| pubmed-article:16431844 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16431844 | lifeskim:mentions | umls-concept:C1442823 | lld:lifeskim |
| pubmed-article:16431844 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:16431844 | lifeskim:mentions | umls-concept:C0040648 | lld:lifeskim |
| pubmed-article:16431844 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:16431844 | lifeskim:mentions | umls-concept:C0017982 | lld:lifeskim |
| pubmed-article:16431844 | lifeskim:mentions | umls-concept:C1148673 | lld:lifeskim |
| pubmed-article:16431844 | lifeskim:mentions | umls-concept:C0686907 | lld:lifeskim |
| pubmed-article:16431844 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:16431844 | pubmed:dateCreated | 2006-1-24 | lld:pubmed |
| pubmed-article:16431844 | 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. | lld:pubmed |
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| pubmed-article:16431844 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16431844 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16431844 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16431844 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16431844 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16431844 | pubmed:issn | 1362-4962 | lld:pubmed |
| pubmed-article:16431844 | pubmed:author | pubmed-author:Nasir-ud-Din | lld:pubmed |
| pubmed-article:16431844 | pubmed:author | pubmed-author:HoessliDaniel... | lld:pubmed |
| pubmed-article:16431844 | pubmed:author | pubmed-author:Walker-NasirE... | lld:pubmed |
| pubmed-article:16431844 | pubmed:author | pubmed-author:AhmadIshtiaqI | lld:pubmed |
| pubmed-article:16431844 | pubmed:author | pubmed-author:RafikSaleem... | lld:pubmed |
| pubmed-article:16431844 | pubmed:author | pubmed-author:ShakooriAbdul... | lld:pubmed |
| pubmed-article:16431844 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:16431844 | pubmed:volume | 34 | lld:pubmed |
| pubmed-article:16431844 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16431844 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16431844 | pubmed:pagination | 175-84 | lld:pubmed |
| pubmed-article:16431844 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:16431844 | pubmed:meshHeading | pubmed-meshheading:16431844... | lld:pubmed |
| pubmed-article:16431844 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16431844 | pubmed:articleTitle | Oct-2 DNA binding transcription factor: functional consequences of phosphorylation and glycosylation. | lld:pubmed |
| pubmed-article:16431844 | pubmed:affiliation | Institute of Molecular Sciences and Bioinformatics, Lahore, Pakistan. | lld:pubmed |
| pubmed-article:16431844 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16431844 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16431844 | lld:pubmed |
