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Protein

Cyclin-T1

Gene

CCNT1

Organism
Homo sapiens (Human)
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).2 Publications
(Microbial infection) 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

  • 7SK snRNA binding Source: UniProtKB
  • chromatin binding Source: Ensembl
  • cyclin-dependent protein serine/threonine kinase regulator activity Source: GO_Central
  • DNA binding Source: MGI
  • protein serine/threonine kinase activity Source: Reactome
  • RNA polymerase binding Source: UniProtKB
  • transcription factor binding Source: ParkinsonsUK-UCL
  • transcription regulatory region DNA binding Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

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

Enzyme and pathway databases

ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
R-HSA-176034. Interactions of Tat with host cellular proteins.
R-HSA-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-6807505. RNA polymerase II transcribes snRNA genes.
R-HSA-75955. RNA Polymerase II Transcription Elongation.
SignaLinkiO60563.
SIGNORiO60563.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:1599. CCNT1.

Subcellular locationi

GO - Cellular componenti

  • cyclin/CDK positive transcription elongation factor complex Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus 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.

Chemistry

ChEMBLiCHEMBL2111389.

Polymorphism and mutation databases

BioMutaiCCNT1.

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 – 1171PhosphoserineCombined sources
Modified residuei340 – 3401PhosphoserineCombined sources
Modified residuei388 – 3881PhosphoserineCombined sources
Modified residuei390 – 3901N6-acetyllysineCombined sources
Modified residuei495 – 4951PhosphoserineCombined sources
Modified residuei499 – 4991PhosphoserineCombined sources
Modified residuei564 – 5641PhosphoserineCombined sources
Modified residuei577 – 5771PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO60563.
MaxQBiO60563.
PaxDbiO60563.
PeptideAtlasiO60563.
PRIDEiO60563.

PTM databases

iPTMnetiO60563.
PhosphoSiteiO60563.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

BgeeiENSG00000129315.
CleanExiHS_CCNT1.
GenevisibleiO60563. HS.

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. 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.7 Publications
(Microbial infection) Interacts with the transactivation region of HIV-1, HIV-2 and SIV Tat.5 Publications

Binary interactionsi

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

GO - Molecular functioni

  • RNA polymerase binding Source: UniProtKB
  • transcription factor binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi107343. 74 interactions.
DIPiDIP-29891N.
IntActiO60563. 26 interactions.
MINTiMINT-142682.
STRINGi9606.ENSP00000261900.

Chemistry

BindingDBiO60563.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

eggNOGiKOG0834. Eukaryota.
COG5333. LUCA.
GeneTreeiENSGT00760000119191.
HOGENOMiHOG000068113.
HOVERGENiHBG050843.
InParanoidiO60563.
KOiK15188.
OMAiTMAQLPG.
OrthoDBiEOG091G03Z2.
PhylomeDBiO60563.
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.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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
Corresponds to variant rs201951577 [ dbSNP | Ensembl ].
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:
EMBLi
GenBanki
DDBJi
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.5. human. [O60563-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi107343. 74 interactions.
DIPiDIP-29891N.
IntActiO60563. 26 interactions.
MINTiMINT-142682.
STRINGi9606.ENSP00000261900.

Chemistry

BindingDBiO60563.
ChEMBLiCHEMBL2111389.

PTM databases

iPTMnetiO60563.
PhosphoSiteiO60563.

Polymorphism and mutation databases

BioMutaiCCNT1.

Proteomic databases

EPDiO60563.
MaxQBiO60563.
PaxDbiO60563.
PeptideAtlasiO60563.
PRIDEiO60563.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261900; ENSP00000261900; ENSG00000129315. [O60563-1]
ENST00000417344; ENSP00000399845; ENSG00000129315. [O60563-2]
ENST00000618666; ENSP00000481035; ENSG00000129315. [O60563-2]
GeneIDi904.
KEGGihsa:904.
UCSCiuc001rsd.5. human. [O60563-1]

Organism-specific databases

CTDi904.
GeneCardsiCCNT1.
HGNCiHGNC:1599. CCNT1.
HPAiCAB009016.
HPA004892.
MIMi143055. gene.
neXtProtiNX_O60563.
PharmGKBiPA26163.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0834. Eukaryota.
COG5333. LUCA.
GeneTreeiENSGT00760000119191.
HOGENOMiHOG000068113.
HOVERGENiHBG050843.
InParanoidiO60563.
KOiK15188.
OMAiTMAQLPG.
OrthoDBiEOG091G03Z2.
PhylomeDBiO60563.
TreeFamiTF101014.

Enzyme and pathway databases

ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
R-HSA-176034. Interactions of Tat with host cellular proteins.
R-HSA-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-6807505. RNA polymerase II transcribes snRNA genes.
R-HSA-75955. RNA Polymerase II Transcription Elongation.
SignaLinkiO60563.
SIGNORiO60563.

Miscellaneous databases

EvolutionaryTraceiO60563.
GeneWikiiCyclin_T1.
GenomeRNAii904.
PROiO60563.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000129315.
CleanExiHS_CCNT1.
GenevisibleiO60563. HS.

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...

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: September 7, 2016
This is version 168 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

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.