MED1_HUMAN
ID MED1_HUMAN Reviewed; 1581 AA.
AC Q15648; A2RRQ6; O43810; O75447; Q6P9H7; Q6PK58; Q9HD39;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 4.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 1;
DE AltName: Full=Activator-recruited cofactor 205 kDa component;
DE Short=ARC205;
DE AltName: Full=Mediator complex subunit 1;
DE AltName: Full=Peroxisome proliferator-activated receptor-binding protein;
DE Short=PBP;
DE Short=PPAR-binding protein;
DE AltName: Full=Thyroid hormone receptor-associated protein complex 220 kDa component;
DE Short=Trap220;
DE AltName: Full=Thyroid receptor-interacting protein 2;
DE Short=TR-interacting protein 2;
DE Short=TRIP-2;
DE AltName: Full=Vitamin D receptor-interacting protein complex component DRIP205;
DE AltName: Full=p53 regulatory protein RB18A;
GN Name=MED1;
GN Synonyms=ARC205, CRSP1, CRSP200, DRIP205, DRIP230, PBP, PPARBP, PPARGBP,
GN RB18A, TRAP220, TRIP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DNA-BINDING, INTERACTION WITH TP53,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=9444950; DOI=10.1038/sj.onc.1201492;
RA Drane P., Barel M., Balbo M., Frade R.;
RT "Identification of RB18A, a 205 kDa new p53 regulatory protein which shares
RT antigenic and functional properties with p53.";
RL Oncogene 15:3013-3024(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 157-168;
RP 943-952 AND 1432-1442, FUNCTION, INTERACTION WITH ESR1; PPARA; PPARG; RARA;
RP RXRA; THRA AND VDR, TISSUE SPECIFICITY, AND MUTAGENESIS OF 607-LEU-LEU-608
RP AND 648-LEU-LEU-649.
RX PubMed=9653119; DOI=10.1073/pnas.95.14.7939;
RA Yuan C.-X., Ito M., Fondell J.D., Fu Z.-Y., Roeder R.G.;
RT "The TRAP220 component of a thyroid hormone receptor-associated protein
RT (TRAP) coactivator complex interacts directly with nuclear receptors in a
RT ligand-dependent fashion.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:7939-7944(1998).
RN [3]
RP ERRATUM OF PUBMED:9653119.
RA Yuan C.-X., Ito M., Fondell J.D., Fu Z.-Y., Roeder R.G.;
RL Proc. Natl. Acad. Sci. U.S.A. 95:14584-14584(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Colon, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 1-13 AND 1452-1464, AND IDENTIFICATION IN THE ARC
RP COMPLEX.
RX PubMed=10235267; DOI=10.1038/19789;
RA Naeaer A.M., Beaurang P.A., Zhou S., Abraham S., Solomon W.B., Tjian R.;
RT "Composite co-activator ARC mediates chromatin-directed transcriptional
RT activation.";
RL Nature 398:828-832(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-1581 (ISOFORM 1), INTERACTION WITH VDR,
RP AND MUTAGENESIS OF 607-LEU-LEU-608 AND 648-LEU-LEU-649.
RX PubMed=10733574; DOI=10.1128/mcb.20.8.2718-2726.2000;
RA Rachez C., Gamble M., Chang C.-P.B., Atkins G.B., Lazar M.A.,
RA Freedman L.P.;
RT "The DRIP complex and SRC-1/p160 coactivators share similar nuclear
RT receptor binding determinants but constitute functionally distinct
RT complexes.";
RL Mol. Cell. Biol. 20:2718-2726(2000).
RN [8]
RP PROTEIN SEQUENCE OF 307-315 AND 584-597, IDENTIFICATION IN THE DRIP
RP COMPLEX, AND INTERACTION WITH VDR.
RC TISSUE=Cervix carcinoma;
RX PubMed=10235266; DOI=10.1038/19783;
RA Rachez C., Lemon B.D., Suldan Z., Bromleigh V., Gamble M., Naeaer A.M.,
RA Erdjument-Bromage H., Tempst P., Freedman L.P.;
RT "Ligand-dependent transcription activation by nuclear receptors requires
RT the DRIP complex.";
RL Nature 398:824-828(1999).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 622-711.
RX PubMed=7776974; DOI=10.1210/mend.9.2.7776974;
RA Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.;
RT "Two classes of proteins dependent on either the presence or absence of
RT thyroid hormone for interaction with the thyroid hormone receptor.";
RL Mol. Endocrinol. 9:243-254(1995).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SMCC
RP COMPLEX.
RX PubMed=10024883; DOI=10.1016/s1097-2765(00)80178-1;
RA Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X., Martinez E.,
RA Qin J., Roeder R.G.;
RT "A novel human SRB/MED-containing cofactor complex, SMCC, involved in
RT transcription regulation.";
RL Mol. Cell 3:97-108(1999).
RN [11]
RP ERRATUM OF PUBMED:10024883.
RA Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X., Martinez E.,
RA Qin J., Roeder R.G.;
RL Mol. Cell 3:541-541(1999).
RN [12]
RP FUNCTION, AND INTERACTION WITH MED24; THRA; THRB AND VDR.
RX PubMed=10406464; DOI=10.1210/mend.13.7.0295;
RA Zhang J., Fondell J.D.;
RT "Identification of mouse TRAP100: a transcriptional coregulatory factor for
RT thyroid hormone and vitamin D receptors.";
RL Mol. Endocrinol. 13:1130-1140(1999).
RN [13]
RP INTERACTION WITH RORA.
RX PubMed=10478845; DOI=10.1210/mend.13.9.0343;
RA Atkins G.B., Hu X., Guenther M.G., Rachez C., Freedman L.P., Lazar M.A.;
RT "Coactivators for the orphan nuclear receptor RORalpha.";
RL Mol. Endocrinol. 13:1550-1557(1999).
RN [14]
RP INTERACTION WITH ESR1; ESR2 AND VDR, AND MUTAGENESIS OF 607-LEU-LEU-608 AND
RP 648-LEU-LEU-649.
RX PubMed=10770935; DOI=10.1074/jbc.m002013200;
RA Burakov D., Wong C.-W., Rachez C., Cheskis B.J., Freedman L.P.;
RT "Functional interactions between the estrogen receptor and DRIP205, a
RT subunit of the heteromeric DRIP coactivator complex.";
RL J. Biol. Chem. 275:20928-20934(2000).
RN [15]
RP INTERACTION WITH ESR1 AND ESR2, AND MUTAGENESIS OF 599-SER--GLY-612;
RP LEU-604; LEU-607; LEU-645 AND LEU-648.
RX PubMed=11303023; DOI=10.1074/jbc.m011651200;
RA Waernmark A., Almloef T., Leers J., Gustafsson J.-A., Treuter E.;
RT "Differential recruitment of the mammalian mediator subunit TRAP220 by
RT estrogen receptors ERalpha and ERbeta.";
RL J. Biol. Chem. 276:23397-23404(2001).
RN [16]
RP FUNCTION, INTERACTION WITH AR, AND ASSOCIATION WITH PROMOTER REGIONS.
RX PubMed=12218053; DOI=10.1074/jbc.m206061200;
RA Wang Q., Sharma D., Ren Y., Fondell J.D.;
RT "A coregulatory role for the TRAP-mediator complex in androgen receptor-
RT mediated gene expression.";
RL J. Biol. Chem. 277:42852-42858(2002).
RN [17]
RP FUNCTION, AND INTERACTION OF THE MEDIATOR COMPLEX WITH PPARG.
RX PubMed=12037571; DOI=10.1038/417563a;
RA Ge K., Guermah M., Yuan C.-X., Ito M., Wallberg A.E., Spiegelman B.M.,
RA Roeder R.G.;
RT "Transcription coactivator TRAP220 is required for PPAR gamma 2-stimulated
RT adipogenesis.";
RL Nature 417:563-567(2002).
RN [18]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE
RP MEDIATOR COMPLEX, AND INTERACTION OF THE MEDIATOR COMPLEX WITH ESR1 AND
RP ESR2.
RX PubMed=11867769; DOI=10.1073/pnas.261715899;
RA Kang Y.K., Guermah M., Yuan C.-X., Roeder R.G.;
RT "The TRAP/Mediator coactivator complex interacts directly with estrogen
RT receptors alpha and beta through the TRAP220 subunit and directly enhances
RT estrogen receptor function in vitro.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2642-2647(2002).
RN [19]
RP ASSOCIATION WITH PROMOTER REGIONS.
RX PubMed=12034878; DOI=10.1073/pnas.122004799;
RA Sharma D., Fondell J.D.;
RT "Ordered recruitment of histone acetyltransferases and the TRAP/Mediator
RT complex to thyroid hormone-responsive promoters in vivo.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7934-7939(2002).
RN [20]
RP FUNCTION, INTERACTION WITH ESR1; PPARG; RARA; RXRA AND THRB, AND
RP MUTAGENESIS OF 600-GLN--SER-612; 607-LEU-LEU-608; 639-THR--PRO-653 AND
RP 648-LEU-LEU-649.
RX PubMed=12556447; DOI=10.1074/jbc.m212950200;
RA Coulthard V.H., Matsuda S., Heery D.M.;
RT "An extended LXXLL motif sequence determines the nuclear receptor binding
RT specificity of TRAP220.";
RL J. Biol. Chem. 278:10942-10951(2003).
RN [21]
RP FUNCTION, INTERACTION WITH PPARGC1A, AND MUTAGENESIS OF 607-LEU-LEU-608 AND
RP 648-LEU-LEU-649.
RX PubMed=14636573; DOI=10.1016/s1097-2765(03)00391-5;
RA Wallberg A.E., Yamamura S., Malik S., Spiegelman B.M., Roeder R.G.;
RT "Coordination of p300-mediated chromatin remodeling and TRAP/mediator
RT function through coactivator PGC-1alpha.";
RL Mol. Cell 12:1137-1149(2003).
RN [22]
RP FUNCTION, INTERACTION WITH ESR1, AND SUBCELLULAR LOCATION.
RX PubMed=15471764; DOI=10.1074/jbc.m409778200;
RA Wu Q., Burghardt R., Safe S.;
RT "Vitamin D-interacting protein 205 (DRIP205) coactivation of estrogen
RT receptor alpha (ERalpha) involves multiple domains of both proteins.";
RL J. Biol. Chem. 279:53602-53612(2004).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE MEDIATOR
RP COMPLEX.
RX PubMed=15175163; DOI=10.1016/j.molcel.2004.05.006;
RA Sato S., Tomomori-Sato C., Parmely T.J., Florens L., Zybailov B.,
RA Swanson S.K., Banks C.A.S., Jin J., Cai Y., Washburn M.P., Conaway J.W.,
RA Conaway R.C.;
RT "A set of consensus mammalian mediator subunits identified by
RT multidimensional protein identification technology.";
RL Mol. Cell 14:685-691(2004).
RN [24]
RP FUNCTION, INTERACTION OF THE MEDIATOR COMPLEX WITH THRA, AND MUTAGENESIS OF
RP 607-LEU-LEU-608 AND 648-LEU-LEU-649.
RX PubMed=15340084; DOI=10.1128/mcb.24.18.8244-8254.2004;
RA Malik S., Guermah M., Yuan C.-X., Wu W., Yamamura S., Roeder R.G.;
RT "Structural and functional organization of TRAP220, the TRAP/mediator
RT subunit that is targeted by nuclear receptors.";
RL Mol. Cell. Biol. 24:8244-8254(2004).
RN [25]
RP FUNCTION, ASSOCIATION WITH PROMOTER REGIONS, INTERACTION WITH CCNC; MED6;
RP MED10; MED11; MED12; MED13; MED14; MED15; MED16; MED17; MED18; MED19;
RP MED20; MED21; MED23; MED24; MED25; MED26; MED28; MED29 AND MED30,
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR
RP COMPLEX, AND ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
RX PubMed=15989967; DOI=10.1016/j.molcel.2005.05.015;
RA Zhang X., Krutchinsky A., Fukuda A., Chen W., Yamamura S., Chait B.T.,
RA Roeder R.G.;
RT "MED1/TRAP220 exists predominantly in a TRAP/Mediator subpopulation
RT enriched in RNA polymerase II and is required for ER-mediated
RT transcription.";
RL Mol. Cell 19:89-100(2005).
RN [26]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-1032 AND THR-1457, AND
RP MUTAGENESIS OF THR-1032 AND THR-1457.
RX PubMed=16314496; DOI=10.1128/mcb.25.24.10695-10710.2005;
RA Pandey P.K., Udayakumar T.S., Lin X., Sharma D., Shapiro P.S.,
RA Fondell J.D.;
RT "Activation of TRAP/mediator subunit TRAP220/Med1 is regulated by mitogen-
RT activated protein kinase-dependent phosphorylation.";
RL Mol. Cell. Biol. 25:10695-10710(2005).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [28]
RP FUNCTION, INTERACTION WITH GABPA, ASSOCIATION WITH PROMOTER REGIONS, AND
RP SUBCELLULAR LOCATION.
RX PubMed=16574658; DOI=10.1074/jbc.m600163200;
RA Udayakumar T.S., Belakavadi M., Choi K.-H., Pandey P.K., Fondell J.D.;
RT "Regulation of Aurora-A kinase gene expression via GABP recruitment of
RT TRAP220/MED1.";
RL J. Biol. Chem. 281:14691-14699(2006).
RN [29]
RP INTERACTION WITH CDK8.
RX PubMed=17000779; DOI=10.1128/mcb.00443-06;
RA Zhou H., Kim S., Ishii S., Boyer T.G.;
RT "Mediator modulates Gli3-dependent Sonic hedgehog signaling.";
RL Mol. Cell. Biol. 26:8667-8682(2006).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-795; THR-805 AND THR-1057,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-805; THR-1057; SER-1207 AND
RP THR-1215, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664; THR-1051; THR-1057;
RP SER-1207; THR-1215; SER-1463; SER-1479; SER-1481 AND SER-1482, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [34]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-805 AND THR-1215, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [36]
RP INTERACTION WITH RXRA.
RX PubMed=19786558; DOI=10.1124/mol.109.057000;
RA Cho Y., Noshiro M., Choi M., Morita K., Kawamoto T., Fujimoto K., Kato Y.,
RA Makishima M.;
RT "The basic helix-loop-helix proteins differentiated embryo chondrocyte
RT (DEC) 1 and DEC2 function as corepressors of retinoid X receptors.";
RL Mol. Pharmacol. 76:1360-1369(2009).
RN [37]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664; THR-1051; THR-1057;
RP SER-1463; SER-1479; SER-1481 AND SER-1482, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [38]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1177 AND LYS-1529, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [39]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664; THR-805; THR-1057;
RP SER-1207; THR-1215; SER-1347; SER-1403 AND SER-1433, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [40]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [41]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1051; SER-1156; SER-1207;
RP THR-1215; SER-1223 AND SER-1479, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [42]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588; SER-664; THR-805;
RP THR-1051; THR-1057; SER-1156; SER-1207; THR-1215; SER-1223; SER-1302;
RP SER-1433; THR-1440; SER-1463; SER-1479; SER-1481 AND SER-1482, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [43]
RP FUNCTION, AND INTERACTION WITH GATA1 AND CCAR1.
RX PubMed=24245781; DOI=10.1111/gtc.12104;
RA Mizuta S., Minami T., Fujita H., Kaminaga C., Matsui K., Ishino R.,
RA Fujita A., Oda K., Kawai A., Hasegawa N., Urahama N., Roeder R.G., Ito M.;
RT "CCAR1/CoCoA pair-mediated recruitment of the Mediator defines a novel
RT pathway for GATA1 function.";
RL Genes Cells 19:28-51(2014).
RN [44]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [45]
RP PHOSPHORYLATION AT SER-887, INTERACTION WITH PSIP1, DOMAIN IBM MOTIF, AND
RP MUTAGENESIS OF SER-886; SER-887 AND SER-889.
RX PubMed=29997176; DOI=10.1073/pnas.1803909115;
RA Sharma S., Cermakova K., De Rijck J., Demeulemeester J., Fabry M.,
RA El Ashkar S., Van Belle S., Lepsik M., Tesina P., Duchoslav V., Novak P.,
RA Hubalek M., Srb P., Christ F., Rezacova P., Hodges H.C., Debyser Z.,
RA Veverka V.;
RT "Affinity switching of the LEDGF/p75 IBD interactome is governed by kinase-
RT dependent phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E7053-E7062(2018).
CC -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC the regulated transcription of nearly all RNA polymerase II-dependent
CC genes. Mediator functions as a bridge to convey information from gene-
CC specific regulatory proteins to the basal RNA polymerase II
CC transcription machinery. Mediator is recruited to promoters by direct
CC interactions with regulatory proteins and serves as a scaffold for the
CC assembly of a functional preinitiation complex with RNA polymerase II
CC and the general transcription factors (PubMed:10406464,
CC PubMed:11867769, PubMed:12037571, PubMed:12218053, PubMed:12556447,
CC PubMed:14636573, PubMed:15340084, PubMed:15471764, PubMed:15989967,
CC PubMed:16574658, PubMed:9653119). Acts as a coactivator for GATA1-
CC mediated transcriptional activation during erythroid differentiation of
CC K562 erythroleukemia cells (PubMed:24245781).
CC {ECO:0000269|PubMed:10406464, ECO:0000269|PubMed:11867769,
CC ECO:0000269|PubMed:12037571, ECO:0000269|PubMed:12218053,
CC ECO:0000269|PubMed:12556447, ECO:0000269|PubMed:14636573,
CC ECO:0000269|PubMed:15340084, ECO:0000269|PubMed:15471764,
CC ECO:0000269|PubMed:15989967, ECO:0000269|PubMed:16574658,
CC ECO:0000269|PubMed:24245781, ECO:0000269|PubMed:9653119}.
CC -!- SUBUNIT: Component of the Mediator complex, which is composed of MED1,
CC MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L,
CC MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23,
CC MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and
CC CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct
CC module termed the CDK8 module. Mediator containing the CDK8 module is
CC less active than Mediator lacking this module in supporting
CC transcriptional activation. Individual preparations of the Mediator
CC complex lacking one or more distinct subunits have been variously
CC termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. This subunit specifically
CC interacts with a number of nuclear receptors in a ligand-dependent
CC fashion including AR, ESR1, ESR2, PPARA, PPARG, RORA, RXRA, RXRG, THRA,
CC THRB and VDR. Interacts with CTNNB1, GABPA, GLI3, PPARGC1A and TP53.
CC Interacts with YWHAH. Interacts with CLOCK; this interaction requires
CC the presence of THRAP3 (By similarity). Interacts with GATA1 and CCAR1.
CC Interacts with NR4A3 (By similarity). Interacts (via IBM motif) with
CC PSIP1 (via IBD domain); phosphorylation increases its affinity for
CC PSIP1 (PubMed:29997176). {ECO:0000250|UniProtKB:Q925J9,
CC ECO:0000269|PubMed:10024883, ECO:0000269|PubMed:10235266,
CC ECO:0000269|PubMed:10235267, ECO:0000269|PubMed:10406464,
CC ECO:0000269|PubMed:10478845, ECO:0000269|PubMed:10733574,
CC ECO:0000269|PubMed:10770935, ECO:0000269|PubMed:11303023,
CC ECO:0000269|PubMed:11867769, ECO:0000269|PubMed:12037571,
CC ECO:0000269|PubMed:12218053, ECO:0000269|PubMed:12556447,
CC ECO:0000269|PubMed:14636573, ECO:0000269|PubMed:15175163,
CC ECO:0000269|PubMed:15340084, ECO:0000269|PubMed:15471764,
CC ECO:0000269|PubMed:15989967, ECO:0000269|PubMed:16574658,
CC ECO:0000269|PubMed:17000779, ECO:0000269|PubMed:19786558,
CC ECO:0000269|PubMed:24245781, ECO:0000269|PubMed:29997176,
CC ECO:0000269|PubMed:9444950, ECO:0000269|PubMed:9653119}.
CC -!- INTERACTION:
CC Q15648; P03372: ESR1; NbExp=3; IntAct=EBI-394459, EBI-78473;
CC Q15648; P15976: GATA1; NbExp=6; IntAct=EBI-394459, EBI-3909284;
CC Q15648; Q13503: MED21; NbExp=3; IntAct=EBI-394459, EBI-394678;
CC Q15648; O43513: MED7; NbExp=6; IntAct=EBI-394459, EBI-394632;
CC Q15648; P10276: RARA; NbExp=6; IntAct=EBI-394459, EBI-413374;
CC Q15648; P19793: RXRA; NbExp=6; IntAct=EBI-394459, EBI-78598;
CC Q15648; P10827: THRA; NbExp=4; IntAct=EBI-394459, EBI-286285;
CC Q15648; P11473: VDR; NbExp=4; IntAct=EBI-394459, EBI-286357;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15471764,
CC ECO:0000269|PubMed:16314496, ECO:0000269|PubMed:16574658}. Note=A
CC subset of the protein may enter the nucleolus subsequent to
CC phosphorylation by MAPK1 or MAPK3.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15648-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15648-3; Sequence=VSP_027906, VSP_027907;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:9444950, ECO:0000269|PubMed:9653119}.
CC -!- PTM: Phosphorylated by MAPK1 or MAPK3 during G2/M phase which may
CC enhance protein stability and promote entry into the nucleolus
CC (PubMed:16314496). Phosphorylation increases its interaction with PSIP1
CC (PubMed:29997176). {ECO:0000269|PubMed:16314496,
CC ECO:0000269|PubMed:29997176}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC39854.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH06517.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=CAA73867.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Y13467; CAA73867.1; ALT_FRAME; mRNA.
DR EMBL; AF055994; AAC39854.1; ALT_FRAME; mRNA.
DR EMBL; CH471152; EAW60575.1; -; Genomic_DNA.
DR EMBL; BC006517; AAH06517.1; ALT_TERM; mRNA.
DR EMBL; BC060758; AAH60758.1; -; mRNA.
DR EMBL; BC131783; AAI31784.1; -; mRNA.
DR EMBL; AF283812; AAF98352.1; -; mRNA.
DR EMBL; L40366; AAC41736.1; -; mRNA.
DR CCDS; CCDS11336.1; -. [Q15648-1]
DR RefSeq; NP_004765.2; NM_004774.3. [Q15648-1]
DR PDB; 1RJK; X-ray; 1.99 A; C=640-652.
DR PDB; 1RK3; X-ray; 2.20 A; C=640-652.
DR PDB; 1RKG; X-ray; 1.90 A; C=640-652.
DR PDB; 1RKH; X-ray; 2.28 A; C=640-652.
DR PDB; 2O4J; X-ray; 1.74 A; C=640-652.
DR PDB; 2O4R; X-ray; 1.98 A; C=640-652.
DR PDB; 2ZFX; X-ray; 1.99 A; C=640-652.
DR PDB; 3A2H; X-ray; 2.50 A; B=640-652.
DR PDB; 3AUN; X-ray; 1.81 A; B=640-652.
DR PDB; 3VJS; X-ray; 1.93 A; C=640-652.
DR PDB; 3VJT; X-ray; 2.00 A; C=640-652.
DR PDB; 3VRT; X-ray; 2.40 A; C=640-652.
DR PDB; 3VRU; X-ray; 2.00 A; C=640-652.
DR PDB; 3VRV; X-ray; 1.90 A; C=640-652.
DR PDB; 3VRW; X-ray; 2.40 A; C=640-652.
DR PDB; 3W0G; X-ray; 1.94 A; C=640-652.
DR PDB; 3W0H; X-ray; 1.80 A; C=640-652.
DR PDB; 3W0I; X-ray; 1.90 A; C=640-652.
DR PDB; 3W0J; X-ray; 1.84 A; C=640-652.
DR PDB; 3W5P; X-ray; 1.90 A; C=640-652.
DR PDB; 3W5Q; X-ray; 1.90 A; C=640-652.
DR PDB; 3W5R; X-ray; 2.20 A; C=640-652.
DR PDB; 3W5T; X-ray; 2.29 A; C=640-652.
DR PDB; 3WT5; X-ray; 1.90 A; C=640-652.
DR PDB; 3WT6; X-ray; 2.00 A; C=640-652.
DR PDB; 3WT7; X-ray; 2.40 A; C=640-652.
DR PDB; 3WTQ; X-ray; 2.10 A; C=640-652.
DR PDB; 4YNK; X-ray; 2.30 A; C=640-652.
DR PDB; 5AWJ; X-ray; 2.20 A; C=640-652.
DR PDB; 5AWK; X-ray; 2.90 A; C=640-652.
DR PDB; 5B41; X-ray; 1.89 A; C=640-652.
DR PDB; 5B5B; X-ray; 2.00 A; C/F=640-652.
DR PDB; 5GIC; X-ray; 2.35 A; C=641-650.
DR PDB; 5GID; X-ray; 2.15 A; C=641-649.
DR PDB; 5GIE; X-ray; 2.39 A; C/E=641-650.
DR PDB; 5XPM; X-ray; 2.20 A; C=640-652.
DR PDB; 5XPN; X-ray; 1.96 A; C=640-652.
DR PDB; 5XPO; X-ray; 2.28 A; C=640-652.
DR PDB; 5XPP; X-ray; 2.85 A; C=640-652.
DR PDB; 5XUQ; X-ray; 2.80 A; C=640-652.
DR PDB; 5XZF; X-ray; 2.10 A; C=640-652.
DR PDB; 5XZH; X-ray; 2.00 A; C=640-652.
DR PDB; 5ZWE; X-ray; 2.72 A; C=640-652.
DR PDB; 5ZWF; X-ray; 2.10 A; C=640-652.
DR PDB; 5ZWH; X-ray; 2.38 A; C=640-652.
DR PDB; 5ZWI; X-ray; 2.40 A; C=640-652.
DR PDB; 6D94; X-ray; 1.90 A; B=632-655.
DR PDB; 6JEZ; X-ray; 2.30 A; C=640-652.
DR PDB; 6K5O; X-ray; 1.80 A; C=640-652.
DR PDB; 6ONJ; X-ray; 2.30 A; C=638-656.
DR PDB; 7C7V; X-ray; 2.00 A; C=640-652.
DR PDB; 7C7W; X-ray; 1.90 A; C=640-652.
DR PDB; 7EMF; EM; 3.50 A; A=1-1581.
DR PDB; 7ENA; EM; 4.07 A; a=1-1581.
DR PDB; 7ENC; EM; 4.13 A; a=1-1581.
DR PDB; 7ENJ; EM; 4.40 A; A=1-1581.
DR PDB; 7VQP; X-ray; 1.94 A; C=640-652.
DR PDBsum; 1RJK; -.
DR PDBsum; 1RK3; -.
DR PDBsum; 1RKG; -.
DR PDBsum; 1RKH; -.
DR PDBsum; 2O4J; -.
DR PDBsum; 2O4R; -.
DR PDBsum; 2ZFX; -.
DR PDBsum; 3A2H; -.
DR PDBsum; 3AUN; -.
DR PDBsum; 3VJS; -.
DR PDBsum; 3VJT; -.
DR PDBsum; 3VRT; -.
DR PDBsum; 3VRU; -.
DR PDBsum; 3VRV; -.
DR PDBsum; 3VRW; -.
DR PDBsum; 3W0G; -.
DR PDBsum; 3W0H; -.
DR PDBsum; 3W0I; -.
DR PDBsum; 3W0J; -.
DR PDBsum; 3W5P; -.
DR PDBsum; 3W5Q; -.
DR PDBsum; 3W5R; -.
DR PDBsum; 3W5T; -.
DR PDBsum; 3WT5; -.
DR PDBsum; 3WT6; -.
DR PDBsum; 3WT7; -.
DR PDBsum; 3WTQ; -.
DR PDBsum; 4YNK; -.
DR PDBsum; 5AWJ; -.
DR PDBsum; 5AWK; -.
DR PDBsum; 5B41; -.
DR PDBsum; 5B5B; -.
DR PDBsum; 5GIC; -.
DR PDBsum; 5GID; -.
DR PDBsum; 5GIE; -.
DR PDBsum; 5XPM; -.
DR PDBsum; 5XPN; -.
DR PDBsum; 5XPO; -.
DR PDBsum; 5XPP; -.
DR PDBsum; 5XUQ; -.
DR PDBsum; 5XZF; -.
DR PDBsum; 5XZH; -.
DR PDBsum; 5ZWE; -.
DR PDBsum; 5ZWF; -.
DR PDBsum; 5ZWH; -.
DR PDBsum; 5ZWI; -.
DR PDBsum; 6D94; -.
DR PDBsum; 6JEZ; -.
DR PDBsum; 6K5O; -.
DR PDBsum; 6ONJ; -.
DR PDBsum; 7C7V; -.
DR PDBsum; 7C7W; -.
DR PDBsum; 7EMF; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7ENJ; -.
DR PDBsum; 7VQP; -.
DR AlphaFoldDB; Q15648; -.
DR SMR; Q15648; -.
DR BioGRID; 111465; 167.
DR ComplexPortal; CPX-3227; Core mediator complex.
DR CORUM; Q15648; -.
DR DIP; DIP-24212N; -.
DR ELM; Q15648; -.
DR IntAct; Q15648; 79.
DR MINT; Q15648; -.
DR STRING; 9606.ENSP00000300651; -.
DR DrugBank; DB04891; Becocalcidiol.
DR GlyGen; Q15648; 7 sites, 2 O-linked glycans (7 sites).
DR iPTMnet; Q15648; -.
DR PhosphoSitePlus; Q15648; -.
DR SwissPalm; Q15648; -.
DR BioMuta; MED1; -.
DR DMDM; 158518535; -.
DR EPD; Q15648; -.
DR jPOST; Q15648; -.
DR MassIVE; Q15648; -.
DR MaxQB; Q15648; -.
DR PaxDb; Q15648; -.
DR PeptideAtlas; Q15648; -.
DR PRIDE; Q15648; -.
DR ProteomicsDB; 60685; -. [Q15648-1]
DR ProteomicsDB; 60686; -. [Q15648-3]
DR Antibodypedia; 4326; 531 antibodies from 39 providers.
DR DNASU; 5469; -.
DR Ensembl; ENST00000300651.11; ENSP00000300651.6; ENSG00000125686.12. [Q15648-1]
DR Ensembl; ENST00000394287.7; ENSP00000377828.3; ENSG00000125686.12. [Q15648-3]
DR GeneID; 5469; -.
DR KEGG; hsa:5469; -.
DR MANE-Select; ENST00000300651.11; ENSP00000300651.6; NM_004774.4; NP_004765.2.
DR UCSC; uc002hru.3; human. [Q15648-1]
DR CTD; 5469; -.
DR DisGeNET; 5469; -.
DR GeneCards; MED1; -.
DR HGNC; HGNC:9234; MED1.
DR HPA; ENSG00000125686; Low tissue specificity.
DR MIM; 604311; gene.
DR neXtProt; NX_Q15648; -.
DR OpenTargets; ENSG00000125686; -.
DR PharmGKB; PA33556; -.
DR VEuPathDB; HostDB:ENSG00000125686; -.
DR eggNOG; ENOG502QPZ7; Eukaryota.
DR GeneTree; ENSGT00660000095569; -.
DR HOGENOM; CLU_019440_0_0_1; -.
DR InParanoid; Q15648; -.
DR OMA; HAMKLTY; -.
DR OrthoDB; 57581at2759; -.
DR PhylomeDB; Q15648; -.
DR TreeFam; TF324954; -.
DR PathwayCommons; Q15648; -.
DR Reactome; R-HSA-1368082; RORA activates gene expression.
DR Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-HSA-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-HSA-400253; Circadian Clock.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR Reactome; R-HSA-9707616; Heme signaling.
DR SignaLink; Q15648; -.
DR SIGNOR; Q15648; -.
DR BioGRID-ORCS; 5469; 399 hits in 1107 CRISPR screens.
DR ChiTaRS; MED1; human.
DR EvolutionaryTrace; Q15648; -.
DR GeneWiki; MED1; -.
DR GenomeRNAi; 5469; -.
DR Pharos; Q15648; Tbio.
DR PRO; PR:Q15648; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q15648; protein.
DR Bgee; ENSG00000125686; Expressed in tendon of biceps brachii and 209 other tissues.
DR ExpressionAtlas; Q15648; baseline and differential.
DR Genevisible; Q15648; HS.
DR GO; GO:0070847; C:core mediator complex; IPI:ComplexPortal.
DR GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IMP:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0050693; F:LBD domain binding; IPI:UniProtKB.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IPI:UniProtKB.
DR GO; GO:0016922; F:nuclear receptor binding; IDA:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IMP:UniProtKB.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; IPI:UniProtKB.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IDA:UniProtKB.
DR GO; GO:0042809; F:nuclear vitamin D receptor binding; IPI:UniProtKB.
DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IPI:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0001223; F:transcription coactivator binding; IPI:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0006702; P:androgen biosynthetic process; IMP:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0000902; P:cell morphogenesis; IMP:UniProtKB.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071383; P:cellular response to steroid hormone stimulus; IDA:UniProtKB.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IDA:UniProtKB.
DR GO; GO:0035050; P:embryonic heart tube development; IEA:Ensembl.
DR GO; GO:0035162; P:embryonic hemopoiesis; IEA:Ensembl.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl.
DR GO; GO:0001892; P:embryonic placenta development; IEA:Ensembl.
DR GO; GO:0048822; P:enucleate erythrocyte development; IEA:Ensembl.
DR GO; GO:0060750; P:epithelial cell proliferation involved in mammary gland duct elongation; IEA:Ensembl.
DR GO; GO:0048821; P:erythrocyte development; ISS:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; IDA:MGI.
DR GO; GO:0045023; P:G0 to G1 transition; IEA:Ensembl.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; IEA:Ensembl.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0030216; P:keratinocyte differentiation; IMP:UniProtKB.
DR GO; GO:0007595; P:lactation; IEA:Ensembl.
DR GO; GO:0002088; P:lens development in camera-type eye; ISS:UniProtKB.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0060745; P:mammary gland branching involved in pregnancy; IEA:Ensembl.
DR GO; GO:0060744; P:mammary gland branching involved in thelarche; IEA:Ensembl.
DR GO; GO:0035855; P:megakaryocyte development; ISS:UniProtKB.
DR GO; GO:0030224; P:monocyte differentiation; IEA:Ensembl.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IMP:UniProtKB.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0070318; P:positive regulation of G0 to G1 transition; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:2000347; P:positive regulation of hepatocyte proliferation; IEA:Ensembl.
DR GO; GO:0060335; P:positive regulation of interferon-gamma-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR GO; GO:2001141; P:regulation of RNA biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0070562; P:regulation of vitamin D receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0003406; P:retinal pigment epithelium development; IEA:Ensembl.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR GO; GO:0006590; P:thyroid hormone generation; IEA:Ensembl.
DR GO; GO:0002154; P:thyroid hormone mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IEA:Ensembl.
DR IDEAL; IID00173; -.
DR InterPro; IPR019680; Mediator_Med1.
DR Pfam; PF10744; Med1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..1581
FT /note="Mediator of RNA polymerase II transcription subunit
FT 1"
FT /id="PRO_0000058552"
FT REGION 1..670
FT /note="Interaction with the Mediator complex and THRA"
FT REGION 16..590
FT /note="Interaction with ESR1"
FT REGION 108..212
FT /note="Interaction with the Mediator complex"
FT REGION 215..390
FT /note="Interaction with the Mediator complex"
FT REGION 405..644
FT /note="Interaction with THRA"
FT REGION 542..789
FT /note="Interaction with VDR"
FT REGION 609..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..701
FT /note="Interaction with PPARGC1A and THRA"
FT /evidence="ECO:0000269|PubMed:14636573"
FT REGION 656..1066
FT /note="Interaction with ESR1"
FT REGION 681..715
FT /note="Interaction with GATA1"
FT /evidence="ECO:0000269|PubMed:24245781"
FT REGION 792..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..1566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1249..1421
FT /note="Interaction with TP53"
FT /evidence="ECO:0000269|PubMed:9444950"
FT MOTIF 604..608
FT /note="LXXLL motif 1"
FT MOTIF 645..649
FT /note="LXXLL motif 2"
FT MOTIF 875..902
FT /note="Integrase domain-binding motif (IBM)"
FT /evidence="ECO:0000269|PubMed:29997176"
FT COMPBIAS 652..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1020
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1052
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1349..1366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1367..1388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1508..1530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1531..1556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 795
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 805
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 887
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:29997176"
FT MOD_RES 953
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q925J9"
FT MOD_RES 1032
FT /note="Phosphothreonine; by MAPK1 or MAPK3"
FT /evidence="ECO:0000269|PubMed:16314496"
FT MOD_RES 1051
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1057
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1177
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1215
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1440
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1457
FT /note="Phosphothreonine; by MAPK1 or MAPK3"
FT /evidence="ECO:0000269|PubMed:16314496"
FT MOD_RES 1463
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 1465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q925J9"
FT MOD_RES 1479
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 1482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 1529
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 548..556
FT /note="YGMTTGNNP -> SKNPELGSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027906"
FT VAR_SEQ 557..1581
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027907"
FT VARIANT 753
FT /note="P -> T (in dbSNP:rs1139825)"
FT /id="VAR_053955"
FT VARIANT 1240
FT /note="S -> G (in dbSNP:rs35668211)"
FT /id="VAR_034938"
FT MUTAGEN 599..612
FT /note="SQNPILTSLLQITG->EKHKILHRLLQDSS: Enhances interaction
FT with ESR1."
FT /evidence="ECO:0000269|PubMed:11303023"
FT MUTAGEN 600..612
FT /note="QNPILTSLLQITG->RHKILHRLLQEGS: Enhances interaction
FT with ESR1."
FT /evidence="ECO:0000269|PubMed:12556447"
FT MUTAGEN 604
FT /note="L->A: Impairs interaction with ESR2; when associated
FT with A-607; A-645 and A-648."
FT /evidence="ECO:0000269|PubMed:11303023"
FT MUTAGEN 607..608
FT /note="LL->AA: Impairs interaction with ESR1, PPARG, RXRA
FT and THRB. Impairs interaction with THRA; when associated
FT with 648-A-A-649."
FT /evidence="ECO:0000269|PubMed:10733574,
FT ECO:0000269|PubMed:10770935, ECO:0000269|PubMed:12556447,
FT ECO:0000269|PubMed:14636573, ECO:0000269|PubMed:15340084,
FT ECO:0000269|PubMed:9653119"
FT MUTAGEN 607
FT /note="L->A: Impairs interaction with ESR2; when associated
FT with A-604; A-645 and A-648."
FT /evidence="ECO:0000269|PubMed:11303023"
FT MUTAGEN 639..653
FT /note="TKNHPMLMNLLKDNP->VSRHKILHRLLQEGS: Enhances
FT interaction with ESR1."
FT /evidence="ECO:0000269|PubMed:12556447"
FT MUTAGEN 645
FT /note="L->A: Impairs interaction with ESR2; when associated
FT with A-604; A-607 and A-648."
FT /evidence="ECO:0000269|PubMed:11303023"
FT MUTAGEN 648..649
FT /note="LL->AA: Impairs interaction with ESR1, PPARG, THRB
FT and VDR. Impairs interaction with THRA; when associated
FT with 607-A-A-608."
FT /evidence="ECO:0000269|PubMed:10733574,
FT ECO:0000269|PubMed:10770935, ECO:0000269|PubMed:12556447,
FT ECO:0000269|PubMed:14636573, ECO:0000269|PubMed:15340084,
FT ECO:0000269|PubMed:9653119"
FT MUTAGEN 648
FT /note="L->A: Impairs interaction with ESR2; when associated
FT with A-604; A-607 and A-645."
FT /evidence="ECO:0000269|PubMed:11303023"
FT MUTAGEN 886
FT /note="S->D: Increased interaction with PSIP1; when
FT associated with D-887 or D-887 and D-889."
FT /evidence="ECO:0000269|PubMed:29997176"
FT MUTAGEN 887
FT /note="S->D: Phosphomimetic mutant. Increased interaction
FT with PSIP1; when associated with D-886 or D-886 and D-889."
FT /evidence="ECO:0000269|PubMed:29997176"
FT MUTAGEN 889
FT /note="S->D: Increased interaction with PSIP1; when
FT associated with D-886 and D-887."
FT /evidence="ECO:0000269|PubMed:29997176"
FT MUTAGEN 1032
FT /note="T->A: Enhances protein stability; when associated
FT with A-1457."
FT /evidence="ECO:0000269|PubMed:16314496"
FT MUTAGEN 1457
FT /note="T->A: Enhances protein stability; when associated
FT with A-1032."
FT /evidence="ECO:0000269|PubMed:16314496"
FT CONFLICT 86
FT /note="R -> G (in Ref. 1; CAA73867)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="F -> S (in Ref. 1; CAA73867)"
FT /evidence="ECO:0000305"
FT CONFLICT 471..472
FT /note="DS -> GL (in Ref. 1; CAA73867)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="P -> S (in Ref. 1; CAA73867 and 7; AAF98352)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="T -> A (in Ref. 1; CAA73867 and 7; AAF98352)"
FT /evidence="ECO:0000305"
FT CONFLICT 651
FT /note="D -> N (in Ref. 5; AAH06517)"
FT /evidence="ECO:0000305"
FT CONFLICT 673
FT /note="S -> F (in Ref. 9; AAC41736)"
FT /evidence="ECO:0000305"
FT CONFLICT 702..708
FT /note="Missing (in Ref. 9; AAC41736)"
FT /evidence="ECO:0000305"
FT CONFLICT 721
FT /note="N -> K (in Ref. 2; AAC39854)"
FT /evidence="ECO:0000305"
FT CONFLICT 728
FT /note="M -> R (in Ref. 7; AAF98352)"
FT /evidence="ECO:0000305"
FT CONFLICT 756..761
FT /note="VPHPQP -> FYLTPQ (in Ref. 5; AAH06517)"
FT /evidence="ECO:0000305"
FT CONFLICT 1388
FT /note="G -> S (in Ref. 2; AAC39854)"
FT /evidence="ECO:0000305"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 34..45
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 74..88
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 147..160
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 168..194
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 249..261
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 300..314
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 315..325
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 339..348
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 371..375
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 389..400
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 404..422
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 438..446
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 449..455
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 457..469
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 475..480
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 491..501
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 504..517
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 639..641
FT /evidence="ECO:0007829|PDB:6D94"
FT HELIX 643..649
FT /evidence="ECO:0007829|PDB:2O4J"
SQ 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
