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};
 ---------------------------------------------------------------------------
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 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

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