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http://purl.uniprot.org/SHA-384/A477FB3D5DEBAE2631AC7CA4868341747A501AFB3EE53EBDC98786488C1C5345E8A7F584F77F4CA32506C28B3C7E026Fhttp://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/A477FB3D5DEBAE2631AC7CA4868341747A501AFB3EE53EBDC98786488C1C5345E8A7F584F77F4CA32506C28B3C7E026Fhttp://www.w3.org/2000/01/rdf-schema#comment"serine hydroxymethyltransferase 2 (SHMT2) is acetylated at K95 in colorectal cancer (CRC) cells. SHMT2-K95-Ac disrupts its functional tetramer structure and inhibits its enzymatic activity. SHMT2-K95-Ac promotes its degradation via the K63-ubiquitin-lysosome pathway in a glucose-dependent manner. SHMT2-K95-Ac is decreased in human CRC samples which is correlated with poorer postoperative overall survival."xsd:string
http://purl.uniprot.org/uniprot/#_3968DAB9D048C07F49ABB696EAFE5714DC444D1628203A7E261484905D73692E5659DA7D533A75213A63D9E660D0833Bhttp://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/A477FB3D5DEBAE2631AC7CA4868341747A501AFB3EE53EBDC98786488C1C5345E8A7F584F77F4CA32506C28B3C7E026F
http://purl.uniprot.org/uniprot/B4DLV4http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/A477FB3D5DEBAE2631AC7CA4868341747A501AFB3EE53EBDC98786488C1C5345E8A7F584F77F4CA32506C28B3C7E026F
http://purl.uniprot.org/uniprot/#_B4DLV4-mappedCitation-30367038http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/A477FB3D5DEBAE2631AC7CA4868341747A501AFB3EE53EBDC98786488C1C5345E8A7F584F77F4CA32506C28B3C7E026F