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O60563

- CCNT1_HUMAN

UniProt

O60563 - CCNT1_HUMAN

Protein

Cyclin-T1

Gene

CCNT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    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). In case of HIV or SIV infections, binds to the transactivation domain of the viral nuclear transcriptional activator, Tat, thereby increasing Tat's affinity for the transactivating response RNA element (TAR RNA). Serves as an essential cofactor for Tat, by promoting RNA Pol II activation, allowing transcription of viral genes.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei261 – 2611Essential for interacting with HIV-1 Tat

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. DNA binding Source: MGI
    3. protein binding Source: UniProtKB
    4. snRNA binding Source: Ensembl
    5. transcription regulatory region DNA binding Source: Ensembl

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell division Source: UniProtKB-KW
    3. gene expression Source: Reactome
    4. positive regulation of transcription from RNA polymerase II promoter Source: Reactome
    5. positive regulation of viral transcription Source: Reactome
    6. protein phosphorylation Source: MGI
    7. regulation of cyclin-dependent protein serine/threonine kinase activity Source: ProtInc
    8. transcription, DNA-templated Source: Reactome
    9. transcription elongation from RNA polymerase II promoter Source: Reactome
    10. transcription from RNA polymerase II promoter Source: Reactome
    11. transcription initiation from RNA polymerase II promoter Source: Reactome
    12. transforming growth factor beta receptor signaling pathway Source: Reactome
    13. viral process Source: Reactome

    Keywords - Molecular functioni

    Cyclin

    Keywords - Biological processi

    Cell cycle, Cell division, Host-virus interaction, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
    REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
    REACT_6244. Pausing and recovery of HIV elongation.
    REACT_6259. HIV elongation arrest and recovery.
    REACT_6344. Tat-mediated HIV elongation arrest and recovery.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_6905. Interactions of Tat with host cellular proteins.
    REACT_833. RNA Polymerase II Transcription Elongation.
    SignaLinkiO60563.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclin-T1
    Short name:
    CycT1
    Short name:
    Cyclin-T
    Gene namesi
    Name:CCNT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:1599. CCNT1.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleus Source: UniProtKB
    3. positive transcription elongation factor complex b Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi261 – 2611C → Y: Loss of HIV-1 Tat transactivation. 1 Publication

    Organism-specific databases

    PharmGKBiPA26163.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 726726Cyclin-T1PRO_0000080491Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei117 – 1171Phosphoserine1 Publication
    Modified residuei340 – 3401Phosphoserine1 Publication
    Modified residuei390 – 3901N6-acetyllysine1 Publication
    Modified residuei495 – 4951Phosphoserine1 Publication
    Modified residuei499 – 4991Phosphoserine1 Publication
    Modified residuei577 – 5771Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO60563.
    PaxDbiO60563.
    PeptideAtlasiO60563.
    PRIDEiO60563.

    PTM databases

    PhosphoSiteiO60563.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.

    Gene expression databases

    ArrayExpressiO60563.
    BgeeiO60563.
    CleanExiHS_CCNT1.
    GenevestigatoriO60563.

    Organism-specific databases

    HPAiCAB009016.
    HPA004892.

    Interactioni

    Subunit structurei

    Cyclin-T1 is the predominant cyclin that associates with CDK9 to form a heterodimer called P-TEFb. P-TEFb forms a complex with AFF4/AF5Q31. Interacts with the transactivation region of HIV-1, HIV-2 and SIV Tat. Component of a complex which is at least composed of HTATSF1/Tat-SF1, P-TEFb complex, RNA pol II, SUPT5H, and NCL/nucleolin. 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. Interacts with MDFIC.12 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AFF4Q9UHB75EBI-2479671,EBI-395282
    CDK9P5075013EBI-2479671,EBI-1383449
    tatP046085EBI-2479671,EBI-6164389From a different organism.

    Protein-protein interaction databases

    BioGridi107343. 62 interactions.
    DIPiDIP-29891N.
    IntActiO60563. 21 interactions.
    MINTiMINT-142682.
    STRINGi9606.ENSP00000261900.

    Structurei

    Secondary structure

    1
    726
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni8 – 125
    Helixi16 – 205
    Helixi25 – 273
    Helixi31 – 5222
    Helixi56 – 6914
    Turni70 – 723
    Turni75 – 773
    Helixi80 – 9415
    Helixi101 – 11212
    Beta strandi114 – 1163
    Helixi124 – 14320
    Turni144 – 1463
    Helixi153 – 16311
    Helixi168 – 18417
    Helixi187 – 1893
    Helixi193 – 20715
    Beta strandi216 – 2183
    Helixi221 – 2244
    Helixi231 – 24616
    Helixi249 – 2513
    Helixi252 – 2554
    Turni258 – 2625

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PK2X-ray2.67A/B/C/D1-281[»]
    3BLHX-ray2.48B2-259[»]
    3BLQX-ray2.90B2-259[»]
    3BLRX-ray2.80B2-259[»]
    3LQ5X-ray3.00B2-259[»]
    3MI9X-ray2.10B1-266[»]
    3MIAX-ray3.00B1-266[»]
    3MY1X-ray2.80B2-259[»]
    3TN8X-ray2.95B2-259[»]
    3TNHX-ray3.20B1-259[»]
    3TNIX-ray3.23B1-259[»]
    4BCFX-ray3.01B2-259[»]
    4BCGX-ray3.08B2-259[»]
    4BCHX-ray2.96B2-259[»]
    4BCIX-ray3.10B2-259[»]
    4BCJX-ray3.16B2-259[»]
    4EC8X-ray3.60B2-259[»]
    4EC9X-ray3.21B2-259[»]
    4IMYX-ray2.94B/D/F1-264[»]
    4OGRX-ray3.00B/F/K1-264[»]
    4OR5X-ray2.90B/G1-266[»]
    ProteinModelPortaliO60563.
    SMRiO60563. Positions 7-252.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60563.

    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 signal, and interaction with Tat-TAR RNASequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi506 – 53025His-richAdd
    BLAST
    Compositional biasi548 – 62982Ser-richAdd
    BLAST
    Compositional biasi708 – 72518Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the cyclin family. Cyclin C subfamily.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5333.
    HOGENOMiHOG000013208.
    HOVERGENiHBG050843.
    InParanoidiO60563.
    KOiK15188.
    OMAiFELTIDH.
    OrthoDBiEOG7VQJCR.
    PhylomeDBiO60563.
    TreeFamiTF101014.

    Family and domain databases

    Gene3Di1.10.472.10. 1 hit.
    InterProiIPR028863. CCNT1.
    IPR013763. Cyclin-like.
    IPR015429. Cyclin_C/H/T/L.
    IPR006671. Cyclin_N.
    [Graphical view]
    PANTHERiPTHR10026. PTHR10026. 1 hit.
    PTHR10026:SF42. PTHR10026:SF42. 1 hit.
    PfamiPF00134. Cyclin_N. 1 hit.
    [Graphical view]
    SMARTiSM00385. CYCLIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF47954. SSF47954. 2 hits.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O60563-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEGERKNNNK RWYFTREQLE NSPSRRFGVD PDKELSYRQQ AANLLQDMGQ    50
    RLNVSQLTIN TAIVYMHRFY MIQSFTQFPG NSVAPAALFL AAKVEEQPKK 100
    LEHVIKVAHT CLHPQESLPD TRSEAYLQQV QDLVILESII LQTLGFELTI 150
    DHPHTHVVKC TQLVRASKDL AQTSYFMATN SLHLTTFSLQ YTPPVVACVC 200
    IHLACKWSNW EIPVSTDGKH WWEYVDATVT LELLDELTHE FLQILEKTPN 250
    RLKRIWNWRA CEAAKKTKAD DRGTDEKTSE QTILNMISQS SSDTTIAGLM 300
    SMSTSTTSAV PSLPVSEESS SNLTSVEMLP GKRWLSSQPS FKLEPTQGHR 350
    TSENLALTGV DHSLPQDGSN AFISQKQNSK SVPSAKVSLK EYRAKHAEEL 400
    AAQKRQLENM EANVKSQYAY AAQNLLSHHD SHSSVILKMP IEGSENPERP 450
    FLEKADKTAL KMRIPVAGGD KAASSKPEEI KMRIKVHAAA DKHNSVEDSV 500
    TKSREHKEKH KTHPSNHHHH HNHHSHKHSH SQLPVGTGNK RPGDPKHSSQ 550
    TSNLAHKTYS LSSSFSSSSS TRKRGPSEET GGAVFDHPAK IAKSTKSSSL 600
    NFSFPSLPTM GQMPGHSSDT SGLSFSQPSC KTRVPHSKLD KGPTGANGHN 650
    TTQTIDYQDT VNMLHSLLSA QGVQPTQPTA FEFVRPYSDY LNPRSGGISS 700
    RSGNTDKPRP PPLPSEPPPP LPPLPK 726
    Length:726
    Mass (Da):80,685
    Last modified:August 1, 1998 - v1
    Checksum:i4637EFB2DDEDFE13
    GO
    Isoform 2 (identifier: O60563-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         181-184: SLHL → RTDT
         185-726: Missing.

    Show »
    Length:184
    Mass (Da):21,206
    Checksum:i331262690A9FCE9B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti77 – 771Q → R in AAC39664. (PubMed:9499409)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti362 – 3621H → R.
    Corresponds to variant rs17123261 [ dbSNP | Ensembl ].
    VAR_053054
    Natural varianti541 – 5411R → C.1 Publication
    VAR_069400

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei181 – 1844SLHL → RTDT in isoform 2. 1 PublicationVSP_054569
    Alternative sequencei185 – 726542Missing in isoform 2. 1 PublicationVSP_054570Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF045161 mRNA. Translation: AAC39638.1.
    AF048730 mRNA. Translation: AAC39664.1.
    EF688064 mRNA. Translation: ABV58572.1.
    AC079951 Genomic DNA. No translation available.
    CCDSiCCDS61109.1. [O60563-2]
    CCDS8766.1. [O60563-1]
    RefSeqiNP_001231.2. NM_001240.3. [O60563-1]
    NP_001264771.1. NM_001277842.1. [O60563-2]
    UniGeneiHs.92308.

    Genome annotation databases

    EnsembliENST00000261900; ENSP00000261900; ENSG00000129315. [O60563-1]
    ENST00000417344; ENSP00000399845; ENSG00000129315. [O60563-2]
    GeneIDi904.
    KEGGihsa:904.
    UCSCiuc001rsd.4. human. [O60563-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF045161 mRNA. Translation: AAC39638.1 .
    AF048730 mRNA. Translation: AAC39664.1 .
    EF688064 mRNA. Translation: ABV58572.1 .
    AC079951 Genomic DNA. No translation available.
    CCDSi CCDS61109.1. [O60563-2 ]
    CCDS8766.1. [O60563-1 ]
    RefSeqi NP_001231.2. NM_001240.3. [O60563-1 ]
    NP_001264771.1. NM_001277842.1. [O60563-2 ]
    UniGenei Hs.92308.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2PK2 X-ray 2.67 A/B/C/D 1-281 [» ]
    3BLH X-ray 2.48 B 2-259 [» ]
    3BLQ X-ray 2.90 B 2-259 [» ]
    3BLR X-ray 2.80 B 2-259 [» ]
    3LQ5 X-ray 3.00 B 2-259 [» ]
    3MI9 X-ray 2.10 B 1-266 [» ]
    3MIA X-ray 3.00 B 1-266 [» ]
    3MY1 X-ray 2.80 B 2-259 [» ]
    3TN8 X-ray 2.95 B 2-259 [» ]
    3TNH X-ray 3.20 B 1-259 [» ]
    3TNI X-ray 3.23 B 1-259 [» ]
    4BCF X-ray 3.01 B 2-259 [» ]
    4BCG X-ray 3.08 B 2-259 [» ]
    4BCH X-ray 2.96 B 2-259 [» ]
    4BCI X-ray 3.10 B 2-259 [» ]
    4BCJ X-ray 3.16 B 2-259 [» ]
    4EC8 X-ray 3.60 B 2-259 [» ]
    4EC9 X-ray 3.21 B 2-259 [» ]
    4IMY X-ray 2.94 B/D/F 1-264 [» ]
    4OGR X-ray 3.00 B/F/K 1-264 [» ]
    4OR5 X-ray 2.90 B/G 1-266 [» ]
    ProteinModelPortali O60563.
    SMRi O60563. Positions 7-252.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107343. 62 interactions.
    DIPi DIP-29891N.
    IntActi O60563. 21 interactions.
    MINTi MINT-142682.
    STRINGi 9606.ENSP00000261900.

    Chemistry

    BindingDBi O60563.
    ChEMBLi CHEMBL2108.

    PTM databases

    PhosphoSitei O60563.

    Proteomic databases

    MaxQBi O60563.
    PaxDbi O60563.
    PeptideAtlasi O60563.
    PRIDEi O60563.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261900 ; ENSP00000261900 ; ENSG00000129315 . [O60563-1 ]
    ENST00000417344 ; ENSP00000399845 ; ENSG00000129315 . [O60563-2 ]
    GeneIDi 904.
    KEGGi hsa:904.
    UCSCi uc001rsd.4. human. [O60563-1 ]

    Organism-specific databases

    CTDi 904.
    GeneCardsi GC12M049087.
    HGNCi HGNC:1599. CCNT1.
    HPAi CAB009016.
    HPA004892.
    MIMi 143055. gene.
    neXtProti NX_O60563.
    PharmGKBi PA26163.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5333.
    HOGENOMi HOG000013208.
    HOVERGENi HBG050843.
    InParanoidi O60563.
    KOi K15188.
    OMAi FELTIDH.
    OrthoDBi EOG7VQJCR.
    PhylomeDBi O60563.
    TreeFami TF101014.

    Enzyme and pathway databases

    Reactomei REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
    REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
    REACT_6244. Pausing and recovery of HIV elongation.
    REACT_6259. HIV elongation arrest and recovery.
    REACT_6344. Tat-mediated HIV elongation arrest and recovery.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_6905. Interactions of Tat with host cellular proteins.
    REACT_833. RNA Polymerase II Transcription Elongation.
    SignaLinki O60563.

    Miscellaneous databases

    EvolutionaryTracei O60563.
    GeneWikii Cyclin_T1.
    GenomeRNAii 904.
    NextBioi 35465417.
    PROi O60563.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60563.
    Bgeei O60563.
    CleanExi HS_CCNT1.
    Genevestigatori O60563.

    Family and domain databases

    Gene3Di 1.10.472.10. 1 hit.
    InterProi IPR028863. CCNT1.
    IPR013763. Cyclin-like.
    IPR015429. Cyclin_C/H/T/L.
    IPR006671. Cyclin_N.
    [Graphical view ]
    PANTHERi PTHR10026. PTHR10026. 1 hit.
    PTHR10026:SF42. PTHR10026:SF42. 1 hit.
    Pfami PF00134. Cyclin_N. 1 hit.
    [Graphical view ]
    SMARTi SM00385. CYCLIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47954. SSF47954. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA."
      Wei P., Garber M.E., Fang S.-M., Fischer W.H., Jones K.A.
      Cell 92:451-462(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, INTERACTION WITH HIV-1 TAT.
      Tissue: T-cell lymphoma.
    2. "Identification of multiple cyclin subunits of human P-TEFb."
      Peng J.-M., Zhu Y., Milton J.T., Price D.H.
      Genes Dev. 12:755-762(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Mammary cancer.
    3. Wu X., Liu Q., Guo D.
      Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    4. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-1 transcription."
      Parada C.A., Roeder R.G.
      EMBO J. 18:3688-3701(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH HTATSF1; CDK9; RNA POL II; SUPT5H AND NCL.
    6. "Cyclin T1 domains involved in complex formation with Tat and TAR RNA are critical for tat-activation."
      Ivanov D., Kwak Y.T., Nee E., Guo J., Garcia-Martinez L.F., Gaynor R.B.
      J. Mol. Biol. 288:41-56(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 TAT.
    7. "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: MUTAGENESIS OF CYS-261, INTERACTION WITH HIV-1 TAT.
    8. "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: INTERACTION WITH HIV-1 TAT, ROLE OF CYS-261.
    9. "Analysis of the effect of natural sequence variation in Tat and in cyclin T on the formation and RNA binding properties of Tat-cyclin T complexes."
      Bieniasz P.D., Grdina T.A., Bogerd H.P., Cullen B.R.
      J. Virol. 73:5777-5786(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 TAT; HIV-2 TAT AND SIV TAT.
    10. "Relief of two built-In autoinhibitory mechanisms in P-TEFb is required for assembly of a multicomponent transcription elongation complex at the human immunodeficiency virus type 1 promoter."
      Fong Y.W., Zhou Q.
      Mol. Cell. Biol. 20:5897-5907(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HTATSF1.
    11. "MCEF, the newest member of the AF4 family of transcription factors involved in leukemia, is a positive transcription elongation factor-b-associated protein."
      Estable M.C., Naghavi M.H., Kato H., Xiao H., Qin J., Vahlne A., Roeder R.G.
      J. Biomed. Sci. 9:234-245(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AFF4.
    12. "The human I-mfa domain-containing protein, HIC, interacts with cyclin T1 and modulates P-TEFb-dependent transcription."
      Young T.M., Wang Q., Pe'ery T., Mathews M.B.
      Mol. Cell. Biol. 23:6373-6384(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MDFIC, SUBCELLULAR LOCATION.
    13. "Evidence for conformational flexibility in the Tat-TAR recognition motif of cyclin T1."
      Das C., Edgcomb S.P., Peteranderl R., Chen L., Frankel A.D.
      Virology 318:306-317(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    14. "The bromodomain protein Brd4 is a positive regulatory component of P-TEFb and stimulates RNA polymerase II-dependent transcription."
      Jang M.K., Mochizuki K., Zhou M., Jeong H.S., Brady J.N., Ozato K.
      Mol. Cell 19:523-534(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BRD4.
    15. "Recruitment of P-TEFb for stimulation of transcriptional elongation by the bromodomain protein Brd4."
      Yang Z., Yik J.H., Chen R., He N., Jang M.K., Ozato K., Zhou Q.
      Mol. Cell 19:535-545(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BRD4.
    16. "Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme."
      Jeronimo C., Forget D., Bouchard A., Li Q., Chua G., Poitras C., Therien C., Bergeron D., Bourassa S., Greenblatt J., Chabot B., Poirier G.G., Hughes T.R., Blanchette M., Price D.H., Coulombe B.
      Mol. Cell 27:262-274(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE 7SK SNRNP COMPLEX.
    17. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495 AND SER-577, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117 AND SER-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: VARIANT CYS-541.

    Entry informationi

    Entry nameiCCNT1_HUMAN
    AccessioniPrimary (citable) accession number: O60563
    Secondary accession number(s): A9XU13, E7EX76, O60581
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 147 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Interaction between Tat and cyclin-T1 requires zinc.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3