GENTAUR Molecular Products.

 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.
 10-OCT-2018, entry version 185.
 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.
 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.
 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).
 -!- 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). {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:9444950,
     ECO:0000269|PubMed:9653119}.
 -!- INTERACTION:
     P15976:GATA1; NbExp=6; IntAct=EBI-394459, EBI-3909284;
     O43513:MED7; NbExp=4; IntAct=EBI-394459, EBI-394632;
     P10276:RARA; NbExp=6; IntAct=EBI-394459, EBI-413374;
     P19793:RXRA; NbExp=6; IntAct=EBI-394459, EBI-78598;
     P10827:THRA; NbExp=4; IntAct=EBI-394459, EBI-286285;
     P11473:VDR; NbExp=3; 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.
     {ECO:0000269|PubMed:16314496}.
 -!- SIMILARITY: Belongs to the Mediator complex subunit 1 family.
     {ECO:0000305}.
 -!- SEQUENCE CAUTION:
     Sequence=AAC39854.1; Type=Frameshift; Positions=543, 545; Evidence={ECO:0000305};
     Sequence=AAH06517.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
     Sequence=CAA73867.1; Type=Frameshift; Positions=4; 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]
 UniGene; Hs.643754; -.
 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; 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.
 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; 5XPO; -.
 PDBsum; 5XPP; -.
 PDBsum; 5XUQ; -.
 PDBsum; 5XZF; -.
 PDBsum; 5XZH; -.
 ProteinModelPortal; Q15648; -.
 SMR; Q15648; -.
 BioGrid; 111465; 104.
 ComplexPortal; CPX-3227; Core mediator complex.
 CORUM; Q15648; -.
 DIP; DIP-24212N; -.
 ELM; Q15648; -.
 IntAct; Q15648; 51.
 MINT; Q15648; -.
 STRING; 9606.ENSP00000300651; -.
 iPTMnet; Q15648; -.
 PhosphoSitePlus; Q15648; -.
 BioMuta; MED1; -.
 DMDM; 158518535; -.
 EPD; Q15648; -.
 MaxQB; Q15648; -.
 PaxDb; Q15648; -.
 PeptideAtlas; Q15648; -.
 PRIDE; Q15648; -.
 ProteomicsDB; 60685; -.
 ProteomicsDB; 60686; -. [Q15648-3]
 DNASU; 5469; -.
 Ensembl; ENST00000300651; ENSP00000300651; ENSG00000125686. [Q15648-1]
 Ensembl; ENST00000394287; ENSP00000377828; ENSG00000125686. [Q15648-3]
 GeneID; 5469; -.
 KEGG; hsa:5469; -.
 UCSC; uc002hru.3; human. [Q15648-1]
 CTD; 5469; -.
 DisGeNET; 5469; -.
 EuPathDB; HostDB:ENSG00000125686.11; -.
 GeneCards; MED1; -.
 HGNC; HGNC:9234; MED1.
 HPA; CAB017696; -.
 HPA; HPA052818; -.
 MIM; 604311; gene.
 neXtProt; NX_Q15648; -.
 OpenTargets; ENSG00000125686; -.
 PharmGKB; PA33556; -.
 eggNOG; ENOG410IEFR; Eukaryota.
 eggNOG; ENOG410XR2E; LUCA.
 GeneTree; ENSGT00660000095569; -.
 HOVERGEN; HBG101127; -.
 InParanoid; Q15648; -.
 KO; K15144; -.
 OMA; HPMLMNL; -.
 OrthoDB; EOG091G035E; -.
 PhylomeDB; Q15648; -.
 TreeFam; TF324954; -.
 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 Peroxisome proliferator-activated receptor alpha (PPARalpha).
 Reactome; R-HSA-400253; Circadian Clock.
 Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
 SignaLink; Q15648; -.
 SIGNOR; Q15648; -.
 ChiTaRS; MED1; human.
 EvolutionaryTrace; Q15648; -.
 GeneWiki; MED1; -.
 GenomeRNAi; 5469; -.
 PRO; PR:Q15648; -.
 Proteomes; UP000005640; Chromosome 17.
 Bgee; ENSG00000125686; Expressed in 236 organ(s), highest expression level in upper lobe of lung.
 CleanEx; HS_MED1; -.
 ExpressionAtlas; Q15648; baseline and differential.
 Genevisible; Q15648; HS.
 GO; GO:0000785; C:chromatin; IEA:Ensembl.
 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:0032993; C:protein-DNA complex; IEA:Ensembl.
 GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
 GO; GO:0003682; F:chromatin binding; IMP:UniProtKB.
 GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
 GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
 GO; GO:0030331; F:estrogen receptor binding; IPI:UniProtKB.
 GO; GO:0050693; F:LBD domain binding; IPI:UniProtKB.
 GO; GO:0036033; F:mediator complex binding; IDA:UniProtKB.
 GO; GO:0035257; F:nuclear hormone receptor binding; IPI:UniProtKB.
 GO; GO:0016922; F:nuclear receptor binding; IDA:UniProtKB.
 GO; GO:0030374; F:nuclear receptor transcription coactivator activity; IMP:UniProtKB.
 GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IPI:UniProtKB.
 GO; GO:0042974; F:retinoic acid receptor binding; IPI:UniProtKB.
 GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:UniProtKB.
 GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
 GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
 GO; GO:0038023; F:signaling receptor activity; IDA:UniProtKB.
 GO; GO:0046966; F:thyroid hormone receptor binding; IDA:UniProtKB.
 GO; GO:0030375; F:thyroid hormone receptor coactivator activity; IMP:UniProtKB.
 GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
 GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB.
 GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
 GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
 GO; GO:0042809; F:vitamin D receptor binding; IPI:UniProtKB.
 GO; GO:0006702; P:androgen biosynthetic process; IMP:UniProtKB.
 GO; GO:0030521; P:androgen receptor signaling pathway; IDA: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:0070371; P:ERK1 and ERK2 cascade; IDA:UniProtKB.
 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:0033601; P:positive regulation of mammary gland epithelial cell proliferation; IEA:Ensembl.
 GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; IEA:Ensembl.
 GO; GO:2000273; P:positive regulation of signaling receptor activity; IMP:UniProtKB.
 GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
 GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
 GO; GO:0051726; P:regulation of cell cycle; NAS:UniProtKB.
 GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
 GO; GO:2001141; P:regulation of RNA biosynthetic process; IMP:UniProtKB.
 GO; GO:0006356; P:regulation of transcription by RNA polymerase I; IDA:UniProtKB.
 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:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
 GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IEA:Ensembl.
 InterPro; IPR019680; Mediator_Med1.
 Pfam; PF10744; Med1; 1.
 1: Evidence at protein level;
 3D-structure; Acetylation; Activator; Alternative splicing;
 Complete proteome; Direct protein sequencing; DNA-binding; Nucleus;
 Phosphoprotein; Polymorphism; Reference proteome; Repeat;
 Transcription; Transcription regulation.
 CHAIN         1   1581       Mediator of RNA polymerase II
                              transcription subunit 1.
                              /FTId=PRO_0000058552.
 REGION        1    670       Interaction with the Mediator complex and
                              THRA.
 REGION       16    590       Interaction with ESR1.
 REGION      108    212       Interaction with the Mediator complex.
 REGION      215    390       Interaction with the Mediator complex.
 REGION      405    644       Interaction with THRA.
 REGION      542    789       Interaction with VDR.
 REGION      622    701       Interaction with PPARGC1A and THRA.
                              {ECO:0000269|PubMed:14636573}.
 REGION      656   1066       Interaction with ESR1.
 REGION      681    715       Interaction with GATA1.
                              {ECO:0000269|PubMed:24245781}.
 REGION     1249   1421       Interaction with TP53.
                              {ECO:0000269|PubMed:9444950}.
 MOTIF       604    608       LXXLL motif 1.
 MOTIF       645    649       LXXLL motif 2.
 COMPBIAS   1078   1482       Ser-rich.
 COMPBIAS   1496   1529       Lys-rich.
 MOD_RES     588    588       Phosphoserine.
                              {ECO:0000244|PubMed:23186163}.
 MOD_RES     664    664       Phosphoserine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:19690332,
                              ECO:0000244|PubMed:20068231,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES     795    795       Phosphoserine.
                              {ECO:0000244|PubMed:16964243}.
 MOD_RES     805    805       Phosphothreonine.
                              {ECO:0000244|PubMed:16964243,
                              ECO:0000244|PubMed:18691976,
                              ECO:0000244|PubMed:19369195,
                              ECO:0000244|PubMed:20068231,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES     953    953       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q925J9}.
 MOD_RES    1032   1032       Phosphothreonine; by MAPK1 or MAPK3.
                              {ECO:0000269|PubMed:16314496}.
 MOD_RES    1051   1051       Phosphothreonine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:19690332,
                              ECO:0000244|PubMed:21406692,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES    1057   1057       Phosphothreonine.
                              {ECO:0000244|PubMed:16964243,
                              ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:18691976,
                              ECO:0000244|PubMed:19690332,
                              ECO:0000244|PubMed:20068231,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES    1156   1156       Phosphoserine.
                              {ECO:0000244|PubMed:21406692,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES    1177   1177       N6-acetyllysine.
                              {ECO:0000244|PubMed:19608861}.
 MOD_RES    1207   1207       Phosphoserine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:18691976,
                              ECO:0000244|PubMed:20068231,
                              ECO:0000244|PubMed:21406692,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES    1215   1215       Phosphothreonine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:18691976,
                              ECO:0000244|PubMed:19369195,
                              ECO:0000244|PubMed:20068231,
                              ECO:0000244|PubMed:21406692,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES    1223   1223       Phosphoserine.
                              {ECO:0000244|PubMed:21406692,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES    1302   1302       Phosphoserine.
                              {ECO:0000244|PubMed:23186163}.
 MOD_RES    1347   1347       Phosphoserine.
                              {ECO:0000244|PubMed:20068231}.
 MOD_RES    1403   1403       Phosphoserine.
                              {ECO:0000244|PubMed:20068231}.
 MOD_RES    1433   1433       Phosphoserine.
                              {ECO:0000244|PubMed:20068231,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES    1440   1440       Phosphothreonine.
                              {ECO:0000244|PubMed:23186163}.
 MOD_RES    1457   1457       Phosphothreonine; by MAPK1 or MAPK3.
                              {ECO:0000269|PubMed:16314496}.
 MOD_RES    1463   1463       Phosphoserine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:19690332,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES    1465   1465       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q925J9}.
 MOD_RES    1479   1479       Phosphoserine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:19690332,
                              ECO:0000244|PubMed:21406692,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES    1481   1481       Phosphoserine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:19690332,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES    1482   1482       Phosphoserine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:19690332,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES    1529   1529       N6-acetyllysine.
                              {ECO:0000244|PubMed:19608861}.
 VAR_SEQ     548    556       YGMTTGNNP -> SKNPELGSG (in isoform 2).
                              {ECO:0000303|PubMed:15489334}.
                              /FTId=VSP_027906.
 VAR_SEQ     557   1581       Missing (in isoform 2).
                              {ECO:0000303|PubMed:15489334}.
                              /FTId=VSP_027907.
 VARIANT     753    753       P -> T (in dbSNP:rs1139825).
                              /FTId=VAR_053955.
 VARIANT    1240   1240       S -> G (in dbSNP:rs35668211).
                              /FTId=VAR_034938.
 MUTAGEN     599    612       SQNPILTSLLQITG->EKHKILHRLLQDSS: Enhances
                              interaction with ESR1.
                              {ECO:0000269|PubMed:11303023}.
 MUTAGEN     600    612       QNPILTSLLQITG->RHKILHRLLQEGS: Enhances
                              interaction with ESR1.
                              {ECO:0000269|PubMed:12556447}.
 MUTAGEN     604    604       L->A: Impairs interaction with ESR2; when
                              associated with A-607; A-645 and A-648.
                              {ECO:0000269|PubMed:11303023}.
 MUTAGEN     607    608       LL->AA: Impairs interaction with ESR1,
                              PPARG, RXRA and THRB. Impairs interaction
                              with THRA; when associated with 648-A-A-
                              649. {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    607       L->A: Impairs interaction with ESR2; when
                              associated with A-604; A-645 and A-648.
                              {ECO:0000269|PubMed:11303023}.
 MUTAGEN     639    653       TKNHPMLMNLLKDNP->VSRHKILHRLLQEGS:
                              Enhances interaction with ESR1.
                              {ECO:0000269|PubMed:12556447}.
 MUTAGEN     645    645       L->A: Impairs interaction with ESR2; when
                              associated with A-604; A-607 and A-648.
                              {ECO:0000269|PubMed:11303023}.
 MUTAGEN     648    649       LL->AA: Impairs interaction with ESR1,
                              PPARG, THRB and VDR. Impairs interaction
                              with THRA; when associated with 607-A-A-
                              608. {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    648       L->A: Impairs interaction with ESR2; when
                              associated with A-604; A-607 and A-645.
                              {ECO:0000269|PubMed:11303023}.
 MUTAGEN    1032   1032       T->A: Enhances protein stability; when
                              associated with A-1457.
                              {ECO:0000269|PubMed:16314496}.
 MUTAGEN    1457   1457       T->A: Enhances protein stability; when
                              associated with A-1032.
                              {ECO:0000269|PubMed:16314496}.
 CONFLICT     86     86       R -> G (in Ref. 1; CAA73867).
                              {ECO:0000305}.
 CONFLICT    147    147       F -> S (in Ref. 1; CAA73867).
                              {ECO:0000305}.
 CONFLICT    471    472       DS -> GL (in Ref. 1; CAA73867).
                              {ECO:0000305}.
 CONFLICT    563    563       P -> S (in Ref. 1; CAA73867 and 7;
                              AAF98352). {ECO:0000305}.
 CONFLICT    573    573       T -> A (in Ref. 1; CAA73867 and 7;
                              AAF98352). {ECO:0000305}.
 CONFLICT    651    651       D -> N (in Ref. 5; AAH06517).
                              {ECO:0000305}.
 CONFLICT    673    673       S -> F (in Ref. 9; AAC41736).
                              {ECO:0000305}.
 CONFLICT    702    708       Missing (in Ref. 9; AAC41736).
                              {ECO:0000305}.
 CONFLICT    721    721       N -> K (in Ref. 2; AAC39854).
                              {ECO:0000305}.
 CONFLICT    728    728       M -> R (in Ref. 7; AAF98352).
                              {ECO:0000305}.
 CONFLICT    756    761       VPHPQP -> FYLTPQ (in Ref. 5; AAH06517).
                              {ECO:0000305}.
 CONFLICT   1388   1388       G -> S (in Ref. 2; AAC39854).
                              {ECO:0000305}.
 HELIX       643    649       {ECO:0000244|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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