT MUTAGEN 261
FT /note="Y->C: Binding to HIV-1 Tat similar to human CCNT1."
FT /evidence="ECO:0000269|PubMed:10329126,
FT ECO:0000269|PubMed:9832504"
FT MUTAGEN 262
FT /note="Q->E: No effect."
FT /evidence="ECO:0000269|PubMed:10329126"
FT MUTAGEN 265
FT /note="M->K: No effect."
FT /evidence="ECO:0000269|PubMed:10329126"
FT MUTAGEN 277
FT /note="N->K: No effect."
FT /evidence="ECO:0000269|PubMed:10329126"
FT CONFLICT 48
FT /note="M -> V (in Ref. 3; AAD19654)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="S -> F (in Ref. 4; AAD17205)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 724 AA; 80598 MW; 6D090F5CA7C3A79C CRC64;
MEGERKNNNK RWYFTREQLE NSPSRRFGVD SDKELSYRQQ AANLLQDMGQ RLNVSQLTIN
TAIVYMHRFY MIQSFTQFHR YSMAPAALFL AAKVEEQPKK LEHVIKVAHT CLHPQESLPD
TRSEAYLQQV QDLVILESII LQTLGFELTI DHPHTHVVKC TQLVRASKDL AQTSYFMATN
SLHLTTFSLQ YTPPVVACVC IHLACKWSNW EIPVSTDGKH WWEYVDATVT LELLDELTHE
FLQILEKTPS RLKRIRNWRA YQAAMKTKPD DRGADENTSE QTILNMISQT SSDTTIAGLM
SMSTASTSAV PSLPSSEESS SSLTSVDMLQ GERWLSSQPP FKLEAAQGHR TSESLALIGV
DHSLQQDGSS AFGSQKQASK SVPSAKVSLK EYRAKHAEEL AAQKRQLENM EANVKSQYAY
AAQNLLSHDS HSSVILKMPI ESSENPERPF LDKADKSALK MRLPVASGDK AVSSKPEEIK
MRIKVHSAGD KHNSIEDSVT KSREHKEKQR THPSNHHHHH NHHSHRHSHL QLPAGPVSKR
PSDPKHSSQT STLAHKTYSL SSTLSSSSST RKRGPPEETG AAVFDHPAKI AKSTKSSLNF
PFPPLPTMTQ LPGHSSDTSG LPFSQPSCKT RVPHMKLDKG PPGANGHNAT QSIDYQDTVN
MLHSLLSAQG VQPTQAPAFE FVHSYGEYMN PRAGAISSRS GTTDKPRPPP LPSEPPPPLP
PLPK
