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{{Infobox_gene}}
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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]].<ref name="entrez"/><ref name="pmid9115274">{{cite journal |vauthors=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 |date=May 1997 | pmid = 9115274 | doi = 10.1074/jbc.272.18.12062| url = http://www.jbc.org/cgi/content/full/272/18/12062 }}</ref><ref name="pmid9191165">{{cite journal |vauthors=Le Douarin B, Nielsen AL, You J, Chambon P, Losson R | 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 |date=May 1997 | pmid = 9191165 | doi = | url = }}</ref>
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== Function ==
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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 receptor|estrogen]], [[retinoic acid receptor|retinoic acid]], and [[calcitriol receptor|vitamin D<sub>3</sub> receptor]]s. 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 family|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|coiled-coil]] region. Two [[alternative splicing|alternatively spliced]] transcript variants encoding different isoforms have been described for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: TRIM24 tripartite motif-containing 24| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8805| accessdate = }}</ref>
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Tripartite motif-containing 24
| HGNCid = 11812
| Symbol = TRIM24
| AltSymbols =; PTC6; RNF82; TF1A; TIF1; TIF1A; TIF1ALPHA; hTIF1
| OMIM = 603406
| ECnumber = 
| Homologene = 20830
| MGIid = 109275
| GeneAtlas_image1 = PBB_GE_TRIM24_204391_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_TRIM24_213301_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003704 |text = specific RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016922 |text = ligand-dependent nuclear receptor binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 8805
    | Hs_Ensembl = ENSG00000122779
    | Hs_RefseqProtein = NP_003843
    | Hs_RefseqmRNA = NM_003852
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 137795619
    | Hs_GenLoc_end = 137921233
    | Hs_Uniprot = O15164
    | Mm_EntrezGene = 21848
    | Mm_Ensembl = ENSMUSG00000029833
    | Mm_RefseqmRNA = NM_145076
    | Mm_RefseqProtein = NP_659542
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 6
    | Mm_GenLoc_start = 37800419
    | Mm_GenLoc_end = 37895904
    | Mm_Uniprot = Q3TLF2
  }}
}}
'''Tripartite motif-containing 24''', also known as '''TRIM24''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TRIM24 tripartite motif-containing 24| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8805| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
==Interactions==
{{PBB_Summary
TRIM24 has been shown to [[Protein-protein interaction|interact]] with [[Mineralocorticoid receptor]],<ref name=pmid9115274 /><ref name=pmid11518808>{{cite journal |last=Zennaro |first=M C |authorlink= |author2=Souque A |author3=Viengchareun S |author4=Poisson E |author5=Lombès M  |date=September 2001 |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 |publisher= |location = United States| issn = 0888-8809| pmid = 11518808 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1210/mend.15.9.0689 }}</ref> [[TRIM33]],<ref name=pmid12096914>{{cite journal |last=Peng |first=Hongzhuang |authorlink= |author2=Feldman Irina |author3=Rauscher Frank J  |date=July 2002 |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 |publisher= |location = England| issn = 0022-2836| pmid = 12096914 |doi = 10.1016/S0022-2836(02)00477-1 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[Estrogen receptor alpha]]<ref name=pmid9115274/><ref name=pmid10598587>{{cite journal |last=Thénot |first=S |authorlink= |author2=Bonnet S |author3=Boulahtouf A |author4=Margeat E |author5=Royer C A |author6=Borgna J L |author7=Cavaillès V  |date=Dec 1999 |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 |publisher= |location = United States| issn = 0888-8809| pmid = 10598587 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1210/me.13.12.2137 }}</ref> and [[Retinoid X receptor alpha]].<ref name=pmid9115274/><ref name=pmid11851396>{{cite journal |last=Lee |first=Wen-yi |authorlink= |author2=Noy Noa  |date=February 2002 |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 |publisher= |location = United States| issn = 0006-2960| pmid = 11851396 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1021/bi011764 }}</ref>
| 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.<ref name="entrez">{{cite web | title = Entrez Gene: TRIM24 tripartite motif-containing 24| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8805| accessdate = }}</ref>
}}


==See also==
==See also==
Line 59: Line 13:


==References==
==References==
{{reflist|2}}
{{Reflist}}


==Further reading==
==Further reading==
{{refbegin | 2}}
{{Refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading
| citations =  
| 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   |vauthors=Le Douarin B, Nielsen AL, You J, etal |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=  }}
*{{cite journal   |vauthors=Moosmann P, Georgiev O, Le Douarin B, etal |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  | pmc=146346 }}
*{{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=  }}
*{{cite journal  |vauthors=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= }}
*{{cite journal   |vauthors=Fraser RA, Heard DJ, Adam S, etal |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=  }}
*{{cite journal   |vauthors=Eng FC, Barsalou A, Akutsu N, etal |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   |vauthors=Venturini L, You J, Stadler M, etal |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   |vauthors=Remboutsika E, Lutz Y, Gansmuller A, etal |title=The putative nuclear receptor mediator TIF1alpha is tightly associated with euchromatin |journal=J. Cell Sci. |volume=112 |issue=  11|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  |vauthors=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   |vauthors=Nielsen AL, Ortiz JA, You J, etal |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 | pmc=1171701 }}
*{{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= }}
*{{cite journal   |vauthors=Thénot S, Bonnet S, Boulahtouf A, etal |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   |vauthors=Zhong S, Delva L, Rachez C, etal |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=  }}
*{{cite journal   |vauthors=Hellal-Levy C, Fagart J, Souque A, etal |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/mend.14.8.0502 }}
*{{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   |vauthors=Seeler JS, Marchio A, Losson R, etal |title=Common Properties of Nuclear Body Protein SP100 and TIF1α 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 | pmc=100253 }}
*{{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   |vauthors=Reymond A, Meroni G, Fantozzi A, etal |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 | pmc=125245 }}
*{{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=  }}
*{{cite journal   |vauthors=Zennaro MC, Souque A, Viengchareun S, etal |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/mend.15.9.0689 }}
*{{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=  }}
*{{cite journal  |vauthors=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   |vauthors=Gandini D, De Angeli C, Aguiari G, etal |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  |vauthors=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 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 | pmc=139241 |bibcode=2002PNAS...9916899M }}
}}
}}
{{refend}}
{{Refend}}
 
==External links==
==External links==
* {{MeshName|TRIM24+protein,+human}}
* {{MeshName|TRIM24+protein,+human|3=TRIM24 protein, human}}
 
* {{NURSA|C150}}
{{protein-stub}}
{{NLM content}}
{{NLM content}}
{{Transcription coregulators}}
{{Transcription coregulators}}
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{{PBB_Controls
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[[Category:Gene expression]]
[[Category:Gene expression]]
[[Category:Transcription coregulators]]
[[Category:Transcription coregulators]]
{{WikiDoc Sources}}

Latest revision as of 23:35, 13 July 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
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Wikidata
View/Edit Human

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]

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.[1]

Interactions

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

References

  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.

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