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
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesTRIM24, PTC6, RNF82, TF1A, TIF1, TIF1A, TIF1ALPHA, hTIF1, tripartite motif containing 24
External IDsOMIM: 603406 MGI: 109275 HomoloGene: 20830 GeneCards: TRIM24
Gene location (Human)
Chr.Chromosome 7 (human)[1]
Band7q33-q34Start138,460,259 bp[1]
End138,589,996 bp[1]
RNA expression pattern


More reference expression data
Orthologs
SpeciesHumanMouse
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 MbChr 6: 37.87 – 37.97 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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

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. doi:10.1042/bst0250605. 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

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

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