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http://purl.uniprot.org/citations/9738465http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9738465http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9738465http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/9738465http://www.w3.org/2000/01/rdf-schema#comment"A novel cDNA encoding a cysteine protease of the papain family named cathepsin X was obtained by PCR amplification from a human ovary cDNA library. The cathepsin X cDNA is ubiquitously expressed in human tissues and contains an open reading frame of 912 nucleotides encoding a predicted protein of 303 amino acids. All highly conserved regions in papain-like cysteine proteases including the catalytic residues are present in cathepsin X. The mature part of cathepsin X is 26-32% identical to human cathepsins B, C, H, K, L, O, S and W. The cathepsin X sequence contains several unique features: (i) a very short proregion; (ii) a three amino acid residue insertion in a highly conserved region between the glutamine of the putative oxyanion hole and the active site cysteine; and (iii) a second insertion of 15 amino acid residues that can be aligned with the occluding loop region in cathepsin B."xsd:string
http://purl.uniprot.org/citations/9738465http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(98)00964-8"xsd:string
http://purl.uniprot.org/citations/9738465http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(98)00964-8"xsd:string
http://purl.uniprot.org/citations/9738465http://purl.uniprot.org/core/author"Menard R."xsd:string
http://purl.uniprot.org/citations/9738465http://purl.uniprot.org/core/author"Menard R."xsd:string
http://purl.uniprot.org/citations/9738465http://purl.uniprot.org/core/author"Naegler D.K."xsd:string
http://purl.uniprot.org/citations/9738465http://purl.uniprot.org/core/author"Naegler D.K."xsd:string
http://purl.uniprot.org/citations/9738465http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9738465http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9738465http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/9738465http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/9738465http://purl.uniprot.org/core/pages"135-139"xsd:string
http://purl.uniprot.org/citations/9738465http://purl.uniprot.org/core/pages"135-139"xsd:string
http://purl.uniprot.org/citations/9738465http://purl.uniprot.org/core/title"Human cathepsin X: a novel cysteine protease of the papain family with a very short proregion and unique insertions."xsd:string
http://purl.uniprot.org/citations/9738465http://purl.uniprot.org/core/title"Human cathepsin X: a novel cysteine protease of the papain family with a very short proregion and unique insertions."xsd:string
http://purl.uniprot.org/citations/9738465http://purl.uniprot.org/core/volume"434"xsd:string
http://purl.uniprot.org/citations/9738465http://purl.uniprot.org/core/volume"434"xsd:string
http://purl.uniprot.org/citations/9738465http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9738465
http://purl.uniprot.org/citations/9738465http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9738465
http://purl.uniprot.org/citations/9738465http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9738465
http://purl.uniprot.org/citations/9738465http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9738465
http://purl.uniprot.org/citations/9738465http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9738465