MED4

MED4
Identifiers
Aliases	MED4, ARC36, DRIP36, HSPC126, TRAP36, VDRIP, mediator complex subunit 4
External IDs	MGI: 1914631 HomoloGene: 8568 GeneCards: MED4
Gene ontology Molecular function • thyroid hormone receptor binding • protein binding • transcription cofactor activity • ligand-dependent nuclear receptor transcription coactivator activity • vitamin D receptor binding • receptor activity • RNA polymerase II transcription cofactor activity Cellular component • core mediator complex • membrane • nucleus • mediator complex • nucleoplasm Biological process • regulation of transcription from RNA polymerase II promoter • positive regulation of transcription, DNA-templated • androgen receptor signaling pathway • intracellular steroid hormone receptor signaling pathway • regulation of transcription, DNA-templated • transcription from RNA polymerase II promoter • transcription, DNA-templated • transcription initiation from RNA polymerase II promoter Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	29079	67381
Ensembl	ENSG00000136146	ENSMUSG00000022109
UniProt	Q9NPJ6	Q9CQA5
RefSeq (mRNA)	NM_014166 NM_001270629	NM_026119
RefSeq (protein)	NP_001257558.1 NP_054885.1	NP_080395.1
Location (UCSC)	Chr 13: 48.05 – 48.1 Mb	Chr 14: 73.51 – 73.52 Mb
PubMed search	[1]	[2]
Wikidata

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Med4
Identifiers
Symbol	Med4
Pfam	PF10018
InterPro	IPR019258
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Mediator of RNA polymerase II transcription subunit 4 also known as mediator complex subunit 4 (MED4), a component of Mediator or vitamin D3 receptor-interacting protein complex 36 kDa component (DRIP36) is a protein that in humans is encoded by the MED4 gene.^[3][4][5]

Function

The protein encoded by this gene is a component of the vitamin D receptor-interacting protein (DRIP) complex which functions as a nuclear receptor coactivator. The DRIP complex is capable of activating nuclear receptors in a ligand-dependent manner.^[4]

Interactions

MED4 has been shown to interact with MED25.^[6]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. "Entrez Gene: MED4 mediator of RNA polymerase II transcription, subunit 4 homolog (S. cerevisiae)".
4. Rachez C, Lemon BD, Suldan Z, Bromleigh V, Gamble M, Näär AM, Erdjument-Bromage H, Tempst P, Freedman LP (April 1999). "Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex". Nature. 398 (6730): 824–8. doi:10.1038/19783. PMID 10235266.
5. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z (October 2000). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Research. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
6. Tomomori-Sato C, Sato S, Parmely TJ, Banks CA, Sorokina I, Florens L, Zybailov B, Washburn MP, Brower CS, Conaway RC, Conaway JW (Feb 2004). "A mammalian mediator subunit that shares properties with Saccharomyces cerevisiae mediator subunit Cse2". J. Biol. Chem. 279 (7): 5846–51. doi:10.1074/jbc.M312523200. PMID 14638676.

Further reading

• Conaway JW, Florens L, Sato S, Tomomori-Sato C, Parmely TJ, Yao T, Swanson SK, Banks CA, Washburn MP, Conaway RC (2005). "The mammalian Mediator complex.". FEBS Lett. 579 (4): 904–8. doi:10.1016/j.febslet.2004.11.031. PMID 15680972.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene. 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene. 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Ito M, Yuan CX, Malik S, Gu W, Fondell JD, Yamamura S, Fu ZY, Zhang X, Qin J, Roeder RG (1999). "Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators.". Mol. Cell. 3 (3): 361–70. doi:10.1016/S1097-2765(00)80463-3. PMID 10198638.
• Rachez C, Lemon BD, Suldan Z, Bromleigh V, Gamble M, Näär AM, Erdjument-Bromage H, Tempst P, Freedman LP (1999). "Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex.". Nature. 398 (6730): 824–8. doi:10.1038/19783. PMID 10235266.
• Näär AM, Beaurang PA, Zhou S, Abraham S, Solomon W, Tjian R (1999). "Composite co-activator ARC mediates chromatin-directed transcriptional activation.". Nature. 398 (6730): 828–32. doi:10.1038/19789. PMID 10235267.
• Malik S, Gu W, Wu W, Qin J, Roeder RG (2000). "The USA-derived transcriptional coactivator PC2 is a submodule of TRAP/SMCC and acts synergistically with other PCs.". Mol. Cell. 5 (4): 753–60. doi:10.1016/S1097-2765(00)80254-3. PMID 10882111.
• Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z (2001). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells.". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.