MED1

MED1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases MED1, CRSP1, CRSP200, DRIP205, DRIP230, PBP, PPARBP, PPARGBP, RB18A, TRAP220, TRIP2, mediator complex subunit 1
External IDs MGI: 1100846 HomoloGene: 21002 GeneCards: MED1
RNA expression pattern


More reference expression data
Orthologs
Species Human Mouse
Entrez

5469

19014

Ensembl

ENSG00000125686

ENSMUSG00000018160

UniProt

Q15648

Q925J9

RefSeq (mRNA)

NM_004774

NM_001080118
NM_013634
NM_134027

RefSeq (protein)

NP_004765.2

NP_001073587.1
NP_038662.2
NP_598788.2

Location (UCSC) Chr 17: 39.4 – 39.45 Mb Chr 11: 98.15 – 98.19 Mb
PubMed search [1] [2]
Wikidata
View/Edit HumanView/Edit Mouse

Mediator of RNA polymerase II transcription subunit 1 also known as DRIP205 or Trap220 is a subunit of the Mediator complex and is a protein that in humans is encoded by the MED1 gene.[3][4][5] MED1 functions as a nuclear receptor coactivator.

Med1
Identifiers
Symbol Med1
Pfam PF10744
InterPro IPR019680

Function

The activation of gene transcription is a multistep process that is triggered by factors that recognize transcriptional enhancer sites in DNA. These factors work with co-activators to direct transcriptional initiation by the RNA polymerase II apparatus. The mediator of RNA polymerase II transcription subunit 1 protein is a subunit of the CRSP (cofactor required for SP1 activation) complex, which, along with TFIID, is required for efficient activation by SP1. This protein is also a component of other multisubunit complexes [e.g., thyroid hormone receptor-(TR-) associated proteins that interact with TR and facilitate TR function on DNA templates in conjunction with initiation factors and cofactors]. It also regulates p53-dependent apoptosis and it is essential for adipogenesis. This protein is known to have the ability to self-oligomerize.[5]

Interactions

MED1 has been shown to interact with:

Protein family

This entry represents subunit Med1 of the Mediator complex. The Med1 forms part of the Med9 submodule of the Srb/Med complex. It is one of three subunits essential for viability of the whole organism via its role in environmentally-directed cell-fate decisions.[21]

References

  1. ↑ "Human PubMed Reference:".
  2. ↑ "Mouse PubMed Reference:".
  3. ↑ Zhu Y, Qi C, Jain S, Rao MS, Reddy JK (November 1997). "Isolation and characterization of PBP, a protein that interacts with peroxisome proliferator-activated receptor". J Biol Chem. 272 (41): 25500–6. doi:10.1074/jbc.272.41.25500. PMID 9325263.
  4. ↑ Zhu Y, Qi C, Jain S, Le Beau MM, Espinosa R, Atkins GB, Lazar MA, Yeldandi AV, Rao MS, Reddy JK (October 1999). "Amplification and overexpression of peroxisome proliferator-activated receptor binding protein (PBP/PPARBP) gene in breast cancer". Proc Natl Acad Sci U S A. 96 (19): 10848–53. doi:10.1073/pnas.96.19.10848. PMC 17971Freely accessible. PMID 10485914.
  5. 1 2 "Entrez Gene: PPARBP PPAR binding protein".
  6. ↑ Wang Q, Sharma D, Ren Y, Fondell JD (November 2002). "A coregulatory role for the TRAP-mediator complex in androgen receptor-mediated gene expression". J. Biol. Chem. 277 (45): 42852–8. doi:10.1074/jbc.M206061200. PMID 12218053.
  7. ↑ Wada O, Oishi H, Takada I, Yanagisawa J, Yano T, Kato S (August 2004). "BRCA1 function mediates a TRAP/DRIP complex through direct interaction with TRAP220". Oncogene. 23 (35): 6000–5. doi:10.1038/sj.onc.1207786. PMID 15208681.
  8. 1 2 Ito M, Yuan CX, Malik S, Gu W, Fondell JD, Yamamura S, Fu ZY, Zhang X, Qin J, Roeder RG (March 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.
  9. 1 2 Kitagawa H, Fujiki R, Yoshimura K, Mezaki Y, Uematsu Y, Matsui D, Ogawa S, Unno K, Okubo M, Tokita A, Nakagawa T, Ito T, Ishimi Y, Nagasawa H, Matsumoto T, Yanagisawa J, Kato S (June 2003). "The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome". Cell. 113 (7): 905–17. doi:10.1016/s0092-8674(03)00436-7. PMID 12837248.
  10. 1 2 Kang YK, Guermah M, Yuan CX, Roeder RG (March 2002). "The TRAP/Mediator coactivator complex interacts directly with estrogen receptors alpha and beta through the TRAP220 subunit and directly enhances estrogen receptor function in vitro". Proc. Natl. Acad. Sci. U.S.A. 99 (5): 2642–7. doi:10.1073/pnas.261715899. PMC 122401Freely accessible. PMID 11867769.
  11. ↑ Zilliacus J, Holter E, Wakui H, Tazawa H, Treuter E, Gustafsson JA (April 2001). "Regulation of glucocorticoid receptor activity by 14--3-3-dependent intracellular relocalization of the corepressor RIP140". Mol. Endocrinol. 15 (4): 501–11. doi:10.1210/mend.15.4.0624. PMID 11266503.
  12. ↑ Hittelman AB, Burakov D, Iñiguez-Lluhí JA, Freedman LP, Garabedian MJ (October 1999). "Differential regulation of glucocorticoid receptor transcriptional activation via AF-1-associated proteins". EMBO J. 18 (19): 5380–8. doi:10.1093/emboj/18.19.5380. PMC 1171607Freely accessible. PMID 10508170.
  13. ↑ Maeda Y, Rachez C, Hawel L, Byus CV, Freedman LP, Sladek FM (July 2002). "Polyamines modulate the interaction between nuclear receptors and vitamin D receptor-interacting protein 205". Mol. Endocrinol. 16 (7): 1502–10. doi:10.1210/mend.16.7.0883. PMID 12089346.
  14. ↑ Malik S, Wallberg AE, Kang YK, Roeder RG (August 2002). "TRAP/SMCC/mediator-dependent transcriptional activation from DNA and chromatin templates by orphan nuclear receptor hepatocyte nuclear factor 4". Mol. Cell. Biol. 22 (15): 5626–37. doi:10.1128/mcb.22.15.5626-5637.2002. PMC 133960Freely accessible. PMID 12101254.
  15. ↑ Frade R, Balbo M, Barel M (December 2000). "RB18A, whose gene is localized on chromosome 17q12-q21.1, regulates in vivo p53 transactivating activity". Cancer Res. 60 (23): 6585–9. PMID 11118038.
  16. ↑ Drané P, Barel M, Balbo M, Frade R (December 1997). "Identification of RB18A, a 205 kDa new p53 regulatory protein which shares antigenic and functional properties with p53". Oncogene. 15 (25): 3013–24. doi:10.1038/sj.onc.1201492. PMID 9444950.
  17. ↑ Wallberg AE, Yamamura S, Malik S, Spiegelman BM, Roeder RG (November 2003). "Coordination of p300-mediated chromatin remodeling and TRAP/mediator function through coactivator PGC-1alpha". Mol. Cell. 12 (5): 1137–49. doi:10.1016/s1097-2765(03)00391-5. PMID 14636573.
  18. ↑ Kodera Y, Takeyama K, Murayama A, Suzawa M, Masuhiro Y, Kato S (October 2000). "Ligand type-specific interactions of peroxisome proliferator-activated receptor gamma with transcriptional coactivators". J. Biol. Chem. 275 (43): 33201–4. doi:10.1074/jbc.C000517200. PMID 10944516.
  19. ↑ Misra P, Qi C, Yu S, Shah SH, Cao WQ, Rao MS, Thimmapaya B, Zhu Y, Reddy JK (May 2002). "Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation". J. Biol. Chem. 277 (22): 20011–9. doi:10.1074/jbc.M201739200. PMID 11912212.
  20. ↑ Yuan CX, Ito M, Fondell JD, Fu ZY, Roeder RG (July 1998). "The TRAP220 component of a thyroid hormone receptor- associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion". Proc. Natl. Acad. Sci. U.S.A. 95 (14): 7939–44. doi:10.1073/pnas.95.14.7939. PMC 20908Freely accessible. PMID 9653119.
  21. ↑ Boube M, Joulia L, Cribbs DL, Bourbon HM (July 2002). "Evidence for a mediator of RNA polymerase II transcriptional regulation conserved from yeast to man". Cell. 110 (2): 143–51. doi:10.1016/s0092-8674(02)00830-9. PMID 12150923.

Further reading

This article incorporates text from the public domain Pfam and InterPro IPR019680

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