TRIM24

From Wikipedia, the free encyclopedia
Jump to: navigation, search
TRIM24
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases TRIM24, PTC6, RNF82, TF1A, TIF1, TIF1A, TIF1ALPHA, hTIF1, tripartite motif containing 24
External IDs MGI: 109275 HomoloGene: 20830 GeneCards: TRIM24
RNA expression pattern
PBB GE TRIM24 204391 x at fs.png

PBB GE TRIM24 213301 x at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003852
NM_015905

NM_001272064
NM_001272076
NM_145076

RefSeq (protein)

NP_003843
NP_056989

Location (UCSC) Chr 7: 138.46 – 138.59 Mb Chr 6: 37.87 – 37.97 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

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.[3][4][5]

Function[edit]

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.[3]

Interactions[edit]

TRIM24 has been shown to interact with Mineralocorticoid receptor,[4][6] TRIM33,[7] Estrogen receptor alpha[4][8] and Retinoid X receptor alpha.[4][9]

See also[edit]

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ a b "Entrez Gene: TRIM24 tripartite motif-containing 24". 
  4. ^ 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. 
  5. ^ 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. 
  6. ^ 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. 
  7. ^ 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. 
  8. ^ 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. 
  9. ^ 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. 

External links[edit]

Further reading[edit]

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