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Protein

Cyclin-T1

Gene

CCNT1

Organism
Equus caballus (Horse)
Status
Reviewed-Annotation score: Annotation score: 4 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 production elongation by phosphorylating the CTD (carboxy-terminal domain) of the large subunit of RNA polymerase II (RNAP II) (By similarity). In case of equine infectious anemia virus (EIAV) infection, binds to the nuclear transcriptional activator Tat, 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.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-T1
Short name:
CycT1
Short name:
Cyclin-T
Gene namesi
Name:CCNT1
OrganismiEquus caballus (Horse)
Taxonomic identifieri9796 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
Proteomesi
  • UP000002281 Componenti: Chromosome 6

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 727727Cyclin-T1PRO_0000080492Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei117 – 1171PhosphoserineBy similarity
Modified residuei392 – 3921N6-acetyllysineBy similarity
Modified residuei497 – 4971PhosphoserineBy similarity
Modified residuei501 – 5011PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9XT26.

Interactioni

Subunit structurei

Associates with CDK9 to form P-TEFb. Cyclin-T1 is the predominant cyclin associated with CDK9. P-TEFb forms a complex with AFF4/AF5Q31. Interacts with MDFIC (By similarity). Interacts with the transactivation region of EIAV Tat, but not with HIV-1 tat. Component of a complex which is at least composed of HTATSF1/Tat-SF1, P-TEFb, RNA pol II. 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

Protein-protein interaction databases

STRINGi9796.ENSECAP00000013646.

Structurei

Secondary structure

1
727
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 123Combined sources
Turni16 – 183Combined sources
Turni23 – 253Combined sources
Beta strandi26 – 283Combined sources
Helixi31 – 5222Combined sources
Helixi56 – 6914Combined sources
Turni75 – 773Combined sources
Helixi80 – 9415Combined sources
Helixi101 – 11212Combined sources
Helixi126 – 14318Combined sources
Turni144 – 1463Combined sources
Helixi153 – 1575Combined sources
Beta strandi160 – 1645Combined sources
Helixi168 – 1703Combined sources
Helixi175 – 1784Combined sources
Turni179 – 1846Combined sources
Helixi186 – 1894Combined sources
Helixi193 – 20210Combined sources
Helixi204 – 2074Combined sources
Turni216 – 2183Combined sources
Turni221 – 2255Combined sources
Helixi231 – 24515Combined sources
Beta strandi246 – 2483Combined sources
Beta strandi262 – 2654Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2W2HX-ray3.25A/B5-267[»]
ProteinModelPortaliQ9XT26.
SMRiQ9XT26. Positions 8-263.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9XT26.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili386 – 42742Sequence 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 biasi508 – 53225His-richAdd
BLAST
Compositional biasi550 – 57324Ser-richAdd
BLAST
Compositional biasi709 – 72618Pro-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.
InParanoidiQ9XT26.
KOiK15188.
OMAiFELTIDH.
OrthoDBiEOG7VQJCR.
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.

Q9XT26-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGERKNNNK RWYFTREQLE NSPSRRFGLD PDKELSYRQQ AANLLQDMGQ
60 70 80 90 100
RLNVSQLTIN TAIVYMHRFY MIQSFTQFHR NSVAPAALFL AAKVEEQPKK
110 120 130 140 150
LEHVIKVAHA 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
RLKRIRNWRA CQAAKKTKAD DRGTDENTSE QTILNMISQS SSDTTIAGLM
310 320 330 340 350
SMSTSSTTST VPSLPTTEES SSNLSGVEML QGERWLSSQP PFKLEPAQGH
360 370 380 390 400
RTSENLALIG VDHSLQQDGS NAFISQKQNS SKSVPSAKVS LKEYRAKHAE
410 420 430 440 450
ELAAQKRQLE NMEANVKSQY AYAAQNLLSH HDSHSSVILK MPIEGSENPE
460 470 480 490 500
RPFLEKPDKT ALKMRIPVAS GDKAASSKPE EIKMRIKVHA APDKHNSIDD
510 520 530 540 550
SVTKSREHKE KHKTHPSNHH HHHNHHSHKH SHSQLPAGTG NKRPGDPKHS
560 570 580 590 600
SQTSTLAHKT YSLSSSFSSS SSSRKRGPPE ETGGALFDHP AKIAKSTKSS
610 620 630 640 650
SINFFPPLPT MAQLPGHSSD TSGLPFSQPS CKTRVPHMKL DKGPTGANGH
660 670 680 690 700
NTTQTIDYQD TVNMLHSLLH AQGVQPTQPP ALEFVHSYGE YLNPRAGGMP
710 720
SRSGNTDKPR LPPLPSEPPP PLPPLPK
Length:727
Mass (Da):81,013
Last modified:November 1, 1999 - v1
Checksum:iBFC2A398D6B35BCE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961E → G in AAF04138 (PubMed:10623752).Curated
Sequence conflicti256 – 2561R → W in AAF04138 (PubMed:10623752).Curated
Sequence conflicti262 – 2621Q → E in AAF04138 (PubMed:10623752).Curated
Sequence conflicti277 – 2771N → K in AAF04138 (PubMed:10623752).Curated
Sequence conflicti359 – 3591I → T in AAF04138 (PubMed:10623752).Curated
Sequence conflicti537 – 5371A → V in AAF04138 (PubMed:10623752).Curated
Sequence conflicti681 – 6811A → T in AAF04138 (PubMed:10623752).Curated
Sequence conflicti687 – 6871S → P in AAF04138 (PubMed:10623752).Curated
Sequence conflicti699 – 6991M → I in AAF04138 (PubMed:10623752).Curated
Sequence conflicti711 – 7111L → P in AAF04138 (PubMed:10623752).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF137509 mRNA. Translation: AAD38518.1.
AF190905 mRNA. Translation: AAF04138.1.
RefSeqiNP_001075315.1. NM_001081846.1.
UniGeneiEca.12914.

Genome annotation databases

EnsembliENSECAT00000016868; ENSECAP00000013646; ENSECAG00000015768.
GeneIDi100033893.
KEGGiecb:100033893.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF137509 mRNA. Translation: AAD38518.1.
AF190905 mRNA. Translation: AAF04138.1.
RefSeqiNP_001075315.1. NM_001081846.1.
UniGeneiEca.12914.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2W2HX-ray3.25A/B5-267[»]
ProteinModelPortaliQ9XT26.
SMRiQ9XT26. Positions 8-263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9796.ENSECAP00000013646.

Proteomic databases

PaxDbiQ9XT26.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSECAT00000016868; ENSECAP00000013646; ENSECAG00000015768.
GeneIDi100033893.
KEGGiecb:100033893.

Organism-specific databases

CTDi904.

Phylogenomic databases

eggNOGiKOG0834. Eukaryota.
COG5333. LUCA.
GeneTreeiENSGT00760000119191.
HOGENOMiHOG000013208.
HOVERGENiHBG050843.
InParanoidiQ9XT26.
KOiK15188.
OMAiFELTIDH.
OrthoDBiEOG7VQJCR.
TreeFamiTF101014.

Miscellaneous databases

EvolutionaryTraceiQ9XT26.

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

  1. "Highly divergent lentiviral Tat proteins activate viral gene expression by a common mechanism."
    Bieniasz P.D., Grdina T.A., Bogerd H.P., Cullen B.R.
    Mol. Cell. Biol. 19:4592-4599(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH EIAV TAT.
    Tissue: Fibroblast.
  2. "Interactions between equine cyclin T1, Tat, and TAR are disrupted by a leucine-to-valine substitution found in human cyclin T1."
    Taube R., Fujinaga K., Irwin D., Wimmer J., Geyer M., Peterlin B.M.
    J. Virol. 74:892-898(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "An in vitro transcription system that recapitulates equine infectious anemia virus tat-mediated inhibition of human immunodeficiency virus type 1 Tat activity demonstrates a role for positive transcription elongation factor b and associated proteins in the mechanism of Tat activation."
    Sune C., Goldstrohm A.C., Peng J., Price D.H., Garcia-Blanco M.A.
    Virology 274:356-366(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH HTATSF1; P-TEFB AND RNA POL II.

Entry informationi

Entry nameiCCNT1_HORSE
AccessioniPrimary (citable) accession number: Q9XT26
Secondary accession number(s): Q9TTX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: May 11, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.