Oct-2 DNA binding transcription factor: functional consequences of phosphorylation and glycosylation

Nucleic Acids Res. 2006 Jan 8;34(1):175-84. doi: 10.1093/nar/gkj401. Print 2006.


Phosphorylation and O-GlcNAc modification often induce conformational changes and allow the protein to specifically interact with other proteins. Interplay of phosphorylation and O-GlcNAc modification at the same conserved site may result in the protein undergoing functional switches. We describe that at conserved Ser/Thr residues of human Oct-2, alternative phosphorylation and O-GlcNAc modification (Yin Yang sites) can be predicted by the YinOYang1.2 method. We propose here that alternative phosphorylation and O-GlcNAc modification at Ser191 in the N-terminal region, Ser271 and 274 in the linker region of two POU sub-domains and Thr301 and Ser323 in the POUh subdomain are involved in the differential binding behavior of Oct-2 to the octamer DNA motif. This implies that phosphorylation or O-GlcNAc modification of the same amino acid may result in a different binding capacity of the modified protein. In the C-terminal domain, Ser371, 389 and 394 are additional Yin Yang sites that could be involved in the modulation of Oct-2 binding properties.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Dogs
  • Glycosylation
  • Humans
  • Mice
  • Molecular Sequence Data
  • Octamer Transcription Factor-2 / chemistry*
  • Octamer Transcription Factor-2 / classification
  • Octamer Transcription Factor-2 / metabolism*
  • Phosphorylation
  • Phylogeny
  • Protein Binding
  • Protein Structure, Tertiary
  • Rats
  • Sequence Alignment
  • Serine / metabolism
  • Threonine / metabolism


  • Octamer Transcription Factor-2
  • Threonine
  • Serine