<http://purl.uniprot.org/SHA-384/C21B3B056858C49F845AEABF8A3080F81D1BF59B12435411BA9ED4FCE6B755E0B6BEE905617A424C8A06B41B5BB6B10F> <http://www.w3.org/1999/02/22-rdf-syntax-ns#type> <http://purl.uniprot.org/core/PTM_Annotation> .
<http://purl.uniprot.org/SHA-384/C21B3B056858C49F845AEABF8A3080F81D1BF59B12435411BA9ED4FCE6B755E0B6BEE905617A424C8A06B41B5BB6B10F> <http://www.w3.org/2000/01/rdf-schema#comment> "O-glycosylation at Thr-440 in the SET domain by OGT is essential for the histone methyltransferase and the coactivator activity toward RARA in granulopoiesis (By similarity). The absence of Thr-440 glycosylation in assays done in vitro may explain why PubMed:18952892 and PubMed:19264965 did not detected any histone methyltransferase activity for this protein." .
<http://purl.uniprot.org/uniprot/Q3UG20> <http://purl.uniprot.org/core/annotation> <http://purl.uniprot.org/SHA-384/C21B3B056858C49F845AEABF8A3080F81D1BF59B12435411BA9ED4FCE6B755E0B6BEE905617A424C8A06B41B5BB6B10F> .