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

section_title =
summary_text = 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.cite web | title = Entrez Gene: TRIM24 tripartite motif-containing 24| url =| accessdate = ]

ee also

* Transcription coregulator


External links


Further reading

citations =
*cite journal | author=Le Douarin B, Nielsen AL, You J, "et al." |title=TIF1 alpha: a chromatin-specific mediator for the ligand-dependent activation function AF-2 of nuclear receptors? |journal=Biochem. Soc. Trans. |volume=25 |issue= 2 |pages= 605–12 |year= 1997 |pmid= 9191165 |doi=
*cite journal | author=Moosmann P, Georgiev O, Le Douarin B, "et al." |title=Transcriptional repression by RING finger protein TIF1 beta that interacts with the KRAB repressor domain of KOX1. |journal=Nucleic Acids Res. |volume=24 |issue= 24 |pages= 4859–67 |year= 1997 |pmid= 9016654 |doi=10.1093/nar/24.24.4859
*cite journal | author=Thénot S, Henriquet C, Rochefort H, Cavaillès V |title=Differential interaction of nuclear receptors with the putative human transcriptional coactivator hTIF1. |journal=J. Biol. Chem. |volume=272 |issue= 18 |pages= 12062–8 |year= 1997 |pmid= 9115274 |doi=10.1074/jbc.272.18.12062
*cite journal | author=Fraser RA, Heard DJ, Adam S, "et al." |title=The putative cofactor TIF1alpha is a protein kinase that is hyperphosphorylated upon interaction with liganded nuclear receptors. |journal=J. Biol. Chem. |volume=273 |issue= 26 |pages= 16199–204 |year= 1998 |pmid= 9632676 |doi=10.1074/jbc.273.26.16199
*cite journal | author=Eng FC, Barsalou A, Akutsu N, "et al." |title=Different classes of coactivators recognize distinct but overlapping binding sites on the estrogen receptor ligand binding domain. |journal=J. Biol. Chem. |volume=273 |issue= 43 |pages= 28371–7 |year= 1998 |pmid= 9774463 |doi=10.1074/jbc.273.43.28371
*cite journal | author=Venturini L, You J, Stadler M, "et al." |title=TIF1gamma, a novel member of the transcriptional intermediary factor 1 family. |journal=Oncogene |volume=18 |issue= 5 |pages= 1209–17 |year= 1999 |pmid= 10022127 |doi= 10.1038/sj.onc.1202655
*cite journal | author=Remboutsika E, Lutz Y, Gansmuller A, "et al." |title=The putative nuclear receptor mediator TIF1alpha is tightly associated with euchromatin. |journal=J. Cell. Sci. |volume=112 ( Pt 11) |issue= |pages= 1671–83 |year= 1999 |pmid= 10318760 |doi=
*cite journal | author=Klugbauer S, Rabes HM |title=The transcription coactivator HTIF1 and a related protein are fused to the RET receptor tyrosine kinase in childhood papillary thyroid carcinomas. |journal=Oncogene |volume=18 |issue= 30 |pages= 4388–93 |year= 1999 |pmid= 10439047 |doi= 10.1038/sj.onc.1202824
*cite journal | author=Nielsen AL, Ortiz JA, You J, "et al." |title=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. |journal=Embo J. |volume=18 |issue= 22 |pages= 6385–95 |year= 2000 |pmid= 10562550 |doi= 10.1093/emboj/18.22.6385
*cite journal | author=Thénot S, Bonnet S, Boulahtouf A, "et al." |title=Effect of ligand and DNA binding on the interaction between human transcription intermediary factor 1alpha and estrogen receptors. |journal=Mol. Endocrinol. |volume=13 |issue= 12 |pages= 2137–50 |year= 2000 |pmid= 10598587 |doi=10.1210/me.13.12.2137
*cite journal | author=Zhong S, Delva L, Rachez C, "et al." |title=A RA-dependent, tumour-growth suppressive transcription complex is the target of the PML-RARalpha and T18 oncoproteins. |journal=Nat. Genet. |volume=23 |issue= 3 |pages= 287–95 |year= 1999 |pmid= 10610177 |doi= 10.1038/15463
*cite journal | author=Hellal-Levy C, Fagart J, Souque A, "et al." |title=Crucial role of the H11-H12 loop in stabilizing the active conformation of the human mineralocorticoid receptor. |journal=Mol. Endocrinol. |volume=14 |issue= 8 |pages= 1210–21 |year= 2001 |pmid= 10935545 |doi=10.1210/me.14.8.1210
*cite journal | author=Seeler JS, Marchio A, Losson R, "et al." |title=Common properties of nuclear body protein SP100 and TIF1alpha chromatin factor: role of SUMO modification. |journal=Mol. Cell. Biol. |volume=21 |issue= 10 |pages= 3314–24 |year= 2001 |pmid= 11313457 |doi= 10.1128/MCB.21.10.3314-3324.2001
*cite journal | author=Reymond A, Meroni G, Fantozzi A, "et al." |title=The tripartite motif family identifies cell compartments. |journal=Embo J. |volume=20 |issue= 9 |pages= 2140–51 |year= 2001 |pmid= 11331580 |doi= 10.1093/emboj/20.9.2140
*cite journal | author=Zennaro MC, Souque A, Viengchareun S, "et al." |title=A new human MR splice variant is a ligand-independent transactivator modulating corticosteroid action. |journal=Mol. Endocrinol. |volume=15 |issue= 9 |pages= 1586–98 |year= 2002 |pmid= 11518808 |doi=10.1210/me.15.9.1586
*cite journal | author=Lee WY, Noy N |title=Interactions of RXR with coactivators are differentially mediated by helix 11 of the receptor's ligand binding domain. |journal=Biochemistry |volume=41 |issue= 8 |pages= 2500–8 |year= 2002 |pmid= 11851396 |doi=10.1021/bi011764+
*cite journal | author=Gandini D, De Angeli C, Aguiari G, "et al." |title=Preferential expression of the transcription coactivator HTIF1alpha gene in acute myeloid leukemia and MDS-related AML. |journal=Leukemia |volume=16 |issue= 5 |pages= 886–93 |year= 2002 |pmid= 11986951 |doi= 10.1038/sj.leu.2402452
*cite journal | author=Peng H, Feldman I, Rauscher FJ |title=Hetero-oligomerization among the TIF family of RBCC/TRIM domain-containing nuclear cofactors: a potential mechanism for regulating the switch between coactivation and corepression. |journal=J. Mol. Biol. |volume=320 |issue= 3 |pages= 629–44 |year= 2002 |pmid= 12096914 |doi= 10.1016/S0022-2836(02)00477-1
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899

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