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External IDsGeneCards: [1]
RefSeq (mRNA)



RefSeq (protein)



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


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]


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

See also


  1. 1.0 1.1 "Entrez Gene: TRIM24 tripartite motif-containing 24".
  2. 2.0 2.1 2.2 2.3 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.
  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 (September 2001). "A new human MR splice variant is a ligand-independent transactivator modulating corticosteroid action". Mol. Endocrinol. United States. 15 (9): 1586–98. doi:10.1210/mend.15.9.0689. ISSN 0888-8809. PMID 11518808.
  5. Peng, Hongzhuang; Feldman Irina; Rauscher Frank J (July 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. doi:10.1210/me.13.12.2137. ISSN 0888-8809. PMID 10598587.
  7. Lee, Wen-yi; Noy Noa (February 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. doi:10.1021/bi011764. ISSN 0006-2960. PMID 11851396.

Further reading

External links

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