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http://purl.uniprot.org/SHA-384/C142841D26129DBF1F28011B1C73A940DA256660B3E2C56375A944B2045BA4FFD59647710C581F8881F8AC1D5CAE4E3Dhttp://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/C142841D26129DBF1F28011B1C73A940DA256660B3E2C56375A944B2045BA4FFD59647710C581F8881F8AC1D5CAE4E3Dhttp://www.w3.org/2000/01/rdf-schema#comment"Data suggest that mature KLK9 (kallikrein 9) is a glycosylated chymotrypsin-like enzyme with strong preference for tyrosine over phenylalanine at P1 cleavage position; substrate specificity of KLK9 appears to extend to KLK10 and midkine; enzyme activity is enhanced by Mg2+ and Ca2+ but is reversibly attenuated by Zn2+; KLK9 is inhibited in vitro by many naturally occurring or synthetic protease inhibitors."xsd:string
http://purl.uniprot.org/uniprot/#_0764136604FA93A13A1B13AE2491543D5E389F2789B1074F9D66291B6E5BB802798ED5A438773DB4ABF3A83E8DAA5FC1http://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/C142841D26129DBF1F28011B1C73A940DA256660B3E2C56375A944B2045BA4FFD59647710C581F8881F8AC1D5CAE4E3D
http://purl.uniprot.org/uniprot/P21741http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/C142841D26129DBF1F28011B1C73A940DA256660B3E2C56375A944B2045BA4FFD59647710C581F8881F8AC1D5CAE4E3D
http://purl.uniprot.org/uniprot/#_P21741-mappedCitation-28559305http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/C142841D26129DBF1F28011B1C73A940DA256660B3E2C56375A944B2045BA4FFD59647710C581F8881F8AC1D5CAE4E3D