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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2006-1-24
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pubmed:abstractText |
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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16431844-10521537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16431844-10580136,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16431844-10600390,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16431844-9790834
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1362-4962
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
34
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
175-84
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16431844-Amino Acid Sequence,
pubmed-meshheading:16431844-Animals,
pubmed-meshheading:16431844-Dogs,
pubmed-meshheading:16431844-Glycosylation,
pubmed-meshheading:16431844-Humans,
pubmed-meshheading:16431844-Mice,
pubmed-meshheading:16431844-Molecular Sequence Data,
pubmed-meshheading:16431844-Octamer Transcription Factor-2,
pubmed-meshheading:16431844-Phosphorylation,
pubmed-meshheading:16431844-Phylogeny,
pubmed-meshheading:16431844-Protein Binding,
pubmed-meshheading:16431844-Protein Structure, Tertiary,
pubmed-meshheading:16431844-Rats,
pubmed-meshheading:16431844-Sequence Alignment,
pubmed-meshheading:16431844-Serine,
pubmed-meshheading:16431844-Threonine
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pubmed:year |
2006
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pubmed:articleTitle |
Oct-2 DNA binding transcription factor: functional consequences of phosphorylation and glycosylation.
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pubmed:affiliation |
Institute of Molecular Sciences and Bioinformatics, Lahore, Pakistan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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