GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Mediator of RNA polymerase II transcription subunit 1 (Activator-recruited cofactor 205 kDa component) (ARC205) (Mediator complex subunit 1) (Peroxisome proliferator-activated receptor-binding protein) (PBP) (PPAR-binding protein) (Thyroid hormone receptor-associated protein complex 220 kDa component) (Trap220) (Thyroid receptor-interacting protein 2) (TR-interacting protein 2) (TRIP-2) (Vitamin D receptor-interacting protein complex component DRIP205) (p53 regulatory protein RB18A)

 MED1_HUMAN              Reviewed;        1581 AA.
Q15648; A2RRQ6; O43810; O75447; Q6P9H7; Q6PK58; Q9HD39;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
11-SEP-2007, sequence version 4.
23-FEB-2022, entry version 206.
RecName: Full=Mediator of RNA polymerase II transcription subunit 1;
AltName: Full=Activator-recruited cofactor 205 kDa component;
Short=ARC205;
AltName: Full=Mediator complex subunit 1;
AltName: Full=Peroxisome proliferator-activated receptor-binding protein;
Short=PBP;
Short=PPAR-binding protein;
AltName: Full=Thyroid hormone receptor-associated protein complex 220 kDa component;
Short=Trap220;
AltName: Full=Thyroid receptor-interacting protein 2;
Short=TR-interacting protein 2;
Short=TRIP-2;
AltName: Full=Vitamin D receptor-interacting protein complex component DRIP205;
AltName: Full=p53 regulatory protein RB18A;
Name=MED1;
Synonyms=ARC205, CRSP1, CRSP200, DRIP205, DRIP230, PBP, PPARBP, PPARGBP,
RB18A, TRAP220, TRIP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DNA-BINDING, INTERACTION WITH TP53,
AND TISSUE SPECIFICITY.
TISSUE=Heart;
PubMed=9444950; DOI=10.1038/sj.onc.1201492;
Drane P., Barel M., Balbo M., Frade R.;
"Identification of RB18A, a 205 kDa new p53 regulatory protein which shares
antigenic and functional properties with p53.";
Oncogene 15:3013-3024(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 157-168;
943-952 AND 1432-1442, FUNCTION, INTERACTION WITH ESR1; PPARA; PPARG; RARA;
RXRA; THRA AND VDR, TISSUE SPECIFICITY, AND MUTAGENESIS OF 607-LEU-LEU-608
AND 648-LEU-LEU-649.
PubMed=9653119; DOI=10.1073/pnas.95.14.7939;
Yuan C.-X., Ito M., Fondell J.D., Fu Z.-Y., Roeder R.G.;
"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. 95:7939-7944(1998).
[3]
ERRATUM OF PUBMED:9653119.
Yuan C.-X., Ito M., Fondell J.D., Fu Z.-Y., Roeder R.G.;
Proc. Natl. Acad. Sci. U.S.A. 95:14584-14584(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Colon, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 1-13 AND 1452-1464, AND IDENTIFICATION IN THE ARC
COMPLEX.
PubMed=10235267; DOI=10.1038/19789;
Naeaer A.M., Beaurang P.A., Zhou S., Abraham S., Solomon W.B., Tjian R.;
"Composite co-activator ARC mediates chromatin-directed transcriptional
activation.";
Nature 398:828-832(1999).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 16-1581 (ISOFORM 1), INTERACTION WITH VDR,
AND MUTAGENESIS OF 607-LEU-LEU-608 AND 648-LEU-LEU-649.
PubMed=10733574; DOI=10.1128/mcb.20.8.2718-2726.2000;
Rachez C., Gamble M., Chang C.-P.B., Atkins G.B., Lazar M.A.,
Freedman L.P.;
"The DRIP complex and SRC-1/p160 coactivators share similar nuclear
receptor binding determinants but constitute functionally distinct
complexes.";
Mol. Cell. Biol. 20:2718-2726(2000).
[8]
PROTEIN SEQUENCE OF 307-315 AND 584-597, IDENTIFICATION IN THE DRIP
COMPLEX, AND INTERACTION WITH VDR.
TISSUE=Cervix carcinoma;
PubMed=10235266; DOI=10.1038/19783;
Rachez C., Lemon B.D., Suldan Z., Bromleigh V., Gamble M., Naeaer A.M.,
Erdjument-Bromage H., Tempst P., Freedman L.P.;
"Ligand-dependent transcription activation by nuclear receptors requires
the DRIP complex.";
Nature 398:824-828(1999).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 622-711.
PubMed=7776974; DOI=10.1210/mend.9.2.7776974;
Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.;
"Two classes of proteins dependent on either the presence or absence of
thyroid hormone for interaction with the thyroid hormone receptor.";
Mol. Endocrinol. 9:243-254(1995).
[10]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SMCC
COMPLEX.
PubMed=10024883; DOI=10.1016/s1097-2765(00)80178-1;
Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X., Martinez E.,
Qin J., Roeder R.G.;
"A novel human SRB/MED-containing cofactor complex, SMCC, involved in
transcription regulation.";
Mol. Cell 3:97-108(1999).
[11]
ERRATUM OF PUBMED:10024883.
Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X., Martinez E.,
Qin J., Roeder R.G.;
Mol. Cell 3:541-541(1999).
[12]
FUNCTION, AND INTERACTION WITH MED24; THRA; THRB AND VDR.
PubMed=10406464; DOI=10.1210/mend.13.7.0295;
Zhang J., Fondell J.D.;
"Identification of mouse TRAP100: a transcriptional coregulatory factor for
thyroid hormone and vitamin D receptors.";
Mol. Endocrinol. 13:1130-1140(1999).
[13]
INTERACTION WITH RORA.
PubMed=10478845; DOI=10.1210/mend.13.9.0343;
Atkins G.B., Hu X., Guenther M.G., Rachez C., Freedman L.P., Lazar M.A.;
"Coactivators for the orphan nuclear receptor RORalpha.";
Mol. Endocrinol. 13:1550-1557(1999).
[14]
INTERACTION WITH ESR1; ESR2 AND VDR, AND MUTAGENESIS OF 607-LEU-LEU-608 AND
648-LEU-LEU-649.
PubMed=10770935; DOI=10.1074/jbc.m002013200;
Burakov D., Wong C.-W., Rachez C., Cheskis B.J., Freedman L.P.;
"Functional interactions between the estrogen receptor and DRIP205, a
subunit of the heteromeric DRIP coactivator complex.";
J. Biol. Chem. 275:20928-20934(2000).
[15]
INTERACTION WITH ESR1 AND ESR2, AND MUTAGENESIS OF 599-SER--GLY-612;
LEU-604; LEU-607; LEU-645 AND LEU-648.
PubMed=11303023; DOI=10.1074/jbc.m011651200;
Waernmark A., Almloef T., Leers J., Gustafsson J.-A., Treuter E.;
"Differential recruitment of the mammalian mediator subunit TRAP220 by
estrogen receptors ERalpha and ERbeta.";
J. Biol. Chem. 276:23397-23404(2001).
[16]
FUNCTION, INTERACTION WITH AR, AND ASSOCIATION WITH PROMOTER REGIONS.
PubMed=12218053; DOI=10.1074/jbc.m206061200;
Wang Q., Sharma D., Ren Y., Fondell J.D.;
"A coregulatory role for the TRAP-mediator complex in androgen receptor-
mediated gene expression.";
J. Biol. Chem. 277:42852-42858(2002).
[17]
FUNCTION, AND INTERACTION OF THE MEDIATOR COMPLEX WITH PPARG.
PubMed=12037571; DOI=10.1038/417563a;
Ge K., Guermah M., Yuan C.-X., Ito M., Wallberg A.E., Spiegelman B.M.,
Roeder R.G.;
"Transcription coactivator TRAP220 is required for PPAR gamma 2-stimulated
adipogenesis.";
Nature 417:563-567(2002).
[18]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE
MEDIATOR COMPLEX, AND INTERACTION OF THE MEDIATOR COMPLEX WITH ESR1 AND
ESR2.
PubMed=11867769; DOI=10.1073/pnas.261715899;
Kang Y.K., Guermah M., Yuan C.-X., Roeder R.G.;
"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. 99:2642-2647(2002).
[19]
ASSOCIATION WITH PROMOTER REGIONS.
PubMed=12034878; DOI=10.1073/pnas.122004799;
Sharma D., Fondell J.D.;
"Ordered recruitment of histone acetyltransferases and the TRAP/Mediator
complex to thyroid hormone-responsive promoters in vivo.";
Proc. Natl. Acad. Sci. U.S.A. 99:7934-7939(2002).
[20]
FUNCTION, INTERACTION WITH ESR1; PPARG; RARA; RXRA AND THRB, AND
MUTAGENESIS OF 600-GLN--SER-612; 607-LEU-LEU-608; 639-THR--PRO-653 AND
648-LEU-LEU-649.
PubMed=12556447; DOI=10.1074/jbc.m212950200;
Coulthard V.H., Matsuda S., Heery D.M.;
"An extended LXXLL motif sequence determines the nuclear receptor binding
specificity of TRAP220.";
J. Biol. Chem. 278:10942-10951(2003).
[21]
FUNCTION, INTERACTION WITH PPARGC1A, AND MUTAGENESIS OF 607-LEU-LEU-608 AND
648-LEU-LEU-649.
PubMed=14636573; DOI=10.1016/s1097-2765(03)00391-5;
Wallberg A.E., Yamamura S., Malik S., Spiegelman B.M., Roeder R.G.;
"Coordination of p300-mediated chromatin remodeling and TRAP/mediator
function through coactivator PGC-1alpha.";
Mol. Cell 12:1137-1149(2003).
[22]
FUNCTION, INTERACTION WITH ESR1, AND SUBCELLULAR LOCATION.
PubMed=15471764; DOI=10.1074/jbc.m409778200;
Wu Q., Burghardt R., Safe S.;
"Vitamin D-interacting protein 205 (DRIP205) coactivation of estrogen
receptor alpha (ERalpha) involves multiple domains of both proteins.";
J. Biol. Chem. 279:53602-53612(2004).
[23]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE MEDIATOR
COMPLEX.
PubMed=15175163; DOI=10.1016/j.molcel.2004.05.006;
Sato S., Tomomori-Sato C., Parmely T.J., Florens L., Zybailov B.,
Swanson S.K., Banks C.A.S., Jin J., Cai Y., Washburn M.P., Conaway J.W.,
Conaway R.C.;
"A set of consensus mammalian mediator subunits identified by
multidimensional protein identification technology.";
Mol. Cell 14:685-691(2004).
[24]
FUNCTION, INTERACTION OF THE MEDIATOR COMPLEX WITH THRA, AND MUTAGENESIS OF
607-LEU-LEU-608 AND 648-LEU-LEU-649.
PubMed=15340084; DOI=10.1128/mcb.24.18.8244-8254.2004;
Malik S., Guermah M., Yuan C.-X., Wu W., Yamamura S., Roeder R.G.;
"Structural and functional organization of TRAP220, the TRAP/mediator
subunit that is targeted by nuclear receptors.";
Mol. Cell. Biol. 24:8244-8254(2004).
[25]
FUNCTION, ASSOCIATION WITH PROMOTER REGIONS, INTERACTION WITH CCNC; MED6;
MED10; MED11; MED12; MED13; MED14; MED15; MED16; MED17; MED18; MED19;
MED20; MED21; MED23; MED24; MED25; MED26; MED28; MED29 AND MED30,
IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR
COMPLEX, AND ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
PubMed=15989967; DOI=10.1016/j.molcel.2005.05.015;
Zhang X., Krutchinsky A., Fukuda A., Chen W., Yamamura S., Chait B.T.,
Roeder R.G.;
"MED1/TRAP220 exists predominantly in a TRAP/Mediator subpopulation
enriched in RNA polymerase II and is required for ER-mediated
transcription.";
Mol. Cell 19:89-100(2005).
[26]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-1032 AND THR-1457, AND
MUTAGENESIS OF THR-1032 AND THR-1457.
PubMed=16314496; DOI=10.1128/mcb.25.24.10695-10710.2005;
Pandey P.K., Udayakumar T.S., Lin X., Sharma D., Shapiro P.S.,
Fondell J.D.;
"Activation of TRAP/mediator subunit TRAP220/Med1 is regulated by mitogen-
activated protein kinase-dependent phosphorylation.";
Mol. Cell. Biol. 25:10695-10710(2005).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling
networks.";
Cell 127:635-648(2006).
[28]
FUNCTION, INTERACTION WITH GABPA, ASSOCIATION WITH PROMOTER REGIONS, AND
SUBCELLULAR LOCATION.
PubMed=16574658; DOI=10.1074/jbc.m600163200;
Udayakumar T.S., Belakavadi M., Choi K.-H., Pandey P.K., Fondell J.D.;
"Regulation of Aurora-A kinase gene expression via GABP recruitment of
TRAP220/MED1.";
J. Biol. Chem. 281:14691-14699(2006).
[29]
INTERACTION WITH CDK8.
PubMed=17000779; DOI=10.1128/mcb.00443-06;
Zhou H., Kim S., Ishii S., Boyer T.G.;
"Mediator modulates Gli3-dependent Sonic hedgehog signaling.";
Mol. Cell. Biol. 26:8667-8682(2006).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-795; THR-805 AND THR-1057,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation
analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-805; THR-1057; SER-1207 AND
THR-1215, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the
kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664; THR-1051; THR-1057;
SER-1207; THR-1215; SER-1463; SER-1479; SER-1481 AND SER-1482, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-805 AND THR-1215, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[36]
INTERACTION WITH RXRA.
PubMed=19786558; DOI=10.1124/mol.109.057000;
Cho Y., Noshiro M., Choi M., Morita K., Kawamoto T., Fujimoto K., Kato Y.,
Makishima M.;
"The basic helix-loop-helix proteins differentiated embryo chondrocyte
(DEC) 1 and DEC2 function as corepressors of retinoid X receptors.";
Mol. Pharmacol. 76:1360-1369(2009).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664; THR-1051; THR-1057;
SER-1463; SER-1479; SER-1481 AND SER-1482, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[38]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1177 AND LYS-1529, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664; THR-805; THR-1057;
SER-1207; THR-1215; SER-1347; SER-1403 AND SER-1433, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[40]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[41]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1051; SER-1156; SER-1207;
THR-1215; SER-1223 AND SER-1479, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[42]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588; SER-664; THR-805;
THR-1051; THR-1057; SER-1156; SER-1207; THR-1215; SER-1223; SER-1302;
SER-1433; THR-1440; SER-1463; SER-1479; SER-1481 AND SER-1482, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[43]
FUNCTION, AND INTERACTION WITH GATA1 AND CCAR1.
PubMed=24245781; DOI=10.1111/gtc.12104;
Mizuta S., Minami T., Fujita H., Kaminaga C., Matsui K., Ishino R.,
Fujita A., Oda K., Kawai A., Hasegawa N., Urahama N., Roeder R.G., Ito M.;
"CCAR1/CoCoA pair-mediated recruitment of the Mediator defines a novel
pathway for GATA1 function.";
Genes Cells 19:28-51(2014).
[44]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[45]
PHOSPHORYLATION AT SER-887, INTERACTION WITH PSIP1, DOMAIN IBM MOTIF, AND
MUTAGENESIS OF SER-886; SER-887 AND SER-889.
PubMed=29997176; DOI=10.1073/pnas.1803909115;
Sharma S., Cermakova K., De Rijck J., Demeulemeester J., Fabry M.,
El Ashkar S., Van Belle S., Lepsik M., Tesina P., Duchoslav V., Novak P.,
Hubalek M., Srb P., Christ F., Rezacova P., Hodges H.C., Debyser Z.,
Veverka V.;
"Affinity switching of the LEDGF/p75 IBD interactome is governed by kinase-
dependent phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 115:E7053-E7062(2018).
-!- FUNCTION: Component of the Mediator complex, a coactivator involved in
the regulated transcription of nearly all RNA polymerase II-dependent
genes. Mediator functions as a bridge to convey information from gene-
specific regulatory proteins to the basal RNA polymerase II
transcription machinery. Mediator is recruited to promoters by direct
interactions with regulatory proteins and serves as a scaffold for the
assembly of a functional preinitiation complex with RNA polymerase II
and the general transcription factors (PubMed:10406464,
PubMed:11867769, PubMed:12037571, PubMed:12218053, PubMed:12556447,
PubMed:14636573, PubMed:15340084, PubMed:15471764, PubMed:15989967,
PubMed:16574658, PubMed:9653119). Acts as a coactivator for GATA1-
mediated transcriptional activation during erythroid differentiation of
K562 erythroleukemia cells (PubMed:24245781).
{ECO:0000269|PubMed:10406464, ECO:0000269|PubMed:11867769,
ECO:0000269|PubMed:12037571, ECO:0000269|PubMed:12218053,
ECO:0000269|PubMed:12556447, ECO:0000269|PubMed:14636573,
ECO:0000269|PubMed:15340084, ECO:0000269|PubMed:15471764,
ECO:0000269|PubMed:15989967, ECO:0000269|PubMed:16574658,
ECO:0000269|PubMed:24245781, ECO:0000269|PubMed:9653119}.
-!- SUBUNIT: Component of the Mediator complex, which is composed of MED1,
MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L,
MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23,
MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and
CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct
module termed the CDK8 module. Mediator containing the CDK8 module is
less active than Mediator lacking this module in supporting
transcriptional activation. Individual preparations of the Mediator
complex lacking one or more distinct subunits have been variously
termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. This subunit specifically
interacts with a number of nuclear receptors in a ligand-dependent
fashion including AR, ESR1, ESR2, PPARA, PPARG, RORA, RXRA, RXRG, THRA,
THRB and VDR. Interacts with CTNNB1, GABPA, GLI3, PPARGC1A and TP53.
Interacts with YWHAH. Interacts with CLOCK; this interaction requires
the presence of THRAP3 (By similarity). Interacts with GATA1 and CCAR1.
Interacts with NR4A3 (By similarity). Interacts (via IBM motif) with
PSIP1 (via IBD domain); phosphorylation increases its affinity for
PSIP1 (PubMed:29997176). {ECO:0000250|UniProtKB:Q925J9,
ECO:0000269|PubMed:10024883, ECO:0000269|PubMed:10235266,
ECO:0000269|PubMed:10235267, ECO:0000269|PubMed:10406464,
ECO:0000269|PubMed:10478845, ECO:0000269|PubMed:10733574,
ECO:0000269|PubMed:10770935, ECO:0000269|PubMed:11303023,
ECO:0000269|PubMed:11867769, ECO:0000269|PubMed:12037571,
ECO:0000269|PubMed:12218053, ECO:0000269|PubMed:12556447,
ECO:0000269|PubMed:14636573, ECO:0000269|PubMed:15175163,
ECO:0000269|PubMed:15340084, ECO:0000269|PubMed:15471764,
ECO:0000269|PubMed:15989967, ECO:0000269|PubMed:16574658,
ECO:0000269|PubMed:17000779, ECO:0000269|PubMed:19786558,
ECO:0000269|PubMed:24245781, ECO:0000269|PubMed:29997176,
ECO:0000269|PubMed:9444950, ECO:0000269|PubMed:9653119}.
-!- INTERACTION:
Q15648; P03372: ESR1; NbExp=3; IntAct=EBI-394459, EBI-78473;
Q15648; P15976: GATA1; NbExp=6; IntAct=EBI-394459, EBI-3909284;
Q15648; Q13503: MED21; NbExp=3; IntAct=EBI-394459, EBI-394678;
Q15648; O43513: MED7; NbExp=6; IntAct=EBI-394459, EBI-394632;
Q15648; P10276: RARA; NbExp=6; IntAct=EBI-394459, EBI-413374;
Q15648; P19793: RXRA; NbExp=6; IntAct=EBI-394459, EBI-78598;
Q15648; P10827: THRA; NbExp=4; IntAct=EBI-394459, EBI-286285;
Q15648; P11473: VDR; NbExp=4; IntAct=EBI-394459, EBI-286357;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15471764,
ECO:0000269|PubMed:16314496, ECO:0000269|PubMed:16574658}. Note=A
subset of the protein may enter the nucleolus subsequent to
phosphorylation by MAPK1 or MAPK3.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q15648-1; Sequence=Displayed;
Name=2;
IsoId=Q15648-3; Sequence=VSP_027906, VSP_027907;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:9444950, ECO:0000269|PubMed:9653119}.
-!- PTM: Phosphorylated by MAPK1 or MAPK3 during G2/M phase which may
enhance protein stability and promote entry into the nucleolus
(PubMed:16314496). Phosphorylation increases its interaction with PSIP1
(PubMed:29997176). {ECO:0000269|PubMed:16314496,
ECO:0000269|PubMed:29997176}.
-!- SIMILARITY: Belongs to the Mediator complex subunit 1 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC39854.1; Type=Frameshift; Evidence={ECO:0000305};
Sequence=AAH06517.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=CAA73867.1; Type=Frameshift; Evidence={ECO:0000305};
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; Y13467; CAA73867.1; ALT_FRAME; mRNA.
EMBL; AF055994; AAC39854.1; ALT_FRAME; mRNA.
EMBL; CH471152; EAW60575.1; -; Genomic_DNA.
EMBL; BC006517; AAH06517.1; ALT_TERM; mRNA.
EMBL; BC060758; AAH60758.1; -; mRNA.
EMBL; BC131783; AAI31784.1; -; mRNA.
EMBL; AF283812; AAF98352.1; -; mRNA.
EMBL; L40366; AAC41736.1; -; mRNA.
CCDS; CCDS11336.1; -. [Q15648-1]
RefSeq; NP_004765.2; NM_004774.3. [Q15648-1]
PDB; 1RJK; X-ray; 1.99 A; C=640-652.
PDB; 1RK3; X-ray; 2.20 A; C=640-652.
PDB; 1RKG; X-ray; 1.90 A; C=640-652.
PDB; 1RKH; X-ray; 2.28 A; C=640-652.
PDB; 2O4J; X-ray; 1.74 A; C=640-652.
PDB; 2O4R; X-ray; 1.98 A; C=640-652.
PDB; 2ZFX; X-ray; 1.99 A; C=640-652.
PDB; 3A2H; X-ray; 2.50 A; B=640-652.
PDB; 3AUN; X-ray; 1.81 A; B=640-652.
PDB; 3VJS; X-ray; 1.93 A; C=640-652.
PDB; 3VJT; X-ray; 2.00 A; C=640-652.
PDB; 3VRT; X-ray; 2.40 A; C=640-652.
PDB; 3VRU; X-ray; 2.00 A; C=640-652.
PDB; 3VRV; X-ray; 1.90 A; C=640-652.
PDB; 3VRW; X-ray; 2.40 A; C=640-652.
PDB; 3W0G; X-ray; 1.94 A; C=640-652.
PDB; 3W0H; X-ray; 1.80 A; C=640-652.
PDB; 3W0I; X-ray; 1.90 A; C=640-652.
PDB; 3W0J; X-ray; 1.84 A; C=640-652.
PDB; 3W5P; X-ray; 1.90 A; C=640-652.
PDB; 3W5Q; X-ray; 1.90 A; C=640-652.
PDB; 3W5R; X-ray; 2.20 A; C=640-652.
PDB; 3W5T; X-ray; 2.29 A; C=640-652.
PDB; 3WT5; X-ray; 1.90 A; C=640-652.
PDB; 3WT6; X-ray; 2.00 A; C=640-652.
PDB; 3WT7; X-ray; 2.40 A; C=640-652.
PDB; 3WTQ; X-ray; 2.10 A; C=640-652.
PDB; 4YNK; X-ray; 2.30 A; C=640-652.
PDB; 5AWJ; X-ray; 2.20 A; C=640-652.
PDB; 5AWK; X-ray; 2.90 A; C=640-652.
PDB; 5B41; X-ray; 1.89 A; C=640-652.
PDB; 5B5B; X-ray; 2.00 A; C/F=640-652.
PDB; 5GIC; X-ray; 2.35 A; C=641-650.
PDB; 5GID; X-ray; 2.15 A; C=641-649.
PDB; 5GIE; X-ray; 2.39 A; C/E=641-650.
PDB; 5XPM; X-ray; 2.20 A; C=640-652.
PDB; 5XPN; X-ray; 1.96 A; C=640-652.
PDB; 5XPO; X-ray; 2.28 A; C=640-652.
PDB; 5XPP; X-ray; 2.85 A; C=640-652.
PDB; 5XUQ; X-ray; 2.80 A; C=640-652.
PDB; 5XZF; X-ray; 2.10 A; C=640-652.
PDB; 5XZH; X-ray; 2.00 A; C=640-652.
PDB; 5ZWE; X-ray; 2.72 A; C=640-652.
PDB; 5ZWF; X-ray; 2.10 A; C=640-652.
PDB; 5ZWH; X-ray; 2.38 A; C=640-652.
PDB; 5ZWI; X-ray; 2.40 A; C=640-652.
PDB; 6D94; X-ray; 1.90 A; B=632-655.
PDB; 6JEZ; X-ray; 2.30 A; C=640-652.
PDB; 6K5O; X-ray; 1.80 A; C=640-652.
PDB; 6ONJ; X-ray; 2.30 A; C=638-656.
PDB; 7C7V; X-ray; 2.00 A; C=640-652.
PDB; 7C7W; X-ray; 1.90 A; C=640-652.
PDB; 7EMF; EM; 3.50 A; A=1-1581.
PDB; 7ENA; EM; 4.07 A; a=1-1581.
PDB; 7ENC; EM; 4.13 A; a=1-1581.
PDB; 7ENJ; EM; 4.40 A; A=1-1581.
PDBsum; 1RJK; -.
PDBsum; 1RK3; -.
PDBsum; 1RKG; -.
PDBsum; 1RKH; -.
PDBsum; 2O4J; -.
PDBsum; 2O4R; -.
PDBsum; 2ZFX; -.
PDBsum; 3A2H; -.
PDBsum; 3AUN; -.
PDBsum; 3VJS; -.
PDBsum; 3VJT; -.
PDBsum; 3VRT; -.
PDBsum; 3VRU; -.
PDBsum; 3VRV; -.
PDBsum; 3VRW; -.
PDBsum; 3W0G; -.
PDBsum; 3W0H; -.
PDBsum; 3W0I; -.
PDBsum; 3W0J; -.
PDBsum; 3W5P; -.
PDBsum; 3W5Q; -.
PDBsum; 3W5R; -.
PDBsum; 3W5T; -.
PDBsum; 3WT5; -.
PDBsum; 3WT6; -.
PDBsum; 3WT7; -.
PDBsum; 3WTQ; -.
PDBsum; 4YNK; -.
PDBsum; 5AWJ; -.
PDBsum; 5AWK; -.
PDBsum; 5B41; -.
PDBsum; 5B5B; -.
PDBsum; 5GIC; -.
PDBsum; 5GID; -.
PDBsum; 5GIE; -.
PDBsum; 5XPM; -.
PDBsum; 5XPN; -.
PDBsum; 5XPO; -.
PDBsum; 5XPP; -.
PDBsum; 5XUQ; -.
PDBsum; 5XZF; -.
PDBsum; 5XZH; -.
PDBsum; 5ZWE; -.
PDBsum; 5ZWF; -.
PDBsum; 5ZWH; -.
PDBsum; 5ZWI; -.
PDBsum; 6D94; -.
PDBsum; 6JEZ; -.
PDBsum; 6K5O; -.
PDBsum; 6ONJ; -.
PDBsum; 7C7V; -.
PDBsum; 7C7W; -.
PDBsum; 7EMF; -.
PDBsum; 7ENA; -.
PDBsum; 7ENC; -.
PDBsum; 7ENJ; -.
SMR; Q15648; -.
BioGRID; 111465; 157.
ComplexPortal; CPX-3227; Core mediator complex.
CORUM; Q15648; -.
DIP; DIP-24212N; -.
ELM; Q15648; -.
IntAct; Q15648; 79.
MINT; Q15648; -.
STRING; 9606.ENSP00000300651; -.
DrugBank; DB04891; Becocalcidiol.
GlyGen; Q15648; 7 sites, 2 O-linked glycans (7 sites).
iPTMnet; Q15648; -.
PhosphoSitePlus; Q15648; -.
SwissPalm; Q15648; -.
BioMuta; MED1; -.
DMDM; 158518535; -.
EPD; Q15648; -.
jPOST; Q15648; -.
MassIVE; Q15648; -.
MaxQB; Q15648; -.
PaxDb; Q15648; -.
PeptideAtlas; Q15648; -.
PRIDE; Q15648; -.
ProteomicsDB; 60685; -. [Q15648-1]
ProteomicsDB; 60686; -. [Q15648-3]
Antibodypedia; 4326; 518 antibodies from 38 providers.
DNASU; 5469; -.
Ensembl; ENST00000300651; ENSP00000300651; ENSG00000125686.
Ensembl; ENST00000394287; ENSP00000377828; ENSG00000125686. [Q15648-3]
GeneID; 5469; -.
KEGG; hsa:5469; -.
MANE-Select; ENST00000300651.11; ENSP00000300651.6; NM_004774.4; NP_004765.2.
UCSC; uc002hru.3; human. [Q15648-1]
CTD; 5469; -.
DisGeNET; 5469; -.
GeneCards; MED1; -.
HGNC; HGNC:9234; MED1.
HPA; ENSG00000125686; Low tissue specificity.
MIM; 604311; gene.
neXtProt; NX_Q15648; -.
OpenTargets; ENSG00000125686; -.
PharmGKB; PA33556; -.
VEuPathDB; HostDB:ENSG00000125686; -.
eggNOG; ENOG502QPZ7; Eukaryota.
GeneTree; ENSGT00660000095569; -.
HOGENOM; CLU_019440_0_0_1; -.
InParanoid; Q15648; -.
OMA; SHEDDFH; -.
OrthoDB; 57581at2759; -.
PhylomeDB; Q15648; -.
TreeFam; TF324954; -.
PathwayCommons; Q15648; -.
Reactome; R-HSA-1368082; RORA activates gene expression.
Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-212436; Generic Transcription Pathway.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
Reactome; R-HSA-400206; Regulation of lipid metabolism by PPARalpha.
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
Reactome; R-HSA-9707616; Heme signaling.
SignaLink; Q15648; -.
SIGNOR; Q15648; -.
BioGRID-ORCS; 5469; 392 hits in 1072 CRISPR screens.
ChiTaRS; MED1; human.
EvolutionaryTrace; Q15648; -.
GeneWiki; MED1; -.
GenomeRNAi; 5469; -.
Pharos; Q15648; Tbio.
PRO; PR:Q15648; -.
Proteomes; UP000005640; Chromosome 17.
RNAct; Q15648; protein.
Bgee; ENSG00000125686; Expressed in upper lobe of lung and 250 other tissues.
ExpressionAtlas; Q15648; baseline and differential.
Genevisible; Q15648; HS.
GO; GO:0070847; C:core mediator complex; IPI:ComplexPortal.
GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IMP:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
GO; GO:0030331; F:estrogen receptor binding; IPI:UniProtKB.
GO; GO:0050693; F:LBD domain binding; IPI:UniProtKB.
GO; GO:0016922; F:nuclear receptor binding; IDA:UniProtKB.
GO; GO:0030374; F:nuclear receptor coactivator activity; IMP:UniProtKB.
GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IPI:UniProtKB.
GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0042974; F:retinoic acid receptor binding; IPI:UniProtKB.
GO; GO:0046966; F:thyroid hormone receptor binding; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0001223; F:transcription coactivator binding; IPI:UniProtKB.
GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
GO; GO:0042809; F:vitamin D receptor binding; IPI:UniProtKB.
GO; GO:0006702; P:androgen biosynthetic process; IMP:UniProtKB.
GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0000902; P:cell morphogenesis; IMP:UniProtKB.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:UniProtKB.
GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEA:Ensembl.
GO; GO:0071383; P:cellular response to steroid hormone stimulus; IDA:UniProtKB.
GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IDA:UniProtKB.
GO; GO:0035050; P:embryonic heart tube development; IEA:Ensembl.
GO; GO:0035162; P:embryonic hemopoiesis; IEA:Ensembl.
GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl.
GO; GO:0001892; P:embryonic placenta development; IEA:Ensembl.
GO; GO:0048822; P:enucleate erythrocyte development; IEA:Ensembl.
GO; GO:0060750; P:epithelial cell proliferation involved in mammary gland duct elongation; IEA:Ensembl.
GO; GO:0048821; P:erythrocyte development; ISS:UniProtKB.
GO; GO:0045444; P:fat cell differentiation; IDA:MGI.
GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IDA:UniProtKB.
GO; GO:0030216; P:keratinocyte differentiation; IMP:UniProtKB.
GO; GO:0007595; P:lactation; IEA:Ensembl.
GO; GO:0002088; P:lens development in camera-type eye; ISS:UniProtKB.
GO; GO:0001889; P:liver development; IEA:Ensembl.
GO; GO:0060745; P:mammary gland branching involved in pregnancy; IEA:Ensembl.
GO; GO:0060744; P:mammary gland branching involved in thelarche; IEA:Ensembl.
GO; GO:0035855; P:megakaryocyte development; ISS:UniProtKB.
GO; GO:0030224; P:monocyte differentiation; IEA:Ensembl.
GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IMP:UniProtKB.
GO; GO:0045665; P:negative regulation of neuron differentiation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; IEA:Ensembl.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:UniProtKB.
GO; GO:0070318; P:positive regulation of G0 to G1 transition; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:2000347; P:positive regulation of hepatocyte proliferation; IEA:Ensembl.
GO; GO:0060335; P:positive regulation of interferon-gamma-mediated signaling pathway; IEA:Ensembl.
GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IEA:Ensembl.
GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
GO; GO:2001141; P:regulation of RNA biosynthetic process; IMP:UniProtKB.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0070562; P:regulation of vitamin D receptor signaling pathway; IEA:Ensembl.
GO; GO:0003406; P:retinal pigment epithelium development; IEA:Ensembl.
GO; GO:0006590; P:thyroid hormone generation; IEA:Ensembl.
GO; GO:0002154; P:thyroid hormone mediated signaling pathway; IMP:UniProtKB.
GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IEA:Ensembl.
IDEAL; IID00173; -.
InterPro; IPR019680; Mediator_Med1.
Pfam; PF10744; Med1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Transcription; Transcription regulation.
CHAIN 1..1581
/note="Mediator of RNA polymerase II transcription subunit
1"
/id="PRO_0000058552"
REGION 1..670
/note="Interaction with the Mediator complex and THRA"
REGION 16..590
/note="Interaction with ESR1"
REGION 108..212
/note="Interaction with the Mediator complex"
REGION 215..390
/note="Interaction with the Mediator complex"
REGION 405..644
/note="Interaction with THRA"
REGION 542..789
/note="Interaction with VDR"
REGION 609..705
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 622..701
/note="Interaction with PPARGC1A and THRA"
/evidence="ECO:0000269|PubMed:14636573"
REGION 656..1066
/note="Interaction with ESR1"
REGION 681..715
/note="Interaction with GATA1"
/evidence="ECO:0000269|PubMed:24245781"
REGION 792..820
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 874..893
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 948..1566
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1249..1421
/note="Interaction with TP53"
/evidence="ECO:0000269|PubMed:9444950"
MOTIF 604..608
/note="LXXLL motif 1"
MOTIF 645..649
/note="LXXLL motif 2"
MOTIF 875..902
/note="Integrase domain-binding motif (IBM)"
/evidence="ECO:0000269|PubMed:29997176"
COMPBIAS 652..682
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 806..820
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 995..1020
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1021..1052
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1075..1197
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1219..1301
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1328..1348
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1349..1366
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1367..1388
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1421..1484
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1508..1530
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1531..1556
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 588
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 664
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:23186163"
MOD_RES 795
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:16964243"
MOD_RES 805
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:16964243,
ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
MOD_RES 887
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:29997176"
MOD_RES 953
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q925J9"
MOD_RES 1032
/note="Phosphothreonine; by MAPK1 or MAPK3"
/evidence="ECO:0000269|PubMed:16314496"
MOD_RES 1051
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
ECO:0007744|PubMed:23186163"
MOD_RES 1057
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:16964243,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:23186163"
MOD_RES 1156
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21406692,
ECO:0007744|PubMed:23186163"
MOD_RES 1177
/note="N6-acetyllysine"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 1207
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
MOD_RES 1215
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
ECO:0007744|PubMed:23186163"
MOD_RES 1223
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21406692,
ECO:0007744|PubMed:23186163"
MOD_RES 1302
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 1347
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:20068231"
MOD_RES 1403
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:20068231"
MOD_RES 1433
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:23186163"
MOD_RES 1440
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 1457
/note="Phosphothreonine; by MAPK1 or MAPK3"
/evidence="ECO:0000269|PubMed:16314496"
MOD_RES 1463
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
MOD_RES 1465
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q925J9"
MOD_RES 1479
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
ECO:0007744|PubMed:23186163"
MOD_RES 1481
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
MOD_RES 1482
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
MOD_RES 1529
/note="N6-acetyllysine"
/evidence="ECO:0007744|PubMed:19608861"
VAR_SEQ 548..556
/note="YGMTTGNNP -> SKNPELGSG (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_027906"
VAR_SEQ 557..1581
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_027907"
VARIANT 753
/note="P -> T (in dbSNP:rs1139825)"
/id="VAR_053955"
VARIANT 1240
/note="S -> G (in dbSNP:rs35668211)"
/id="VAR_034938"
MUTAGEN 599..612
/note="SQNPILTSLLQITG->EKHKILHRLLQDSS: Enhances interaction
with ESR1."
/evidence="ECO:0000269|PubMed:11303023"
MUTAGEN 600..612
/note="QNPILTSLLQITG->RHKILHRLLQEGS: Enhances interaction
with ESR1."
/evidence="ECO:0000269|PubMed:12556447"
MUTAGEN 604
/note="L->A: Impairs interaction with ESR2; when associated
with A-607; A-645 and A-648."
/evidence="ECO:0000269|PubMed:11303023"
MUTAGEN 607..608
/note="LL->AA: Impairs interaction with ESR1, PPARG, RXRA
and THRB. Impairs interaction with THRA; when associated
with 648-A-A-649."
/evidence="ECO:0000269|PubMed:10733574,
ECO:0000269|PubMed:10770935, ECO:0000269|PubMed:12556447,
ECO:0000269|PubMed:14636573, ECO:0000269|PubMed:15340084,
ECO:0000269|PubMed:9653119"
MUTAGEN 607
/note="L->A: Impairs interaction with ESR2; when associated
with A-604; A-645 and A-648."
/evidence="ECO:0000269|PubMed:11303023"
MUTAGEN 639..653
/note="TKNHPMLMNLLKDNP->VSRHKILHRLLQEGS: Enhances
interaction with ESR1."
/evidence="ECO:0000269|PubMed:12556447"
MUTAGEN 645
/note="L->A: Impairs interaction with ESR2; when associated
with A-604; A-607 and A-648."
/evidence="ECO:0000269|PubMed:11303023"
MUTAGEN 648..649
/note="LL->AA: Impairs interaction with ESR1, PPARG, THRB
and VDR. Impairs interaction with THRA; when associated
with 607-A-A-608."
/evidence="ECO:0000269|PubMed:10733574,
ECO:0000269|PubMed:10770935, ECO:0000269|PubMed:12556447,
ECO:0000269|PubMed:14636573, ECO:0000269|PubMed:15340084,
ECO:0000269|PubMed:9653119"
MUTAGEN 648
/note="L->A: Impairs interaction with ESR2; when associated
with A-604; A-607 and A-645."
/evidence="ECO:0000269|PubMed:11303023"
MUTAGEN 886
/note="S->D: Increased interaction with PSIP1; when
associated with D-887 or D-887 and D-889."
/evidence="ECO:0000269|PubMed:29997176"
MUTAGEN 887
/note="S->D: Phosphomimetic mutant. Increased interaction
with PSIP1; when associated with D-886 or D-886 and D-889."
/evidence="ECO:0000269|PubMed:29997176"
MUTAGEN 889
/note="S->D: Increased interaction with PSIP1; when
associated with D-886 and D-887."
/evidence="ECO:0000269|PubMed:29997176"
MUTAGEN 1032
/note="T->A: Enhances protein stability; when associated
with A-1457."
/evidence="ECO:0000269|PubMed:16314496"
MUTAGEN 1457
/note="T->A: Enhances protein stability; when associated
with A-1032."
/evidence="ECO:0000269|PubMed:16314496"
CONFLICT 86
/note="R -> G (in Ref. 1; CAA73867)"
/evidence="ECO:0000305"
CONFLICT 147
/note="F -> S (in Ref. 1; CAA73867)"
/evidence="ECO:0000305"
CONFLICT 471..472
/note="DS -> GL (in Ref. 1; CAA73867)"
/evidence="ECO:0000305"
CONFLICT 563
/note="P -> S (in Ref. 1; CAA73867 and 7; AAF98352)"
/evidence="ECO:0000305"
CONFLICT 573
/note="T -> A (in Ref. 1; CAA73867 and 7; AAF98352)"
/evidence="ECO:0000305"
CONFLICT 651
/note="D -> N (in Ref. 5; AAH06517)"
/evidence="ECO:0000305"
CONFLICT 673
/note="S -> F (in Ref. 9; AAC41736)"
/evidence="ECO:0000305"
CONFLICT 702..708
/note="Missing (in Ref. 9; AAC41736)"
/evidence="ECO:0000305"
CONFLICT 721
/note="N -> K (in Ref. 2; AAC39854)"
/evidence="ECO:0000305"
CONFLICT 728
/note="M -> R (in Ref. 7; AAF98352)"
/evidence="ECO:0000305"
CONFLICT 756..761
/note="VPHPQP -> FYLTPQ (in Ref. 5; AAH06517)"
/evidence="ECO:0000305"
CONFLICT 1388
/note="G -> S (in Ref. 2; AAC39854)"
/evidence="ECO:0000305"
HELIX 639..641
/evidence="ECO:0007829|PDB:6D94"
HELIX 643..649
/evidence="ECO:0007829|PDB:2O4J"
SEQUENCE 1581 AA; 168478 MW; FCE0FE87EF08B887 CRC64;
MKAQGETEES EKLSKMSSLL ERLHAKFNQN RPWSETIKLV RQVMEKRVVM SSGGHQHLVS
CLETLQKALK VTSLPAMTDR LESIARQNGL GSHLSASGTE CYITSDMFYV EVQLDPAGQL
CDVKVAHHGE NPVSCPELVQ QLREKNFDEF SKHLKGLVNL YNLPGDNKLK TKMYLALQSL
EQDLSKMAIM YWKATNAGPL DKILHGSVGY LTPRSGGHLM NLKYYVSPSD LLDDKTASPI
ILHENNVSRS LGMNASVTIE GTSAVYKLPI APLIMGSHPV DNKWTPSFSS ITSANSVDLP
ACFFLKFPQP IPVSRAFVQK LQNCTGIPLF ETQPTYAPLY ELITQFELSK DPDPIPLNHN
MRFYAALPGQ QHCYFLNKDA PLPDGRSLQG TLVSKITFQH PGRVPLILNL IRHQVAYNTL
IGSCVKRTIL KEDSPGLLQF EVCPLSESRF SVSFQHPVND SLVCVVMDVQ DSTHVSCKLY
KGLSDALICT DDFIAKVVQR CMSIPVTMRA IRRKAETIQA DTPALSLIAE TVEDMVKKNL
PPASSPGYGM TTGNNPMSGT TTPTNTFPGG PITTLFNMSM SIKDRHESVG HGEDFSKVSQ
NPILTSLLQI TGNGGSTIGS SPTPPHHTPP PVSSMAGNTK NHPMLMNLLK DNPAQDFSTL
YGSSPLERQN SSSGSPRMEI CSGSNKTKKK KSSRLPPEKP KHQTEDDFQR ELFSMDVDSQ
NPIFDVNMTA DTLDTPHITP APSQCSTPPT TYPQPVPHPQ PSIQRMVRLS SSDSIGPDVT
DILSDIAEEA SKLPSTSDDC PAIGTPLRDS SSSGHSQSTL FDSDVFQTNN NENPYTDPAD
LIADAAGSPS SDSPTNHFFH DGVDFNPDLL NSQSQSGFGE EYFDESSQSG DNDDFKGFAS
QALNTLGVPM LGGDNGETKF KGNNQADTVD FSIISVAGKA LAPADLMEHH SGSQGPLLTT
GDLGKEKTQK RVKEGNGTSN STLSGPGLDS KPGKRSRTPS NDGKSKDKPP KRKKADTEGK
SPSHSSSNRP FTPPTSTGGS KSPGSAGRSQ TPPGVATPPI PKITIQIPKG TVMVGKPSSH
SQYTSSGSVS SSGSKSHHSH SSSSSSSAST SGKMKSSKSE GSSSSKLSSS MYSSQGSSGS
SQSKNSSQSG GKPGSSPITK HGLSSGSSST KMKPQGKPSS LMNPSLSKPN ISPSHSRPPG
GSDKLASPMK PVPGTPPSSK AKSPISSGSG GSHMSGTSSS SGMKSSSGLG SSGSLSQKTP
PSSNSCTASS SSFSSSGSSM SSSQNQHGSS KGKSPSRNKK PSLTAVIDKL KHGVVTSGPG
GEDPLDGQMG VSTNSSSHPM SSKHNMSGGE FQGKREKSDK DKSKVSTSGS SVDSSKKTSE
SKNVGSTGVA KIIISKHDGG SPSIKAKVTL QKPGESSGEG LRPQMASSKN YGSPLISGST
PKHERGSPSH SKSPAYTPQN LDSESESGSS IAEKSYQNSP SSDDGIRPLP EYSTEKHKKH
KKEKKKVKDK DRDRDRDKDR DKKKSHSIKP ESWSKSPISS DQSLSMTSNT ILSADRPSRL
SPDFMIGEED DDLMDVALIG N


Related products :

Catalog number Product name Quantity
18-003-42176 Thyroid hormone receptor-associated protein complex 95 kDa component - Trap95; Thyroid hormone receptor-associated protein 5; Vitamin D3 receptor-interacting protein complex component DRIP92 Polyclona 0.1 mg Protein A
18-003-42687 Thyroid receptor-interacting protein 13 - Thyroid hormone receptor interactor 13; Trip-13; Human papillomavirus type 16 E1 protein-binding protein; HPV16 E1 protein-binding protein; 16E1-BP Polyclonal 0.1 mg Protein A
18-003-43213 Thyroid receptor-interacting protein 13 - Thyroid hormone receptor interactor 13; Trip-13; Human papillomavirus type 16 E1 protein-binding protein; HPV16 E1 protein-binding protein; 16E1-BP Polyclonal 0.1 mg Protein A
10-288-22014F Thyroid receptor-interacting protein 13 - Thyroid hormone receptor interactor 13; Trip-13; Human papillomavirus type 16 E1 protein-binding protein; HPV16 E1 protein-binding protein; 16E1-BP 0.1 mg
10-288-22014F Thyroid receptor-interacting protein 13 - Thyroid hormone receptor interactor 13; Trip-13; Human papillomavirus type 16 E1 protein-binding protein; HPV16 E1 protein-binding protein; 16E1-BP 0.05 mg
EIAAB32177 ATP-dependent helicase PRIC285,Homo sapiens,Human,KIAA1769,PDIP1,Peroxisomal proliferator-activated receptor A-interacting complex 285 kDa protein,PPAR-alpha-interacting complex protein 285,PPAR-gamma
EIAAB47949 HNF-4a coactivator,Homo sapiens,Human,Thyroid hormone receptor interactor 3,Thyroid receptor-interacting protein 3,TR-interacting protein 3,TRIP3,TRIP-3,Zinc finger HIT domain-containing protein 3,ZNH
EIAAB30147 Pachytene checkpoint protein 2 homolog,Pch2,Rat,Rattus norvegicus,Thyroid hormone receptor interactor 13,Thyroid receptor-interacting protein 13,TR-interacting protein 13,Trip13,TRIP-13
EIAAB47947 Mouse,Mus musculus,Thyroid hormone receptor interactor 3,Thyroid receptor-interacting protein 3,TR-interacting protein 3,Trip3,TRIP-3,Zinc finger HIT domain-containing protein 3,Znhit3
EIAAB30151 Mouse,Mus musculus,Pachytene checkpoint protein 2 homolog,Pch2,Thyroid hormone receptor interactor 13,Thyroid receptor-interacting protein 13,TR-interacting protein 13,Trip13,TRIP-13
EIAAB30150 Pachytene checkpoint protein 2 homolog,PCH2,Pig,Sus scrofa,Thyroid hormone receptor interactor 13,Thyroid receptor-interacting protein 13,TR-interacting protein 13,TRIP13,TRIP-13
EIAAB07420 Cdc42-interacting protein 4,CIP4,Homo sapiens,hSTP,Human,Protein Felic,Salt tolerant protein,STOT,STP,Thyroid receptor-interacting protein 10,TR-interacting protein 10,TRIP10,TRIP-10
EIAAB07421 Cdc42-interacting protein 4,Cip4,Rat,Rattus norvegicus,Salt tolerant protein,Stp,Thyroid receptor-interacting protein 10,TR-interacting protein 10,Trip10,TRIP-10
EIAAB44012 Homo sapiens,Human,OIP1,OIP-1,Opa-interacting protein 1,Thyroid receptor-interacting protein 6,TR-interacting protein 6,TRIP6,TRIP-6,ZRP-1,Zyxin-related protein 1
EIAAB43730 Homo sapiens,Human,THRAP3,Thyroid hormone receptor-associated protein 3,Thyroid hormone receptor-associated protein complex 150 kDa component,Trap150,TRAP150
EIAAB07419 Cdc42-interacting protein 4,Cip4,Mouse,Mus musculus,Thyroid receptor-interacting protein 10,TR-interacting protein 10,Trip10,TRIP-10
EIAAB43728 Rat,Rattus norvegicus,Thrap3,Thyroid hormone receptor-associated protein 3,Thyroid hormone receptor-associated protein complex 150 kDa component,Trap150,Trap150
EIAAB43729 Mouse,Mus musculus,Thrap3,Thyroid hormone receptor-associated protein 3,Thyroid hormone receptor-associated protein complex 150 kDa component,Trap150,Trap150
EIAAB07148 ATP-dependent helicase CHD9,Chd9,CHD-9,Chromodomain-helicase-DNA-binding protein 9,Kiaa0308,Mouse,Mus musculus,Peroxisomal proliferator-activated receptor A-interacting complex 320 kDa protein,PPAR-al
EIAAB09602 Alien homolog,COP9 signalosome complex subunit 2,Cops2,Csn2,JAB1-containing signalosome subunit 2,Mouse,Mus musculus,SGN2,Signalosome subunit 2,Thyroid receptor-interacting protein 15,TR-interacting p
EIAAB09601 Alien homolog,COP9 signalosome complex subunit 2,COPS2,CSN2,Homo sapiens,Human,JAB1-containing signalosome subunit 2,SGN2,Signalosome subunit 2,Thyroid receptor-interacting protein 15,TR-interacting p
EIAAB44014 CEV14,Clonal evolution-related gene on chromosome 14 protein,GMAP-210,Golgi-associated microtubule-binding protein 210,Homo sapiens,Human,Thyroid receptor-interacting protein 11,TR-interacting protein
EIAAB44011 Mouse,Mus musculus,Thyroid receptor-interacting protein 6,TR-interacting protein 6,Trip6,TRIP-6,Zrp1,ZRP-1,Zyxin-related protein 1
EIAAB36467 49 kDa TATA box-binding protein-interacting protein,49 kDa TBP-interacting protein,54 kDa erythrocyte cytosolic protein,ECP-54,Homo sapiens,Human,INO80 complex subunit H,INO80H,NMP 238,NMP238,Nuclear
EIAAB36469 48 kDa TATA box-binding protein-interacting protein,48 kDa TBP-interacting protein,51 kDa erythrocyte cytosolic protein,CGI-46,ECP-51,Homo sapiens,Human,INO80 complex subunit J,INO80J,Repressing ponti
Pathways :
WP2272: Pathogenic Escherichia coli infection
WP2292: Chemokine signaling pathway
WP1531: Vitamin D synthesis
WP1624: Bacterial secretion system
WP1694: Pyrimidine metabolism
WP1693: Purine metabolism
WP731: Sterol regulatory element binding protein related
WP1663: Homologous recombination
WP1672: Mismatch repair
WP1644: DNA replication
WP1692: Protein export
WP1713: Two-component system
WP1616: ABC transporters
WP1566: Citrate cycle (TCA cycle)
WP1909: Signal regulatory protein (SIRP) family interactions
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1675: Nitrogen metabolism
WP2203: TSLP Signaling Pathway
WP2371: Parkinsons Disease Pathway
WP1690: Propanoate metabolism
WP1654: gamma-Hexachlorocyclohexane degradation
WP1888: Post-translational protein modification
WP232: G Protein Signaling Pathways
WP813: G Protein Signaling Pathways

Related Genes :
[MED1 ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2] Mediator of RNA polymerase II transcription subunit 1 (Activator-recruited cofactor 205 kDa component) (ARC205) (Mediator complex subunit 1) (Peroxisome proliferator-activated receptor-binding protein) (PBP) (PPAR-binding protein) (Thyroid hormone receptor-associated protein complex 220 kDa component) (Trap220) (Thyroid receptor-interacting protein 2) (TR-interacting protein 2) (TRIP-2) (Vitamin D receptor-interacting protein complex component DRIP205) (p53 regulatory protein RB18A)
[Med1 Crsp210 Drip205 Pbp Pparbp Trap220 Trip2] Mediator of RNA polymerase II transcription subunit 1 (Mediator complex subunit 1) (Peroxisome proliferator-activated receptor-binding protein) (PBP) (PPAR-binding protein) (Thyroid hormone receptor-associated protein complex 220 kDa component) (Trap220) (Thyroid receptor-interacting protein 2) (TR-interacting protein 2) (TRIP-2)
[MED24 ARC100 CRSP4 DRIP100 KIAA0130 THRAP4 TRAP100] Mediator of RNA polymerase II transcription subunit 24 (Activator-recruited cofactor 100 kDa component) (ARC100) (Cofactor required for Sp1 transcriptional activation subunit 4) (CRSP complex subunit 4) (Mediator complex subunit 24) (Thyroid hormone receptor-associated protein 4) (Thyroid hormone receptor-associated protein complex 100 kDa component) (Trap100) (hTRAP100) (Vitamin D3 receptor-interacting protein complex 100 kDa component) (DRIP100)
[MED13 ARC250 KIAA0593 THRAP1 TRAP240] Mediator of RNA polymerase II transcription subunit 13 (Activator-recruited cofactor 250 kDa component) (ARC250) (Mediator complex subunit 13) (Thyroid hormone receptor-associated protein 1) (Thyroid hormone receptor-associated protein complex 240 kDa component) (Trap240) (Vitamin D3 receptor-interacting protein complex component DRIP250) (DRIP250)
[MED17 ARC77 CRSP6 DRIP77 DRIP80 TRAP80] Mediator of RNA polymerase II transcription subunit 17 (Activator-recruited cofactor 77 kDa component) (ARC77) (Cofactor required for Sp1 transcriptional activation subunit 6) (CRSP complex subunit 6) (Mediator complex subunit 17) (Thyroid hormone receptor-associated protein complex 80 kDa component) (Trap80) (Transcriptional coactivator CRSP77) (Vitamin D3 receptor-interacting protein complex 80 kDa component) (DRIP80)
[MED14 ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170] Mediator of RNA polymerase II transcription subunit 14 (Activator-recruited cofactor 150 kDa component) (ARC150) (Cofactor required for Sp1 transcriptional activation subunit 2) (CRSP complex subunit 2) (Mediator complex subunit 14) (RGR1 homolog) (hRGR1) (Thyroid hormone receptor-associated protein complex 170 kDa component) (Trap170) (Transcriptional coactivator CRSP150) (Vitamin D3 receptor-interacting protein complex 150 kDa component) (DRIP150)
[MED16 DRIP92 THRAP5] Mediator of RNA polymerase II transcription subunit 16 (Mediator complex subunit 16) (Thyroid hormone receptor-associated protein 5) (Thyroid hormone receptor-associated protein complex 95 kDa component) (Trap95) (Vitamin D3 receptor-interacting protein complex 92 kDa component) (DRIP92)
[MED4 ARC36 DRIP36 VDRIP HSPC126] Mediator of RNA polymerase II transcription subunit 4 (Activator-recruited cofactor 36 kDa component) (ARC36) (Mediator complex subunit 4) (TRAP/SMCC/PC2 subunit p36 subunit) (Vitamin D3 receptor-interacting protein complex 36 kDa component) (DRIP36)
[MED12 ARC240 CAGH45 HOPA KIAA0192 TNRC11 TRAP230] Mediator of RNA polymerase II transcription subunit 12 (Activator-recruited cofactor 240 kDa component) (ARC240) (CAG repeat protein 45) (Mediator complex subunit 12) (OPA-containing protein) (Thyroid hormone receptor-associated protein complex 230 kDa component) (Trap230) (Trinucleotide repeat-containing gene 11 protein)
[MED23 ARC130 CRSP3 DRIP130 KIAA1216 SUR2] Mediator of RNA polymerase II transcription subunit 23 (Activator-recruited cofactor 130 kDa component) (ARC130) (Cofactor required for Sp1 transcriptional activation subunit 3) (CRSP complex subunit 3) (Mediator complex subunit 23) (Protein sur-2 homolog) (hSur-2) (Transcriptional coactivator CRSP130) (Vitamin D3 receptor-interacting protein complex 130 kDa component) (DRIP130)
[MED30 THRAP6 TRAP25] Mediator of RNA polymerase II transcription subunit 30 (Mediator complex subunit 30) (TRAP/Mediator complex component TRAP25) (Thyroid hormone receptor-associated protein 6) (Thyroid hormone receptor-associated protein complex 25 kDa component) (Trap25)
[Ncoa6 Aib3 Prip Rap250 Trbp] Nuclear receptor coactivator 6 (Activating signal cointegrator 2) (ASC-2) (Amplified in breast cancer protein 3) (Cancer-amplified transcriptional coactivator ASC-2) (Nuclear receptor coactivator RAP250) (NRC) (Nuclear receptor-activating protein, 250 kDa) (Peroxisome proliferator-activated receptor-interacting protein) (PPAR-interacting protein) (Thyroid hormone receptor-binding protein)
[Med30 Thrap6 Trap25] Mediator of RNA polymerase II transcription subunit 30 (Mediator complex subunit 30) (Thyroid hormone receptor-associated protein 6) (Thyroid hormone receptor-associated protein complex 25 kDa component) (Trap25)
[MED13L KIAA1025 PROSIT240 THRAP2 TRAP240L] Mediator of RNA polymerase II transcription subunit 13-like (Mediator complex subunit 13-like) (Thyroid hormone receptor-associated protein 2) (Thyroid hormone receptor-associated protein complex 240 kDa component-like)
[Med24 D11Ertd307e Thrap4 Trap100] Mediator of RNA polymerase II transcription subunit 24 (Mediator complex subunit 24) (Thyroid hormone receptor-associated protein 4) (Thyroid hormone receptor-associated protein complex 100 kDa component) (Trap100) (mTRAP100)
[Med17 Crsp6 Trap80] Mediator of RNA polymerase II transcription subunit 17 (Cofactor required for Sp1 transcriptional activation subunit 6) (CRSP complex subunit 6) (Mediator complex subunit 17) (Thyroid hormone receptor-associated protein complex 80 kDa component)
[Ncoa6 Aib3 Rap250 Trbp] Nuclear receptor coactivator 6 (Activating signal cointegrator 2) (ASC-2) (Amplified in breast cancer protein 3) (Cancer-amplified transcriptional coactivator ASC-2) (Nuclear receptor coactivator RAP250) (NRC) (Nuclear receptor-activating protein, 250 kDa) (Peroxisome proliferator-activated receptor-interacting protein) (PPAR-interacting protein) (PRIP) (Thyroid hormone receptor-binding protein) (Fragment)
[NCOA6 AIB3 KIAA0181 RAP250 TRBP] Nuclear receptor coactivator 6 (Activating signal cointegrator 2) (ASC-2) (Amplified in breast cancer protein 3) (Cancer-amplified transcriptional coactivator ASC-2) (Nuclear receptor coactivator RAP250) (NRC RAP250) (Nuclear receptor-activating protein, 250 kDa) (Peroxisome proliferator-activated receptor-interacting protein) (PPAR-interacting protein) (PRIP) (Thyroid hormone receptor-binding protein)
[Med12 Kiaa0192 Mopa Tnrc11 Trap230] Mediator of RNA polymerase II transcription subunit 12 (Mediator complex subunit 12) (OPA-containing protein) (Thyroid hormone receptor-associated protein complex 230 kDa component) (Trap230) (Trinucleotide repeat-containing gene 11 protein)
[MED25 ACID1 ARC92 PTOV2 TCBAP0758] Mediator of RNA polymerase II transcription subunit 25 (Activator interaction domain-containing protein 1) (Activator-recruited cofactor 92 kDa component) (ARC92) (Mediator complex subunit 25) (p78)
[Med14 Crsp2 Gm641 Trap170] Mediator of RNA polymerase II transcription subunit 14 (Cofactor required for Sp1 transcriptional activation subunit 2) (CRSP complex subunit 2) (Mediator complex subunit 14) (Thyroid hormone receptor-associated protein complex 170 kDa component) (Trap170)
[MED6 ARC33] Mediator of RNA polymerase II transcription subunit 6 (Activator-recruited cofactor 33 kDa component) (ARC33) (Mediator complex subunit 6) (hMed6) (Renal carcinoma antigen NY-REN-28)
[Cops2 Csn2 Trip15] COP9 signalosome complex subunit 2 (SGN2) (Signalosome subunit 2) (Alien homolog) (JAB1-containing signalosome subunit 2) (Thyroid receptor-interacting protein 15) (TR-interacting protein 15) (TRIP-15)
[MED15 ARC105 CTG7A PCQAP TIG1 TNRC7] Mediator of RNA polymerase II transcription subunit 15 (Activator-recruited cofactor 105 kDa component) (ARC105) (CTG repeat protein 7a) (Mediator complex subunit 15) (Positive cofactor 2 glutamine/Q-rich-associated protein) (PC2 glutamine/Q-rich-associated protein) (TPA-inducible gene 1 protein) (TIG-1) (Trinucleotide repeat-containing gene 7 protein)
[MED7 ARC34 CRSP9] Mediator of RNA polymerase II transcription subunit 7 (hMED7) (Activator-recruited cofactor 34 kDa component) (ARC34) (Cofactor required for Sp1 transcriptional activation subunit 9) (CRSP complex subunit 9) (Mediator complex subunit 7) (RNA polymerase transcriptional regulation mediator subunit 7 homolog) (Transcriptional coactivator CRSP33)
[MED8] Mediator of RNA polymerase II transcription subunit 8 (Activator-recruited cofactor 32 kDa component) (ARC32) (Mediator complex subunit 8)
[MED26 ARC70 CRSP7] Mediator of RNA polymerase II transcription subunit 26 (Activator-recruited cofactor 70 kDa component) (ARC70) (Cofactor required for Sp1 transcriptional activation subunit 7) (CRSP complex subunit 7) (Mediator complex subunit 26) (Transcriptional coactivator CRSP70)
[COPS2 CSN2 TRIP15] COP9 signalosome complex subunit 2 (SGN2) (Signalosome subunit 2) (Alien homolog) (JAB1-containing signalosome subunit 2) (Thyroid receptor-interacting protein 15) (TR-interacting protein 15) (TRIP-15)
[med12 kto mot trap230] Mediator of RNA polymerase II transcription subunit 12 (Mediator complex subunit 12) (Protein kohtalo) (Protein motionless) (Thyroid hormone receptor-associated protein complex 230 kDa component) (Trap230)
[Cops2 Csn2 Trip15] COP9 signalosome complex subunit 2 (SGN2) (Signalosome subunit 2) (Alien homolog) (JAB1-containing signalosome subunit 2) (Thyroid receptor-interacting protein 15) (TR-interacting protein 15) (TRIP-15)

Bibliography :