Cyclin T2

Protein-coding gene in the species Homo sapiens
CCNT2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2IVX

Identifiers
AliasesCCNT2, CYCT2, cyclin T2
External IDsOMIM: 603862; MGI: 1920199; HomoloGene: 14043; GeneCards: CCNT2; OMA:CCNT2 - orthologs
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for CCNT2
Genomic location for CCNT2
Band2q21.3Start134,918,235 bp[1]
End134,959,342 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for CCNT2
Genomic location for CCNT2
Band1|1 E3Start127,701,901 bp[2]
End127,735,798 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Achilles tendon

  • body of pancreas

  • visceral pleura

  • endothelial cell

  • testicle

  • monocyte

  • Brodmann area 23

  • rectum

  • germinal epithelium

  • endometrium
Top expressed in
  • medullary collecting duct

  • Rostral migratory stream

  • renal corpuscle

  • substantia nigra

  • aortic valve

  • zygote

  • secondary oocyte

  • ascending aorta

  • retinal pigment epithelium

  • mammillary body
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • protein kinase binding
  • 7SK snRNA binding
  • transcription coactivator binding
  • cyclin-dependent protein serine/threonine kinase regulator activity
  • RNA polymerase binding
  • protein binding
  • protein serine/threonine kinase activity
  • chromatin binding
  • cyclin-dependent protein serine/threonine kinase activator activity
Cellular component
  • cyclin/CDK positive transcription elongation factor complex
  • nucleus
  • perinuclear region of cytoplasm
  • cytoplasm
  • nucleoplasm
  • cytosol
  • plasma membrane
  • cyclin-dependent protein kinase holoenzyme complex
Biological process
  • regulation of muscle cell differentiation
  • early viral transcription
  • positive regulation of phosphorylation of RNA polymerase II C-terminal domain
  • cell cycle
  • late viral transcription
  • cell division
  • regulation of cyclin-dependent protein serine/threonine kinase activity
  • positive regulation of cyclin-dependent protein serine/threonine kinase activity
  • transcription elongation from RNA polymerase II promoter
  • regulation of transcription, DNA-templated
  • transcription by RNA polymerase II
  • positive regulation of transcription by RNA polymerase II
  • viral process
  • transcription, DNA-templated
  • snRNA transcription by RNA polymerase II
  • protein phosphorylation
  • skeletal muscle tissue development
  • regulation of transcription by RNA polymerase II
  • positive regulation of DNA-templated transcription, elongation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

905

72949

Ensembl

ENSG00000082258

ENSMUSG00000026349

UniProt

O60583

Q7TQK0

RefSeq (mRNA)

NM_001241
NM_058241
NM_001320748
NM_001320749

NM_028399

RefSeq (protein)

NP_001232
NP_001307677
NP_001307678
NP_490595

NP_082675

Location (UCSC)Chr 2: 134.92 – 134.96 MbChr 1: 127.7 – 127.74 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Cyclin-T2 is a protein that in humans is encoded by the CCNT2 gene.[5][6][7]

Function

The protein encoded by this gene belongs to the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle. Cyclins function as regulators of CDK kinases. Different cyclins exhibit distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. This cyclin and its kinase partner CDK9 were found to be subunits of the transcription elongation factor p-TEFb. The p-TEFb complex containing this cyclin was reported to interact with, and act as a negative regulator of human immunodeficiency virus type 1 (HIV-1) Tat protein. Two alternatively spliced transcript variants, which encode distinct isoforms, have been described.[7]

Interactions

Cyclin T2 has been shown to interact with CDK9[5] and Retinoblastoma protein.[8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000082258 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026349 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b Peng J, Zhu Y, Milton JT, Price DH (Apr 1998). "Identification of multiple cyclin subunits of human P-TEFb". Genes Dev. 12 (5): 755–62. doi:10.1101/gad.12.5.755. PMC 316581. PMID 9499409.
  6. ^ Napolitano G, Licciardo P, Gallo P, Majello B, Giordano A, Lania L (Nov 1999). "The CDK9-associated cyclins T1 and T2 exert opposite effects on HIV-1 Tat activity". AIDS. 13 (12): 1453–9. doi:10.1097/00002030-199908200-00003. PMID 10465067.
  7. ^ a b "Entrez Gene: CCNT2 cyclin T2".
  8. ^ Simone C, Bagella L, Bellan C, Giordano A (Jun 2002). "Physical interaction between pRb and cdk9/cyclinT2 complex". Oncogene. 21 (26): 4158–65. doi:10.1038/sj.onc.1205511. PMID 12037672. S2CID 44657967.

Further reading

  • Wolff A (1976). "[Problem of occupational disability hazards]". Lebensversicher Med. 28 (3): 76–7. PMID 9544.
  • Wimmer J, Fujinaga K, Taube R, Cujec TP, Zhu Y, Peng J, Price DH, Peterlin BM (1999). "Interactions between Tat and TAR and human immunodeficiency virus replication are facilitated by human cyclin T1 but not cyclins T2a or T2b". Virology. 255 (1): 182–9. doi:10.1006/viro.1998.9589. PMID 10049833.
  • Kwak YT, Ivanov D, Guo J, Nee E, Gaynor RB (1999). "Role of the human and murine cyclin T proteins in regulating HIV-1 tat-activation". J. Mol. Biol. 288 (1): 57–69. doi:10.1006/jmbi.1999.2664. PMID 10329126.
  • Bieniasz PD, Grdina TA, Bogerd HP, Cullen BR (1999). "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". J. Virol. 73 (7): 5777–86. doi:10.1128/JVI.73.7.5777-5786.1999. PMC 112638. PMID 10364329.
  • Herrmann CH, Mancini MA (2001). "The Cdk9 and cyclin T subunits of TAK/P-TEFb localize to splicing factor-rich nuclear speckle regions". J. Cell Sci. 114 (Pt 8): 1491–503. doi:10.1242/jcs.114.8.1491. PMID 11282025.
  • Nguyen VT, Kiss T, Michels AA, Bensaude O (2001). "7SK small nuclear RNA binds to and inhibits the activity of CDK9/cyclin T complexes". Nature. 414 (6861): 322–5. Bibcode:2001Natur.414..322N. doi:10.1038/35104581. PMID 11713533. S2CID 4341651.
  • Tolstonog GV, Mothes E, Shoeman RL, Traub P (2001). "Isolation of SDS-stable complexes of the intermediate filament protein vimentin with repetitive, mobile, nuclear matrix attachment region, and mitochondrial DNA sequence elements from cultured mouse and human fibroblasts". DNA Cell Biol. 20 (9): 531–54. doi:10.1089/104454901317094954. PMID 11747605.
  • Simone C, Bagella L, Bellan C, Giordano A (2002). "Physical interaction between pRb and cdk9/cyclinT2 complex". Oncogene. 21 (26): 4158–65. doi:10.1038/sj.onc.1205511. PMID 12037672. S2CID 44657967.
  • Michels AA, Nguyen VT, Fraldi A, Labas V, Edwards M, Bonnet F, Lania L, Bensaude O (2003). "MAQ1 and 7SK RNA interact with CDK9/cyclin T complexes in a transcription-dependent manner". Mol. Cell. Biol. 23 (14): 4859–69. doi:10.1128/MCB.23.14.4859-4869.2003. PMC 162212. PMID 12832472.
  • Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
  • Kurosu T, Zhang F, Peterlin BM (2004). "Transcriptional activity and substrate recognition of cyclin T2 from P-TEFb". Gene. 343 (1): 173–9. doi:10.1016/j.gene.2004.08.027. PMID 15563843.
  • Jang MK, Mochizuki K, Zhou M, Jeong HS, Brady JN, Ozato K (2005). "The bromodomain protein Brd4 is a positive regulatory component of P-TEFb and stimulates RNA polymerase II-dependent transcription". Mol. Cell. 19 (4): 523–34. doi:10.1016/j.molcel.2005.06.027. PMID 16109376.
  • Cottone G, Baldi A, Palescandolo E, Manente L, Penta R, Paggi MG, De Luca A (2006). "Pkn is a novel partner of cyclin T2a in muscle differentiation". J. Cell. Physiol. 207 (1): 232–7. doi:10.1002/jcp.20566. PMID 16331689. S2CID 7382847.
  • Simone C, Giordano A (2007). "Abrogation of signal-dependent activation of the cdk9/cyclin T2a complex in human RD rhabdomyosarcoma cells". Cell Death Differ. 14 (1): 192–5. doi:10.1038/sj.cdd.4402008. PMID 16841087.
  • Fu J, Yoon HG, Qin J, Wong J (2007). "Regulation of P-TEFb elongation complex activity by CDK9 acetylation". Mol. Cell. Biol. 27 (13): 4641–51. doi:10.1128/MCB.00857-06. PMC 1951478. PMID 17452463.

External links

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  • 2ivx: CRYSTAL STRUCTURE OF HUMAN CYCLIN T2 AT 1.8 A RESOLUTION (CASP TARGET)
    2ivx: CRYSTAL STRUCTURE OF HUMAN CYCLIN T2 AT 1.8 A RESOLUTION (CASP TARGET)
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