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Nuclear receptor coactivator 1 (NCoA-1) (EC 2.3.1.48) (Nuclear receptor coactivator protein 1) (mNRC-1) (Steroid receptor coactivator 1) (SRC-1)

 NCOA1_MOUSE             Reviewed;        1447 AA.
P70365; P70366; Q61202; Q66JL7; Q8CBI9;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 2.
13-NOV-2019, entry version 190.
RecName: Full=Nuclear receptor coactivator 1;
Short=NCoA-1;
EC=2.3.1.48;
AltName: Full=Nuclear receptor coactivator protein 1;
Short=mNRC-1;
AltName: Full=Steroid receptor coactivator 1;
Short=SRC-1;
Name=Ncoa1; Synonyms=Src1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND INTERACTION WITH
EP300 AND CREBBP.
PubMed=8616895; DOI=10.1016/s0092-8674(00)81118-6;
Kamei Y., Xu L., Heinzel T., Torchia J., Kurokawa R., Gloss B.,
Lin S.-C., Heyman R.A., Rose D.W., Glass C.K., Rosenfeld M.G.;
"A CBP integrator complex mediates transcriptional activation and AP-1
inhibition by nuclear receptors.";
Cell 85:403-414(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9041124;
Zhu Y., Qi C., Calandra C., Rao M.S., Reddy J.K.;
"Cloning and identification of mouse steroid receptor coactivator-1
(mSRC-1), as a coactivator of peroxisome proliferator-activated
receptor gamma.";
Gene Expr. 6:185-195(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND INTERACTION WITH EP300 AND RAR.
PubMed=8855229; DOI=10.1073/pnas.93.20.10626;
Yao T.-P., Ku G., Zhou N., Scully R., Livingston D.M.;
"The nuclear hormone receptor coactivator SRC-1 is a specific target
of p300.";
Proc. Natl. Acad. Sci. U.S.A. 93:10626-10631(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 MRNA] (ISOFORMS 2 AND 4).
STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 21-33, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[7]
ROLE OF LXXLL MOTIFS, TISSUE SPECIFICITY, AND MUTAGENESIS OF
695-HIS--LEU-698 AND 756-ARG--LEU-759.
PubMed=9192892; DOI=10.1038/42652;
Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K.,
Rosenfeld M.G.;
"The transcriptional co-activator p/CIP binds CBP and mediates
nuclear-receptor function.";
Nature 387:677-684(1997).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=9506940; DOI=10.1126/science.279.5358.1922;
Xu J., Qiu Y., DeMayo F.J., Tsai S.Y., Tsai M.-J., O'Malley B.W.;
"Partial hormone resistance in mice with disruption of the steroid
receptor coactivator-1 (SRC-1) gene.";
Science 279:1922-1925(1998).
[9]
INTERACTION WITH CARM1.
PubMed=10381882; DOI=10.1126/science.284.5423.2174;
Chen D., Ma H., Hong H., Koh S.S., Huang S.-M., Schurter B.T.,
Aswad D.W., Stallcup M.R.;
"Regulation of transcription by a protein methyltransferase.";
Science 284:2174-2177(1999).
[10]
FUNCTION.
PubMed=12507421; DOI=10.1016/s0092-8674(02)01169-8;
Picard F., Gehin M., Annicotte J.-S., Rocchi S., Champy M.-F.,
O'Malley B.W., Chambon P., Auwerx J.;
"SRC-1 and TIF2 control energy balance between white and brown adipose
tissues.";
Cell 111:931-941(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 AS COACTIVATOR, AND INTERACTION WITH RORC.
PubMed=16148126; DOI=10.4049/jimmunol.175.6.3800;
Xie H., Sadim M.S., Sun Z.;
"RORgammat recruits steroid receptor coactivators to ensure thymocyte
survival.";
J. Immunol. 175:3800-3809(2005).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-372 AND SER-702,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-559, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Lung, Pancreas, and Spleen;
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).
[15]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1079; ARG-1097; ARG-1130 AND
ARG-1137, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.o113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[16]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 257-385 IN COMPLEX WITH
STAT6.
PubMed=14757047; DOI=10.1016/j.jmb.2003.12.057;
Razeto A., Ramakrishnan V., Litterst C.M., Giller K., Griesinger C.,
Carlomagno T., Lakomek N., Heimburg T., Lodrini M., Pfitzner E.,
Becker S.;
"Structure of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif
of the STAT6 transactivation domain.";
J. Mol. Biol. 336:319-329(2004).
-!- FUNCTION: Nuclear receptor coactivator that directly binds nuclear
receptors and stimulates the transcriptional activities in a
hormone-dependent fashion. Involved in the coactivation of
different nuclear receptors, such as for steroids (PGR, GR and
ER), retinoids (RXRs), thyroid hormone (TRs) and prostanoids
(PPARs). Also involved in coactivation mediated by STAT3, STAT5A,
STAT5B and STAT6 transcription factors. Displays histone
acetyltransferase activity toward H3 and H4; the relevance of such
activity remains however unclear. Plays a central role in creating
multisubunit coactivator complexes that act via remodeling of
chromatin, and possibly acts by participating in both chromatin
remodeling and recruitment of general transcription factors.
Required with NCOA2 to control energy balance between white and
brown adipose tissues. Required for mediating steroid hormone
response. Isoform 2 has a higher thyroid hormone-dependent
transactivation activity than isoform 1 and isoform 3.
{ECO:0000269|PubMed:12507421, ECO:0000269|PubMed:16148126,
ECO:0000269|PubMed:8616895, ECO:0000269|PubMed:9506940}.
-!- CATALYTIC ACTIVITY:
Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-
acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-
COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378,
ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
ChEBI:CHEBI:61930; EC=2.3.1.48;
-!- SUBUNIT: Interacts with NCOA6 and NCOA2. Interacts with the FDL
motif of STAT5A and STAT5B. Interacts with the LXXLL motif of
STAT6. Interacts with STAT3 following IL-6 stimulation. Interacts
with the basal transcription factor GTF2B. Interacts with COPS5,
NR3C1, PCAF and TTLL5/STAMP. Interacts with the histone
acetyltransferases EP300 and CREBBP, and the methyltransferase
CARM1. Interacts with PSMB9. Interacts with UBE2L3; they
functionally interact to regulate progesterone receptor
transcriptional activity. Interacts with PRMT2 and DDX5. Interacts
with ASXL1. Interacts with PRMT6. Interacts (via LXXLL 1, 2 and 3
motifs) with RORC (via AF-2 motif). Interacts in a ligand-
dependent fashion with RXRA. Interacts with TRIP4. Interacts with
NR4A3 (PubMed:12709428). Interacts with VDR (By similarity).
{ECO:0000250|UniProtKB:Q15788, ECO:0000269|PubMed:10381882,
ECO:0000269|PubMed:12709428, ECO:0000269|PubMed:14757047,
ECO:0000269|PubMed:16148126, ECO:0000269|PubMed:8616895,
ECO:0000269|PubMed:8855229}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00981, ECO:0000269|PubMed:8855229}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=SRC-1A, SRC1a;
IsoId=P70365-1; Sequence=Displayed;
Name=2; Synonyms=SRC-1E, SRC1e;
IsoId=P70365-2; Sequence=VSP_011740;
Name=3;
IsoId=P70365-3; Sequence=VSP_011741;
Note=No experimental confirmation available.;
Name=4;
IsoId=P70365-4; Sequence=VSP_027855, VSP_027856;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8855229,
ECO:0000269|PubMed:9192892}.
-!- DOMAIN: The C-terminal (1113-1447) part mediates the histone
acetyltransferase (HAT) activity. {ECO:0000250}.
-!- DOMAIN: Contains 7 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. LXXLL
motifs 3, 4 and 5 are essential for the association with nuclear
receptors. LXXLL motif 7, which is not present in isoform 2,
increases the affinity for steroid receptors in vitro.
-!- PTM: Sumoylated; sumoylation increases its interaction with PGR
and prolongs its retention in the nucleus. It does not prevent its
ubiquitination and does not exert a clear effect on the stability
of the protein (By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated; leading to proteasome-mediated degradation.
Ubiquitination and sumoylation take place at different sites (By
similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice show partial hormone resistance: target
organs such as uterus, prostate, testis and mammary gland
exhibiting decreased growth and development in response to steroid
hormones. Moreover, such mice are prone to obesity due to reduced
energy expenditure. {ECO:0000269|PubMed:9506940}.
-!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator
family. {ECO:0000305}.
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EMBL; U56920; AAB01228.1; -; mRNA.
EMBL; U64606; AAB06177.1; -; mRNA.
EMBL; U64828; AAB38841.1; -; mRNA.
EMBL; AK035922; BAC29244.1; -; mRNA.
EMBL; BC068177; AAH68177.1; -; mRNA.
EMBL; BC080866; AAH80866.1; -; mRNA.
CCDS; CCDS25789.1; -. [P70365-2]
RefSeq; NP_035011.1; NM_010881.2. [P70365-2]
RefSeq; XP_006515068.1; XM_006515005.3. [P70365-1]
RefSeq; XP_006515069.1; XM_006515006.3. [P70365-1]
RefSeq; XP_006515070.1; XM_006515007.3. [P70365-1]
RefSeq; XP_011242143.1; XM_011243841.2. [P70365-2]
PDB; 1OJ5; X-ray; 2.20 A; A=257-385.
PDB; 2O9I; X-ray; 2.80 A; C/D=686-700.
PDB; 4DMA; X-ray; 2.30 A; E/F=690-704.
PDB; 5NWX; X-ray; 2.51 A; A=257-385.
PDB; 5Y7W; X-ray; 2.25 A; A/B=257-367.
PDBsum; 1OJ5; -.
PDBsum; 2O9I; -.
PDBsum; 4DMA; -.
PDBsum; 5NWX; -.
PDBsum; 5Y7W; -.
SMR; P70365; -.
BioGrid; 201707; 11.
ComplexPortal; CPX-864; PPARgamma-NCOA1 activated nuclear receptor complex.
CORUM; P70365; -.
IntAct; P70365; 3.
MINT; P70365; -.
STRING; 10090.ENSMUSP00000082971; -.
iPTMnet; P70365; -.
PhosphoSitePlus; P70365; -.
jPOST; P70365; -.
MaxQB; P70365; -.
PaxDb; P70365; -.
PeptideAtlas; P70365; -.
PRIDE; P70365; -.
Ensembl; ENSMUST00000085814; ENSMUSP00000082971; ENSMUSG00000020647. [P70365-2]
Ensembl; ENSMUST00000217794; ENSMUSP00000151716; ENSMUSG00000020647. [P70365-4]
Ensembl; ENSMUST00000220434; ENSMUSP00000151358; ENSMUSG00000020647. [P70365-1]
GeneID; 17977; -.
KEGG; mmu:17977; -.
UCSC; uc007mxr.2; mouse. [P70365-1]
UCSC; uc007mxs.2; mouse. [P70365-2]
CTD; 8648; -.
MGI; MGI:1276523; Ncoa1.
eggNOG; ENOG410IQ5S; Eukaryota.
eggNOG; ENOG410XPF9; LUCA.
GeneTree; ENSGT00950000183021; -.
HOGENOM; HOG000230947; -.
InParanoid; P70365; -.
KO; K09101; -.
OMA; MTHGTAI; -.
OrthoDB; 59971at2759; -.
PhylomeDB; P70365; -.
TreeFam; TF332652; -.
Reactome; R-MMU-159418; Recycling of bile acids and salts.
Reactome; R-MMU-192105; Synthesis of bile acids and bile salts.
Reactome; R-MMU-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-MMU-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
Reactome; R-MMU-211976; Endogenous sterols.
Reactome; R-MMU-3214847; HATs acetylate histones.
Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
Reactome; R-MMU-400206; Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
Reactome; R-MMU-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
Reactome; R-MMU-9623433; NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis.
ChiTaRS; Ncoa1; mouse.
EvolutionaryTrace; P70365; -.
PRO; PR:P70365; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000020647; Expressed in 302 organ(s), highest expression level in rostral migratory stream.
ExpressionAtlas; P70365; baseline and differential.
Genevisible; P70365; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0017162; F:aryl hydrocarbon receptor binding; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0030331; F:estrogen receptor binding; ISO:MGI.
GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0035257; F:nuclear hormone receptor binding; ISO:MGI.
GO; GO:0016922; F:nuclear receptor binding; ISO:MGI.
GO; GO:0030374; F:nuclear receptor transcription coactivator activity; ISO:MGI.
GO; GO:0033142; F:progesterone receptor binding; ISO:MGI.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0042974; F:retinoic acid receptor binding; ISO:MGI.
GO; GO:0046965; F:retinoid X receptor binding; ISO:MGI.
GO; GO:0001012; F:RNA polymerase II regulatory region DNA binding; ISO:MGI.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0032870; P:cellular response to hormone stimulus; ISO:MGI.
GO; GO:1904017; P:cellular response to Thyroglobulin triiodothyronine; IGI:MGI.
GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0044849; P:estrous cycle; IEA:Ensembl.
GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
GO; GO:0043967; P:histone H4 acetylation; IMP:UniProtKB.
GO; GO:0021854; P:hypothalamus development; IEA:Ensembl.
GO; GO:0060713; P:labyrinthine layer morphogenesis; IGI:MGI.
GO; GO:0007595; P:lactation; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0060179; P:male mating behavior; ISO:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0045925; P:positive regulation of female receptivity; ISO:MGI.
GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0000435; P:positive regulation of transcription from RNA polymerase II promoter by galactose; IMP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:2001038; P:regulation of cellular response to drug; IMP:UniProtKB.
GO; GO:2001141; P:regulation of RNA biosynthetic process; IMP:UniProtKB.
GO; GO:0002155; P:regulation of thyroid hormone mediated signaling pathway; IGI:MGI.
GO; GO:0032355; P:response to estradiol; ISO:MGI.
GO; GO:0032570; P:response to progesterone; ISO:MGI.
GO; GO:0032526; P:response to retinoic acid; ISO:MGI.
GO; GO:0006351; P:transcription, DNA-templated; ISO:MGI.
CDD; cd00083; HLH; 1.
CDD; cd00130; PAS; 1.
Gene3D; 1.10.287.1070; -; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR010011; DUF1518.
InterPro; IPR036638; HLH_DNA-bd_sf.
InterPro; IPR028819; NCOA1.
InterPro; IPR009110; Nuc_rcpt_coact.
InterPro; IPR014920; Nuc_rcpt_coact_Ncoa-typ.
InterPro; IPR037077; Nuc_rcpt_coact_Ncoa_int_sf.
InterPro; IPR017426; Nuclear_rcpt_coactivator.
InterPro; IPR000014; PAS.
InterPro; IPR035965; PAS-like_dom_sf.
InterPro; IPR013767; PAS_fold.
InterPro; IPR014935; SRC/p160_LXXLL.
PANTHER; PTHR10684; PTHR10684; 1.
PANTHER; PTHR10684:SF1; PTHR10684:SF1; 1.
Pfam; PF07469; DUF1518; 2.
Pfam; PF00010; HLH; 1.
Pfam; PF08815; Nuc_rec_co-act; 1.
Pfam; PF00989; PAS; 1.
Pfam; PF08832; SRC-1; 1.
PIRSF; PIRSF038181; Nuclear_receptor_coactivator; 1.
SMART; SM01151; DUF1518; 2.
SMART; SM00353; HLH; 1.
SMART; SM00091; PAS; 1.
SUPFAM; SSF47459; SSF47459; 1.
SUPFAM; SSF55785; SSF55785; 2.
SUPFAM; SSF69125; SSF69125; 1.
PROSITE; PS50888; BHLH; 1.
PROSITE; PS50112; PAS; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Acyltransferase;
Alternative splicing; Complete proteome; Direct protein sequencing;
Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Transcription; Transcription regulation;
Transferase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q15788}.
CHAIN 2 1447 Nuclear receptor coactivator 1.
/FTId=PRO_0000094401.
DOMAIN 23 80 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
DOMAIN 109 180 PAS. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
REGION 361 568 Interaction with STAT3.
REGION 787 994 Interaction with CREBBP.
{ECO:0000269|PubMed:8616895}.
MOTIF 46 50 LXXLL motif 1.
MOTIF 112 116 LXXLL motif 2.
MOTIF 637 641 LXXLL motif 3.
MOTIF 694 698 LXXLL motif 4.
MOTIF 755 759 LXXLL motif 5.
MOTIF 919 923 LXXLL motif 6.
MOTIF 1441 1445 LXXLL motif 7.
COMPBIAS 389 686 Ser-rich.
COMPBIAS 1059 1144 Gln-rich.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q15788}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 372 372 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 395 395 Phosphoserine.
{ECO:0000250|UniProtKB:Q15788}.
MOD_RES 518 518 Phosphoserine.
{ECO:0000250|UniProtKB:Q15788}.
MOD_RES 559 559 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 570 570 Phosphoserine.
{ECO:0000250|UniProtKB:Q15788}.
MOD_RES 702 702 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 1039 1039 Phosphoserine.
{ECO:0000250|UniProtKB:Q15788}.
MOD_RES 1079 1079 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1097 1097 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1130 1130 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1137 1137 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1185 1185 Phosphothreonine.
{ECO:0000250|UniProtKB:Q15788}.
MOD_RES 1191 1191 Phosphoserine.
{ECO:0000250|UniProtKB:Q15788}.
MOD_RES 1378 1378 Phosphoserine.
{ECO:0000250|UniProtKB:Q15788}.
CROSSLNK 738 738 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 780 780 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 852 852 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q15788}.
VAR_SEQ 1300 1376 NVFSQAVQSQPAPAQPGVYNNMSITVSMAGGNANIQNMNPM
MGQMQMSSLQMPGMNTVCSEQMNDPALRHTGLYCNQ -> K
WKRKHSEHESNDGPDANELSADARDEYCVL (in
isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_027855.
VAR_SEQ 1377 1447 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_027856.
VAR_SEQ 1392 1447 QVQQVQVFADVQCTVNLVGGDPYLNQPGPLGTQKPTSGPQT
PQAQQKSLLQQLLTE -> DKKTEEFFSVVTTD (in
isoform 2). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8616895,
ECO:0000303|PubMed:8855229}.
/FTId=VSP_011740.
VAR_SEQ 1392 1447 QVQQVQVFADVQCTVNLVGGDPYLNQPGPLGTQKPTSGPQT
PQAQQKSLLQQLLTE -> VSKKDNPSAELADSITLDTWRT
SHGIC (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_011741.
MUTAGEN 695 698 HRLL->AAAA: Abolishes the interactions
with estrogen and retinoid-acids
receptors. {ECO:0000269|PubMed:9192892}.
MUTAGEN 756 759 RYLL->AAAA: Abolishes the interactions
with estrogen and retinoid-acids
receptors. {ECO:0000269|PubMed:9192892}.
CONFLICT 45 45 E -> G (in Ref. 1; AAB01228).
{ECO:0000305}.
CONFLICT 223 223 C -> R (in Ref. 2; AAB06177).
{ECO:0000305}.
CONFLICT 234 234 E -> G (in Ref. 2; AAB06177).
{ECO:0000305}.
CONFLICT 237 237 E -> K (in Ref. 5; AAH80866).
{ECO:0000305}.
CONFLICT 465 466 SS -> TT (in Ref. 1; AAB01228).
{ECO:0000305}.
CONFLICT 699 699 Q -> P (in Ref. 2; AAB06177).
{ECO:0000305}.
CONFLICT 1115 1115 L -> M (in Ref. 4; BAC29244).
{ECO:0000305}.
CONFLICT 1130 1130 R -> K (in Ref. 1; AAB01228).
{ECO:0000305}.
CONFLICT 1137 1138 RA -> KP (in Ref. 1; AAB01228).
{ECO:0000305}.
CONFLICT 1142 1142 R -> K (in Ref. 1; AAB01228).
{ECO:0000305}.
CONFLICT 1162 1162 T -> D (in Ref. 1; AAB01228).
{ECO:0000305}.
CONFLICT 1164 1164 R -> S (in Ref. 2; AAB06177).
{ECO:0000305}.
CONFLICT 1166 1166 P -> L (in Ref. 1; AAB01228).
{ECO:0000305}.
STRAND 261 266 {ECO:0000244|PDB:1OJ5}.
STRAND 272 276 {ECO:0000244|PDB:1OJ5}.
HELIX 278 281 {ECO:0000244|PDB:1OJ5}.
HELIX 288 299 {ECO:0000244|PDB:1OJ5}.
HELIX 309 320 {ECO:0000244|PDB:1OJ5}.
STRAND 321 324 {ECO:0000244|PDB:1OJ5}.
STRAND 328 331 {ECO:0000244|PDB:1OJ5}.
STRAND 337 347 {ECO:0000244|PDB:1OJ5}.
STRAND 357 365 {ECO:0000244|PDB:1OJ5}.
TURN 687 690 {ECO:0000244|PDB:2O9I}.
HELIX 693 699 {ECO:0000244|PDB:4DMA}.
SEQUENCE 1447 AA; 157016 MW; 65C08AFFCF14241D CRC64;
MSGLGDSSSD PANPDSHKRK GSPCDTLASS TEKRRREQEN KYLEELAELL SANISDIDSL
SVKPDKCKIL KKTVDQIQLM KRMEQEKSTT DDDVQKSDIS SSSQGVIEKE SLGPLLLEAL
DGFFFVVNCE GRIVFVSENV TSYLGYNQEE LMNTSVYSIL HVGDHAEFVK NLLPKSLVNG
VPWPQEATRR NSHTFNCRML IHPPEDPGTE NQEACQRYEV MQCFTVSQPK SIQEDGEDFQ
SCLICIARRL PRPPAITGVE SFMTKQDTTG KIISIDTSSL RAAGRTGWED LVRKCIYAFF
QPQGREPSYA RQLFQEVMTR GTASSPSYRF ILNDGTMLSA HTKCKLCYPQ SPDMQPFIMG
IHIIDREHSG LSPQDDSNSG MSIPRINPSV NPGISPAHGV TRSSTLPPSN NNMVSARVNR
QQSSDLNSSS SHTNSSNNQG NFGCSPGNQI VANVALNQGQ AGSQSSNPSL NLNNSPMEGT
GIALSQFMSP RRQANSGLAT RARMSNNSFP PNIPTLSSPV GITSGACNNN NRSYSNIPVT
SLQGMNEGPN NSVGFSAGSP VLRQMSSQNS PSRLSMQPAK AESKDSKEIA SILNEMIQSD
NSDNSANEGK PLDSGLLHNN DRLSEGDSKY SQTSHKLVQL LTTTAEQQLR HADIDTSCKD
VLSCTGTSSS ASSNPSGGTC PSSHSSLTER HKILHRLLQE GSPSDITTLS VEPEKKDSVP
ASTAVSVSGQ SQGSASIKLE LDAAKKKESK DHQLLRYLLD KDEKDLRSTP NLCLDDVKVK
VEKKEQMDPC NTNPTPMTKP APEEVKLESQ SQFTADLDQF DQLLPTLEKA AQLPSLCETD
RMDGAVTGVS IKAEVLPASL QPTTARAAPR LSRLPELELE AIDNQFGQPG AGDQIPWANN
TLTTINQNKP EDQCISSQLD ELLCPPTTVE GRNDEKALLE QLVSFLSGKD ETELAELDRA
LGIDKLVQGG GLDVLSERFP PQQATPPLMM EDRPTLYSQP YSSPSPTAGL SGPFQGMVRQ
KPSLGAMPVQ VTPPRGTFSP NMGMQPRQTL NRPPAAPNQL RLQLQQRLQG QQQLMHQNRQ
AILNQFAANA PVGMNMRSGM QQQITPQPPL NAQMLAQRQR ELYSQQHRQR QIIQQQRAML
MRHQSFGNNI PPSSGLPVQM GTPRLPQGAP QQFPYPPNYG TNPGTPPAST SPFSQLAANP
EASLATRSSM VNRGMAGNMG GQFGAGISPQ MQQNVFQYPG PGLVPQGEAT FAPSLSPGSS
MVPMPVPPPQ SSLLQQTPPT SGYQSPDMKA WQQGTMGNNN VFSQAVQSQP APAQPGVYNN
MSITVSMAGG NANIQNMNPM MGQMQMSSLQ MPGMNTVCSE QMNDPALRHT GLYCNQLSST
DLLKTDADGN QQVQQVQVFA DVQCTVNLVG GDPYLNQPGP LGTQKPTSGP QTPQAQQKSL
LQQLLTE


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[NCOA3 AIB1 BHLHE42 RAC3 TRAM1] Nuclear receptor coactivator 3 (NCoA-3) (EC 2.3.1.48) (ACTR) (Amplified in breast cancer 1 protein) (AIB-1) (CBP-interacting protein) (pCIP) (Class E basic helix-loop-helix protein 42) (bHLHe42) (Receptor-associated coactivator 3) (RAC-3) (Steroid receptor coactivator protein 3) (SRC-3) (Thyroid hormone receptor activator molecule 1) (TRAM-1)
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[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)
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[Rorc Nr1f3 Rorg Thor] Nuclear receptor ROR-gamma (Nuclear receptor RZR-gamma) (Nuclear receptor subfamily 1 group F member 3) (RAR-related orphan receptor C) (Retinoid-related orphan receptor-gamma) (Thymus orphan receptor) (TOR)
[Nr2c1 Tr2 Tr2-11] Nuclear receptor subfamily 2 group C member 1 (Orphan nuclear receptor TR2) (Testicular receptor 2) (mTR2)
[Nr2c2 Mtr2r1 Tak1 Tr4] Nuclear receptor subfamily 2 group C member 2 (Orphan nuclear receptor TAK1) (Orphan nuclear receptor TR4) (Testicular receptor 4)
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[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)
[Rxra Nr2b1] Retinoic acid receptor RXR-alpha (Nuclear receptor subfamily 2 group B member 1) (Retinoid X receptor alpha)
[NR5A1 AD4BP FTZF1 SF1] Steroidogenic factor 1 (SF-1) (STF-1) (hSF-1) (Adrenal 4-binding protein) (Fushi tarazu factor homolog 1) (Nuclear receptor subfamily 5 group A member 1) (Steroid hormone receptor Ad4BP)
[RXRA NR2B1] Retinoic acid receptor RXR-alpha (Nuclear receptor subfamily 2 group B member 1) (Retinoid X receptor alpha)
[Rora Nr1f1 Rzra] Nuclear receptor ROR-alpha (Nuclear receptor RZR-alpha) (Nuclear receptor subfamily 1 group F member 1) (RAR-related orphan receptor A) (Retinoid-related orphan receptor-alpha)
[Esr1 Esr Estr Estra Nr3a1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[Carm1 Prmt4] Histone-arginine methyltransferase CARM1 (EC 2.1.1.319) (Coactivator-associated arginine methyltransferase 1) (Protein arginine N-methyltransferase 4)
[ESRRA ERR1 ESRL1 NR3B1] Steroid hormone receptor ERR1 (Estrogen receptor-like 1) (Estrogen-related receptor alpha) (ERR-alpha) (Nuclear receptor subfamily 3 group B member 1)
[Esr1 Esr Estr Nr3a1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[VDR NR1I1] Vitamin D3 receptor (VDR) (1,25-dihydroxyvitamin D3 receptor) (Nuclear receptor subfamily 1 group I member 1)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[THRB ERBA2 NR1A2 THR1] Thyroid hormone receptor beta (Nuclear receptor subfamily 1 group A member 2) (c-erbA-2) (c-erbA-beta)
[NR1H4 BAR FXR HRR1 RIP14] Bile acid receptor (Farnesoid X-activated receptor) (Farnesol receptor HRR-1) (Nuclear receptor subfamily 1 group H member 4) (Retinoid X receptor-interacting protein 14) (RXR-interacting protein 14)
[RORA NR1F1 RZRA] Nuclear receptor ROR-alpha (Nuclear receptor RZR-alpha) (Nuclear receptor subfamily 1 group F member 1) (RAR-related orphan receptor A) (Retinoid-related orphan receptor-alpha)
[RORC NR1F3 RORG RZRG] Nuclear receptor ROR-gamma (Nuclear receptor RZR-gamma) (Nuclear receptor subfamily 1 group F member 3) (RAR-related orphan receptor C) (Retinoid-related orphan receptor-gamma)
[RARA NR1B1] Retinoic acid receptor alpha (RAR-alpha) (Nuclear receptor subfamily 1 group B member 1)

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