DNA Binding Site

Accessions: 3ri4_E (3D-footprint 20210203), 3wts_D (3D-footprint 20210203), 3wtt_D (3D-footprint 20210203), 3wtt_I (3D-footprint 20210203), 3wtu_D (3D-footprint 20210203), 3wtu_I (3D-footprint 20210203), 3wtv_D (3D-footprint 20210203), 3wtv_I (3D-footprint 20210203), 3wtw_D (3D-footprint 20210203), 3wtw_I (3D-footprint 20210203), 3wtx_D (3D-footprint 20210203), 3wtx_I (3D-footprint 20210203), 3wty_D (3D-footprint 20210203), 3wty_I (3D-footprint 20210203), 3wu1_C (3D-footprint 20210203), 4l0y_C (3D-footprint 20210203), 4l0z_C (3D-footprint 20210203), 4l18_C (3D-footprint 20210203), 4l18_G (3D-footprint 20210203)
Organisms: Homo sapiens, Mus musculus
Libraries: 3D-footprint 20210203 1
1 Contreras-Moreira B. 3D-footprint: a database for the structural analysis of protein-DNA complexes. Nucleic acids research 38:D91-7 (2010). [Pubmed]
Length: 15
Sequence: GAAGCCACATCCTCT
Type: Heterodimer
Binding TFs: 3wtx_C (Ets-domain)
3ri4_D (Ets-domain)
3wts_A (Runt domain)
3wts_C / 3wtt_C / 3wtu_C / 3wtv_C / 3wtw_C (Ets-domain)
3wtt_F / 3wtx_F / 3wty_F (Runt domain)
3wtu_F (Runt domain)
3wtv_F (Runt domain)
3wtw_F (Runt domain)
3wty_C (Ets-domain)
3wu1_A (Runt domain)
3wu1_B (Ets-domain)
4l0y_A (Runt domain)
4l0y_B (Ets-domain)
4l0z_B (Ets-domain)
4l18_B (Ets-domain)
4l18_E (Runt domain)
4l18_F (Ets-domain)
Binding Motifs: 4l18_E AAGCCACA
3ri4_D CATCCT
3wts_A TGTGGctT
3wts_AC AGGATGTGGctt
3wts_C aGGa
3wtt_AC gCCACATCCt
3wtt_F TGTGGctT
3wtu_AC GCCACATCCT
3wtu_F AAGCCACA
3wtv_AC AGGATGTGGC
3wtv_F agCCACA
3wtw_AC GCCACATCCT
3wtw_F TGTGGctw
3wtx_AC GCCACATCCT
3wtx_F TGTGGcTt
3wty_AC GCCACATCCT
3wty_F TGTGGC
3wu1_A AAGCCACA
3wu1_AB AGGATGTGGCTT
4l0y_A AAGCCACA
4l0y_AB AAGCCACATCCT
4l0z_AB AAgCCACATCCT
4l0z_B aGGA
4l18_AB aGGATGTGGCTT
4l18_B aTCCt
4l18_EF AGGATGTGGCTT
Publications: Babayeva N.D, Baranovskaya O.I, Tahirov T.H. Structural basis of Ets1 cooperative binding to widely separated sites on promoter DNA. PloS one 7:e33698 (2012). [Pubmed]

Shiina M, Hamada K, Inoue-Bungo T, Shimamura M, Uchiyama A, Baba S, Sato K, Yamamoto M, Ogata K. A Novel Allosteric Mechanism on Protein-DNA Interactions underlying the Phosphorylation-Dependent Regulation of Ets1 Target Gene Expressions. Journal of molecular biology 427:1655-69 (2015). [Pubmed]

Shrivastava T, Mino K, Babayeva N.D, Baranovskaya O.I, Rizzino A, Tahirov T.H. Structural basis of Ets1 activation by Runx1. Leukemia 28:2040-8 (2014). [Pubmed]

Disclaimer

These data are available AS IS and at your own risk. The EEAD/CSIC do not give any representation or warranty nor assume any liability or responsibility for the data nor the results posted (whether as to their accuracy, completeness, quality or otherwise). Access to these data is available free of charge for ordinary use in the course of research.