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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.
25-OCT-2017, entry version 137.
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.
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.
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).
{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;
Note=No experimental confirmation available. {ECO:0000305};
Name=2 {ECO:0000303|PubMed:15489334};
IsoId=Q925J9-2; Sequence=VSP_051893, VSP_051896;
Note=No experimental confirmation available. {ECO:0000305};
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 E9.5-10.5, expression is strongest in
neural tissues. At E11.5-E12.5, 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 E13.5-E14.5, 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 E9.5-E13.5. {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.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the Mediator complex subunit 1 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH21440.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; 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; CAM21264.1; -; Genomic_DNA.
EMBL; AL591205; CAM21266.1; -; 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]
UniGene; Mm.12926; -.
PDB; 1XDK; X-ray; 2.90 A; C/D/G/H=641-654.
PDBsum; 1XDK; -.
ProteinModelPortal; Q925J9; -.
SMR; Q925J9; -.
BioGrid; 202318; 5.
CORUM; Q925J9; -.
DIP; DIP-59232N; -.
ELM; Q925J9; -.
IntAct; Q925J9; 10.
MINT; MINT-4123213; -.
STRING; 10090.ENSMUSP00000103169; -.
iPTMnet; Q925J9; -.
PhosphoSitePlus; Q925J9; -.
EPD; Q925J9; -.
PaxDb; Q925J9; -.
PeptideAtlas; Q925J9; -.
PRIDE; Q925J9; -.
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.
eggNOG; ENOG410IEFR; Eukaryota.
eggNOG; ENOG410XR2E; LUCA.
GeneTree; ENSGT00660000095569; -.
HOVERGEN; HBG101127; -.
InParanoid; Q925J9; -.
KO; K15144; -.
OMA; HPMLMNL; -.
OrthoDB; EOG091G035E; -.
PhylomeDB; Q925J9; -.
TreeFam; TF324954; -.
Reactome; R-MMU-212436; Generic Transcription Pathway.
Reactome; R-MMU-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
Reactome; R-MMU-400206; Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
Reactome; R-MMU-442533; Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
EvolutionaryTrace; Q925J9; -.
PRO; PR:Q925J9; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000018160; -.
CleanEx; MM_MED1; -.
ExpressionAtlas; Q925J9; baseline and differential.
Genevisible; Q925J9; MM.
GO; GO:0000785; C:chromatin; IEA:Ensembl.
GO; GO:0016592; C:mediator complex; IDA:MGI.
GO; GO:0016020; C:membrane; ISO: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; IEA:Ensembl.
GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
GO; GO:0001047; F:core promoter binding; IDA: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:ligand-dependent nuclear receptor binding; ISO:MGI.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; ISS:UniProtKB.
GO; GO:0036033; F:mediator complex binding; ISO:MGI.
GO; GO:0035257; F:nuclear hormone receptor binding; IPI:UniProtKB.
GO; GO:0042975; F:peroxisome proliferator activated receptor binding; ISO:MGI.
GO; GO:0032403; F:protein complex binding; IDA:MGI.
GO; GO:0004872; F:receptor activity; ISS:UniProtKB.
GO; GO:0042974; F:retinoic acid receptor binding; ISO:MGI.
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; ISS:UniProtKB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IMP:UniProtKB.
GO; GO:0046966; F:thyroid hormone receptor binding; ISS:UniProtKB.
GO; GO:0030375; F:thyroid hormone receptor coactivator activity; ISO:MGI.
GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
GO; GO:0003712; F:transcription cofactor activity; ISO:MGI.
GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
GO; GO:0042809; F:vitamin D receptor binding; ISO:MGI.
GO; GO:0006702; P:androgen biosynthetic process; ISS:UniProtKB.
GO; GO:0030521; P:androgen receptor signaling pathway; 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:0070371; P:ERK1 and ERK2 cascade; ISO: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 from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IMP:MGI.
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 from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; IMP:MGI.
GO; GO:0008284; P:positive regulation of cell 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:0033601; P:positive regulation of mammary gland epithelial cell proliferation; IMP:MGI.
GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; IMP:MGI.
GO; GO:2000273; P:positive regulation of receptor activity; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:2001141; P:regulation of RNA biosynthetic process; ISS:UniProtKB.
GO; GO:0006356; P:regulation of transcription from RNA polymerase I promoter; ISS:UniProtKB.
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 from RNA polymerase II promoter; IC:MGI.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IMP:BHF-UCL.
InterPro; IPR019680; Mediator_Med1.
Pfam; PF10744; Med1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Complete proteome; Developmental protein; DNA-binding; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Transcription;
Transcription regulation.
CHAIN 1 1575 Mediator of RNA polymerase II
transcription subunit 1.
/FTId=PRO_0000058553.
REGION 1 670 Interaction with the Mediator complex and
THRA. {ECO:0000250}.
REGION 16 590 Interaction with ESR1. {ECO:0000250}.
REGION 108 212 Interaction with the Mediator complex.
{ECO:0000250}.
REGION 215 390 Interaction with the Mediator complex.
{ECO:0000250}.
REGION 405 644 Interaction with THRA. {ECO:0000250}.
REGION 542 789 Interaction with VDR. {ECO:0000250}.
REGION 622 701 Interaction with GATA1.
{ECO:0000269|PubMed:17132730}.
REGION 622 701 Interaction with PPARGC1A and THRA.
{ECO:0000250}.
REGION 656 1066 Interaction with ESR1. {ECO:0000250}.
REGION 1251 1423 Interaction with TP53. {ECO:0000250}.
MOTIF 604 608 LXXLL motif 1.
MOTIF 645 649 LXXLL motif 2.
COMPBIAS 1078 1484 Ser-rich. {ECO:0000255}.
COMPBIAS 1498 1523 Lys-rich. {ECO:0000255}.
MOD_RES 588 588 Phosphoserine.
{ECO:0000250|UniProtKB:Q15648}.
MOD_RES 664 664 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 795 795 Phosphoserine.
{ECO:0000250|UniProtKB:Q15648}.
MOD_RES 805 805 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 953 953 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 955 955 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:21183079}.
MOD_RES 1032 1032 Phosphothreonine; by MAPK1 or MAPK3.
{ECO:0000250|UniProtKB:Q15648}.
MOD_RES 1051 1051 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1057 1057 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1158 1158 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1179 1179 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q15648}.
MOD_RES 1209 1209 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1217 1217 Phosphothreonine.
{ECO:0000250|UniProtKB:Q15648}.
MOD_RES 1225 1225 Phosphoserine.
{ECO:0000250|UniProtKB:Q15648}.
MOD_RES 1304 1304 Phosphoserine.
{ECO:0000250|UniProtKB:Q15648}.
MOD_RES 1349 1349 Phosphoserine.
{ECO:0000250|UniProtKB:Q15648}.
MOD_RES 1405 1405 Phosphoserine.
{ECO:0000250|UniProtKB:Q15648}.
MOD_RES 1435 1435 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1442 1442 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1459 1459 Phosphothreonine; by MAPK1 or MAPK3.
{ECO:0000250|UniProtKB:Q15648}.
MOD_RES 1465 1465 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1467 1467 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1481 1481 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1483 1483 Phosphoserine.
{ECO:0000250|UniProtKB:Q15648}.
MOD_RES 1484 1484 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1523 1523 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q15648}.
VAR_SEQ 1 15 Missing (in isoform 4).
{ECO:0000303|PubMed:11471062,
ECO:0000303|PubMed:9325263}.
/FTId=VSP_051892.
VAR_SEQ 548 632 YGMTTGNNPMSGTTTPTNTFPGGPITTLFNMSMSIKDRHES
VGHGEDFSKVSQNPILTSLLQITGNGGSTIGSSPTPPHHTP
PPV -> VEEKRQDKPSLGHLPPIQVCSPSCLKDGKDMKST
CTYLLLLLLLLEFMVFCFFFFFLTYSSVFGLHVKGLWTKIC
SDVQEYFSVS (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_051893.
VAR_SEQ 548 556 YGMTTGNNP -> SKNPELGSG (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_051894.
VAR_SEQ 557 1575 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_051895.
VAR_SEQ 633 1575 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_051896.
VARIANT 960 960 T -> S (in strain: ISS and 129/Ola).
{ECO:0000269|PubMed:11471062,
ECO:0000269|PubMed:14500757}.
VARIANT 1348 1348 T -> M (in strain: ISS and 129/Ola).
{ECO:0000269|PubMed:11471062,
ECO:0000269|PubMed:14500757}.
CONFLICT 84 84 I -> L (in Ref. 1; AAC31118).
{ECO:0000305}.
CONFLICT 198 198 A -> T (in Ref. 6; AAH21440).
{ECO:0000305}.
CONFLICT 211 211 L -> H (in Ref. 4; BAE27757).
{ECO:0000305}.
CONFLICT 303 303 F -> S (in Ref. 1; AAC31118).
{ECO:0000305}.
CONFLICT 382 389 LPDGQSLQ -> VLPNKAVS (in Ref. 4;
BAC35779). {ECO:0000305}.
CONFLICT 948 948 E -> K (in Ref. 4; BAC33607).
{ECO:0000305}.
CONFLICT 964 964 G -> A (in Ref. 4; BAC33607).
{ECO:0000305}.
CONFLICT 1323 1323 G -> S (in Ref. 1; AAC31118).
{ECO:0000305}.
CONFLICT 1387 1387 G -> R (in Ref. 1; AAC31118).
{ECO:0000305}.
HELIX 643 649 {ECO:0000244|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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