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DESCRIBE <http://purl.uniprot.org/SHA-384/94CB36E06480CEEF3B07793BBEF907B6E07078713FB3C24CD4D2DC94A490B9FE65BFB69DE60CE1AF3779CE7520E3A1FA>
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http://purl.uniprot.org/SHA-384/94CB36E06480CEEF3B07793BBEF907B6E07078713FB3C24CD4D2DC94A490B9FE65BFB69DE60CE1AF3779CE7520E3A1FA
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/94CB36E06480CEEF3B07793BBEF907B6E07078713FB3C24CD4D2DC94A490B9FE65BFB69DE60CE1AF3779CE7520E3A1FA
http://www.w3.org/2000/01/rdf-schema#comment
"Studies indicate that switching from pyruvate kinase spliced isoform PKM1 to PKM2 promotes aerobic glycolysis and provides a selective advantage for tumor formation and the alternative splicing is controlled by hnRNP family members."
xsd:string
http://purl.uniprot.org/uniprot/#_299669450F56535603AAFBBEE44FEE9F45C5820B57AE3E81B62CF0A196FF456FDB4A90F6912E118C31CF9D2BC78B81D3
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/94CB36E06480CEEF3B07793BBEF907B6E07078713FB3C24CD4D2DC94A490B9FE65BFB69DE60CE1AF3779CE7520E3A1FA
http://purl.uniprot.org/uniprot/P30613
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/94CB36E06480CEEF3B07793BBEF907B6E07078713FB3C24CD4D2DC94A490B9FE65BFB69DE60CE1AF3779CE7520E3A1FA
http://purl.uniprot.org/uniprot/#_P30613-mappedCitation-20978194
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/94CB36E06480CEEF3B07793BBEF907B6E07078713FB3C24CD4D2DC94A490B9FE65BFB69DE60CE1AF3779CE7520E3A1FA