GENTAUR Molecular Products.
Monoclonal Antibody, ELISA Kit, Polyclonal Antibody, Recombinant/Purified Protein.Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery
Mediator of RNA polymerase II transcription subunit 1 (Activator-recruited cofactor 205 kDa component) (ARC205) (Mediator complex subunit 1) (Peroxisome proliferator-activated receptor-binding protein) (PBP) (PPAR-binding protein) (Thyroid hormone receptor-associated protein complex 220 kDa component) (Trap220) (Thyroid receptor-interacting protein 2) (TR-interacting protein 2) (TRIP-2) (Vitamin D receptor-interacting protein complex component DRIP205) (p53 regulatory protein RB18A)
MED1_HUMAN Reviewed; 1581 AA.
Q15648; A2RRQ6; O43810; O75447; Q6P9H7; Q6PK58; Q9HD39;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
11-SEP-2007, sequence version 4.
28-MAR-2018, entry version 180.
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;
Q00987:MDM2; NbExp=3; IntAct=EBI-394459, EBI-389668;
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;
P04637:TP53; NbExp=3; IntAct=EBI-394459, EBI-366083;
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};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs 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.
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; -.
ProteinModelPortal; Q15648; -.
SMR; Q15648; -.
BioGrid; 111465; 104.
CORUM; Q15648; -.
DIP; DIP-24212N; -.
ELM; Q15648; -.
IntAct; Q15648; 52.
MINT; Q15648; -.
STRING; 9606.ENSP00000300651; -.
iPTMnet; Q15648; -.
PhosphoSitePlus; Q15648; -.
BioMuta; MED1; -.
DMDM; 158518535; -.
EPD; Q15648; -.
MaxQB; Q15648; -.
PaxDb; Q15648; -.
PeptideAtlas; Q15648; -.
PRIDE; Q15648; -.
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-2032785; YAP1- and WWTR1 (TAZ)-stimulated 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-8951671; RUNX3 regulates YAP1-mediated transcription.
SignaLink; Q15648; -.
SIGNOR; Q15648; -.
ChiTaRS; MED1; human.
EvolutionaryTrace; Q15648; -.
GeneWiki; MED1; -.
GenomeRNAi; 5469; -.
PRO; PR:Q15648; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000125686; -.
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:0016922; F:ligand-dependent nuclear receptor binding; IDA:UniProtKB.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IMP:UniProtKB.
GO; GO:0036033; F:mediator complex binding; IDA:UniProtKB.
GO; GO:0035257; F:nuclear hormone receptor binding; IPI:UniProtKB.
GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IPI:UniProtKB.
GO; GO:0004872; F:receptor activity; IDA:UniProtKB.
GO; GO:0042974; F:retinoic acid receptor binding; IPI:UniProtKB.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0001104; F:RNA polymerase II transcription cofactor activity; IDA:UniProtKB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISS: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 cofactor 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 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
Related products :
GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45
Fax 0032 16 50 90 45
info@gentaur.com | Gentaur
GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur
GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50
Fax 01 43 25 01 60
RCS Paris B 484 237 888
SIRET 48423788800017
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
france@gentaur.com | Gentaur
GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88
Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur
GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com
Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123
GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel: 0208-080893 Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62 SWIFT RABONL2U
GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur
ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF
GENTAUR Poland Sp. z o.o.
ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX 058 710 33 48
poland@gentaur.com | Gentaur
Other countries
Österreich +43720880899
Canada Montreal +15149077481
Ceská republika Praha +420246019719
Danmark +4569918806
Finland Helsset +358942419041
Magyarország Budapest +3619980547
Ireland Dublin+35316526556
Luxembourg+35220880274
Norge Oslo+4721031366
Sverige Stockholm+46852503438
Schweiz Züri+41435006251
US New York+17185132983
GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo
Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur
Pathways :
WP2272: Pathogenic Escherichia coli infection
WP2292: Chemokine signaling pathway
WP1531: Vitamin D synthesis
WP1624: Bacterial secretion system
WP1644: DNA replication
WP1663: Homologous recombination
WP1672: Mismatch repair
WP1692: Protein export
WP1693: Purine metabolism
WP1694: Pyrimidine metabolism
WP1713: Two-component system
WP731: Sterol regulatory element binding protein related
WP1566: Citrate cycle (TCA cycle)
WP1616: ABC transporters
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1909: Signal regulatory protein (SIRP) family interactions
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1502: Mitochondrial biogenesis
WP1613: 1,4-Dichlorobenzene degradation
WP1625: Base excision repair
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
Related Genes :
[MED30 THRAP6 TRAP25] Mediator of RNA polymerase II transcription subunit 30 (Mediator complex subunit 30) (TRAP/Mediator complex component TRAP25) (Thyroid hormone receptor-associated protein 6) (Thyroid hormone receptor-associated protein complex 25 kDa component) (Trap25)
[MED7 ARC34 CRSP9] Mediator of RNA polymerase II transcription subunit 7 (hMED7) (Activator-recruited cofactor 34 kDa component) (ARC34) (Cofactor required for Sp1 transcriptional activation subunit 9) (CRSP complex subunit 9) (Mediator complex subunit 7) (RNA polymerase transcriptional regulation mediator subunit 7 homolog) (Transcriptional coactivator CRSP33)
[skd bli Med13 pap Trap240 CG9936] Mediator of RNA polymerase II transcription subunit 13 (Mediator complex subunit 13) (Mediator complex subunit Skuld) (Protein blind spot) (Protein poils aux pattes) (dTRAP240)
[kto Med12 Trap230 CG8491] Mediator of RNA polymerase II transcription subunit 12 (Mediator complex subunit 12) (Mediator complex subunit Kohtalo) (dTRAP230)
[SRB4 MED17 YER022W] Mediator of RNA polymerase II transcription subunit 17 (Mediator complex subunit 17) (Suppressor of RNA polymerase B 4)
[SRB5 MED18 YGR104C] Mediator of RNA polymerase II transcription subunit 18 (Mediator complex subunit 18) (Suppressor of RNA polymerase B 5)
[MED11 YMR112C YM9718.11C] Mediator of RNA polymerase II transcription subunit 11 (Mediator complex subunit 11)
[MED8 YBR193C YBR1403] Mediator of RNA polymerase II transcription subunit 8 (Mediator complex subunit 8)
[SRB2 HRS2 MED20 YHR041C] Mediator of RNA polymerase II transcription subunit 20 (Hyper-recombination suppressor protein 2) (Mediator complex subunit 20) (Suppressor of RNA polymerase B 2)
[MED1 ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2] Mediator of RNA polymerase II transcription subunit 1 (Activator-recruited cofactor 205 kDa component) (ARC205) (Mediator complex subunit 1) (Peroxisome proliferator-activated receptor-binding protein) (PBP) (PPAR-binding protein) (Thyroid hormone receptor-associated protein complex 220 kDa component) (Trap220) (Thyroid receptor-interacting protein 2) (TR-interacting protein 2) (TRIP-2) (Vitamin D receptor-interacting protein complex component DRIP205) (p53 regulatory protein RB18A)
[MED4 YOR174W O3630] Mediator of RNA polymerase II transcription subunit 4 (Mediator complex subunit 4)
[ROX3 MED19 NUT3 SSN7 YBL093C YBL0837] Mediator of RNA polymerase II transcription subunit 19 (Hypoxic gene repressor protein 3) (Mediator complex subunit 19) (Negative regulator of URS2 protein 3) (SNF1 suppressor protein 7)
[NUT2 MED10 YPR168W P9325.2] Mediator of RNA polymerase II transcription subunit 10 (Mediator complex subunit 10) (Negative regulator of URS2 protein 2)
[MED1 YPR070W YP9499.25 YPR063W] Mediator of RNA polymerase II transcription subunit 1 (Mediator complex subunit 1)
[SRB6 MED22 YBR253W YBR1721] Mediator of RNA polymerase II transcription subunit 22 (Mediator complex subunit 22) (Suppressor of RNA polymerase B 6)
[RGR1 MED14 YLR071C] Mediator of RNA polymerase II transcription subunit 14 (Glucose repression regulatory protein 1) (Mediator complex subunit 14)
[CSE2 MED9 YNR010W N2046] Mediator of RNA polymerase II transcription subunit 9 (Chromosome segregation protein 2) (Mediator complex subunit 9)
[SRB7 MED21 YDR308C D9740.17] Mediator of RNA polymerase II transcription subunit 21 (Mediator complex subunit 21) (RNAPII complex component SRB7) (Suppressor of RNA polymerase B 7)
[NUT1 MED5 YGL151W G1876] Mediator of RNA polymerase II transcription subunit 5 (Mediator complex subunit 5) (Negative regulator of URS2 protein 1)
[GAL11 ABE1 MED15 RAR3 SDS4 SPT13 YOL051W] Mediator of RNA polymerase II transcription subunit 15 (Autonomous replication regulatory protein 3) (Basal expression activator protein 1) (Defective silencing suppressor protein 4) (Mediator complex subunit 15) (Transcription regulatory protein GAL11) (Ty insertion suppressor protein 13)
[SIN4 BEL2 GAL22 MED16 RYE1 SDI3 SSF5 SSN4 TSF3 YNL236W N1135] Mediator of RNA polymerase II transcription subunit 16 (Global transcriptional regulator SIN4) (Mediator complex subunit 16) (SNF1 suppressor protein 4) (SWI4 suppressor protein 5) (Transcriptional silencing factor 3) (YGP1 expression regulatory protein 1)
[MED2 YDL005C D2930] Mediator of RNA polymerase II transcription subunit 2 (Mediator complex subunit 2)
[PGD1 HRS1 MED3 YGL025C] Mediator of RNA polymerase II transcription subunit 3 (Hyper-recombination suppressor protein 1) (Mediator complex subunit 3) (Poly-glutamine domain protein 1)
[MED6 ARC33] Mediator of RNA polymerase II transcription subunit 6 (Activator-recruited cofactor 33 kDa component) (ARC33) (Mediator complex subunit 6) (hMed6) (Renal carcinoma antigen NY-REN-28)
[MED25 ACID1 ARC92 PTOV2 TCBAP0758] Mediator of RNA polymerase II transcription subunit 25 (Activator interaction domain-containing protein 1) (Activator-recruited cofactor 92 kDa component) (ARC92) (Mediator complex subunit 25) (p78)
[SOH1 MED31 YGL127C G2864] Mediator of RNA polymerase II transcription subunit 31 (Hpr1 suppressor protein 1) (Mediator complex subunit 31)
[MED23 ARC130 CRSP3 DRIP130 KIAA1216 SUR2] Mediator of RNA polymerase II transcription subunit 23 (Activator-recruited cofactor 130 kDa component) (ARC130) (Cofactor required for Sp1 transcriptional activation subunit 3) (CRSP complex subunit 3) (Mediator complex subunit 23) (Protein sur-2 homolog) (hSur-2) (Transcriptional coactivator CRSP130) (Vitamin D3 receptor-interacting protein complex 130 kDa component) (DRIP130)
[MED14 ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170] Mediator of RNA polymerase II transcription subunit 14 (Activator-recruited cofactor 150 kDa component) (ARC150) (Cofactor required for Sp1 transcriptional activation subunit 2) (CRSP complex subunit 2) (Mediator complex subunit 14) (RGR1 homolog) (hRGR1) (Thyroid hormone receptor-associated protein complex 170 kDa component) (Trap170) (Transcriptional coactivator CRSP150) (Vitamin D3 receptor-interacting protein complex 150 kDa component) (DRIP150)
[MED29 IXL] Mediator of RNA polymerase II transcription subunit 29 (Intersex-like protein) (Mediator complex subunit 29)
[MED12 ARC240 CAGH45 HOPA KIAA0192 TNRC11 TRAP230] Mediator of RNA polymerase II transcription subunit 12 (Activator-recruited cofactor 240 kDa component) (ARC240) (CAG repeat protein 45) (Mediator complex subunit 12) (OPA-containing protein) (Thyroid hormone receptor-associated protein complex 230 kDa component) (Trap230) (Trinucleotide repeat-containing gene 11 protein)
Bibliography :
No related Items
Enter catalog number :
Favorites Pages:
No Favorits