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Protein

Cyclin-T1

Gene

Ccnt1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin-T1) complex, also called positive transcription elongation factor B (P-TEFb), which is proposed to facilitate the transition from abortive to productive elongation by phosphorylating the CTD (carboxy-terminal domain) of the large subunit of RNA polymerase II (RNA Pol II).

GO - Molecular functioni

  • 7SK snRNA binding Source: UniProtKB
  • chromatin binding Source: MGI
  • DNA binding Source: MGI
  • RNA polymerase binding Source: MGI
  • snRNA binding Source: MGI
  • transcription regulatory region DNA binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-112382. Formation of RNA Pol II elongation complex.
R-MMU-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-MMU-674695. RNA Polymerase II Pre-transcription Events.
R-MMU-75955. RNA Polymerase II Transcription Elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-T1
Short name:
CycT1
Short name:
Cyclin-T
Gene namesi
Name:Ccnt1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1328363. Ccnt1.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • positive transcription elongation factor complex b Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi256 – 2561R → W: No effect. 1 Publication
Mutagenesisi261 – 2611Y → C: Binding to HIV-1 Tat similar to human CCNT1. 2 Publications
Mutagenesisi262 – 2621Q → E: No effect. 1 Publication
Mutagenesisi265 – 2651M → K: No effect. 1 Publication
Mutagenesisi277 – 2771N → K: No effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 724724Cyclin-T1PRO_0000080493Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei117 – 1171PhosphoserineBy similarity
Modified residuei390 – 3901N6-acetyllysineBy similarity
Modified residuei494 – 4941PhosphoserineBy similarity
Modified residuei498 – 4981PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9QWV9.
MaxQBiQ9QWV9.
PaxDbiQ9QWV9.
PRIDEiQ9QWV9.

PTM databases

PhosphoSiteiQ9QWV9.

Expressioni

Gene expression databases

CleanExiMM_CCNT1.
ExpressionAtlasiQ9QWV9. baseline and differential.
GenevisibleiQ9QWV9. MM.

Interactioni

Subunit structurei

Cyclin-T1 is the predominant cyclin that associates with CDK9, therby forming a heterodimer called P-TEFb. P-TEFb forms a complex with AFF4/AF5Q31. Component of a complex which is at least composed of HTATSF1/Tat-SF1, P-TEFb complex, RNA pol II, SUPT5H, and NCL/nucleolin. Interacts with MDFIC (By similarity). Component of the 7SK snRNP complex at least composed of P-TEFb (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2, BCDIN3, SART3 proteins and 7SK and U6 snRNAs. Interacts with BRD4, probably to target chromatin binding (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
BrdtQ91Y442EBI-2655009,EBI-6260929
MaxP285742EBI-2655009,EBI-1183003

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198559. 1 interaction.
IntActiQ9QWV9. 7 interactions.
MINTiMINT-4090105.
STRINGi10090.ENSMUSP00000012104.

Structurei

3D structure databases

ProteinModelPortaliQ9QWV9.
SMRiQ9QWV9. Positions 7-252.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili384 – 42542Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi253 – 27018Nuclear localization signalSequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi319 – 3224Poly-Ser
Compositional biasi505 – 52925His-richAdd
BLAST
Compositional biasi565 – 5695Poly-Ser
Compositional biasi706 – 72318Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the cyclin family. Cyclin C subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0834. Eukaryota.
COG5333. LUCA.
GeneTreeiENSGT00760000119191.
HOGENOMiHOG000013208.
HOVERGENiHBG050843.
InParanoidiQ9QWV9.
KOiK15188.
OMAiFELTIDH.
OrthoDBiEOG7VQJCR.
PhylomeDBiQ9QWV9.
TreeFamiTF101014.

Family and domain databases

Gene3Di1.10.472.10. 1 hit.
InterProiIPR028863. CCNT1.
IPR013763. Cyclin-like.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERiPTHR10026:SF42. PTHR10026:SF42. 3 hits.
PfamiPF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.

Sequencei

Sequence statusi: Complete.

Q9QWV9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGERKNNNK RWYFTREQLE NSPSRRFGVD SDKELSYRQQ AANLLQDMGQ
60 70 80 90 100
RLNVSQLTIN TAIVYMHRFY MIQSFTQFHR YSMAPAALFL AAKVEEQPKK
110 120 130 140 150
LEHVIKVAHT CLHPQESLPD TRSEAYLQQV QDLVILESII LQTLGFELTI
160 170 180 190 200
DHPHTHVVKC TQLVRASKDL AQTSYFMATN SLHLTTFSLQ YTPPVVACVC
210 220 230 240 250
IHLACKWSNW EIPVSTDGKH WWEYVDATVT LELLDELTHE FLQILEKTPS
260 270 280 290 300
RLKRIRNWRA YQAAMKTKPD DRGADENTSE QTILNMISQT SSDTTIAGLM
310 320 330 340 350
SMSTASTSAV PSLPSSEESS SSLTSVDMLQ GERWLSSQPP FKLEAAQGHR
360 370 380 390 400
TSESLALIGV DHSLQQDGSS AFGSQKQASK SVPSAKVSLK EYRAKHAEEL
410 420 430 440 450
AAQKRQLENM EANVKSQYAY AAQNLLSHDS HSSVILKMPI ESSENPERPF
460 470 480 490 500
LDKADKSALK MRLPVASGDK AVSSKPEEIK MRIKVHSAGD KHNSIEDSVT
510 520 530 540 550
KSREHKEKQR THPSNHHHHH NHHSHRHSHL QLPAGPVSKR PSDPKHSSQT
560 570 580 590 600
STLAHKTYSL SSTLSSSSST RKRGPPEETG AAVFDHPAKI AKSTKSSLNF
610 620 630 640 650
PFPPLPTMTQ LPGHSSDTSG LPFSQPSCKT RVPHMKLDKG PPGANGHNAT
660 670 680 690 700
QSIDYQDTVN MLHSLLSAQG VQPTQAPAFE FVHSYGEYMN PRAGAISSRS
710 720
GTTDKPRPPP LPSEPPPPLP PLPK
Length:724
Mass (Da):80,598
Last modified:October 3, 2012 - v3
Checksum:i6D090F5CA7C3A79C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481M → V in AAD19654 (PubMed:10329126).Curated
Sequence conflicti567 – 5671S → F in AAD17205 (PubMed:9990016).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF095640 mRNA. Translation: AAD13656.1.
AF109179 mRNA. Translation: AAD19654.1.
AF087662 mRNA. Translation: AAD17798.1.
AF113951 mRNA. Translation: AAD17205.1.
AK133168 mRNA. Translation: BAE21540.1.
AC138221 Genomic DNA. No translation available.
BC131685 mRNA. Translation: AAI31686.1.
CCDSiCCDS27797.1.
RefSeqiNP_033963.1. NM_009833.1.
UniGeneiMm.29941.
Mm.86538.

Genome annotation databases

EnsembliENSMUST00000012104; ENSMUSP00000012104; ENSMUSG00000011960.
ENSMUST00000169707; ENSMUSP00000126874; ENSMUSG00000011960.
GeneIDi12455.
KEGGimmu:12455.
UCSCiuc007xmv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF095640 mRNA. Translation: AAD13656.1.
AF109179 mRNA. Translation: AAD19654.1.
AF087662 mRNA. Translation: AAD17798.1.
AF113951 mRNA. Translation: AAD17205.1.
AK133168 mRNA. Translation: BAE21540.1.
AC138221 Genomic DNA. No translation available.
BC131685 mRNA. Translation: AAI31686.1.
CCDSiCCDS27797.1.
RefSeqiNP_033963.1. NM_009833.1.
UniGeneiMm.29941.
Mm.86538.

3D structure databases

ProteinModelPortaliQ9QWV9.
SMRiQ9QWV9. Positions 7-252.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198559. 1 interaction.
IntActiQ9QWV9. 7 interactions.
MINTiMINT-4090105.
STRINGi10090.ENSMUSP00000012104.

PTM databases

PhosphoSiteiQ9QWV9.

Proteomic databases

EPDiQ9QWV9.
MaxQBiQ9QWV9.
PaxDbiQ9QWV9.
PRIDEiQ9QWV9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000012104; ENSMUSP00000012104; ENSMUSG00000011960.
ENSMUST00000169707; ENSMUSP00000126874; ENSMUSG00000011960.
GeneIDi12455.
KEGGimmu:12455.
UCSCiuc007xmv.1. mouse.

Organism-specific databases

CTDi904.
MGIiMGI:1328363. Ccnt1.

Phylogenomic databases

eggNOGiKOG0834. Eukaryota.
COG5333. LUCA.
GeneTreeiENSGT00760000119191.
HOGENOMiHOG000013208.
HOVERGENiHBG050843.
InParanoidiQ9QWV9.
KOiK15188.
OMAiFELTIDH.
OrthoDBiEOG7VQJCR.
PhylomeDBiQ9QWV9.
TreeFamiTF101014.

Enzyme and pathway databases

ReactomeiR-MMU-112382. Formation of RNA Pol II elongation complex.
R-MMU-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-MMU-674695. RNA Polymerase II Pre-transcription Events.
R-MMU-75955. RNA Polymerase II Transcription Elongation.

Miscellaneous databases

ChiTaRSiCcnt1. mouse.
NextBioi281302.
PROiQ9QWV9.
SOURCEiSearch...

Gene expression databases

CleanExiMM_CCNT1.
ExpressionAtlasiQ9QWV9. baseline and differential.
GenevisibleiQ9QWV9. MM.

Family and domain databases

Gene3Di1.10.472.10. 1 hit.
InterProiIPR028863. CCNT1.
IPR013763. Cyclin-like.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERiPTHR10026:SF42. PTHR10026:SF42. 3 hits.
PfamiPF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Recruitment of a protein complex containing Tat and cyclin T1 to TAR governs the species specificity of HIV-1 Tat."
    Bieniasz P.D., Grdina T.A., Bogerd H.P., Cullen B.R.
    EMBO J. 17:7056-7065(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
  2. "The interaction between HIV-1 Tat and human cyclin T1 requires zinc and a critical cysteine residue that is not conserved in the murine CycT1 protein."
    Garber M.E., Wei P., KewalRamani V.N., Mayall T.P., Herrmann C.H., Rice A.P., Littman D.R., Jones K.A.
    Genes Dev. 12:3512-3527(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF TYR-261.
    Strain: C57BL/6J.
    Tissue: Brain.
  3. "Role of the human and murine cyclin T proteins in regulating HIV-1 Tat-activation."
    Kwak Y.T., Ivanov D., Guo J., Nee E., Gaynor R.B.
    J. Mol. Biol. 288:57-69(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF ARG-256; TYR-261; GLN-262; MET-265 AND ASN-277.
    Tissue: Spleen.
  4. "Interactions between human cyclin T, Tat, and the transactivation response element (TAR) are disrupted by a cysteine to tyrosine substitution found in mouse cyclin T."
    Fujinaga K., Taube R., Wimmer J., Cujec T.P., Peterlin B.M.
    Proc. Natl. Acad. Sci. U.S.A. 96:1285-1290(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS.
    Tissue: Fibroblast.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Testis.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiCCNT1_MOUSE
AccessioniPrimary (citable) accession number: Q9QWV9
Secondary accession number(s): Q3V0G4, Q9Z0U7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 3, 2012
Last modified: May 11, 2016
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.