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O60563

- CCNT1_HUMAN

UniProt

O60563 - CCNT1_HUMAN

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Protein

Cyclin-T1

Gene

CCNT1

Organism
Homo sapiens (Human)
Status
Reviewed - 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). 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. snRNA binding Source: Ensembl
  4. 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
Complete GO annotation...

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
Complete GO annotation...

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

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. 67 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.
GeneTreeiENSGT00760000119191.
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

        10         20         30         40         50
MEGERKNNNK RWYFTREQLE NSPSRRFGVD PDKELSYRQQ AANLLQDMGQ
60 70 80 90 100
RLNVSQLTIN TAIVYMHRFY MIQSFTQFPG NSVAPAALFL 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 FLQILEKTPN
260 270 280 290 300
RLKRIWNWRA CEAAKKTKAD DRGTDEKTSE QTILNMISQS SSDTTIAGLM
310 320 330 340 350
SMSTSTTSAV PSLPVSEESS SNLTSVEMLP GKRWLSSQPS FKLEPTQGHR
360 370 380 390 400
TSENLALTGV DHSLPQDGSN AFISQKQNSK SVPSAKVSLK EYRAKHAEEL
410 420 430 440 450
AAQKRQLENM EANVKSQYAY AAQNLLSHHD SHSSVILKMP IEGSENPERP
460 470 480 490 500
FLEKADKTAL KMRIPVAGGD KAASSKPEEI KMRIKVHAAA DKHNSVEDSV
510 520 530 540 550
TKSREHKEKH KTHPSNHHHH HNHHSHKHSH SQLPVGTGNK RPGDPKHSSQ
560 570 580 590 600
TSNLAHKTYS LSSSFSSSSS TRKRGPSEET GGAVFDHPAK IAKSTKSSSL
610 620 630 640 650
NFSFPSLPTM GQMPGHSSDT SGLSFSQPSC KTRVPHSKLD KGPTGANGHN
660 670 680 690 700
TTQTIDYQDT VNMLHSLLSA QGVQPTQPTA FEFVRPYSDY LNPRSGGISS
710 720
RSGNTDKPRP PPLPSEPPPP LPPLPK
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]
ENST00000618666; ENSP00000481035; ENSG00000129315. [O60563-2]
GeneIDi904.
KEGGihsa:904.
UCSCiuc001rsd.4. human. [O60563-1]
uc009zkz.3. human.

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

Chemistry

BindingDBi O60563.
ChEMBLi CHEMBL2111389.

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 ]
ENST00000618666 ; ENSP00000481035 ; ENSG00000129315 . [O60563-2 ]
GeneIDi 904.
KEGGi hsa:904.
UCSCi uc001rsd.4. human. [O60563-1 ]
uc009zkz.3. human.

Organism-specific databases

CTDi 904.
GeneCardsi GC12M049093.
HGNCi HGNC:1599. CCNT1.
HPAi CAB009016.
HPA004892.
MIMi 143055. gene.
neXtProti NX_O60563.
PharmGKBi PA26163.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5333.
GeneTreei ENSGT00760000119191.
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

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

« Hide 'large scale' publications
  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 29, 2014
This is version 148 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