TRIM24

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Tripartite motif-containing 24
Identifiers
Symbols TRIM24 ; PTC6; RNF82; TF1A; TIF1; TIF1A; TIF1ALPHA; hTIF1
External IDs Template:OMIM5 Template:MGI HomoloGene20830
RNA expression pattern
File:PBB GE TRIM24 204391 x at tn.png
File:PBB GE TRIM24 213301 x at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Tripartite motif-containing 24, also known as TRIM24, is a human gene.[1]

The protein encoded by this gene mediates transcriptional control by interaction with the activation function 2 (AF2) region of several nuclear receptors, including the estrogen, retinoic acid, and vitamin D3 receptors. The protein localizes to nuclear bodies and is thought to associate with chromatin and heterochromatin-associated factors. The protein is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains - a RING, a B-box type 1 and a B-box type 2 - and a coiled-coil region. Two alternatively spliced transcript variants encoding different isoforms have been described for this gene.[1]

See also

References

  1. 1.0 1.1 "Entrez Gene: TRIM24 tripartite motif-containing 24".

Further reading

  • Le Douarin B, Nielsen AL, You J; et al. (1997). "TIF1 alpha: a chromatin-specific mediator for the ligand-dependent activation function AF-2 of nuclear receptors?". Biochem. Soc. Trans. 25 (2): 605–12. PMID 9191165.
  • Moosmann P, Georgiev O, Le Douarin B; et al. (1997). "Transcriptional repression by RING finger protein TIF1 beta that interacts with the KRAB repressor domain of KOX1". Nucleic Acids Res. 24 (24): 4859–67. PMID 9016654.
  • Thénot S, Henriquet C, Rochefort H, Cavaillès V (1997). "Differential interaction of nuclear receptors with the putative human transcriptional coactivator hTIF1". J. Biol. Chem. 272 (18): 12062–8. PMID 9115274.
  • Fraser RA, Heard DJ, Adam S; et al. (1998). "The putative cofactor TIF1alpha is a protein kinase that is hyperphosphorylated upon interaction with liganded nuclear receptors". J. Biol. Chem. 273 (26): 16199–204. PMID 9632676.
  • Eng FC, Barsalou A, Akutsu N; et al. (1998). "Different classes of coactivators recognize distinct but overlapping binding sites on the estrogen receptor ligand binding domain". J. Biol. Chem. 273 (43): 28371–7. PMID 9774463.
  • Venturini L, You J, Stadler M; et al. (1999). "TIF1gamma, a novel member of the transcriptional intermediary factor 1 family". Oncogene. 18 (5): 1209–17. doi:10.1038/sj.onc.1202655. PMID 10022127.
  • Remboutsika E, Lutz Y, Gansmuller A; et al. (1999). "The putative nuclear receptor mediator TIF1alpha is tightly associated with euchromatin". J. Cell. Sci. 112 ( Pt 11): 1671–83. PMID 10318760.
  • Klugbauer S, Rabes HM (1999). "The transcription coactivator HTIF1 and a related protein are fused to the RET receptor tyrosine kinase in childhood papillary thyroid carcinomas". Oncogene. 18 (30): 4388–93. doi:10.1038/sj.onc.1202824. PMID 10439047.
  • Nielsen AL, Ortiz JA, You J; et al. (2000). "Interaction with members of the heterochromatin protein 1 (HP1) family and histone deacetylation are differentially involved in transcriptional silencing by members of the TIF1 family". EMBO J. 18 (22): 6385–95. doi:10.1093/emboj/18.22.6385. PMID 10562550.
  • Thénot S, Bonnet S, Boulahtouf A; et al. (2000). "Effect of ligand and DNA binding on the interaction between human transcription intermediary factor 1alpha and estrogen receptors". Mol. Endocrinol. 13 (12): 2137–50. PMID 10598587.
  • Zhong S, Delva L, Rachez C; et al. (1999). "A RA-dependent, tumour-growth suppressive transcription complex is the target of the PML-RARalpha and T18 oncoproteins". Nat. Genet. 23 (3): 287–95. doi:10.1038/15463. PMID 10610177.
  • Hellal-Levy C, Fagart J, Souque A; et al. (2001). "Crucial role of the H11-H12 loop in stabilizing the active conformation of the human mineralocorticoid receptor". Mol. Endocrinol. 14 (8): 1210–21. PMID 10935545.
  • Seeler JS, Marchio A, Losson R; et al. (2001). "Common properties of nuclear body protein SP100 and TIF1alpha chromatin factor: role of SUMO modification". Mol. Cell. Biol. 21 (10): 3314–24. doi:10.1128/MCB.21.10.3314-3324.2001. PMID 11313457.
  • Reymond A, Meroni G, Fantozzi A; et al. (2001). "The tripartite motif family identifies cell compartments". EMBO J. 20 (9): 2140–51. doi:10.1093/emboj/20.9.2140. PMID 11331580.
  • Zennaro MC, Souque A, Viengchareun S; et al. (2002). "A new human MR splice variant is a ligand-independent transactivator modulating corticosteroid action". Mol. Endocrinol. 15 (9): 1586–98. PMID 11518808.
  • Lee WY, Noy N (2002). "Interactions of RXR with coactivators are differentially mediated by helix 11 of the receptor's ligand binding domain". Biochemistry. 41 (8): 2500–8. PMID 11851396.
  • Gandini D, De Angeli C, Aguiari G; et al. (2002). "Preferential expression of the transcription coactivator HTIF1alpha gene in acute myeloid leukemia and MDS-related AML". Leukemia. 16 (5): 886–93. doi:10.1038/sj.leu.2402452. PMID 11986951.
  • Peng H, Feldman I, Rauscher FJ (2002). "Hetero-oligomerization among the TIF family of RBCC/TRIM domain-containing nuclear cofactors: a potential mechanism for regulating the switch between coactivation and corepression". J. Mol. Biol. 320 (3): 629–44. doi:10.1016/S0022-2836(02)00477-1. PMID 12096914.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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