DNA Binding Motif

						

			
Accessions: FOXO1_HOXB13_2_3 (HumanTF2 1.0)

			
Names: FOXO1_HOXB13
Organisms: Homo sapiens
Libraries: HumanTF2 1.0 1
1 Jolma A, Yin Y, Nitta KR, Dave K, Popov A, Taipale M, Enge M, Kivioja T, Morgunova E, Taipale J. DNA-dependent formation of transcription factor pairs alters their binding specificity. Nature 527:384-8 (2015). [Pubmed]
Notes: Site type: heterodimeric; Experiment type: CAP-SELEX
Length: 16
Consensus: rwmaACAsymrTwAAa
Weblogo: 
PSSM: P0      A      C      G      T
01     75     51    102     12      r
02     80     30     19     97      w
03     80     97      0     14      m
04    177     55      6     30      a
05    177     25     24      6      A
06      0    177      5     31      C
07    177     16      1      6      A
08     34    117     60     27      s
09     13    101     13     76      y
10     79     99      8     34      m
11     98      7     79     19      r
12     28     15      8    177      T
13    119      0      8     58      w
14    177      1      3     32      A
15    177      7      5      5      A
16    177     96     56     90      a
Type: Heterodimer
Binding TFs: FOXO1_TF1 / FOXO1_TF2 (Fork head domain)
HOXB13_TF1 / HOXB13_TF2 (Homeobox domain)
HOXB13_Full (Homeobox domain, Hox protein A13 N terminal)
			
Publications: Jolma A, Yin Y, Nitta KR, Dave K, Popov A, Taipale M, Enge M, Kivioja T, Morgunova E, Taipale J. DNA-dependent formation of transcription factor pairs alters their binding specificity. Nature 527:384-8 (2015). [Pubmed]

	
			


			

				

				
				
				
				

			

			

		

	
Disclaimer and license


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. Downloaded data have CC-BY-NC-SA license. FootprintDB is also available at RSAT::Plants, part of the INB/ELIXIR-ES resources portfolio.