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Tripartite motif-containing 24
Identifiers
Symbols TRIM24; PTC6; RNF82; TF1A; TIF1; TIF1A; TIF1ALPHA; hTIF1
External IDs OMIM603406 MGI109275 HomoloGene20830 GeneCards: TRIM24 Gene
RNA expression pattern
PBB GE TRIM24 204391 x at tn.png
PBB GE TRIM24 213301 x at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 8805 21848
Ensembl ENSG00000122779 ENSMUSG00000029833
UniProt O15164 Q3TLF2
RefSeq (mRNA) NM_003852 NM_145076
RefSeq (protein) NP_003843 NP_659542
Location (UCSC) Chr 7:
137.8 - 137.92 Mb
Chr 6:
37.8 - 37.9 Mb
PubMed search [1] [2]

Tripartite motif-containing 24 (TRIM24) also known as transcriptional intermediary factor 1α (TIF1α) is a protein which in humans is encoded by the TRIM24 gene.[1][2][3]

Contents

Function

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]

Interactions

TRIM24 has been shown to interact with Mineralocorticoid receptor,[4][2] TRIM33,[5] Estrogen receptor alpha[2][6] and Retinoid X receptor alpha.[2][7]

See also

References

  1. ^ a b "Entrez Gene: TRIM24 tripartite motif-containing 24". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8805.  
  2. ^ a b c d Thénot S, Henriquet C, Rochefort H, Cavaillès V (May 1997). "Differential interaction of nuclear receptors with the putative human transcriptional coactivator hTIF1". J. Biol. Chem. 272 (18): 12062–8. doi:10.1074/jbc.272.18.12062. PMID 9115274. http://www.jbc.org/cgi/content/full/272/18/12062.  
  3. ^ Le Douarin B, Nielsen AL, You J, Chambon P, Losson R (May 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.  
  4. ^ Zennaro, M C; Souque A, Viengchareun S, Poisson E, Lombès M (Sep. 2001). "A new human MR splice variant is a ligand-independent transactivator modulating corticosteroid action". Mol. Endocrinol. (United States) 15 (9): 1586–98. ISSN 0888-8809. PMID 11518808.  
  5. ^ Peng, Hongzhuang; Feldman Irina, Rauscher Frank J (Jul. 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. (England) 320 (3): 629–44. doi:10.1016/S0022-2836(02)00477-1. ISSN 0022-2836. PMID 12096914.  
  6. ^ Thénot, S; Bonnet S, Boulahtouf A, Margeat E, Royer C A, Borgna J L, Cavaillès V (Dec. 1999). "Effect of ligand and DNA binding on the interaction between human transcription intermediary factor 1alpha and estrogen receptors". Mol. Endocrinol. (UNITED STATES) 13 (12): 2137–50. ISSN 0888-8809. PMID 10598587.  
  7. ^ Lee, Wen-yi; Noy Noa (Feb. 2002). "Interactions of RXR with coactivators are differentially mediated by helix 11 of the receptor's ligand binding domain". Biochemistry (United States) 41 (8): 2500–8. ISSN 0006-2960. PMID 11851396.  

External links

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. doi:10.1093/nar/24.24.4859. 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. doi:10.1074/jbc.272.18.12062. 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. doi:10.1074/jbc.273.26.16199. 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. doi:10.1074/jbc.273.43.28371. 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. doi:10.1210/me.13.12.2137. 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. doi:10.1210/me.14.8.1210. 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. doi:10.1210/me.15.9.1586. 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. doi:10.1021/bi011764+. 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.  

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

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