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Protein

Cyclin-T2

Gene

CCNT2

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 T) 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) (PubMed:9499409, PubMed:15563843). The activity of this complex is regulated by binding with 7SK snRNA (PubMed:11713533). Plays a role during muscle differentiation; P-TEFB complex interacts with MYOD1; this tripartite complex promotes the transcriptional activity of MYOD1 through its CDK9-mediated phosphorylation and binds the chromatin of promoters and enhancers of muscle-specific genes; this event correlates with hyperphosphorylation of the CTD domain of RNA pol II (By similarity). In addition, enhances MYOD1-dependent transcription through interaction with PKN1 (PubMed:16331689). Involved in early embryo development (By similarity).By similarity4 Publications
(Microbial infection) Promotes transcriptional activation of early and late herpes simplex virus 1/HHV-1 promoters.1 Publication

GO - Molecular functioni

  • 7SK snRNA binding Source: UniProtKB
  • chromatin binding Source: UniProtKB
  • cyclin-dependent protein serine/threonine kinase regulator activity Source: GO_Central
  • protein kinase binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: Reactome
  • RNA polymerase binding Source: UniProtKB
  • transcription coactivator binding Source: UniProtKB

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

BioCyciZFISH:ENSG00000082258-MONOMER.
ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-112387. Elongation arrest and recovery.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
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.
SignaLinkiO60583.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-T2By similarity
Short name:
CycT2By similarity
Gene namesi
Name:CCNT2Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:1600. CCNT2.

Subcellular locationi

  • Cytoplasmperinuclear region By similarity
  • Nucleus By similarity

  • Note: Nucleus in differentiating cells.By similarity

GO - Cellular componenti

  • cyclin/CDK positive transcription elongation factor complex Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi260N → C: Activation of HIV-1 Tat function. 1 Publication1

Organism-specific databases

DisGeNETi905.
OpenTargetsiENSG00000082258.
PharmGKBiPA26164.

Polymorphism and mutation databases

BioMutaiCCNT2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000804951 – 730Cyclin-T2Add BLAST730

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei480PhosphoserineCombined sources1
Modified residuei601PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO60583.
MaxQBiO60583.
PaxDbiO60583.
PeptideAtlasiO60583.
PRIDEiO60583.

PTM databases

iPTMnetiO60583.
PhosphoSitePlusiO60583.

Miscellaneous databases

PMAP-CutDBO60583.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

BgeeiENSG00000082258.
CleanExiHS_CCNT2.
ExpressionAtlasiO60583. baseline and differential.
GenevisibleiO60583. HS.

Organism-specific databases

HPAiHPA005559.

Interactioni

Subunit structurei

Interacts with CDK9 to form P-TEFb (PubMed:9499409, PubMed:16331689). Interacts with POLR2A (via the C-terminal domain (CTD)); mediates transcriptional activity (PubMed:15563843). Interacts with HEXIM1; mediates formation of a tripartite complex with KPNA2. Interacts with HEXIM2 (PubMed:19883659). Interacts with PKN1; enhances MYOD1-dependent transcription (PubMed:16331689). P-TEFB complex interacts with RB1; promotes phosphorylation of RB1 (PubMed:12037672). P-TEFB complex interacts with MYOD1; promotes the transcriptional activity of MYOD1 through its CDK9-mediated phosphorylation (By similarity). Interacts with MDFI and MDFIC (PubMed:17289077). Interacts with MON1B; downregulates CCNT2-mediated activation of viral promoters during herpes simplex virus 1/HHV-1 infection (PubMed:21509660).By similarity7 Publications
(Microbial infection) Interacts with HIV-2 and SIV Tat. Does not bind efficiently to the transactivation domain of the HIV-1 Tat (PubMed:10364329).

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB
  • RNA polymerase binding Source: UniProtKB
  • transcription coactivator binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107344. 19 interactors.
IntActiO60583. 11 interactors.
MINTiMINT-2796926.
STRINGi9606.ENSP00000264157.

Structurei

Secondary structure

1730
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 11Combined sources3
Helixi15 – 19Combined sources5
Helixi22 – 25Combined sources4
Helixi30 – 50Combined sources21
Helixi55 – 68Combined sources14
Turni69 – 71Combined sources3
Turni74 – 76Combined sources3
Helixi79 – 93Combined sources15
Helixi100 – 111Combined sources12
Helixi123 – 142Combined sources20
Turni143 – 145Combined sources3
Helixi152 – 162Combined sources11
Helixi167 – 183Combined sources17
Helixi186 – 188Combined sources3
Helixi192 – 207Combined sources16
Helixi220 – 223Combined sources4
Helixi230 – 245Combined sources16
Helixi248 – 261Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IVXX-ray1.80A/B7-263[»]
ProteinModelPortaliO60583.
SMRiO60583.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60583.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini12 – 147Cyclin N-terminalSequence analysisAdd BLAST136

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 300Interaction with MDFIC and MDFI1 PublicationAdd BLAST300
Regioni250 – 300Interaction with POLR2A1 PublicationAdd BLAST51

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi530 – 660Ser-richPROSITE-ProRule annotationAdd BLAST131
Compositional biasi665 – 671Poly-Pro7

Sequence similaritiesi

Belongs to the cyclin family. Cyclin C subfamily.Curated
Contains 1 cyclin N-terminal domain.Sequence analysis

Phylogenomic databases

eggNOGiKOG0834. Eukaryota.
COG5333. LUCA.
GeneTreeiENSGT00760000119191.
HOVERGENiHBG050843.
InParanoidiO60583.
KOiK15188.
OMAiHVNDASH.
OrthoDBiEOG091G03Z2.
PhylomeDBiO60583.
TreeFamiTF101014.

Family and domain databases

Gene3Di1.10.472.10. 1 hit.
InterProiIPR028862. CCNT2.
IPR013763. Cyclin-like.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERiPTHR10026:SF43. PTHR10026:SF43. 2 hits.
PfamiPF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 2 hits.
[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: O60583-1) [UniParc]FASTAAdd to basket
Also known as: B

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
MASGRGASSR WFFTREQLEN TPSRRCGVEA DKELSCRQQA ANLIQEMGQR
60 70 80 90 100
LNVSQLTINT AIVYMHRFYM HHSFTKFNKN IISSTALFLA AKVEEQARKL
110 120 130 140 150
EHVIKVAHAC LHPLEPLLDT KCDAYLQQTQ ELVILETIML QTLGFEITIE
160 170 180 190 200
HPHTDVVKCT QLVRASKDLA QTSYFMATNS LHLTTFCLQY KPTVIACVCI
210 220 230 240 250
HLACKWSNWE IPVSTDGKHW WEYVDPTVTL ELLDELTHEF LQILEKTPNR
260 270 280 290 300
LKKIRNWRAN QAARKPKVDG QVSETPLLGS SLVQNSILVD SVTGVPTNPS
310 320 330 340 350
FQKPSTSAFP APVPLNSGNI SVQDSHTSDN LSMLATGMPS TSYGLSSHQE
360 370 380 390 400
WPQHQDSART EQLYSQKQET SLSGSQYNIN FQQGPSISLH SGLHHRPDKI
410 420 430 440 450
SDHSSVKQEY THKAGSSKHH GPISTTPGII PQKMSLDKYR EKRKLETLDL
460 470 480 490 500
DVRDHYIAAQ VEQQHKQGQS QAASSSSVTS PIKMKIPIAN TEKYMADKKE
510 520 530 540 550
KSGSLKLRIP IPPTDKSASK EELKMKIKVS SSERHSSSDE GSGKSKHSSP
560 570 580 590 600
HISRDHKEKH KEHPSSRHHT SSHKHSHSHS GSSSGGSKHS ADGIPPTVLR
610 620 630 640 650
SPVGLSSDGI SSSSSSSRKR LHVNDASHNH HSKMSKSSKS SGSSSSSSSS
660 670 680 690 700
VKQYISSHNS VFNHPLPPPP PVTYQVGYGH LSTLVKLDKK PVETNGPDAN
710 720 730
HEYSTSSQHM DYKDTFDMLD SLLSAQGMNM
Length:730
Mass (Da):81,029
Last modified:April 26, 2005 - v2
Checksum:iF449DFFC57FB196B
GO
Isoform 2 (identifier: O60583-2) [UniParc]FASTAAdd to basket
Also known as: A

The sequence of this isoform differs from the canonical sequence as follows:
     643-730: SSSSSSSSVK...SLLSAQGMNM → GLRTSQHPRETGQEASGDQRS

Show »
Length:663
Mass (Da):73,682
Checksum:i2B4B8F551631EC16
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti682S → C in AAC39666 (PubMed:9499409).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_001258643 – 730SSSSS…QGMNM → GLRTSQHPRETGQEASGDQR S in isoform 2. 2 PublicationsAdd BLAST88

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF048731 mRNA. Translation: AAC39665.1.
AF048732 mRNA. Translation: AAC39666.1.
AY865621 Genomic DNA. Translation: AAW56073.1.
AK292913 mRNA. Translation: BAF85602.1.
AC016725 Genomic DNA. Translation: AAY14998.1.
CH471058 Genomic DNA. Translation: EAX11644.1.
CH471058 Genomic DNA. Translation: EAX11645.1.
CH471058 Genomic DNA. Translation: EAX11646.1.
CH471058 Genomic DNA. Translation: EAX11647.1.
BC114366 mRNA. Translation: AAI14367.1.
CCDSiCCDS2174.1. [O60583-1]
CCDS2175.1. [O60583-2]
RefSeqiNP_001232.1. NM_001241.3. [O60583-2]
NP_490595.1. NM_058241.2. [O60583-1]
UniGeneiHs.744115.

Genome annotation databases

EnsembliENST00000264157; ENSP00000264157; ENSG00000082258. [O60583-1]
ENST00000295238; ENSP00000295238; ENSG00000082258. [O60583-2]
GeneIDi905.
KEGGihsa:905.
UCSCiuc002tub.3. human. [O60583-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF048731 mRNA. Translation: AAC39665.1.
AF048732 mRNA. Translation: AAC39666.1.
AY865621 Genomic DNA. Translation: AAW56073.1.
AK292913 mRNA. Translation: BAF85602.1.
AC016725 Genomic DNA. Translation: AAY14998.1.
CH471058 Genomic DNA. Translation: EAX11644.1.
CH471058 Genomic DNA. Translation: EAX11645.1.
CH471058 Genomic DNA. Translation: EAX11646.1.
CH471058 Genomic DNA. Translation: EAX11647.1.
BC114366 mRNA. Translation: AAI14367.1.
CCDSiCCDS2174.1. [O60583-1]
CCDS2175.1. [O60583-2]
RefSeqiNP_001232.1. NM_001241.3. [O60583-2]
NP_490595.1. NM_058241.2. [O60583-1]
UniGeneiHs.744115.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IVXX-ray1.80A/B7-263[»]
ProteinModelPortaliO60583.
SMRiO60583.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107344. 19 interactors.
IntActiO60583. 11 interactors.
MINTiMINT-2796926.
STRINGi9606.ENSP00000264157.

PTM databases

iPTMnetiO60583.
PhosphoSitePlusiO60583.

Polymorphism and mutation databases

BioMutaiCCNT2.

Proteomic databases

EPDiO60583.
MaxQBiO60583.
PaxDbiO60583.
PeptideAtlasiO60583.
PRIDEiO60583.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264157; ENSP00000264157; ENSG00000082258. [O60583-1]
ENST00000295238; ENSP00000295238; ENSG00000082258. [O60583-2]
GeneIDi905.
KEGGihsa:905.
UCSCiuc002tub.3. human. [O60583-1]

Organism-specific databases

CTDi905.
DisGeNETi905.
GeneCardsiCCNT2.
HGNCiHGNC:1600. CCNT2.
HPAiHPA005559.
MIMi603862. gene.
neXtProtiNX_O60583.
OpenTargetsiENSG00000082258.
PharmGKBiPA26164.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0834. Eukaryota.
COG5333. LUCA.
GeneTreeiENSGT00760000119191.
HOVERGENiHBG050843.
InParanoidiO60583.
KOiK15188.
OMAiHVNDASH.
OrthoDBiEOG091G03Z2.
PhylomeDBiO60583.
TreeFamiTF101014.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000082258-MONOMER.
ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-112387. Elongation arrest and recovery.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
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.
SignaLinkiO60583.

Miscellaneous databases

ChiTaRSiCCNT2. human.
EvolutionaryTraceiO60583.
GeneWikiiCyclin_T2.
GenomeRNAii905.
PMAP-CutDBO60583.
PROiO60583.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000082258.
CleanExiHS_CCNT2.
ExpressionAtlasiO60583. baseline and differential.
GenevisibleiO60583. HS.

Family and domain databases

Gene3Di1.10.472.10. 1 hit.
InterProiIPR028862. CCNT2.
IPR013763. Cyclin-like.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERiPTHR10026:SF43. PTHR10026:SF43. 2 hits.
PfamiPF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 2 hits.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiCCNT2_HUMAN
AccessioniPrimary (citable) accession number: O60583
Secondary accession number(s): A8KA48
, D3DP73, D3DP74, O60582, Q29R66, Q53SR4, Q5I1Y0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: April 26, 2005
Last modified: November 30, 2016
This is version 161 of the entry and version 2 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.