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- W1978283132 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." @default.
- W1978283132 created "2016-06-24" @default.
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- W1978283132 date "2006-01-08" @default.
- W1978283132 modified "2023-10-10" @default.
- W1978283132 title "Oct-2 DNA binding transcription factor: functional consequences of phosphorylation and glycosylation" @default.
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- W1978283132 doi "https://doi.org/10.1093/nar/gkj401" @default.
- W1978283132 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1326018" @default.
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