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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.
27-SEP-2017, entry version 176.
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:
Q00987:MDM2; NbExp=3; IntAct=EBI-394459, EBI-389668;
O43513:MED7; NbExp=4; IntAct=EBI-394459, EBI-394632;
P10276:RARA; NbExp=3; IntAct=EBI-394459, EBI-413374;
P10827:THRA; NbExp=5; IntAct=EBI-394459, EBI-286285;
P04637:TP53; NbExp=3; IntAct=EBI-394459, EBI-366083;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15471764,
ECO:0000269|PubMed:16314496, ECO:0000269|PubMed:16574658}. Note=A
subset of the protein may enter the nucleolus subsequent to
phosphorylation by MAPK1 or MAPK3.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q15648-1; Sequence=Displayed;
Name=2;
IsoId=Q15648-3; Sequence=VSP_027906, VSP_027907;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:9444950, ECO:0000269|PubMed:9653119}.
-!- PTM: Phosphorylated by MAPK1 or MAPK3 during G2/M phase which may
enhance protein stability and promote entry into the nucleolus.
{ECO:0000269|PubMed:16314496}.
-!- SIMILARITY: Belongs to the Mediator complex subunit 1 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC39854.1; Type=Frameshift; Positions=543, 545; Evidence={ECO:0000305};
Sequence=AAH06517.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=CAA73867.1; Type=Frameshift; Positions=4; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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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; 102.
CORUM; Q15648; -.
DIP; DIP-24212N; -.
ELM; Q15648; -.
IntAct; Q15648; 42.
MINT; MINT-1345780; -.
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; IDA: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:0000978; F:RNA polymerase II core promoter proximal region 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 from RNA polymerase II promoter; 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 from RNA polymerase II promoter; 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 from RNA polymerase II promoter; 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 from RNA polymerase I promoter; IDA:UniProtKB.
GO; GO:0070562; P:regulation of vitamin D receptor signaling pathway; IEA:Ensembl.
GO; GO:0003406; P:retinal pigment epithelium development; IEA:Ensembl.
GO; GO:0006590; P:thyroid hormone generation; IEA:Ensembl.
GO; GO:0002154; P:thyroid hormone mediated signaling pathway; IMP:UniProtKB.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IEA:Ensembl.
InterPro; IPR019680; Mediator_Med1.
Pfam; PF10744; Med1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Complete proteome; Direct protein sequencing; DNA-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Transcription; Transcription regulation.
CHAIN 1 1581 Mediator of RNA polymerase II
transcription subunit 1.
/FTId=PRO_0000058552.
REGION 1 670 Interaction with the Mediator complex and
THRA.
REGION 16 590 Interaction with ESR1.
REGION 108 212 Interaction with the Mediator complex.
REGION 215 390 Interaction with the Mediator complex.
REGION 405 644 Interaction with THRA.
REGION 542 789 Interaction with VDR.
REGION 622 701 Interaction with PPARGC1A and THRA.
{ECO:0000269|PubMed:14636573}.
REGION 656 1066 Interaction with ESR1.
REGION 681 715 Interaction with GATA1.
{ECO:0000269|PubMed:24245781}.
REGION 1249 1421 Interaction with TP53.
{ECO:0000269|PubMed:9444950}.
MOTIF 604 608 LXXLL motif 1.
MOTIF 645 649 LXXLL motif 2.
COMPBIAS 1078 1482 Ser-rich.
COMPBIAS 1496 1529 Lys-rich.
MOD_RES 588 588 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 664 664 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 795 795 Phosphoserine.
{ECO:0000244|PubMed:16964243}.
MOD_RES 805 805 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 953 953 Phosphoserine.
{ECO:0000250|UniProtKB:Q925J9}.
MOD_RES 1032 1032 Phosphothreonine; by MAPK1 or MAPK3.
{ECO:0000269|PubMed:16314496}.
MOD_RES 1051 1051 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1057 1057 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1156 1156 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1177 1177 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1207 1207 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1215 1215 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1223 1223 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1302 1302 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1347 1347 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1403 1403 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1433 1433 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1440 1440 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1457 1457 Phosphothreonine; by MAPK1 or MAPK3.
{ECO:0000269|PubMed:16314496}.
MOD_RES 1463 1463 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1465 1465 Phosphoserine.
{ECO:0000250|UniProtKB:Q925J9}.
MOD_RES 1479 1479 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1481 1481 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1482 1482 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1529 1529 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 548 556 YGMTTGNNP -> SKNPELGSG (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_027906.
VAR_SEQ 557 1581 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_027907.
VARIANT 753 753 P -> T (in dbSNP:rs1139825).
/FTId=VAR_053955.
VARIANT 1240 1240 S -> G (in dbSNP:rs35668211).
/FTId=VAR_034938.
MUTAGEN 599 612 SQNPILTSLLQITG->EKHKILHRLLQDSS: Enhances
interaction with ESR1.
{ECO:0000269|PubMed:11303023}.
MUTAGEN 600 612 QNPILTSLLQITG->RHKILHRLLQEGS: Enhances
interaction with ESR1.
{ECO:0000269|PubMed:12556447}.
MUTAGEN 604 604 L->A: Impairs interaction with ESR2; when
associated with A-607; A-645 and A-648.
{ECO:0000269|PubMed:11303023}.
MUTAGEN 607 608 LL->AA: Impairs interaction with ESR1,
PPARG, RXRA and THRB. Impairs interaction
with THRA; when associated with 648-A-A-
649. {ECO:0000269|PubMed:10733574,
ECO:0000269|PubMed:10770935,
ECO:0000269|PubMed:12556447,
ECO:0000269|PubMed:14636573,
ECO:0000269|PubMed:15340084,
ECO:0000269|PubMed:9653119}.
MUTAGEN 607 607 L->A: Impairs interaction with ESR2; when
associated with A-604; A-645 and A-648.
{ECO:0000269|PubMed:11303023}.
MUTAGEN 639 653 TKNHPMLMNLLKDNP->VSRHKILHRLLQEGS:
Enhances interaction with ESR1.
{ECO:0000269|PubMed:12556447}.
MUTAGEN 645 645 L->A: Impairs interaction with ESR2; when
associated with A-604; A-607 and A-648.
{ECO:0000269|PubMed:11303023}.
MUTAGEN 648 649 LL->AA: Impairs interaction with ESR1,
PPARG, THRB and VDR. Impairs interaction
with THRA; when associated with 607-A-A-
608. {ECO:0000269|PubMed:10733574,
ECO:0000269|PubMed:10770935,
ECO:0000269|PubMed:12556447,
ECO:0000269|PubMed:14636573,
ECO:0000269|PubMed:15340084,
ECO:0000269|PubMed:9653119}.
MUTAGEN 648 648 L->A: Impairs interaction with ESR2; when
associated with A-604; A-607 and A-645.
{ECO:0000269|PubMed:11303023}.
MUTAGEN 1032 1032 T->A: Enhances protein stability; when
associated with A-1457.
{ECO:0000269|PubMed:16314496}.
MUTAGEN 1457 1457 T->A: Enhances protein stability; when
associated with A-1032.
{ECO:0000269|PubMed:16314496}.
CONFLICT 86 86 R -> G (in Ref. 1; CAA73867).
{ECO:0000305}.
CONFLICT 147 147 F -> S (in Ref. 1; CAA73867).
{ECO:0000305}.
CONFLICT 471 472 DS -> GL (in Ref. 1; CAA73867).
{ECO:0000305}.
CONFLICT 563 563 P -> S (in Ref. 1; CAA73867 and 7;
AAF98352). {ECO:0000305}.
CONFLICT 573 573 T -> A (in Ref. 1; CAA73867 and 7;
AAF98352). {ECO:0000305}.
CONFLICT 651 651 D -> N (in Ref. 5; AAH06517).
{ECO:0000305}.
CONFLICT 673 673 S -> F (in Ref. 9; AAC41736).
{ECO:0000305}.
CONFLICT 702 708 Missing (in Ref. 9; AAC41736).
{ECO:0000305}.
CONFLICT 721 721 N -> K (in Ref. 2; AAC39854).
{ECO:0000305}.
CONFLICT 728 728 M -> R (in Ref. 7; AAF98352).
{ECO:0000305}.
CONFLICT 756 761 VPHPQP -> FYLTPQ (in Ref. 5; AAH06517).
{ECO:0000305}.
CONFLICT 1388 1388 G -> S (in Ref. 2; AAC39854).
{ECO:0000305}.
HELIX 643 649 {ECO:0000244|PDB:2O4J}.
SEQUENCE 1581 AA; 168478 MW; FCE0FE87EF08B887 CRC64;
MKAQGETEES EKLSKMSSLL ERLHAKFNQN RPWSETIKLV RQVMEKRVVM SSGGHQHLVS
CLETLQKALK VTSLPAMTDR LESIARQNGL GSHLSASGTE CYITSDMFYV EVQLDPAGQL
CDVKVAHHGE NPVSCPELVQ QLREKNFDEF SKHLKGLVNL YNLPGDNKLK TKMYLALQSL
EQDLSKMAIM YWKATNAGPL DKILHGSVGY LTPRSGGHLM NLKYYVSPSD LLDDKTASPI
ILHENNVSRS LGMNASVTIE GTSAVYKLPI APLIMGSHPV DNKWTPSFSS ITSANSVDLP
ACFFLKFPQP IPVSRAFVQK LQNCTGIPLF ETQPTYAPLY ELITQFELSK DPDPIPLNHN
MRFYAALPGQ QHCYFLNKDA PLPDGRSLQG TLVSKITFQH PGRVPLILNL IRHQVAYNTL
IGSCVKRTIL KEDSPGLLQF EVCPLSESRF SVSFQHPVND SLVCVVMDVQ DSTHVSCKLY
KGLSDALICT DDFIAKVVQR CMSIPVTMRA IRRKAETIQA DTPALSLIAE TVEDMVKKNL
PPASSPGYGM TTGNNPMSGT TTPTNTFPGG PITTLFNMSM SIKDRHESVG HGEDFSKVSQ
NPILTSLLQI TGNGGSTIGS SPTPPHHTPP PVSSMAGNTK NHPMLMNLLK DNPAQDFSTL
YGSSPLERQN SSSGSPRMEI CSGSNKTKKK KSSRLPPEKP KHQTEDDFQR ELFSMDVDSQ
NPIFDVNMTA DTLDTPHITP APSQCSTPPT TYPQPVPHPQ PSIQRMVRLS SSDSIGPDVT
DILSDIAEEA SKLPSTSDDC PAIGTPLRDS SSSGHSQSTL FDSDVFQTNN NENPYTDPAD
LIADAAGSPS SDSPTNHFFH DGVDFNPDLL NSQSQSGFGE EYFDESSQSG DNDDFKGFAS
QALNTLGVPM LGGDNGETKF KGNNQADTVD FSIISVAGKA LAPADLMEHH SGSQGPLLTT
GDLGKEKTQK RVKEGNGTSN STLSGPGLDS KPGKRSRTPS NDGKSKDKPP KRKKADTEGK
SPSHSSSNRP FTPPTSTGGS KSPGSAGRSQ TPPGVATPPI PKITIQIPKG TVMVGKPSSH
SQYTSSGSVS SSGSKSHHSH SSSSSSSAST SGKMKSSKSE GSSSSKLSSS MYSSQGSSGS
SQSKNSSQSG GKPGSSPITK HGLSSGSSST KMKPQGKPSS LMNPSLSKPN ISPSHSRPPG
GSDKLASPMK PVPGTPPSSK AKSPISSGSG GSHMSGTSSS SGMKSSSGLG SSGSLSQKTP
PSSNSCTASS SSFSSSGSSM SSSQNQHGSS KGKSPSRNKK PSLTAVIDKL KHGVVTSGPG
GEDPLDGQMG VSTNSSSHPM SSKHNMSGGE FQGKREKSDK DKSKVSTSGS SVDSSKKTSE
SKNVGSTGVA KIIISKHDGG SPSIKAKVTL QKPGESSGEG LRPQMASSKN YGSPLISGST
PKHERGSPSH SKSPAYTPQN LDSESESGSS IAEKSYQNSP SSDDGIRPLP EYSTEKHKKH
KKEKKKVKDK DRDRDRDKDR DKKKSHSIKP ESWSKSPISS DQSLSMTSNT ILSADRPSRL
SPDFMIGEED DDLMDVALIG N


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