Oct-2 DNA binding transcription factor: functional consequences of phosphorylation and glycosylation.
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.
Ahmad
Ishtiaq
I
Institute of Molecular Sciences and Bioinformatics, Lahore, Pakistan.
Hoessli
Daniel C
DC
Walker-Nasir
Evelyne
E
Rafik
Saleem M
SM
Shakoori
Abdul R
AR
Nasir-ud-Din
D000595:Amino Acid Sequence; D000818:Animals; D004285:Dogs; D006031:Glycosylation; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D050813:Octamer Transcription Factor-2 / Q000737:chemistry* / Q000145:classification / Q000378:metabolism*; D010766:Phosphorylation; D010802:Phylogeny; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D051381:Rats; D016415:Sequence Alignment; D012694:Serine / Q000378:metabolism; D013912:Threonine / Q000378:metabolism
D050813:Octamer Transcription Factor-2; D013912:Threonine; D012694:Serine