Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Mediator of RNA polymerase II transcription subunit 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)

 MED13_HUMAN             Reviewed;        2174 AA.
Q9UHV7; B2RU05; O60334;
22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 3.
25-OCT-2017, entry version 152.
RecName: Full=Mediator of RNA polymerase II transcription subunit 13;
AltName: Full=Activator-recruited cofactor 250 kDa component;
Short=ARC250;
AltName: Full=Mediator complex subunit 13;
AltName: Full=Thyroid hormone receptor-associated protein 1;
AltName: Full=Thyroid hormone receptor-associated protein complex 240 kDa component;
Short=Trap240;
AltName: Full=Vitamin D3 receptor-interacting protein complex component DRIP250;
Short=DRIP250;
Name=MED13; Synonyms=ARC250, KIAA0593, THRAP1, TRAP240;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 696-713, TISSUE
SPECIFICITY, AND IDENTIFICATION IN TRAP COMPLEX.
TISSUE=Cervix carcinoma;
PubMed=10198638; DOI=10.1016/S1097-2765(00)80463-3;
Ito M., Yuan C.-X., Malik S., Gu W., Fondell J.D., Yamamura S.,
Fu Z.-Y., Zhang X., Qin J., Roeder R.G.;
"Identity between TRAP and SMCC complexes indicates novel pathways for
the function of nuclear receptors and diverse mammalian activators.";
Mol. Cell 3:361-370(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 170-2174.
TISSUE=Brain;
PubMed=9628581; DOI=10.1093/dnares/5.1.31;
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
Ohara O.;
"Prediction of the coding sequences of unidentified human genes. IX.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:31-39(1998).
[6]
SEQUENCE REVISION.
Ohara O., Nagase T., Ishikawa K.;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[7]
PROTEIN SEQUENCE OF 1401-1408 AND 1358-1367, AND IDENTIFICATION IN ARC
COMPLEX.
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).
[8]
IDENTIFICATION IN ARC COMPLEX, AND PROTEIN SEQUENCE OF 1429-1438;
1772-1783 AND 2073-2084.
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).
[9]
IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR
COMPLEX, AND INTERACTION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE
II.
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).
[10]
INTERACTION WITH MED1; MED18; MED21; 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).
[11]
FUNCTION, AND INTERACTION WITH MED1 AND MED10.
PubMed=16595664; DOI=10.1074/jbc.M601983200;
Baek H.J., Kang Y.K., Roeder R.G.;
"Human Mediator enhances basal transcription by facilitating
recruitment of transcription factor IIB during preinitiation complex
assembly.";
J. Biol. Chem. 281:15172-15181(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500 AND SER-1029, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-504 AND SER-537, 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).
[14]
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).
[15]
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395; SER-504; SER-826
AND SER-890, 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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029, AND 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. {ECO:0000269|PubMed:16595664}.
-!- 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. {ECO:0000269|PubMed:10198638, ECO:0000269|PubMed:10235266,
ECO:0000269|PubMed:10235267, ECO:0000269|PubMed:15175163,
ECO:0000269|PubMed:15989967}.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10198638}.
-!- SIMILARITY: Belongs to the Mediator complex subunit 13 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD22032.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF117754; AAD22032.1; ALT_FRAME; mRNA.
EMBL; AC008158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC018628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC060798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471179; EAW51438.1; -; Genomic_DNA.
EMBL; BC140891; AAI40892.1; -; mRNA.
EMBL; AB011165; BAA25519.2; -; mRNA.
CCDS; CCDS42366.1; -.
PIR; T01238; T01238.
RefSeq; NP_005112.2; NM_005121.2.
UniGene; Hs.282678; -.
ProteinModelPortal; Q9UHV7; -.
BioGrid; 115294; 47.
CORUM; Q9UHV7; -.
DIP; DIP-31468N; -.
IntAct; Q9UHV7; 21.
MINT; MINT-4329245; -.
STRING; 9606.ENSP00000380888; -.
iPTMnet; Q9UHV7; -.
PhosphoSitePlus; Q9UHV7; -.
BioMuta; MED13; -.
DMDM; 317373421; -.
EPD; Q9UHV7; -.
MaxQB; Q9UHV7; -.
PaxDb; Q9UHV7; -.
PeptideAtlas; Q9UHV7; -.
PRIDE; Q9UHV7; -.
Ensembl; ENST00000397786; ENSP00000380888; ENSG00000108510.
GeneID; 9969; -.
KEGG; hsa:9969; -.
UCSC; uc002izo.3; human.
CTD; 9969; -.
DisGeNET; 9969; -.
EuPathDB; HostDB:ENSG00000108510.9; -.
GeneCards; MED13; -.
H-InvDB; HIX0014059; -.
HGNC; HGNC:22474; MED13.
HPA; HPA067939; -.
MIM; 603808; gene.
neXtProt; NX_Q9UHV7; -.
OpenTargets; ENSG00000108510; -.
PharmGKB; PA162395168; -.
eggNOG; KOG3600; Eukaryota.
eggNOG; ENOG410XPV2; LUCA.
GeneTree; ENSGT00390000013680; -.
HOGENOM; HOG000012893; -.
HOVERGEN; HBG058069; -.
InParanoid; Q9UHV7; -.
KO; K15164; -.
OMA; MGFSPMN; -.
OrthoDB; EOG091G006C; -.
PhylomeDB; Q9UHV7; -.
TreeFam; TF316867; -.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-212436; Generic Transcription Pathway.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
ChiTaRS; MED13; human.
GeneWiki; MED13; -.
GenomeRNAi; 9969; -.
PRO; PR:Q9UHV7; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108510; -.
CleanEx; HS_MED13; -.
ExpressionAtlas; Q9UHV7; baseline and differential.
Genevisible; Q9UHV7; HS.
GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; NAS:UniProtKB.
GO; GO:0004872; F:receptor activity; IDA:UniProtKB.
GO; GO:0001104; F:RNA polymerase II transcription cofactor activity; IDA:UniProtKB.
GO; GO:0046966; F:thyroid hormone receptor binding; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
GO; GO:0003712; F:transcription cofactor activity; IDA:UniProtKB.
GO; GO:0042809; F:vitamin D receptor binding; NAS:UniProtKB.
GO; GO:0030521; P:androgen receptor signaling pathway; IDA:UniProtKB.
GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IDA:UniProtKB.
GO; GO:1904168; P:negative regulation of thyroid hormone receptor activity; IEA:Ensembl.
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; IDA:UniProtKB.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0070328; P:triglyceride homeostasis; IEA:Ensembl.
InterPro; IPR009401; Mediator_Med13.
InterPro; IPR021643; Mediator_Med13_N_met/fun.
Pfam; PF06333; Med13_C; 1.
Pfam; PF11597; Med13_N; 1.
1: Evidence at protein level;
Activator; Complete proteome; Direct protein sequencing; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor;
Transcription; Transcription regulation.
CHAIN 1 2174 Mediator of RNA polymerase II
transcription subunit 13.
/FTId=PRO_0000065584.
MOTIF 1188 1192 LXXLL motif 1.
MOTIF 1279 1283 LXXLL motif 2.
COMPBIAS 1508 1573 Ser-rich.
MOD_RES 395 395 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 500 500 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 504 504 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 530 530 Phosphoserine.
{ECO:0000250|UniProtKB:Q5SWW4}.
MOD_RES 537 537 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 826 826 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 890 890 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1029 1029 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:24275569}.
VARIANT 1370 1370 A -> P (in dbSNP:rs34805963).
/FTId=VAR_057792.
VARIANT 1385 1385 A -> P (in dbSNP:rs35996128).
/FTId=VAR_057793.
CONFLICT 106 106 V -> M (in Ref. 1; AAD22032).
{ECO:0000305}.
CONFLICT 392 392 R -> K (in Ref. 1; AAD22032).
{ECO:0000305}.
CONFLICT 467 467 K -> E (in Ref. 1; AAD22032).
{ECO:0000305}.
CONFLICT 712 712 K -> A (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 800 800 K -> R (in Ref. 1; AAD22032).
{ECO:0000305}.
CONFLICT 930 930 P -> L (in Ref. 1; AAD22032).
{ECO:0000305}.
CONFLICT 984 984 F -> C (in Ref. 1; AAD22032).
{ECO:0000305}.
CONFLICT 1090 1090 F -> S (in Ref. 1; AAD22032).
{ECO:0000305}.
SEQUENCE 2174 AA; 239297 MW; 0FA54C84FE2C91E2 CRC64;
MSASFVPNGA SLEDCHCNLF CLADLTGIKW KKYVWQGPTS APILFPVTEE DPILSSFSRC
LKADVLGVWR RDQRPGRREL WIFWWGEDPS FADLIHHDLS EEEDGVWENG LSYECRTLLF
KAVHNLLERC LMNRNFVRIG KWFVKPYEKD EKPINKSEHL SCSFTFFLHG DSNVCTSVEI
NQHQPVYLLS EEHITLAQQS NSPFQVILCP FGLNGTLTGQ AFKMSDSATK KLIGEWKQFY
PISCCLKEMS EEKQEDMDWE DDSLAAVEVL VAGVRMIYPA CFVLVPQSDI PTPSPVGSTH
CSSSCLGVHQ VPASTRDPAM SSVTLTPPTS PEEVQTVDPQ SVQKWVKFSS VSDGFNSDST
SHHGGKIPRK LANHVVDRVW QECNMNRAQN KRKYSASSGG LCEEATAAKV ASWDFVEATQ
RTNCSCLRHK NLKSRNAGQQ GQAPSLGQQQ QILPKHKTNE KQEKSEKPQK RPLTPFHHRV
SVSDDVGMDA DSASQRLVIS APDSQVRFSN IRTNDVAKTP QMHGTEMANS PQPPPLSPHP
CDVVDEGVTK TPSTPQSQHF YQMPTPDPLV PSKPMEDRID SLSQSFPPQY QEAVEPTVYV
GTAVNLEEDE ANIAWKYYKF PKKKDVEFLP PQLPSDKFKD DPVGPFGQES VTSVTELMVQ
CKKPLKVSDE LVQQYQIKNQ CLSAIASDAE QEPKIDPYAF VEGDEEFLFP DKKDRQNSER
EAGKKHKVED GTSSVTVLSH EEDAMSLFSP SIKQDAPRPT SHARPPSTSL IYDSDLAVSY
TDLDNLFNSD EDELTPGSKK SANGSDDKAS CKESKTGNLD PLSCISTADL HKMYPTPPSL
EQHIMGFSPM NMNNKEYGSM DTTPGGTVLE GNSSSIGAQF KIEVDEGFCS PKPSEIKDFS
YVYKPENCQI LVGCSMFAPL KTLPSQYLPP IKLPEECIYR QSWTVGKLEL LSSGPSMPFI
KEGDGSNMDQ EYGTAYTPQT HTSFGMPPSS APPSNSGAGI LPSPSTPRFP TPRTPRTPRT
PRGAGGPASA QGSVKYENSD LYSPASTPST CRPLNSVEPA TVPSIPEAHS LYVNLILSES
VMNLFKDCNF DSCCICVCNM NIKGADVGVY IPDPTQEAQY RCTCGFSAVM NRKFGNNSGL
FLEDELDIIG RNTDCGKEAE KRFEALRATS AEHVNGGLKE SEKLSDDLIL LLQDQCTNLF
SPFGAADQDP FPKSGVISNW VRVEERDCCN DCYLALEHGR QFMDNMSGGK VDEALVKSSC
LHPWSKRNDV SMQCSQDILR MLLSLQPVLQ DAIQKKRTVR PWGVQGPLTW QQFHKMAGRG
SYGTDESPEP LPIPTFLLGY DYDYLVLSPF ALPYWERLML EPYGSQRDIA YVVLCPENEA
LLNGAKSFFR DLTAIYESCR LGQHRPVSRL LTDGIMRVGS TASKKLSEKL VAEWFSQAAD
GNNEAFSKLK LYAQVCRYDL GPYLASLPLD SSLLSQPNLV APTSQSLITP PQMTNTGNAN
TPSATLASAA SSTMTVTSGV AISTSVATAN STLTTASTSS SSSSNLNSGV SSNKLPSFPP
FGSMNSNAAG SMSTQANTVQ SGQLGGQQTS ALQTAGISGE SSSLPTQPHP DVSESTMDRD
KVGIPTDGDS HAVTYPPAIV VYIIDPFTYE NTDESTNSSS VWTLGLLRCF LEMVQTLPPH
IKSTVSVQII PCQYLLQPVK HEDREIYPQH LKSLAFSAFT QCRRPLPTST NVKTLTGFGP
GLAMETALRS PDRPECIRLY APPFILAPVK DKQTELGETF GEAGQKYNVL FVGYCLSHDQ
RWILASCTDL YGELLETCII NIDVPNRARR KKSSARKFGL QKLWEWCLGL VQMSSLPWRV
VIGRLGRIGH GELKDWSCLL SRRNLQSLSK RLKDMCRMCG ISAADSPSIL SACLVAMEPQ
GSFVIMPDSV STGSVFGRST TLNMQTSQLN TPQDTSCTHI LVFPTSASVQ VASATYTTEN
LDLAFNPNND GADGMGIFDL LDTGDDLDPD IINILPASPT GSPVHSPGSH YPHGGDAGKG
QSTDRLLSTE PHEEVPNILQ QPLALGYFVS TAKAGPLPDW FWSACPQAQY QCPLFLKASL
HLHVPSVQSD ELLHSKHSHP LDSNQTSDVL RFVLEQYNAL SWLTCDPATQ DRRSCLPIHF
VVLNQLYNFI MNML


Related products :

Catalog number Product name Quantity
18-003-42176 Thyroid hormone receptor-associated protein complex 95 kDa component - Trap95; Thyroid hormone receptor-associated protein 5; Vitamin D3 receptor-interacting protein complex component DRIP92 Polyclona 0.1 mg Protein A
28-735 MED21 belongs to the Mediator complex subunit 21 family. It is the component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent ge 0.05 mg
EIAAB43730 Homo sapiens,Human,THRAP3,Thyroid hormone receptor-associated protein 3,Thyroid hormone receptor-associated protein complex 150 kDa component,Trap150,TRAP150
EIAAB43729 Mouse,Mus musculus,Thrap3,Thyroid hormone receptor-associated protein 3,Thyroid hormone receptor-associated protein complex 150 kDa component,Trap150,Trap150
EIAAB43728 Rat,Rattus norvegicus,Thrap3,Thyroid hormone receptor-associated protein 3,Thyroid hormone receptor-associated protein complex 150 kDa component,Trap150,Trap150
ARP32301_T200 Anti-Thyroid hormone receptor-associated protein complex 95 kDa component(THRAP5) Species_Reactivity: Human
10-288-22355F RNA polymerase transcriptional regulation mediator. subunit 6 homolog - Activator-recruited cofactor 33 kDa component; ARC33; NY-REN-28 antigen 0.05 mg
10-288-22355F RNA polymerase transcriptional regulation mediator. subunit 6 homolog - Activator-recruited cofactor 33 kDa component; ARC33; NY-REN-28 antigen 0.1 mg
EIAAB08495 COG complex subunit 2,Cog2,Component of oligomeric Golgi complex 2,Conserved oligomeric Golgi complex subunit 2,Ldlc,Low density lipoprotein receptor defect C-complementing protein,Mouse,Mus musculus
EIAAB08492 COG complex subunit 1,Cog1,Component of oligomeric Golgi complex 1,Conserved oligomeric Golgi complex subunit 1,Ldlb,Low density lipoprotein receptor defect B-complementing protein,Mouse,Mus musculus
EIAAB08494 COG complex subunit 2,COG2,Component of oligomeric Golgi complex 2,Conserved oligomeric Golgi complex subunit 2,Homo sapiens,Human,LDLC,Low density lipoprotein receptor defect C-complementing protein
25-191 MED6 is a 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 0.05 mg
EIAAB35834 Calcitonin gene-related peptide-receptor component protein,CGRPRCP,CGRP-RCP,CGRP-receptor component protein,Crcp,DNA-directed RNA polymerase III subunit RPC9,Rat,Rattus norvegicus,RNA polymerase III s
EIAAB35835 Calcitonin gene-related peptide-receptor component protein,CGRPRCP,CGRP-RCP,CGRP-receptor component protein,Crcp,DNA-directed RNA polymerase III subunit RPC9,Mouse,Mus musculus,RNA polymerase III subu
EIAAB35836 Calcitonin gene-related peptide-receptor component protein,CGRPRCP,CGRP-RCP,CGRP-receptor component protein,CRCP,DNA-directed RNA polymerase III subunit RPC9,Homo sapiens,HsC17,Human,RNA polymerase II
EIAAB06530 CDK8,Cell division protein kinase 8,Cyclin-dependent kinase 8,Homo sapiens,Human,Mediator complex subunit CDK8,Mediator of RNA polymerase II transcription subunit CDK8,Protein kinase K35
30-917 FEM1B is a component of an E3 ubiquitin-protein ligase complex, in which it may act as a substrate recognition subunit. It involved in apoptosis by acting as a death receptor-associated protein that m 0.05 mg
EIAAB09602 Alien homolog,COP9 signalosome complex subunit 2,Cops2,Csn2,JAB1-containing signalosome subunit 2,Mouse,Mus musculus,SGN2,Signalosome subunit 2,Thyroid receptor-interacting protein 15,TR-interacting p
EIAAB06531 Cdk8,Cell division protein kinase 8,Cyclin-dependent kinase 8,Mediator complex subunit CDK8,Mediator of RNA polymerase II transcription subunit CDK8,Mouse,Mus musculus
EIAAB09601 Alien homolog,COP9 signalosome complex subunit 2,COPS2,CSN2,Homo sapiens,Human,JAB1-containing signalosome subunit 2,SGN2,Signalosome subunit 2,Thyroid receptor-interacting protein 15,TR-interacting p
18-001-30018 COP9 signalosome complex subunit 2 - Signalosome subunit 2; SGN2; JAB1-containing signalosome subunit 2; Thyroid receptor-interacting protein 15; Alien homolog Polyclonal 0.1 mg
18-003-43113 COP9 signalosome complex subunit 2 - Signalosome subunit 2; SGN2; JAB1-containing signalosome subunit 2; Thyroid receptor-interacting protein 15; Alien homolog Polyclonal 0.1 mg Protein A
18-003-43113 COP9 signalosome complex subunit 2 - Signalosome subunit 2; SGN2; JAB1-containing signalosome subunit 2; Thyroid receptor-interacting protein 15; Alien homolog Polyclonal 0.05 mg Aff Pur
EIAAB09600 Alien homolog,COP9 signalosome complex subunit 2,Cops2,Csn2,JAB1-containing signalosome subunit 2,Rat,Rattus norvegicus,SGN2,Signalosome subunit 2,Thyroid receptor-interacting protein 15,TR-interactin
EIAAB47949 HNF-4a coactivator,Homo sapiens,Human,Thyroid hormone receptor interactor 3,Thyroid receptor-interacting protein 3,TR-interacting protein 3,TRIP3,TRIP-3,Zinc finger HIT domain-containing protein 3,ZNH


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur