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http://purl.uniprot.org/enzyme/2.5.1.58http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/2.5.1.58http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.5.1.-
http://purl.uniprot.org/enzyme/2.5.1.58http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.5.-.-
http://purl.uniprot.org/enzyme/2.5.1.58http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.-.-.-
http://purl.uniprot.org/enzyme/2.5.1.58http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/2.5.1.58http://www.w3.org/2000/01/rdf-schema#comment"Catalyzes the formation of a thioether linkage between the C-1 of an isoprenyl group and a cysteine residue fourth from the C-terminus of the protein."xsd:string
http://purl.uniprot.org/enzyme/2.5.1.58http://www.w3.org/2000/01/rdf-schema#comment"This enzyme, along with EC 2.5.1.59 and EC 2.5.1.60, constitutes the protein prenyltransferase family of enzymes."xsd:string
http://purl.uniprot.org/enzyme/2.5.1.58http://www.w3.org/2000/01/rdf-schema#comment"Substrates of the prenyltransferases include Ras, Rho, Rab, other Ras-related small GTP-binding proteins, gamma-subunits of heterotrimeric G-proteins, nuclear lamins, centromeric proteins and many proteins involved in visual signal transduction."xsd:string
http://purl.uniprot.org/enzyme/2.5.1.58http://www.w3.org/2000/01/rdf-schema#comment"These protein acceptors have the C-terminal sequence CA(1)A(2)X, where the terminal residue, X, is preferably serine, methionine, alanine or glutamine; leucine makes the protein a substrate for EC 2.5.1.59."xsd:string
http://purl.uniprot.org/enzyme/2.5.1.58http://www.w3.org/2000/01/rdf-schema#comment"The enzymes are relaxed in specificity for A(1), but cannot act if A(2) is aromatic."xsd:string
http://purl.uniprot.org/enzyme/2.5.1.58http://www.w3.org/2004/02/skos/core#prefLabel"protein farnesyltransferase"xsd:string
http://purl.uniprot.org/enzyme/2.5.1.58http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12374986
http://purl.uniprot.org/enzyme/2.5.1.58http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9657673
http://purl.uniprot.org/enzyme/2.5.1.58http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/11591144
http://purl.uniprot.org/enzyme/2.5.1.58http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/7756316
http://purl.uniprot.org/enzyme/2.5.1.58http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8621375
http://purl.uniprot.org/enzyme/2.5.1.58http://www.w3.org/2004/02/skos/core#altLabel"FTase"xsd:string
http://purl.uniprot.org/enzyme/2.5.1.58http://www.w3.org/2004/02/skos/core#altLabel"CAAX farnesyltransferase"xsd:string
http://purl.uniprot.org/enzyme/2.5.1.58http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/2.5.1.58#SIP2DCFAE96A9AE8F60
http://purl.uniprot.org/enzyme/2.5.1.58http://www.w3.org/2004/02/skos/core#broaderTransitivehttp://purl.uniprot.org/enzyme/2.5.1.-
http://purl.uniprot.org/uniprot/A0AA38XDS5http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.5.1.58
http://purl.uniprot.org/uniprot/A0AA39NKD1http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.5.1.58
http://purl.uniprot.org/uniprot/A0A835Y0T9http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.5.1.58
http://purl.uniprot.org/uniprot/A0A814NT09http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.5.1.58
http://purl.uniprot.org/uniprot/A0A833R840http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.5.1.58