TRIM24

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.[5][6][7]

TRIM24
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2YYN, 3O33, 3O34, 3O35, 3O36, 3O37, 4YAB, 4YAD, 4YAT, 4YAX, 4YBM, 4YBS, 4YBT, 4YC9, 4ZQL
Identifiers
Aliases	TRIM24, PTC6, RNF82, TF1A, TIF1, TIF1A, TIF1ALPHA, hTIF1, tripartite motif containing 24
External IDs	OMIM: 603406 MGI: 109275 HomoloGene: 20830 GeneCards: TRIM24
Gene location (Human) Chr. Chromosome 7 (human)[1] Band 7q33-q34 Start 138,460,259 bp[1] End 138,589,996 bp[1]
Gene location (Mouse) Chr. Chromosome 6 (mouse)[2] Band 6|6 B1 Start 37,870,811 bp[2] End 37,966,296 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • protein kinase activity • sequence-specific DNA binding • DNA binding • GO:1904264, GO:1904822, GO:0090622, GO:0090302 ubiquitin protein ligase activity • GO:0001105 transcription coactivator activity • zinc ion binding • p53 binding • chromatin binding • metal ion binding • ubiquitin-protein transferase activity • methylated histone binding • estrogen response element binding • GO:0001948 protein binding • ligand-dependent nuclear receptor binding • lysine-acetylated histone binding • receptor binding • protein tyrosine kinase activity • transferase activity Cellular component • cytoplasm • nuclear euchromatin • cytosol • intracellular • perichromatin fibrils • cell nucleus • nucleoplasm Biological process • regulation of apoptotic process • regulation of transcription, DNA-templated • regulation of protein stability • calcium ion homeostasis • regulation of signal transduction by p53 class mediator • regulation of vitamin D receptor signaling pathway • transcription from RNA polymerase II promoter • transcription, DNA-templated • cellular response to estrogen stimulus • positive regulation of transcription, DNA-templated • protein phosphorylation • positive regulation of gene expression • protein catabolic process • protein ubiquitination • autophosphorylation • negative regulation of transcription, DNA-templated • negative regulation of cell proliferation • peptidyl-tyrosine phosphorylation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8805	21848
Ensembl	ENSG00000122779	ENSMUSG00000029833
UniProt	O15164	Q64127
RefSeq (mRNA)	NM_003852 NM_015905	NM_001272064 NM_001272076 NM_145076
RefSeq (protein)	NP_003843 NP_056989	NP_001258993 NP_001259005 NP_659542
Location (UCSC)	Chr 7: 138.46 – 138.59 Mb	Chr 6: 37.87 – 37.97 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[5]

Interactions

TRIM24 has been shown to interact with Mineralocorticoid receptor,[6][8] TRIM33,[9] Estrogen receptor alpha[6][10] and Retinoid X receptor alpha.[6][11]

See also

• Transcription coregulator

References

1. GRCh38: Ensembl release 89: ENSG00000122779 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000029833 - 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. "Entrez Gene: TRIM24 tripartite motif-containing 24".
6. 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.
7. 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.
8. 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.
9. 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.
10. 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.
11. 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

• 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. PMC 146346. 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 (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. PMC 1171701. 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/mend.14.8.0502. PMID 10935545.
• Seeler JS, Marchio A, Losson R, et al. (2001). "Common Properties of Nuclear Body Protein SP100 and TIF1α Chromatin Factor: Role of SUMO Modification". Mol. Cell. Biol. 21 (10): 3314–24. doi:10.1128/MCB.21.10.3314-3324.2001. PMC 100253. 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. PMC 125245. 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/mend.15.9.0689. 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.

External links

• TRIM24 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
• NURSA C150

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