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Mediator of RNA polymerase II transcription subunit 1 (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)

 MED1_MOUSE              Reviewed;        1575 AA.
Q925J9; A2A526; A2A528; O88323; Q3UHV0; Q6AXD5; Q8BW37; Q8BX19; Q8VDQ7;
Q925K0;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 2.
23-FEB-2022, entry version 165.
RecName: Full=Mediator of RNA polymerase II transcription subunit 1;
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;
Name=Med1; Synonyms=Crsp210, Drip205, Pbp, Pparbp, Trap220, Trip2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:AAC31118.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, TISSUE SPECIFICITY, AND
INTERACTION WITH PPARA; PPARG; RARA; RXRA AND THRB.
TISSUE=Liver {ECO:0000269|PubMed:9325263};
PubMed=9325263; DOI=10.1074/jbc.272.41.25500;
Zhu Y., Qi C., Jain S., Rao M.S., Reddy J.K.;
"Isolation and characterization of PBP, a protein that interacts with
peroxisome proliferator-activated receptor.";
J. Biol. Chem. 272:25500-25506(1997).
[2] {ECO:0000305, ECO:0000312|EMBL:AAK56102.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND VARIANTS SER-960 AND MET-1348.
STRAIN=ILS {ECO:0000312|EMBL:AAK56102.1}, and
ISS {ECO:0000312|EMBL:AAK56101.1};
PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
"High-throughput sequence identification of gene coding variants within
alcohol-related QTLs.";
Mamm. Genome 12:657-663(2001).
[3] {ECO:0000305, ECO:0000312|EMBL:AAN75014.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND VARIANTS SER-960 AND MET-1348.
STRAIN=129/Ola {ECO:0000312|EMBL:AAN75014.1};
PubMed=14500757; DOI=10.1210/me.2003-0097;
Landles C., Chalk S., Steel J.H., Rosewell I., Spencer-Dene B.,
Lalani E.-N., Parker M.G.;
"The thyroid hormone receptor-associated protein TRAP220 is required at
distinct embryonic stages in placental, cardiac, and hepatic development.";
Mol. Endocrinol. 17:2418-2435(2003).
[4] {ECO:0000305, ECO:0000312|EMBL:BAC35779.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
[LARGE SCALE MRNA] OF 1-389 (ISOFORMS 1/4), AND NUCLEOTIDE SEQUENCE [LARGE
SCALE MRNA] OF 1-964 (ISOFORM 1).
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC35779.2};
TISSUE=Embryonic stem cell {ECO:0000269|PubMed:16141072}, and
Ovary {ECO:0000312|EMBL:BAC35779.2};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of the
mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6] {ECO:0000305, ECO:0000312|EMBL:AAH79636.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH79636.1}, and
Czech II {ECO:0000312|EMBL:AAH21440.1};
TISSUE=Brain {ECO:0000269|PubMed:15489334}, and
Mammary gland {ECO:0000269|PubMed:15489334};
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).
[7]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=10882104; DOI=10.1016/s1097-2765(00)80247-6;
Ito M., Yuan C.-X., Okano H.J., Darnell R.B., Roeder R.G.;
"Involvement of the TRAP220 component of the TRAP/SMCC coactivator complex
in embryonic development and thyroid hormone action.";
Mol. Cell 5:683-693(2000).
[8] {ECO:0000305}
INTERACTION WITH YWHAH.
PubMed=11266503; DOI=10.1210/mend.15.4.0624;
Zilliacus J., Holter E., Wakui H., Tazawa H., Treuter E., Gustafsson J.-A.;
"Regulation of glucocorticoid receptor activity by 14-3-3-dependent
intracellular relocalization of the corepressor RIP140.";
Mol. Endocrinol. 15:501-511(2001).
[9]
FUNCTION.
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).
[10]
FUNCTION, 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).
[11]
INTERACTION WITH NR4A3.
PubMed=12709428; DOI=10.1074/jbc.m300088200;
Wansa K.D., Harris J.M., Yan G., Ordentlich P., Muscat G.E.;
"The AF-1 domain of the orphan nuclear receptor NOR-1 mediates trans-
activation, coactivator recruitment, and activation by the purine anti-
metabolite 6-mercaptopurine.";
J. Biol. Chem. 278:24776-24790(2003).
[12]
FUNCTION, AND INTERACTION WITH PPARGC1A.
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).
[13]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15150259; DOI=10.1074/jbc.m402391200;
Jia Y., Qi C., Kashireddy P., Surapureddi S., Zhu Y.-J., Rao M.S.,
Le Roith D., Chambon P., Gonzalez F.J., Reddy J.K.;
"Transcription coactivator PBP, the peroxisome proliferator-activated
receptor (PPAR)-binding protein, is required for PPARalpha-regulated gene
expression in liver.";
J. Biol. Chem. 279:24427-24434(2004).
[14]
ERRATUM OF PUBMED:15150259.
Jia Y., Qi C., Kashireddy P., Surapureddi S., Zhu Y.-J., Rao M.S.,
Le Roith D., Chambon P., Gonzalez F.J., Reddy J.K.;
J. Biol. Chem. 279:29870-29870(2004).
[15]
FUNCTION, AND INTERACTION OF THE MEDIATOR COMPLEX WITH THRA.
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).
[16]
FUNCTION, AND ASSOCIATION WITH PROMOTER REGIONS.
PubMed=16137621; DOI=10.1016/j.molcel.2005.08.008;
Park S.W., Li G., Lin Y.-P., Barrero M.J., Ge K., Roeder R.G., Wei L.-N.;
"Thyroid hormone-induced juxtaposition of regulatory elements/factors and
chromatin remodeling of Crabp1 dependent on MED1/TRAP220.";
Mol. Cell 19:643-653(2005).
[17]
FUNCTION, INTERACTION WITH GATA1, AND ASSOCIATION WITH PROMOTER REGIONS.
PubMed=17132730; DOI=10.1073/pnas.0604494103;
Stumpf M., Waskow C., Kroetschel M., van Essen D., Rodriguez P., Zhang X.,
Guyot B., Roeder R.G., Borggrefe T.;
"The mediator complex functions as a coactivator for GATA-1 in
erythropoiesis via subunit Med1/TRAP220.";
Proc. Natl. Acad. Sci. U.S.A. 103:18504-18509(2006).
[18]
ERRATUM OF PUBMED:17132730.
Stumpf M., Waskow C., Kroetschel M., van Essen D., Rodriguez P., Zhang X.,
Guyot B., Roeder R.G., Borggrefe T.;
Proc. Natl. Acad. Sci. U.S.A. 104:1442-1442(2007).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-953 AND SER-955, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664; THR-805; SER-955;
THR-1051; THR-1057; SER-1158; SER-1209; SER-1435; THR-1442; SER-1465;
SER-1467; SER-1481 AND SER-1484, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[21]
INTERACTION WITH CLOCK.
PubMed=24043798; DOI=10.1073/pnas.1305980110;
Lande-Diner L., Boyault C., Kim J.Y., Weitz C.J.;
"A positive feedback loop links circadian clock factor CLOCK-BMAL1 to the
basic transcriptional machinery.";
Proc. Natl. Acad. Sci. U.S.A. 110:16021-16026(2013).
[22]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 641-654 IN COMPLEX WITH RARB AND
RXRA.
PubMed=15528208; DOI=10.1074/jbc.m409302200;
Pogenberg V., Guichou J.F., Vivat-Hannah V., Kammerer S., Perez E.,
Germain P., de Lera A.R., Gronemeyer H., Royer C.A., Bourguet W.;
"Characterization of the interaction between retinoic acid
receptor/retinoid X receptor (RAR/RXR) heterodimers and transcriptional
coactivators through structural and fluorescence anisotropy studies.";
J. Biol. Chem. 280:1625-1633(2005).
-!- 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. Essential for embryogenesis,
including development of the central nervous system, heart, liver and
placenta and for erythropoiesis. Also required for normal
transcriptional control of thyroid-stimulating hormone beta (TSHB) in
the pituitary. Acts as a coactivator for GATA1-mediated transcriptional
activation during erythroid differentiation of K562 erythroleukemia
cells (By similarity). {ECO:0000250|UniProtKB:Q15648,
ECO:0000269|PubMed:10882104, ECO:0000269|PubMed:11867769,
ECO:0000269|PubMed:12037571, ECO:0000269|PubMed:14500757,
ECO:0000269|PubMed:14636573, ECO:0000269|PubMed:15150259,
ECO:0000269|PubMed:15340084, ECO:0000269|PubMed:16137621,
ECO:0000269|PubMed:17132730, ECO:0000269|PubMed:9325263}.
-!- 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 GATA1 and YWHAH. Interacts with CLOCK; this interaction
requires the presence of THRAP3. Interacts with CCAR1 (By similarity).
Interacts with NR4A3 (PubMed:12709428). Interacts (via IBM motif) with
PSIP1 (via IBD domain); phosphorylation increases its affinity for
PSIP1 (By similarity). {ECO:0000250|UniProtKB:Q15648,
ECO:0000269|PubMed:11266503, ECO:0000269|PubMed:11867769,
ECO:0000269|PubMed:12709428, ECO:0000269|PubMed:14636573,
ECO:0000269|PubMed:15340084, ECO:0000269|PubMed:15528208,
ECO:0000269|PubMed:17132730, ECO:0000269|PubMed:24043798,
ECO:0000269|PubMed:9325263}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15150259}. Note=A
subset of the protein may enter the nucleolus subsequent to
phosphorylation by MAPK1 or MAPK3. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1 {ECO:0000303|PubMed:16141072};
IsoId=Q925J9-1; Sequence=Displayed;
Name=2 {ECO:0000303|PubMed:15489334};
IsoId=Q925J9-2; Sequence=VSP_051893, VSP_051896;
Name=3 {ECO:0000303|PubMed:16141072};
IsoId=Q925J9-3; Sequence=VSP_051894, VSP_051895;
Name=4 {ECO:0000269|PubMed:11471062, ECO:0000269|PubMed:9325263};
IsoId=Q925J9-4; Sequence=VSP_051892;
-!- TISSUE SPECIFICITY: Widely expressed in the adult, with high levels of
expression in the liver, lung, intestinal mucosa, kidney cortex, thymic
cortex, splenic follicle and seminiferous epithelium in testis. Also
expressed in the adult heart, brain, spleen and skeletal muscle.
{ECO:0000269|PubMed:14500757, ECO:0000269|PubMed:9325263}.
-!- DEVELOPMENTAL STAGE: Widely expressed during embryonic development; at
stages 9.5 dpc-10.5 dpc, expression is strongest in neural tissues. At
11.5 dpc-12.5 dpc, expression is abundant throughout embryonic tissues,
being strongest in the developing liver, primitive gut, nasopharynx,
and developing limb buds. Moderately expressed at this stage in the
brain and optic stalk, branchial arch and urogential ridge. Expressed
at a low level in the heart. By stage 13.5 dpc-14.5 dpc, expression is
abundant in the forebrain, vagus nerve, dorsal root ganglia,
nasopharynx, kidney, liver, pancreas, intestine, gut, thymus, lung,
genital tubercle, tongue and lower jaw. Moderately expressed in the
midbrain and expressed at a low level in the heart and large blood
vessels. In the developing placenta, expression is moderate in the
giant and spongiotrophoblast cell layers and strongest in the
labyrinthine portion throughout 9.5 dpc-13.5 dpc.
{ECO:0000269|PubMed:10882104, ECO:0000269|PubMed:14500757}.
-!- PTM: Phosphorylated by MAPK1 or MAPK3 during G2/M phase which may
enhance protein stability and promote entry into the nucleolus (By
similarity). Phosphorylation increases its interaction with PSIP1 (By
similarity). {ECO:0000250|UniProtKB:Q15648}.
-!- SIMILARITY: Belongs to the Mediator complex subunit 1 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH21440.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
---------------------------------------------------------------------------
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EMBL; AF000294; AAC31118.1; -; mRNA.
EMBL; AF332073; AAK56101.1; -; mRNA.
EMBL; AF332074; AAK56102.1; -; mRNA.
EMBL; AY176046; AAN75014.1; -; Genomic_DNA.
EMBL; AK049203; BAC33607.2; -; mRNA.
EMBL; AK054437; BAC35779.2; -; mRNA.
EMBL; AK147199; BAE27757.1; -; mRNA.
EMBL; AL591205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC021440; AAH21440.1; ALT_INIT; mRNA.
EMBL; BC079636; AAH79636.1; -; mRNA.
CCDS; CCDS25341.1; -. [Q925J9-4]
CCDS; CCDS36300.1; -. [Q925J9-1]
PIR; T02885; T02885.
RefSeq; NP_001073587.1; NM_001080118.1. [Q925J9-1]
RefSeq; NP_038662.2; NM_013634.2. [Q925J9-4]
RefSeq; NP_598788.2; NM_134027.2. [Q925J9-3]
PDB; 1XDK; X-ray; 2.90 A; C/D/G/H=641-654.
PDBsum; 1XDK; -.
SMR; Q925J9; -.
BioGRID; 202318; 13.
ComplexPortal; CPX-3264; Core mediator complex.
CORUM; Q925J9; -.
DIP; DIP-59232N; -.
ELM; Q925J9; -.
IntAct; Q925J9; 10.
MINT; Q925J9; -.
STRING; 10090.ENSMUSP00000103169; -.
iPTMnet; Q925J9; -.
PhosphoSitePlus; Q925J9; -.
EPD; Q925J9; -.
jPOST; Q925J9; -.
MaxQB; Q925J9; -.
PaxDb; Q925J9; -.
PeptideAtlas; Q925J9; -.
PRIDE; Q925J9; -.
ProteomicsDB; 292184; -. [Q925J9-1]
ProteomicsDB; 292185; -. [Q925J9-2]
ProteomicsDB; 292186; -. [Q925J9-3]
ProteomicsDB; 292187; -. [Q925J9-4]
Antibodypedia; 4326; 518 antibodies from 38 providers.
DNASU; 19014; -.
Ensembl; ENSMUST00000018304; ENSMUSP00000018304; ENSMUSG00000018160. [Q925J9-4]
Ensembl; ENSMUST00000107545; ENSMUSP00000103169; ENSMUSG00000018160. [Q925J9-1]
GeneID; 19014; -.
KEGG; mmu:19014; -.
UCSC; uc007lfo.1; mouse. [Q925J9-3]
UCSC; uc007lfp.1; mouse. [Q925J9-1]
CTD; 5469; -.
MGI; MGI:1100846; Med1.
VEuPathDB; HostDB:ENSMUSG00000018160; -.
eggNOG; ENOG502QPZ7; Eukaryota.
GeneTree; ENSGT00660000095569; -.
HOGENOM; CLU_245015_0_0_1; -.
InParanoid; Q925J9; -.
OMA; SHEDDFH; -.
OrthoDB; 57581at2759; -.
PhylomeDB; Q925J9; -.
TreeFam; TF324954; -.
Reactome; R-MMU-212436; Generic Transcription Pathway.
Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
Reactome; R-MMU-400206; Regulation of lipid metabolism by PPARalpha.
Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
BioGRID-ORCS; 19014; 14 hits in 69 CRISPR screens.
ChiTaRS; Med1; mouse.
EvolutionaryTrace; Q925J9; -.
PRO; PR:Q925J9; -.
Proteomes; UP000000589; Chromosome 11.
RNAct; Q925J9; protein.
Bgee; ENSMUSG00000018160; Expressed in rostral migratory stream and 318 other tissues.
ExpressionAtlas; Q925J9; baseline and differential.
Genevisible; Q925J9; MM.
GO; GO:0000785; C:chromatin; ISO:MGI.
GO; GO:0070847; C:core mediator complex; IEA:Ensembl.
GO; GO:0016592; C:mediator complex; IDA:MGI.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0031490; F:chromatin DNA binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0030331; F:estrogen receptor binding; ISO:MGI.
GO; GO:0050693; F:LBD domain binding; ISO:MGI.
GO; GO:0016922; F:nuclear receptor binding; IPI:UniProtKB.
GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
GO; GO:0042975; F:peroxisome proliferator activated receptor binding; ISO:MGI.
GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI.
GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
GO; GO:0042974; F:retinoic acid receptor binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
GO; GO:0046966; F:thyroid hormone receptor binding; ISS:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
GO; GO:0001223; F:transcription coactivator binding; IEA:Ensembl.
GO; GO:0003712; F:transcription coregulator activity; ISS:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
GO; GO:0042809; F:vitamin D receptor binding; ISO:MGI.
GO; GO:0006702; P:androgen biosynthetic process; ISS:UniProtKB.
GO; GO:0001525; P:angiogenesis; IMP:BHF-UCL.
GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
GO; GO:0031100; P:animal organ regeneration; IMP:MGI.
GO; GO:0007420; P:brain development; IMP:MGI.
GO; GO:0043010; P:camera-type eye development; IMP:MGI.
GO; GO:0000902; P:cell morphogenesis; ISS:UniProtKB.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IMP:MGI.
GO; GO:0071383; P:cellular response to steroid hormone stimulus; ISO:MGI.
GO; GO:0097067; P:cellular response to thyroid hormone stimulus; ISO:MGI.
GO; GO:0035050; P:embryonic heart tube development; IMP:MGI.
GO; GO:0035162; P:embryonic hemopoiesis; IMP:MGI.
GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
GO; GO:0001892; P:embryonic placenta development; IMP:MGI.
GO; GO:0048822; P:enucleate erythrocyte development; IMP:MGI.
GO; GO:0060750; P:epithelial cell proliferation involved in mammary gland duct elongation; IMP:MGI.
GO; GO:0048821; P:erythrocyte development; IMP:BHF-UCL.
GO; GO:0045444; P:fat cell differentiation; IMP:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; ISS:UniProtKB.
GO; GO:0030216; P:keratinocyte differentiation; ISS:UniProtKB.
GO; GO:0007595; P:lactation; IMP:MGI.
GO; GO:0002088; P:lens development in camera-type eye; IMP:BHF-UCL.
GO; GO:0001889; P:liver development; IMP:MGI.
GO; GO:0060745; P:mammary gland branching involved in pregnancy; IMP:MGI.
GO; GO:0060744; P:mammary gland branching involved in thelarche; IMP:MGI.
GO; GO:0033598; P:mammary gland epithelial cell proliferation; IMP:MGI.
GO; GO:0035855; P:megakaryocyte development; IMP:BHF-UCL.
GO; GO:0030224; P:monocyte differentiation; IMP:MGI.
GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0010839; P:negative regulation of keratinocyte proliferation; ISS:UniProtKB.
GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; IMP:MGI.
GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
GO; GO:0070318; P:positive regulation of G0 to G1 transition; IMP:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
GO; GO:2000347; P:positive regulation of hepatocyte proliferation; IMP:MGI.
GO; GO:0060335; P:positive regulation of interferon-gamma-mediated signaling pathway; IMP:MGI.
GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IMP:MGI.
GO; GO:0045618; P:positive regulation of keratinocyte differentiation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0006606; P:protein import into nucleus; IMP:MGI.
GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
GO; GO:2001141; P:regulation of RNA biosynthetic process; ISS:UniProtKB.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0070562; P:regulation of vitamin D receptor signaling pathway; IMP:MGI.
GO; GO:0003406; P:retinal pigment epithelium development; IMP:BHF-UCL.
GO; GO:0006590; P:thyroid hormone generation; IMP:MGI.
GO; GO:0002154; P:thyroid hormone mediated signaling pathway; ISS:UniProtKB.
GO; GO:0006366; P:transcription by RNA polymerase II; TAS:MGI.
GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IMP:BHF-UCL.
DisProt; DP02151; -.
InterPro; IPR019680; Mediator_Med1.
Pfam; PF10744; Med1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Developmental protein; DNA-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Transcription; Transcription regulation.
CHAIN 1..1575
/note="Mediator of RNA polymerase II transcription subunit
1"
/id="PRO_0000058553"
REGION 1..670
/note="Interaction with the Mediator complex and THRA"
/evidence="ECO:0000250"
REGION 16..590
/note="Interaction with ESR1"
/evidence="ECO:0000250|UniProtKB:Q15648"
REGION 108..212
/note="Interaction with the Mediator complex"
/evidence="ECO:0000250"
REGION 215..390
/note="Interaction with the Mediator complex"
/evidence="ECO:0000250"
REGION 405..644
/note="Interaction with THRA"
/evidence="ECO:0000250"
REGION 542..789
/note="Interaction with VDR"
/evidence="ECO:0000250"
REGION 609..706
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 622..701
/note="Interaction with GATA1"
/evidence="ECO:0000269|PubMed:17132730"
REGION 622..701
/note="Interaction with PPARGC1A and THRA"
/evidence="ECO:0000250"
REGION 656..1066
/note="Interaction with ESR1"
/evidence="ECO:0000250"
REGION 737..760
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 791..818
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 874..895
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 951..1564
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1251..1423
/note="Interaction with TP53"
/evidence="ECO:0000250"
MOTIF 604..608
/note="LXXLL motif 1"
MOTIF 645..649
/note="LXXLL motif 2"
MOTIF 875..902
/note="Integrase domain-binding motif (IBM)"
/evidence="ECO:0000250|UniProtKB:Q15648"
COMPBIAS 652..680
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 742..756
/note="Pro residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 974..994
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 995..1020
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1021..1053
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1075..1199
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1221..1303
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1329..1350
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1351..1368
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1369..1390
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1428..1486
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1500..1514
/note="Basic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1525..1549
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 588
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q15648"
MOD_RES 664
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 795
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q15648"
MOD_RES 805
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 887
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q15648"
MOD_RES 953
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:17525332"
MOD_RES 955
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:17525332,
ECO:0007744|PubMed:21183079"
MOD_RES 1032
/note="Phosphothreonine; by MAPK1 or MAPK3"
/evidence="ECO:0000250|UniProtKB:Q15648"
MOD_RES 1051
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 1057
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 1158
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 1179
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:Q15648"
MOD_RES 1209
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 1217
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q15648"
MOD_RES 1225
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q15648"
MOD_RES 1304
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q15648"
MOD_RES 1349
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q15648"
MOD_RES 1405
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q15648"
MOD_RES 1435
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 1442
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 1459
/note="Phosphothreonine; by MAPK1 or MAPK3"
/evidence="ECO:0000250|UniProtKB:Q15648"
MOD_RES 1465
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 1467
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 1481
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 1483
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q15648"
MOD_RES 1484
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 1523
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:Q15648"
VAR_SEQ 1..15
/note="Missing (in isoform 4)"
/evidence="ECO:0000303|PubMed:11471062,
ECO:0000303|PubMed:9325263"
/id="VSP_051892"
VAR_SEQ 548..632
/note="YGMTTGNNPMSGTTTPTNTFPGGPITTLFNMSMSIKDRHESVGHGEDFSKVS
QNPILTSLLQITGNGGSTIGSSPTPPHHTPPPV -> VEEKRQDKPSLGHLPPIQVCSP
SCLKDGKDMKSTCTYLLLLLLLLEFMVFCFFFFFLTYSSVFGLHVKGLWTKICSDVQEY
FSVS (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_051893"
VAR_SEQ 548..556
/note="YGMTTGNNP -> SKNPELGSG (in isoform 3)"
/evidence="ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072"
/id="VSP_051894"
VAR_SEQ 557..1575
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072"
/id="VSP_051895"
VAR_SEQ 633..1575
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_051896"
VARIANT 960
/note="T -> S (in strain: ISS and 129/Ola)"
/evidence="ECO:0000269|PubMed:11471062,
ECO:0000269|PubMed:14500757"
VARIANT 1348
/note="T -> M (in strain: ISS and 129/Ola)"
/evidence="ECO:0000269|PubMed:11471062,
ECO:0000269|PubMed:14500757"
CONFLICT 84
/note="I -> L (in Ref. 1; AAC31118)"
/evidence="ECO:0000305"
CONFLICT 198
/note="A -> T (in Ref. 6; AAH21440)"
/evidence="ECO:0000305"
CONFLICT 211
/note="L -> H (in Ref. 4; BAE27757)"
/evidence="ECO:0000305"
CONFLICT 303
/note="F -> S (in Ref. 1; AAC31118)"
/evidence="ECO:0000305"
CONFLICT 382..389
/note="LPDGQSLQ -> VLPNKAVS (in Ref. 4; BAC35779)"
/evidence="ECO:0000305"
CONFLICT 948
/note="E -> K (in Ref. 4; BAC33607)"
/evidence="ECO:0000305"
CONFLICT 964
/note="G -> A (in Ref. 4; BAC33607)"
/evidence="ECO:0000305"
CONFLICT 1323
/note="G -> S (in Ref. 1; AAC31118)"
/evidence="ECO:0000305"
CONFLICT 1387
/note="G -> R (in Ref. 1; AAC31118)"
/evidence="ECO:0000305"
HELIX 643..649
/evidence="ECO:0007829|PDB:1XDK"
SEQUENCE 1575 AA; 167141 MW; C3B8121A26003A22 CRC64;
MKAQGETEDS ERLSKMSSLL ERLHAKFNQN RPWSETIKLV RQVMEKRVVM SSGGHQHLVS
CLETLQKALK VTSLPAMTDR LESIARQNGL GSHLSASGTE CYITSDMFYV EVQLDPAGQL
CDVKVAHHGE NPVSCPELVQ QLREKNFEEF SKHLKGLVNL YNLPGDNKLK TKMYLALQSL
EQDLSKMAIM YWKATNAAPL DKILHGSVGY LTPRSGGHLM NMKYYASPSD LLDDKTASPI
ILHEKNVPRS LGMNASVTIE GTSAMYKLPI APLIMGSHPA DNKWTPSFSA VTSANSVDLP
ACFFLKFPQP IPVSKAFVQK LQNCTGIPLF ETPPTYLPLY ELITQFELSK DPDPLPLNHN
MRFYAALPGQ QHCYFLNKDA PLPDGQSLQG TLVSKITFQH PGRVPLILNM 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 SSSGSPRMEM CSGSNKAKKK KSSRVPPDKP KHQTEDDFQR ELFSMDVDSQ
NPMFDVSMTA DALDTPHITP APSQCSTPPA TYPQPVSHPQ PSIQRMVRLS SSDSIGPDVT
DILSDIAEEA SKLPSTSDDC PPIGTPVRDS SSSGHSQSAL FDSDVFQTNN NENPYTDPAD
LIADAAGSPN SDSPTNHFFP DGVDFNPDLL NSQSQSGFGE EYFDESSQSG DNDDFKGFAS
QALNTLGMPM LGGDNGEPKF KGSSQADTVD FSIISVAGKA LGAADLMEHH SGSQSPLLTT
GELGKEKTQK RVKEGNGTGA SSGSGPGSDS KPGKRSRTPS NDGKSKDKPP KRKKADTEGK
SPSHSSSNRP FTPPTSTGGS KSPGSSGRSQ TPPGVATPPI PKITIQIPKG TVMVGKPSSH
SQYTSSGSVS SSGSKSHHSH SSSSSSLASA STSGKVKSSK SEGSSSSKLS GSMYASQGSS
GSSQSKNSSQ TGGKPGSSPI TKHGLSSGSS STKMKPQGKP SSLMNPSISK PNISPSHSRP
PGGSDKLASP MKPVPGTPPS SKAKSPISSG SSGSHVSGTS SSSGMKSSSG SASSGSVSQK
TPPASNSCTP SSSSFSSSGS SMSSSQNQHG SSKGKSPSRN KKPSLTAVID KLKHGVVTSG
PGGEDPIDSQ MGASTNSSNH PMSSKHNTSG GEFQSKREKS DKDKSKVSAS GGSVDSSKKT
SESKNVGSTG VAKIIISKHD GGSPSIKAKV TLQKPGESGG DGLRPQIASS KNYGSPLISG
STPKHERGSP SHSKSPAYTP QNVDSESESG SSIAERSYQN SPSSEDGIRP LPEYSTEKHK
KHKKEKKKVR DKDRDKKKSH SMKPENWSKS PISSDPTASV TNNPILSADR PSRLSPDFMI
GEEDDDLMDV ALIGN


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Pathways :
WP2292: Chemokine signaling pathway
WP2272: Pathogenic Escherichia coli infection
WP1694: Pyrimidine metabolism
WP1531: Vitamin D synthesis
WP1693: Purine metabolism
WP1663: Homologous recombination
WP1672: Mismatch repair
WP1644: DNA replication
WP1616: ABC transporters
WP1566: Citrate cycle (TCA cycle)
WP731: Sterol regulatory element binding protein related
WP1438: Influenza A virus infection
WP1692: Protein export
WP1713: Two-component system
WP1624: Bacterial secretion system
WP1654: gamma-Hexachlorocyclohexane degradation
WP1888: Post-translational protein modification
WP1493: Carbon assimilation C4 pathway
WP1690: Propanoate metabolism
WP211: BMP signaling pathway
WP1049: G Protein Signaling Pathways
WP1659: Glycine, serine and threonine metabolism
WP2371: Parkinsons Disease Pathway
WP931: G Protein Signaling Pathways
WP73: G Protein Signaling Pathways

Related Genes :
[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)
[Med1 Crsp210 Drip205 Pbp Pparbp Trap220 Trip2] Mediator of RNA polymerase II transcription subunit 1 (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)
[MED24 ARC100 CRSP4 DRIP100 KIAA0130 THRAP4 TRAP100] Mediator of RNA polymerase II transcription subunit 24 (Activator-recruited cofactor 100 kDa component) (ARC100) (Cofactor required for Sp1 transcriptional activation subunit 4) (CRSP complex subunit 4) (Mediator complex subunit 24) (Thyroid hormone receptor-associated protein 4) (Thyroid hormone receptor-associated protein complex 100 kDa component) (Trap100) (hTRAP100) (Vitamin D3 receptor-interacting protein complex 100 kDa component) (DRIP100)
[MED13 ARC250 KIAA0593 THRAP1 TRAP240] Mediator of RNA polymerase II transcription subunit 13 (Activator-recruited cofactor 250 kDa component) (ARC250) (Mediator complex subunit 13) (Thyroid hormone receptor-associated protein 1) (Thyroid hormone receptor-associated protein complex 240 kDa component) (Trap240) (Vitamin D3 receptor-interacting protein complex component DRIP250) (DRIP250)
[MED16 DRIP92 THRAP5] Mediator of RNA polymerase II transcription subunit 16 (Mediator complex subunit 16) (Thyroid hormone receptor-associated protein 5) (Thyroid hormone receptor-associated protein complex 95 kDa component) (Trap95) (Vitamin D3 receptor-interacting protein complex 92 kDa component) (DRIP92)
[MED17 ARC77 CRSP6 DRIP77 DRIP80 TRAP80] Mediator of RNA polymerase II transcription subunit 17 (Activator-recruited cofactor 77 kDa component) (ARC77) (Cofactor required for Sp1 transcriptional activation subunit 6) (CRSP complex subunit 6) (Mediator complex subunit 17) (Thyroid hormone receptor-associated protein complex 80 kDa component) (Trap80) (Transcriptional coactivator CRSP77) (Vitamin D3 receptor-interacting protein complex 80 kDa component) (DRIP80)
[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)
[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)
[Ncoa6 Aib3 Prip Rap250 Trbp] Nuclear receptor coactivator 6 (Activating signal cointegrator 2) (ASC-2) (Amplified in breast cancer protein 3) (Cancer-amplified transcriptional coactivator ASC-2) (Nuclear receptor coactivator RAP250) (NRC) (Nuclear receptor-activating protein, 250 kDa) (Peroxisome proliferator-activated receptor-interacting protein) (PPAR-interacting protein) (Thyroid hormone receptor-binding protein)
[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)
[Med30 Thrap6 Trap25] Mediator of RNA polymerase II transcription subunit 30 (Mediator complex subunit 30) (Thyroid hormone receptor-associated protein 6) (Thyroid hormone receptor-associated protein complex 25 kDa component) (Trap25)
[Ncoa6 Aib3 Rap250 Trbp] Nuclear receptor coactivator 6 (Activating signal cointegrator 2) (ASC-2) (Amplified in breast cancer protein 3) (Cancer-amplified transcriptional coactivator ASC-2) (Nuclear receptor coactivator RAP250) (NRC) (Nuclear receptor-activating protein, 250 kDa) (Peroxisome proliferator-activated receptor-interacting protein) (PPAR-interacting protein) (PRIP) (Thyroid hormone receptor-binding protein) (Fragment)
[MED13L KIAA1025 PROSIT240 THRAP2 TRAP240L] Mediator of RNA polymerase II transcription subunit 13-like (Mediator complex subunit 13-like) (Thyroid hormone receptor-associated protein 2) (Thyroid hormone receptor-associated protein complex 240 kDa component-like)
[Med17 Crsp6 Trap80] Mediator of RNA polymerase II transcription subunit 17 (Cofactor required for Sp1 transcriptional activation subunit 6) (CRSP complex subunit 6) (Mediator complex subunit 17) (Thyroid hormone receptor-associated protein complex 80 kDa component)
[MED4 ARC36 DRIP36 VDRIP HSPC126] Mediator of RNA polymerase II transcription subunit 4 (Activator-recruited cofactor 36 kDa component) (ARC36) (Mediator complex subunit 4) (TRAP/SMCC/PC2 subunit p36 subunit) (Vitamin D3 receptor-interacting protein complex 36 kDa component) (DRIP36)
[NCOA6 AIB3 KIAA0181 RAP250 TRBP] Nuclear receptor coactivator 6 (Activating signal cointegrator 2) (ASC-2) (Amplified in breast cancer protein 3) (Cancer-amplified transcriptional coactivator ASC-2) (Nuclear receptor coactivator RAP250) (NRC RAP250) (Nuclear receptor-activating protein, 250 kDa) (Peroxisome proliferator-activated receptor-interacting protein) (PPAR-interacting protein) (PRIP) (Thyroid hormone receptor-binding protein)
[Med24 D11Ertd307e Thrap4 Trap100] Mediator of RNA polymerase II transcription subunit 24 (Mediator complex subunit 24) (Thyroid hormone receptor-associated protein 4) (Thyroid hormone receptor-associated protein complex 100 kDa component) (Trap100) (mTRAP100)
[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)
[Med12 Kiaa0192 Mopa Tnrc11 Trap230] Mediator of RNA polymerase II transcription subunit 12 (Mediator complex subunit 12) (OPA-containing protein) (Thyroid hormone receptor-associated protein complex 230 kDa component) (Trap230) (Trinucleotide repeat-containing gene 11 protein)
[Cops2 Csn2 Trip15] COP9 signalosome complex subunit 2 (SGN2) (Signalosome subunit 2) (Alien homolog) (JAB1-containing signalosome subunit 2) (Thyroid receptor-interacting protein 15) (TR-interacting protein 15) (TRIP-15)
[Med14 Crsp2 Gm641 Trap170] Mediator of RNA polymerase II transcription subunit 14 (Cofactor required for Sp1 transcriptional activation subunit 2) (CRSP complex subunit 2) (Mediator complex subunit 14) (Thyroid hormone receptor-associated protein complex 170 kDa component) (Trap170)
[TRIP13 PCH2] Pachytene checkpoint protein 2 homolog (Human papillomavirus type 16 E1 protein-binding protein) (16E1-BP) (HPV16 E1 protein-binding protein) (Thyroid hormone receptor interactor 13) (Thyroid receptor-interacting protein 13) (TR-interacting protein 13) (TRIP-13)
[COPS2 CSN2 TRIP15] COP9 signalosome complex subunit 2 (SGN2) (Signalosome subunit 2) (Alien homolog) (JAB1-containing signalosome subunit 2) (Thyroid receptor-interacting protein 15) (TR-interacting protein 15) (TRIP-15)
[Cops2 Csn2 Trip15] COP9 signalosome complex subunit 2 (SGN2) (Signalosome subunit 2) (Alien homolog) (JAB1-containing signalosome subunit 2) (Thyroid receptor-interacting protein 15) (TR-interacting protein 15) (TRIP-15)
[med12 kto mot trap230] Mediator of RNA polymerase II transcription subunit 12 (Mediator complex subunit 12) (Protein kohtalo) (Protein motionless) (Thyroid hormone receptor-associated protein complex 230 kDa component) (Trap230)
[MED12L KIAA1635 TNRC11L TRALP TRALPUSH PRO0314] Mediator of RNA polymerase II transcription subunit 12-like protein (Mediator complex subunit 12-like protein) (Thyroid hormone receptor-associated-like protein) (Trinucleotide repeat-containing gene 11 protein-like)
[MED21 SRB7 SURB7] Mediator of RNA polymerase II transcription subunit 21 (Mediator complex subunit 21) (RNA polymerase II holoenzyme component SRB7) (RNAPII complex component SRB7) (hSrb7)
[TRIP11 CEV14] Thyroid receptor-interacting protein 11 (TR-interacting protein 11) (TRIP-11) (Clonal evolution-related gene on chromosome 14 protein) (Golgi-associated microtubule-binding protein 210) (GMAP-210) (Trip230)
[TRIP6 OIP1] Thyroid receptor-interacting protein 6 (TR-interacting protein 6) (TRIP-6) (Opa-interacting protein 1) (OIP-1) (Zyxin-related protein 1) (ZRP-1)
[Med13 Kiaa0593 Thrap1 Trap240] Mediator of RNA polymerase II transcription subunit 13 (Thyroid hormone receptor-associated protein 1) (Thyroid hormone receptor-associated protein complex 240 kDa component) (Trap240)

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