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http://purl.uniprot.org/SHA-384/F26EDC1858A8EEB4CF2C9A47E021AAE7F64B38A1EAA176AFD76D96E346BA8C5A912A9625C8657983F3DA06330F1BF3F9http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/F26EDC1858A8EEB4CF2C9A47E021AAE7F64B38A1EAA176AFD76D96E346BA8C5A912A9625C8657983F3DA06330F1BF3F9http://www.w3.org/2000/01/rdf-schema#comment"Protein/gene_name: Pax6. Function: Transcription factor involved in the formation of the eye, brain, and central nervous system in vertebrates. Due to various roles in the eye morphogenesis, Pax6 interacts with DNA and various transcription factors via post-translational modifications. Comments: This is an in silico study about predicting the glycosylation positions of Pax6 protein in vertebrates. Also, 3D protein and glycoprotein models were generated using I-TASSER and GLYCAM servers in order to understand the effect of glycosylation on the Pax6 protein structure. Prediction included N-glycosylation, mucin-type O-glycosylation, O-alfa-GlcNAcylation, and O-beta-GlcNAcylation positions on Pax6 protein besides O-GlcNAc modification. Moreover, there are ying-yang positions suggesting the presence of O-GlcNAcylation/phosphorylation competition in Pax6. As to 3D glycoprotein models of Pax6, Ser-24, Ser-65, and Ser-74 residues at the PD domain of Pax6 protein were evaluated as strong candidates for the DNA binding site. Determination of the glycosylation positions on 3D glycoprotein model may facilitate the understanding of glycosylation role on Pax6 protein interactions in transcription and intracellular activities."xsd:string
http://purl.uniprot.org/uniprot/#_4242D8E8504147FA4C400B7BAAAFB0F04905C9C835A0B89539713AC8EE91394A6429B6A0873E56820FF7DC06C11E487Ehttp://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/F26EDC1858A8EEB4CF2C9A47E021AAE7F64B38A1EAA176AFD76D96E346BA8C5A912A9625C8657983F3DA06330F1BF3F9
http://purl.uniprot.org/uniprot/P26367http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/F26EDC1858A8EEB4CF2C9A47E021AAE7F64B38A1EAA176AFD76D96E346BA8C5A912A9625C8657983F3DA06330F1BF3F9
http://purl.uniprot.org/uniprot/#_P26367-mappedCitation-30286322http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/F26EDC1858A8EEB4CF2C9A47E021AAE7F64B38A1EAA176AFD76D96E346BA8C5A912A9625C8657983F3DA06330F1BF3F9