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Nuclear receptor coactivator 2 (NCoA-2) (Class E basic helix-loop-helix protein 75) (bHLHe75) (Transcriptional intermediary factor 2) (hTIF2)

 NCOA2_HUMAN             Reviewed;        1464 AA.
Q15596; Q14CD2;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 2.
22-NOV-2017, entry version 198.
RecName: Full=Nuclear receptor coactivator 2;
Short=NCoA-2;
AltName: Full=Class E basic helix-loop-helix protein 75;
Short=bHLHe75;
AltName: Full=Transcriptional intermediary factor 2;
Short=hTIF2;
Name=NCOA2; Synonyms=BHLHE75, SRC2, TIF2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=8670870;
Voegel J.J., Heine M.J.S., Zechel C., Chambon P., Gronemeyer H.;
"TIF2, a 160 kDa transcriptional mediator for the ligand-dependent
activation function AF-2 of nuclear receptors.";
EMBO J. 15:3667-3675(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-1282.
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 870-939, AND CHROMOSOMAL TRANSLOCATION
WITH KAT6A.
PubMed=9558366;
Carapeti M., Aguiar R.C.T., Goldman J.M., Cross N.C.P.;
"A novel fusion between MOZ and the nuclear receptor coactivator TIF2
in acute myeloid leukemia.";
Blood 91:3127-3133(1998).
[4]
FUNCTION, INTERACTION WITH CREBBP; ESR1; RARA AND RXRA, DOMAIN, AND
MUTAGENESIS OF 644-LEU-LEU-645; 693-LEU-LEU-694; 748-LEU-LEU-749;
1079-LEU--LEU-1083 AND 1081-ASP-GLN-1082.
PubMed=9430642; DOI=10.1093/emboj/17.2.507;
Voegel J.J., Heine M.J.S., Tini M., Vivat V., Chambon P.,
Gronemeyer H.;
"The coactivator TIF2 contains three nuclear receptor-binding motifs
and mediates transactivation through CBP binding-dependent and
-independent pathways.";
EMBO J. 17:507-519(1998).
[5]
INTERACTION WITH NR3C1.
PubMed=9590696; DOI=10.1038/30032;
Fryer C.J., Archer T.K.;
"Chromatin remodelling by the glucocorticoid receptor requires the
BRG1 complex.";
Nature 393:88-91(1998).
[6]
INTERACTION WITH RORA.
PubMed=10478845; DOI=10.1210/mend.13.9.0343;
Atkins G.B., Hu X., Guenther M.G., Rachez C., Freedman L.P.,
Lazar M.A.;
"Coactivators for the orphan nuclear receptor RORalpha.";
Mol. Endocrinol. 13:1550-1557(1999).
[7]
INTERACTION WITH HIF1A; NCOA1 AND APEX.
PubMed=10594042; DOI=10.1128/MCB.20.1.402-415.2000;
Carrero P., Okamoto K., Coumailleau P., O'Brien S., Tanaka H.,
Poellinger L.;
"Redox-regulated recruitment of the transcriptional coactivators CREB-
binding protein and SRC-1 to hypoxia-inducible factor 1alpha.";
Mol. Cell. Biol. 20:402-415(2000).
[8]
INTERACTION WITH DDX5.
PubMed=11250900; DOI=10.1093/emboj/20.6.1341;
Watanabe M., Yanagisawa J., Kitagawa H., Takeyama K., Ogawa S.,
Arao Y., Suzawa M., Kobayashi Y., Yano T., Yoshikawa H., Masuhiro Y.,
Kato S.;
"A subfamily of RNA-binding DEAD-box proteins acts as an estrogen
receptor alpha coactivator through the N-terminal activation domain
(AF-1) with an RNA coactivator, SRA.";
EMBO J. 20:1341-1352(2001).
[9]
IDENTIFICATION IN A COACTIVATOR COMPLEX CONTAINING CREBBP; NCOA3;
IKKA; IKKB AND IKBKG.
PubMed=11971985; DOI=10.1128/MCB.22.10.3549-3561.2002;
Wu R.-C., Qin J., Hashimoto Y., Wong J., Xu J., Tsai S.Y., Tsai M.-J.,
O'Malley B.W.;
"Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator
activity by I kappa B kinase.";
Mol. Cell. Biol. 22:3549-3561(2002).
[10]
CHROMOSOMAL TRANSLOCATION WITH KAT6A.
PubMed=12676584; DOI=10.1016/S1535-6108(03)00051-5;
Deguchi K., Ayton P.M., Carapeti M., Kutok J.L., Snyder C.S.,
Williams I.R., Cross N.C.P., Glass C.K., Cleary M.L., Gilliland D.G.;
"MOZ-TIF2-induced acute myeloid leukemia requires the MOZ nucleosome
binding motif and TIF2-mediated recruitment of CBP.";
Cancer Cell 3:259-271(2003).
[11]
CHROMOSOMAL TRANSLOCATION WITH KAT6A.
PubMed=15657427; DOI=10.1128/MCB.25.3.988-1002.2005;
Kindle K.B., Troke P.J.F., Collins H.M., Matsuda S., Bossi D.,
Bellodi C., Kalkhoven E., Salomoni P., Pelicci P.G., Minucci S.,
Heery D.M.;
"MOZ-TIF2 inhibits transcription by nuclear receptors and p53 by
impairment of CBP function.";
Mol. Cell. Biol. 25:988-1002(2005).
[12]
INTERACTION WITH PSMB9.
PubMed=16957778; DOI=10.1038/sj.emboj.7601306;
Zhang H., Sun L., Liang J., Yu W., Zhang Y., Wang Y., Chen Y., Li R.,
Sun X., Shang Y.;
"The catalytic subunit of the proteasome is engaged in the entire
process of estrogen receptor-regulated transcription.";
EMBO J. 25:4223-4233(2006).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[14]
INTERACTION WITH TTLL5.
TISSUE=Testis;
PubMed=17116691; DOI=10.1128/MCB.01360-06;
He Y., Simons S.S. Jr.;
"STAMP, a novel predicted factor assisting TIF2 actions in
glucocorticoid receptor-mediated induction and repression.";
Mol. Cell. Biol. 27:1467-1485(2007).
[15]
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).
[16]
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).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[18]
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).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-640; LYS-780 AND LYS-785,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487; SER-493 AND
SER-499, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-493; SER-565;
SER-682; SER-699; SER-736 AND SER-771, 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).
[23]
FUNCTION, AND INTERACTION WITH RWDD3 AND NR3C1.
PubMed=23508108; DOI=10.1128/MCB.01470-12;
Druker J., Liberman A.C., Antunica-Noguerol M., Gerez J.,
Paez-Pereda M., Rein T., Iniguez-Lluhi J.A., Holsboer F., Arzt E.;
"RSUME enhances glucocorticoid receptor SUMOylation and
transcriptional activity.";
Mol. Cell. Biol. 33:2116-2127(2013).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493; SER-554; SER-565
AND SER-699, 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).
[25]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1173; ARG-1177; ARG-1190;
ARG-1196; ARG-1203; ARG-1221; ARG-1261 AND ARG-1266, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
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).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-785, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-239; LYS-648; LYS-705;
LYS-731; LYS-785 AND LYS-1454, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Transcriptional coactivator for steroid receptors and
nuclear receptors. Coactivator of the steroid binding domain (AF-
2) but not of the modulating N-terminal domain (AF-1). Required
with NCOA1 to control energy balance between white and brown
adipose tissues. Critical regulator of glucose metabolism
regulation, acts as RORA coactivator to specifically modulate G6PC
expression. Involved in the positive regulation of the
transcriptional activity of the glucocorticoid receptor NR3C1 by
sumoylation enhancer RWDD3. Positively regulates the circadian
clock by acting as a transcriptional coactivator for the CLOCK-
ARNTL/BMAL1 heterodimer (By similarity).
{ECO:0000250|UniProtKB:Q61026, ECO:0000269|PubMed:23508108,
ECO:0000269|PubMed:9430642}.
-!- SUBUNIT: Present in a complex containing NCOA3, IKKA, IKKB, IKBKG
and CREBBP. Interacts (via C-terminus) with CREBBP. Interacts with
ESR1, HIF1A, NCOA1, APEX, NR3C1, NR3C2, CARM1, RARA, and RXRA.
Present in a complex containing CARM1 and EP300/P300. Interacts
with CASP8AP2 and TTLL5/STAMP. Interacts with PSMB9 and DDX5.
Interacts (via LXXLL 1, 2 and 3 motifs) with RORA and RORC (via
AF-2 motif). Interacts with RWDD3. Interacts with CLOCK and
ARNTL/BMAL1 (By similarity). Interacts with NR4A3; potentiates the
activity of the NR4A3 (By similarity).
{ECO:0000250|UniProtKB:Q61026, ECO:0000269|PubMed:10478845,
ECO:0000269|PubMed:10594042, ECO:0000269|PubMed:11250900,
ECO:0000269|PubMed:11971985, ECO:0000269|PubMed:16957778,
ECO:0000269|PubMed:17116691, ECO:0000269|PubMed:23508108,
ECO:0000269|PubMed:9430642, ECO:0000269|PubMed:9590696}.
-!- INTERACTION:
P10275:AR; NbExp=2; IntAct=EBI-81236, EBI-608057;
Q92841:DDX17; NbExp=2; IntAct=EBI-81236, EBI-746012;
P03372:ESR1; NbExp=8; IntAct=EBI-81236, EBI-78473;
O00482-1:NR5A2; NbExp=2; IntAct=EBI-81236, EBI-15960777;
P19793:RXRA; NbExp=5; IntAct=EBI-81236, EBI-78598;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- DOMAIN: Contains four Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. The
LXXLL motifs are essential for the association with nuclear
receptors and are, at least in part, functionally redundant.
{ECO:0000269|PubMed:9430642}.
-!- DOMAIN: The LLXXLXXXL motif is involved in transcriptional
coactivation and CREBBP/CBP binding. {ECO:0000269|PubMed:9430642}.
-!- DOMAIN: Contains 2 C-terminal transcription activation domains
(AD1 and AD2) that can function independently.
{ECO:0000269|PubMed:9430642}.
-!- DISEASE: Note=Chromosomal aberrations involving NCOA2 may be a
cause of acute myeloid leukemias. Inversion inv(8)(p11;q13)
generates the KAT6A-NCOA2 oncogene, which consists of the N-
terminal part of KAT6A and the C-terminal part of NCOA2/TIF2.
KAT6A-NCOA2 binds to CREBBP and disrupts its function in
transcription activation. {ECO:0000269|PubMed:12676584,
ECO:0000269|PubMed:15657427, ECO:0000269|PubMed:9558366}.
-!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator
family. {ECO:0000305}.
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EMBL; X97674; CAA66263.1; -; mRNA.
EMBL; BC114383; AAI14384.1; -; mRNA.
CCDS; CCDS47872.1; -.
RefSeq; NP_001308632.1; NM_001321703.1.
RefSeq; NP_001308636.1; NM_001321707.1.
RefSeq; NP_001308640.1; NM_001321711.1.
RefSeq; NP_001308641.1; NM_001321712.1.
RefSeq; NP_001308642.1; NM_001321713.1.
RefSeq; NP_006531.1; NM_006540.3.
UniGene; Hs.446678; -.
UniGene; Hs.595378; -.
PDB; 1GWQ; X-ray; 2.45 A; C/D=688-696.
PDB; 1GWR; X-ray; 2.40 A; C/D=742-750.
PDB; 1M2Z; X-ray; 2.50 A; B/E=734-754.
PDB; 1MV9; X-ray; 1.90 A; B=686-698.
PDB; 1MVC; X-ray; 1.90 A; B=686-698.
PDB; 1MZN; X-ray; 1.90 A; B/D/F/H=686-698.
PDB; 1P93; X-ray; 2.70 A; E/F/G/H=740-751.
PDB; 1T63; X-ray; 2.07 A; B=740-753.
PDB; 1T65; X-ray; 1.66 A; B=686-698.
PDB; 1UHL; X-ray; 2.90 A; C/D=687-696.
PDB; 1YOK; X-ray; 2.50 A; B/C=740-753.
PDB; 1ZDT; X-ray; 2.10 A; P/Q=741-752.
PDB; 1ZDU; X-ray; 2.50 A; P/Q=741-751.
PDB; 1ZKY; X-ray; 2.25 A; C/D=686-698.
PDB; 2AO6; X-ray; 1.89 A; B=740-753.
PDB; 2B1V; X-ray; 1.80 A; C/D=686-698.
PDB; 2B1Z; X-ray; 1.78 A; C/D=686-698.
PDB; 2B23; X-ray; 2.10 A; C/D=686-698.
PDB; 2FAI; X-ray; 2.10 A; C/D=686-698.
PDB; 2G44; X-ray; 2.65 A; C/D=686-698.
PDB; 2G5O; X-ray; 2.30 A; C/D=686-698.
PDB; 2LDC; NMR; -; A=687-697.
PDB; 2P15; X-ray; 1.94 A; C/D=686-698.
PDB; 2P1T; X-ray; 1.80 A; B=686-698.
PDB; 2P1U; X-ray; 2.20 A; B=686-698.
PDB; 2P1V; X-ray; 2.20 A; B=686-698.
PDB; 2Q7J; X-ray; 1.90 A; B=740-753.
PDB; 2Q7L; X-ray; 1.92 A; B=740-753.
PDB; 2YJD; X-ray; 1.93 A; C/D=687-697.
PDB; 2ZXZ; X-ray; 3.00 A; B=686-698.
PDB; 2ZY0; X-ray; 2.90 A; B/D=686-698.
PDB; 3A9E; X-ray; 2.75 A; I=686-698.
PDB; 3CLD; X-ray; 2.84 A; C/H=740-751.
PDB; 3DZU; X-ray; 3.20 A; E/G=685-697.
PDB; 3DZY; X-ray; 3.10 A; E/G=685-697.
PDB; 3E00; X-ray; 3.10 A; E/G=685-697.
PDB; 3E7C; X-ray; 2.15 A; D/H=741-751.
PDB; 3E94; X-ray; 1.90 A; B=686-698.
PDB; 3ERD; X-ray; 2.03 A; C/D=686-698.
PDB; 3FUG; X-ray; 2.00 A; B=686-698.
PDB; 3GN8; X-ray; 2.50 A; C/E=734-754.
PDB; 3K22; X-ray; 2.10 A; D/H=740-751.
PDB; 3K23; X-ray; 3.00 A; D/E/F=740-751.
PDB; 3KWY; X-ray; 2.30 A; B=686-698.
PDB; 3KYT; X-ray; 2.35 A; C=686-697.
PDB; 3L0E; X-ray; 2.30 A; B=740-751.
PDB; 3L0J; X-ray; 2.40 A; C=688-697.
PDB; 3L0L; X-ray; 1.74 A; C/E=685-697.
PDB; 3O1D; X-ray; 2.40 A; B=686-698.
PDB; 3O1E; X-ray; 2.50 A; B=686-698.
PDB; 3OAP; X-ray; 2.05 A; B=686-696.
PDB; 3OZJ; X-ray; 2.10 A; B/D=686-696.
PDB; 3PCU; X-ray; 2.00 A; B=687-696.
PDB; 3PLZ; X-ray; 1.75 A; C/D=740-753.
PDB; 3Q95; X-ray; 2.05 A; C/D=686-698.
PDB; 3R5M; X-ray; 2.80 A; B/D=687-696.
PDB; 3UP0; X-ray; 1.60 A; P/Q=740-753.
PDB; 3UP3; X-ray; 1.25 A; P=741-754.
PDB; 4CSJ; X-ray; 2.30 A; B=741-753.
PDB; 4DOS; X-ray; 2.00 A; B/C=740-753.
PDB; 4E2J; X-ray; 2.50 A; C/E=741-752.
PDB; 4FHH; X-ray; 2.33 A; B=686-698.
PDB; 4FHI; X-ray; 2.40 A; B=686-698.
PDB; 4IA1; X-ray; 2.44 A; B=686-698.
PDB; 4IA2; X-ray; 2.95 A; B=686-698.
PDB; 4IA3; X-ray; 2.70 A; B=686-698.
PDB; 4IA7; X-ray; 2.70 A; B=686-698.
PDB; 4IQR; X-ray; 2.90 A; I/J/K/L=685-697.
PDB; 4IU7; X-ray; 2.29 A; C/D=687-696.
PDB; 4IUI; X-ray; 2.30 A; C/D=687-696.
PDB; 4IV2; X-ray; 2.14 A; C/D=687-696.
PDB; 4IV4; X-ray; 2.30 A; C/D=687-696.
PDB; 4IVW; X-ray; 2.06 A; C/D=687-696.
PDB; 4IVY; X-ray; 1.95 A; C/D=687-696.
PDB; 4IW6; X-ray; 1.98 A; C/D=687-696.
PDB; 4IW8; X-ray; 2.04 A; C/D=687-696.
PDB; 4IWC; X-ray; 2.24 A; C/D=687-696.
PDB; 4IWF; X-ray; 1.93 A; C/D=687-696.
PDB; 4K4J; X-ray; 2.00 A; B=686-698.
PDB; 4K6I; X-ray; 2.10 A; B=686-698.
PDB; 4M8E; X-ray; 2.40 A; B=686-696.
PDB; 4M8H; X-ray; 2.20 A; B=686-696.
PDB; 4NIE; X-ray; 2.01 A; C/D=686-697.
PDB; 4NQA; X-ray; 3.10 A; C/D/J/K=686-698.
PDB; 4OC7; X-ray; 2.50 A; B=686-698.
PDB; 4P6W; X-ray; 1.95 A; B=741-752.
PDB; 4P6X; X-ray; 2.50 A; B/D/F/H/J/L=740-753.
PDB; 4PLD; X-ray; 1.75 A; B=740-753.
PDB; 4PLE; X-ray; 1.75 A; B/D/F/H=740-753.
PDB; 4POH; X-ray; 2.30 A; B=686-698.
PDB; 4POJ; X-ray; 2.00 A; B=686-698.
PDB; 4PP3; X-ray; 2.00 A; B=686-698.
PDB; 4PP5; X-ray; 2.00 A; B=686-698.
PDB; 4PP6; X-ray; 2.20 A; C/D=688-696.
PDB; 4PPP; X-ray; 2.69 A; C/D=688-696.
PDB; 4PPS; X-ray; 1.93 A; C/D=687-698.
PDB; 4PXM; X-ray; 1.90 A; C/D=686-698.
PDB; 4Q0A; X-ray; 1.90 A; D=687-695.
PDB; 4Q13; X-ray; 2.24 A; C/D=686-698.
PDB; 4QE6; X-ray; 1.65 A; B=740-752.
PDB; 4QE8; X-ray; 2.62 A; C/D=740-752.
PDB; 4RFW; X-ray; 2.40 A; G=686-698.
PDB; 4RMC; X-ray; 2.70 A; B=686-698.
PDB; 4RMD; X-ray; 1.90 A; B=686-698.
PDB; 4RME; X-ray; 2.30 A; B=686-698.
PDB; 4RUO; X-ray; 2.81 A; B=686-698.
PDB; 4UDC; X-ray; 2.50 A; B=740-753.
PDB; 4UDD; X-ray; 1.80 A; B=740-753.
PDB; 4WG0; X-ray; 1.82 A; A/B/C/D/E/F/G/H/I/J/K/L/M=742-752.
PDB; 4ZN7; X-ray; 1.93 A; C/D=686-698.
PDB; 4ZN9; X-ray; 2.21 A; C/D=686-698.
PDB; 4ZNH; X-ray; 1.93 A; C/D=686-698.
PDB; 4ZNS; X-ray; 1.86 A; C/D=686-698.
PDB; 4ZNT; X-ray; 1.90 A; C/D=686-698.
PDB; 4ZNU; X-ray; 2.40 A; C/D=686-698.
PDB; 4ZNV; X-ray; 1.77 A; C/D=686-698.
PDB; 4ZNW; X-ray; 2.31 A; C/D=686-698.
PDB; 4ZO1; X-ray; 3.22 A; A=686-694.
PDB; 4ZSH; X-ray; 1.80 A; B=686-698.
PDB; 5APH; X-ray; 1.54 A; C=686-697.
PDB; 5APJ; X-ray; 2.08 A; C=686-697.
PDB; 5DI7; X-ray; 2.24 A; C/D=686-699.
PDB; 5DID; X-ray; 2.24 A; C/D=686-699.
PDB; 5DIE; X-ray; 2.24 A; C/D=686-699.
PDB; 5DIG; X-ray; 2.24 A; C/D=686-699.
PDB; 5DK9; X-ray; 2.28 A; C/D=686-699.
PDB; 5DKB; X-ray; 2.40 A; C/D=686-699.
PDB; 5DKE; X-ray; 2.60 A; C/D=686-699.
PDB; 5DKG; X-ray; 2.15 A; C/D=686-699.
PDB; 5DKS; X-ray; 2.60 A; C/D=686-699.
PDB; 5DL4; X-ray; 2.10 A; C/D=686-699.
PDB; 5DLR; X-ray; 2.26 A; C/D=686-699.
PDB; 5DMC; X-ray; 2.40 A; C/D=686-699.
PDB; 5DMF; X-ray; 2.40 A; C/D=686-699.
PDB; 5DP0; X-ray; 2.38 A; C/D=686-699.
PDB; 5DRJ; X-ray; 2.07 A; C/D=686-699.
PDB; 5DRM; X-ray; 2.24 A; C/D=686-699.
PDB; 5DTV; X-ray; 2.29 A; C/D=686-699.
PDB; 5DU5; X-ray; 2.19 A; C/D=686-699.
PDB; 5DUE; X-ray; 2.09 A; C/D=686-699.
PDB; 5DUG; X-ray; 2.25 A; C/D=686-699.
PDB; 5DUH; X-ray; 2.24 A; C/D=686-699.
PDB; 5DVS; X-ray; 2.28 A; C/D=686-699.
PDB; 5DVV; X-ray; 2.50 A; C/D=686-699.
PDB; 5DWE; X-ray; 1.92 A; C/D=686-699.
PDB; 5DWG; X-ray; 2.30 A; C/D=686-699.
PDB; 5DWI; X-ray; 2.43 A; C/D=686-699.
PDB; 5DWJ; X-ray; 2.00 A; C/D=686-699.
PDB; 5DX3; X-ray; 2.09 A; C/D=687-697.
PDB; 5DXB; X-ray; 2.08 A; D/E=687-697.
PDB; 5DXE; X-ray; 1.50 A; C/D=687-697.
PDB; 5DXG; X-ray; 1.86 A; C/D=687-697.
PDB; 5DXK; X-ray; 2.23 A; C/D=686-699.
PDB; 5DXM; X-ray; 2.37 A; C/D=686-699.
PDB; 5DXP; X-ray; 2.20 A; C/D=686-699.
PDB; 5DXQ; X-ray; 2.40 A; C/D=686-699.
PDB; 5DXR; X-ray; 2.28 A; C/D=686-699.
PDB; 5DY8; X-ray; 2.03 A; C/D=686-699.
PDB; 5DYB; X-ray; 2.27 A; C/D=686-699.
PDB; 5DYD; X-ray; 2.48 A; C/D=686-699.
PDB; 5DZ0; X-ray; 2.24 A; C/D=686-699.
PDB; 5DZ1; X-ray; 2.20 A; C/D=686-699.
PDB; 5DZ3; X-ray; 2.15 A; C/D=686-699.
PDB; 5DZH; X-ray; 2.11 A; C/D=686-699.
PDB; 5DZI; X-ray; 1.90 A; C/D=686-699.
PDB; 5E0W; X-ray; 2.00 A; C/D=686-699.
PDB; 5E0X; X-ray; 2.01 A; C/D=686-699.
PDB; 5E14; X-ray; 2.22 A; C/D=686-699.
PDB; 5E15; X-ray; 2.10 A; C/D=686-699.
PDB; 5E19; X-ray; 2.24 A; C/D=686-699.
PDB; 5E1C; X-ray; 1.98 A; C/D=686-699.
PDB; 5EC9; X-ray; 2.30 A; B=686-696.
PDB; 5EGV; X-ray; 2.86 A; C/D=686-699.
PDB; 5EHJ; X-ray; 2.50 A; C/D=686-699.
PDB; 5EI1; X-ray; 2.40 A; C/D=686-699.
PDB; 5EIT; X-ray; 2.68 A; C/D=686-699.
PDB; 5G3J; X-ray; 2.40 A; B=740-753.
PDB; 5G42; X-ray; 1.72 A; C=688-697.
PDB; 5G43; X-ray; 2.58 A; C=686-697.
PDB; 5G44; X-ray; 1.84 A; C=686-697.
PDB; 5G45; X-ray; 2.07 A; C=688-697.
PDB; 5G46; X-ray; 1.76 A; C=688-697.
PDB; 5G5W; X-ray; 2.20 A; B=740-753.
PDB; 5H1E; X-ray; 2.60 A; C=740-752.
PDB; 5HYR; X-ray; 2.27 A; F/G=687-697.
PDB; 5I4V; X-ray; 2.61 A; A/B/E/F=687-699.
PDB; 5IAW; X-ray; 2.58 A; C/D=742-751.
PDB; 5ICK; X-ray; 2.47 A; C/D=742-752.
PDB; 5KCC; X-ray; 2.39 A; C/D=686-699.
PDB; 5KCD; X-ray; 1.82 A; C/D=686-699.
PDB; 5KCE; X-ray; 1.85 A; C/D=686-698, C/D=687-696.
PDB; 5KCF; X-ray; 2.07 A; C/D=686-699.
PDB; 5KCT; X-ray; 1.60 A; C/D=686-699.
PDB; 5KCU; X-ray; 2.03 A; C/D=686-699.
PDB; 5KCW; X-ray; 1.91 A; C/D=686-699.
PDB; 5KD9; X-ray; 1.78 A; C/D=686-699.
PDB; 5KR9; X-ray; 2.25 A; C/D=686-699.
PDB; 5KRA; X-ray; 2.40 A; C/D/G/H=686-699.
PDB; 5KRC; X-ray; 2.40 A; C/D=686-699.
PDB; 5KRF; X-ray; 2.19 A; C/D=686-699.
PDB; 5KRH; X-ray; 2.24 A; C/D=686-699.
PDB; 5KRI; X-ray; 2.25 A; C/D=686-699.
PDB; 5KRJ; X-ray; 2.70 A; C/D=686-699.
PDB; 5KRK; X-ray; 2.39 A; C/D=686-699.
PDB; 5KRL; X-ray; 2.40 A; C/D=686-699.
PDB; 5KRM; X-ray; 2.24 A; C/D=686-699.
PDB; 5KRO; X-ray; 2.10 A; C/D=686-699.
PDB; 5L11; X-ray; 1.85 A; C=740-753.
PDB; 5LGA; X-ray; 2.50 A; B=686-698.
PDB; 5LYQ; X-ray; 2.17 A; B=686-698.
PDB; 5NFP; X-ray; 2.10 A; B=740-753.
PDB; 5NFT; X-ray; 2.30 A; B=740-753.
PDB; 5Q17; X-ray; 2.10 A; B=741-752.
PDB; 5SYZ; X-ray; 1.93 A; C=740-754.
PDB; 5T1Z; X-ray; 2.10 A; C/D=686-698.
PDB; 5TLD; X-ray; 2.38 A; C/D=686-698.
PDB; 5TLF; X-ray; 2.20 A; C/D=686-698.
PDB; 5TLG; X-ray; 2.23 A; C/D=686-698.
PDB; 5TLL; X-ray; 2.42 A; C/D=686-698.
PDB; 5TLM; X-ray; 2.50 A; C/D=686-698.
PDB; 5TLO; X-ray; 2.28 A; C/D=686-698.
PDB; 5TLP; X-ray; 2.08 A; C/D=686-698.
PDB; 5TLT; X-ray; 1.90 A; C/D=686-698.
PDB; 5TLU; X-ray; 2.22 A; C/D=686-698.
PDB; 5TLV; X-ray; 2.32 A; C/D=686-698.
PDB; 5TLX; X-ray; 2.10 A; C/D=686-698.
PDB; 5TLY; X-ray; 2.14 A; C/D=686-698.
PDB; 5TM1; X-ray; 2.23 A; C/D=686-698.
PDB; 5TM2; X-ray; 2.60 A; C/D=686-698.
PDB; 5TM3; X-ray; 2.19 A; C/D=686-698.
PDB; 5TM4; X-ray; 2.25 A; C/D=686-698.
PDB; 5TM5; X-ray; 2.24 A; C/D=686-698.
PDB; 5TM6; X-ray; 2.54 A; C/D=686-698.
PDB; 5TM7; X-ray; 2.40 A; C/D=686-698.
PDB; 5TM8; X-ray; 1.99 A; C/D=686-698.
PDB; 5TM9; X-ray; 2.50 A; C/D=686-698.
PDB; 5TML; X-ray; 2.25 A; C/D=686-698.
PDB; 5TMM; X-ray; 2.20 A; C/D=686-698.
PDB; 5TMO; X-ray; 2.17 A; C/D=686-698.
PDB; 5TMQ; X-ray; 2.24 A; C/D=686-698.
PDB; 5TMR; X-ray; 2.30 A; C/D=686-698.
PDB; 5TMS; X-ray; 2.24 A; C/D=686-698.
PDB; 5TMT; X-ray; 2.05 A; C/D=686-698.
PDB; 5TMU; X-ray; 2.43 A; C/D=686-698.
PDB; 5TMV; X-ray; 2.38 A; C/D=686-698.
PDB; 5TMW; X-ray; 2.29 A; C/D=686-698.
PDB; 5TMZ; X-ray; 2.21 A; C/D=686-698.
PDB; 5TN1; X-ray; 2.06 A; C/D=686-698.
PDB; 5TN3; X-ray; 2.54 A; C/D=686-698.
PDB; 5TN4; X-ray; 1.86 A; C/D=686-698.
PDB; 5TN5; X-ray; 1.89 A; C/D=686-698.
PDB; 5TN6; X-ray; 2.09 A; C/D=686-698.
PDB; 5TN7; X-ray; 2.24 A; C/D=686-698.
PDB; 5TN8; X-ray; 2.65 A; C/D=686-698.
PDB; 5U2D; X-ray; 1.86 A; C/D=686-698.
PDB; 5VB3; X-ray; 1.95 A; A=685-697.
PDB; 5VB5; X-ray; 2.23 A; A=685-697.
PDB; 5VB6; X-ray; 2.04 A; A=685-697.
PDB; 5VB7; X-ray; 2.33 A; A=685-697.
PDBsum; 1GWQ; -.
PDBsum; 1GWR; -.
PDBsum; 1M2Z; -.
PDBsum; 1MV9; -.
PDBsum; 1MVC; -.
PDBsum; 1MZN; -.
PDBsum; 1P93; -.
PDBsum; 1T63; -.
PDBsum; 1T65; -.
PDBsum; 1UHL; -.
PDBsum; 1YOK; -.
PDBsum; 1ZDT; -.
PDBsum; 1ZDU; -.
PDBsum; 1ZKY; -.
PDBsum; 2AO6; -.
PDBsum; 2B1V; -.
PDBsum; 2B1Z; -.
PDBsum; 2B23; -.
PDBsum; 2FAI; -.
PDBsum; 2G44; -.
PDBsum; 2G5O; -.
PDBsum; 2LDC; -.
PDBsum; 2P15; -.
PDBsum; 2P1T; -.
PDBsum; 2P1U; -.
PDBsum; 2P1V; -.
PDBsum; 2Q7J; -.
PDBsum; 2Q7L; -.
PDBsum; 2YJD; -.
PDBsum; 2ZXZ; -.
PDBsum; 2ZY0; -.
PDBsum; 3A9E; -.
PDBsum; 3CLD; -.
PDBsum; 3DZU; -.
PDBsum; 3DZY; -.
PDBsum; 3E00; -.
PDBsum; 3E7C; -.
PDBsum; 3E94; -.
PDBsum; 3ERD; -.
PDBsum; 3FUG; -.
PDBsum; 3GN8; -.
PDBsum; 3K22; -.
PDBsum; 3K23; -.
PDBsum; 3KWY; -.
PDBsum; 3KYT; -.
PDBsum; 3L0E; -.
PDBsum; 3L0J; -.
PDBsum; 3L0L; -.
PDBsum; 3O1D; -.
PDBsum; 3O1E; -.
PDBsum; 3OAP; -.
PDBsum; 3OZJ; -.
PDBsum; 3PCU; -.
PDBsum; 3PLZ; -.
PDBsum; 3Q95; -.
PDBsum; 3R5M; -.
PDBsum; 3UP0; -.
PDBsum; 3UP3; -.
PDBsum; 4CSJ; -.
PDBsum; 4DOS; -.
PDBsum; 4E2J; -.
PDBsum; 4FHH; -.
PDBsum; 4FHI; -.
PDBsum; 4IA1; -.
PDBsum; 4IA2; -.
PDBsum; 4IA3; -.
PDBsum; 4IA7; -.
PDBsum; 4IQR; -.
PDBsum; 4IU7; -.
PDBsum; 4IUI; -.
PDBsum; 4IV2; -.
PDBsum; 4IV4; -.
PDBsum; 4IVW; -.
PDBsum; 4IVY; -.
PDBsum; 4IW6; -.
PDBsum; 4IW8; -.
PDBsum; 4IWC; -.
PDBsum; 4IWF; -.
PDBsum; 4K4J; -.
PDBsum; 4K6I; -.
PDBsum; 4M8E; -.
PDBsum; 4M8H; -.
PDBsum; 4NIE; -.
PDBsum; 4NQA; -.
PDBsum; 4OC7; -.
PDBsum; 4P6W; -.
PDBsum; 4P6X; -.
PDBsum; 4PLD; -.
PDBsum; 4PLE; -.
PDBsum; 4POH; -.
PDBsum; 4POJ; -.
PDBsum; 4PP3; -.
PDBsum; 4PP5; -.
PDBsum; 4PP6; -.
PDBsum; 4PPP; -.
PDBsum; 4PPS; -.
PDBsum; 4PXM; -.
PDBsum; 4Q0A; -.
PDBsum; 4Q13; -.
PDBsum; 4QE6; -.
PDBsum; 4QE8; -.
PDBsum; 4RFW; -.
PDBsum; 4RMC; -.
PDBsum; 4RMD; -.
PDBsum; 4RME; -.
PDBsum; 4RUO; -.
PDBsum; 4UDC; -.
PDBsum; 4UDD; -.
PDBsum; 4WG0; -.
PDBsum; 4ZN7; -.
PDBsum; 4ZN9; -.
PDBsum; 4ZNH; -.
PDBsum; 4ZNS; -.
PDBsum; 4ZNT; -.
PDBsum; 4ZNU; -.
PDBsum; 4ZNV; -.
PDBsum; 4ZNW; -.
PDBsum; 4ZO1; -.
PDBsum; 4ZSH; -.
PDBsum; 5APH; -.
PDBsum; 5APJ; -.
PDBsum; 5DI7; -.
PDBsum; 5DID; -.
PDBsum; 5DIE; -.
PDBsum; 5DIG; -.
PDBsum; 5DK9; -.
PDBsum; 5DKB; -.
PDBsum; 5DKE; -.
PDBsum; 5DKG; -.
PDBsum; 5DKS; -.
PDBsum; 5DL4; -.
PDBsum; 5DLR; -.
PDBsum; 5DMC; -.
PDBsum; 5DMF; -.
PDBsum; 5DP0; -.
PDBsum; 5DRJ; -.
PDBsum; 5DRM; -.
PDBsum; 5DTV; -.
PDBsum; 5DU5; -.
PDBsum; 5DUE; -.
PDBsum; 5DUG; -.
PDBsum; 5DUH; -.
PDBsum; 5DVS; -.
PDBsum; 5DVV; -.
PDBsum; 5DWE; -.
PDBsum; 5DWG; -.
PDBsum; 5DWI; -.
PDBsum; 5DWJ; -.
PDBsum; 5DX3; -.
PDBsum; 5DXB; -.
PDBsum; 5DXE; -.
PDBsum; 5DXG; -.
PDBsum; 5DXK; -.
PDBsum; 5DXM; -.
PDBsum; 5DXP; -.
PDBsum; 5DXQ; -.
PDBsum; 5DXR; -.
PDBsum; 5DY8; -.
PDBsum; 5DYB; -.
PDBsum; 5DYD; -.
PDBsum; 5DZ0; -.
PDBsum; 5DZ1; -.
PDBsum; 5DZ3; -.
PDBsum; 5DZH; -.
PDBsum; 5DZI; -.
PDBsum; 5E0W; -.
PDBsum; 5E0X; -.
PDBsum; 5E14; -.
PDBsum; 5E15; -.
PDBsum; 5E19; -.
PDBsum; 5E1C; -.
PDBsum; 5EC9; -.
PDBsum; 5EGV; -.
PDBsum; 5EHJ; -.
PDBsum; 5EI1; -.
PDBsum; 5EIT; -.
PDBsum; 5G3J; -.
PDBsum; 5G42; -.
PDBsum; 5G43; -.
PDBsum; 5G44; -.
PDBsum; 5G45; -.
PDBsum; 5G46; -.
PDBsum; 5G5W; -.
PDBsum; 5H1E; -.
PDBsum; 5HYR; -.
PDBsum; 5I4V; -.
PDBsum; 5IAW; -.
PDBsum; 5ICK; -.
PDBsum; 5KCC; -.
PDBsum; 5KCD; -.
PDBsum; 5KCE; -.
PDBsum; 5KCF; -.
PDBsum; 5KCT; -.
PDBsum; 5KCU; -.
PDBsum; 5KCW; -.
PDBsum; 5KD9; -.
PDBsum; 5KR9; -.
PDBsum; 5KRA; -.
PDBsum; 5KRC; -.
PDBsum; 5KRF; -.
PDBsum; 5KRH; -.
PDBsum; 5KRI; -.
PDBsum; 5KRJ; -.
PDBsum; 5KRK; -.
PDBsum; 5KRL; -.
PDBsum; 5KRM; -.
PDBsum; 5KRO; -.
PDBsum; 5L11; -.
PDBsum; 5LGA; -.
PDBsum; 5LYQ; -.
PDBsum; 5NFP; -.
PDBsum; 5NFT; -.
PDBsum; 5Q17; -.
PDBsum; 5SYZ; -.
PDBsum; 5T1Z; -.
PDBsum; 5TLD; -.
PDBsum; 5TLF; -.
PDBsum; 5TLG; -.
PDBsum; 5TLL; -.
PDBsum; 5TLM; -.
PDBsum; 5TLO; -.
PDBsum; 5TLP; -.
PDBsum; 5TLT; -.
PDBsum; 5TLU; -.
PDBsum; 5TLV; -.
PDBsum; 5TLX; -.
PDBsum; 5TLY; -.
PDBsum; 5TM1; -.
PDBsum; 5TM2; -.
PDBsum; 5TM3; -.
PDBsum; 5TM4; -.
PDBsum; 5TM5; -.
PDBsum; 5TM6; -.
PDBsum; 5TM7; -.
PDBsum; 5TM8; -.
PDBsum; 5TM9; -.
PDBsum; 5TML; -.
PDBsum; 5TMM; -.
PDBsum; 5TMO; -.
PDBsum; 5TMQ; -.
PDBsum; 5TMR; -.
PDBsum; 5TMS; -.
PDBsum; 5TMT; -.
PDBsum; 5TMU; -.
PDBsum; 5TMV; -.
PDBsum; 5TMW; -.
PDBsum; 5TMZ; -.
PDBsum; 5TN1; -.
PDBsum; 5TN3; -.
PDBsum; 5TN4; -.
PDBsum; 5TN5; -.
PDBsum; 5TN6; -.
PDBsum; 5TN7; -.
PDBsum; 5TN8; -.
PDBsum; 5U2D; -.
PDBsum; 5VB3; -.
PDBsum; 5VB5; -.
PDBsum; 5VB6; -.
PDBsum; 5VB7; -.
ProteinModelPortal; Q15596; -.
SMR; Q15596; -.
BioGrid; 115761; 73.
CORUM; Q15596; -.
DIP; DIP-5997N; -.
ELM; Q15596; -.
IntAct; Q15596; 28.
MINT; MINT-122867; -.
STRING; 9606.ENSP00000399968; -.
BindingDB; Q15596; -.
DrugBank; DB06871; 17-METHYL-17-ALPHA-DIHYDROEQUILENIN.
DrugBank; DB07863; 2-chloro-5-nitro-N-phenylbenzamide.
DrugBank; DB07708; 3-CHLORO-2-(4-HYDROXYPHENYL)-2H-INDAZOL-5-OL.
DrugBank; DB07712; 3-ETHYL-2-(4-HYDROXYPHENYL)-2H-INDAZOL-5-OL.
DrugBank; DB01645; Genistein.
DrugBank; DB02998; Methyltrienolone.
DrugBank; DB08773; RALOXIFENE CORE.
DrugBank; DB08601; tributylstannanyl.
iPTMnet; Q15596; -.
PhosphoSitePlus; Q15596; -.
BioMuta; NCOA2; -.
DMDM; 13626594; -.
EPD; Q15596; -.
MaxQB; Q15596; -.
PaxDb; Q15596; -.
PeptideAtlas; Q15596; -.
PRIDE; Q15596; -.
Ensembl; ENST00000452400; ENSP00000399968; ENSG00000140396.
GeneID; 10499; -.
KEGG; hsa:10499; -.
UCSC; uc003xyn.2; human.
CTD; 10499; -.
DisGeNET; 10499; -.
EuPathDB; HostDB:ENSG00000140396.12; -.
GeneCards; NCOA2; -.
HGNC; HGNC:7669; NCOA2.
HPA; HPA060243; -.
MIM; 601993; gene.
neXtProt; NX_Q15596; -.
OpenTargets; ENSG00000140396; -.
PharmGKB; PA31471; -.
eggNOG; ENOG410IQ5S; Eukaryota.
eggNOG; ENOG410XPF9; LUCA.
GeneTree; ENSGT00530000063109; -.
HOGENOM; HOG000230947; -.
HOVERGEN; HBG052583; -.
InParanoid; Q15596; -.
KO; K11255; -.
OMA; PSDMNGW; -.
OrthoDB; EOG091G00US; -.
PhylomeDB; Q15596; -.
TreeFam; TF332652; -.
Reactome; R-HSA-1368082; RORA activates gene expression.
Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
Reactome; R-HSA-159418; Recycling of bile acids and salts.
Reactome; R-HSA-192105; Synthesis of bile acids and bile salts.
Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-HSA-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
Reactome; R-HSA-211976; Endogenous sterols.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
Reactome; R-HSA-3214847; HATs acetylate histones.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-400206; Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
Reactome; R-HSA-8951671; RUNX3 regulates YAP1-mediated transcription.
SignaLink; Q15596; -.
SIGNOR; Q15596; -.
ChiTaRS; NCOA2; human.
EvolutionaryTrace; Q15596; -.
GeneWiki; Nuclear_receptor_coactivator_2; -.
GenomeRNAi; 10499; -.
PRO; PR:Q15596; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000140396; -.
CleanEx; HS_NCOA2; -.
ExpressionAtlas; Q15596; baseline and differential.
Genevisible; Q15596; HS.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0043234; C:protein complex; IMP:CAFA.
GO; GO:0017162; F:aryl hydrocarbon receptor binding; IPI:CAFA.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0016922; F:ligand-dependent nuclear receptor binding; IPI:UniProtKB.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IDA:BHF-UCL.
GO; GO:0035257; F:nuclear hormone receptor binding; IPI:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0001162; F:RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0030375; F:thyroid hormone receptor coactivator activity; IEA:Ensembl.
GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
GO; GO:0015721; P:bile acid and bile salt transport; TAS:Reactome.
GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
GO; GO:1904017; P:cellular response to Thyroglobulin triiodothyronine; IEA:Ensembl.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0030522; P:intracellular receptor signaling pathway; IBA:GO_Central.
GO; GO:0045475; P:locomotor rhythm; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0010906; P:regulation of glucose metabolic process; IEA:Ensembl.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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; IPR032565; DUF4927.
InterPro; IPR036638; HLH_DNA-bd_sf.
InterPro; IPR028822; NCOA2.
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:SF2; PTHR10684:SF2; 1.
Pfam; PF07469; DUF1518; 1.
Pfam; PF16279; DUF4927; 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; 1.
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; Biological rhythms;
Complete proteome; Isopeptide bond; Methylation; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Transcription; Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 1464 Nuclear receptor coactivator 2.
/FTId=PRO_0000094402.
DOMAIN 26 83 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
DOMAIN 119 183 PAS. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
REGION 691 743 CASP8AP2-binding. {ECO:0000250}.
REGION 730 1121 Interaction with ARNTL.
{ECO:0000250|UniProtKB:Q61026}.
MOTIF 641 645 LXXLL motif 1.
MOTIF 690 694 LXXLL motif 2.
MOTIF 745 749 LXXLL motif 3.
MOTIF 878 882 LXXLL motif 4.
MOTIF 1079 1087 LLXXLXXXL motif.
COMPBIAS 1254 1260 Poly-Gln.
SITE 869 870 Breakpoint for translocation to form
KAT6A-NCOA2.
{ECO:0000269|PubMed:12676584,
ECO:0000269|PubMed:15657427,
ECO:0000269|PubMed:9558366}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 338 338 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q61026}.
MOD_RES 487 487 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 493 493 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 499 499 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 554 554 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 565 565 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 636 636 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q61026}.
MOD_RES 640 640 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 682 682 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 699 699 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 736 736 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 771 771 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 780 780 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 785 785 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 864 864 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q61026}.
MOD_RES 874 874 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q61026}.
MOD_RES 1173 1173 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1177 1177 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1190 1190 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1196 1196 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1203 1203 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1221 1221 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1240 1240 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q61026}.
MOD_RES 1261 1261 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1266 1266 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
CROSSLNK 239 239 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 648 648 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 705 705 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 731 731 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 785 785 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1454 1454 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 1282 1282 M -> I (in dbSNP:rs2228591).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_024546.
MUTAGEN 644 645 LL->AA: By itself, does not affect
nuclear receptor binding or
transcriptional coactivation. Abrogates
ligand-induced nuclear receptor binding
and transactivation; when associated with
693-A-A-694 and 748-A-A-749.
{ECO:0000269|PubMed:9430642}.
MUTAGEN 693 694 LL->AA: By itself, does not affect
nuclear receptor binding or
transcriptional coactivation. Abrogates
ligand-induced nuclear receptor binding
and transactivation; when associated with
644-A-A-665 and 748-A-A-749.
{ECO:0000269|PubMed:9430642}.
MUTAGEN 748 749 LL->AA: By itself, does not affect
nuclear receptor binding or
transcriptional coactivation. Abrogates
ligand-induced nuclear receptor binding
and transactivation; when associated with
644-A-A-665 and 693-A-A-694.
{ECO:0000269|PubMed:9430642}.
MUTAGEN 1079 1083 LLDQL->AADQA: Reduces transcriptional
coactivation and disrupts interaction
with CREBBP/CBP.
{ECO:0000269|PubMed:9430642}.
MUTAGEN 1081 1082 DQ->AA: Has little effect on
transcriptional coactivation.
{ECO:0000269|PubMed:9430642}.
HELIX 689 693 {ECO:0000244|PDB:5DXE}.
STRAND 739 741 {ECO:0000244|PDB:1M2Z}.
HELIX 743 750 {ECO:0000244|PDB:3UP3}.
SEQUENCE 1464 AA; 159157 MW; 0A61AA5D1878304B CRC64;
MSGMGENTSD PSRAETRKRK ECPDQLGPSP KRNTEKRNRE QENKYIEELA ELIFANFNDI
DNFNFKPDKC AILKETVKQI RQIKEQEKAA AANIDEVQKS DVSSTGQGVI DKDALGPMML
EALDGFFFVV NLEGNVVFVS ENVTQYLRYN QEELMNKSVY SILHVGDHTE FVKNLLPKSI
VNGGSWSGEP PRRNSHTFNC RMLVKPLPDS EEEGHDNQEA HQKYETMQCF AVSQPKSIKE
EGEDLQSCLI CVARRVPMKE RPVLPSSESF TTRQDLQGKI TSLDTSTMRA AMKPGWEDLV
RRCIQKFHAQ HEGESVSYAK RHHHEVLRQG LAFSQIYRFS LSDGTLVAAQ TKSKLIRSQT
TNEPQLVISL HMLHREQNVC VMNPDLTGQT MGKPLNPISS NSPAHQALCS GNPGQDMTLS
SNINFPINGP KEQMGMPMGR FGGSGGMNHV SGMQATTPQG SNYALKMNSP SQSSPGMNPG
QPTSMLSPRH RMSPGVAGSP RIPPSQFSPA GSLHSPVGVC SSTGNSHSYT NSSLNALQAL
SEGHGVSLGS SLASPDLKMG NLQNSPVNMN PPPLSKMGSL DSKDCFGLYG EPSEGTTGQA
ESSCHPGEQK ETNDPNLPPA VSSERADGQS RLHDSKGQTK LLQLLTTKSD QMEPSPLASS
LSDTNKDSTG SLPGSGSTHG TSLKEKHKIL HRLLQDSSSP VDLAKLTAEA TGKDLSQESS
STAPGSEVTI KQEPVSPKKK ENALLRYLLD KDDTKDIGLP EITPKLERLD SKTDPASNTK
LIAMKTEKEE MSFEPGDQPG SELDNLEEIL DDLQNSQLPQ LFPDTRPGAP AGSVDKQAII
NDLMQLTAEN SPVTPVGAQK TALRISQSTF NNPRPGQLGR LLPNQNLPLD ITLQSPTGAG
PFPPIRNSSP YSVIPQPGMM GNQGMIGNQG NLGNSSTGMI GNSASRPTMP SGEWAPQSSA
VRVTCAATTS AMNRPVQGGM IRNPAASIPM RPSSQPGQRQ TLQSQVMNIG PSELEMNMGG
PQYSQQQAPP NQTAPWPESI LPIDQASFAS QNRQPFGSSP DDLLCPHPAA ESPSDEGALL
DQLYLALRNF DGLEEIDRAL GIPELVSQSQ AVDPEQFSSQ DSNIMLEQKA PVFPQQYASQ
AQMAQGSYSP MQDPNFHTMG QRPSYATLRM QPRPGLRPTG LVQNQPNQLR LQLQHRLQAQ
QNRQPLMNQI SNVSNVNLTL RPGVPTQAPI NAQMLAQRQR EILNQHLRQR QMHQQQQVQQ
RTLMMRGQGL NMTPSMVAPS GMPATMSNPR IPQANAQQFP FPPNYGISQQ PDPGFTGATT
PQSPLMSPRM AHTQSPMMQQ SQANPAYQAP SDINGWAQGN MGGNSMFSQQ SPPHFGQQAN
TSMYSNNMNI NVSMATNTGG MSSMNQMTGQ ISMTSVTSVP TSGLSSMGPE QVNDPALRGG
NLFPNQLPGM DMIKQEGDTT RKYC


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