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

Ahmad, Ishtiaq
Walker-Nasir, Evelyne
Rafik, S. M.
Shakoori, A. R.
Nasir ud, Din
Published in Nucleic Acids Research. 2006, vol. 34, no. 1, p. 175-184
Abstract 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.
Keywords Amino Acid SequenceAnimalsDogsGlycosylationHumansMiceMolecular Sequence DataOctamer Transcription Factor-2/ chemistry/classification/ metabolismPhosphorylationPhylogenyProtein BindingProtein Structure, TertiaryRatsSequence AlignmentSerine/metabolismThreonine/metabolism
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PMID: 16431844
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