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DESCRIBE <http://purl.uniprot.org/SHA-384/D3BF64D8CAE2CF192D12A9276ADED534E8A3F10FEEFD2CBB1AC4B0BC4D5D78C51BE768DAE314A353ABF6AA0A00C603AB>
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http://purl.uniprot.org/SHA-384/D3BF64D8CAE2CF192D12A9276ADED534E8A3F10FEEFD2CBB1AC4B0BC4D5D78C51BE768DAE314A353ABF6AA0A00C603AB
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/D3BF64D8CAE2CF192D12A9276ADED534E8A3F10FEEFD2CBB1AC4B0BC4D5D78C51BE768DAE314A353ABF6AA0A00C603AB
http://www.w3.org/2000/01/rdf-schema#comment
"N-linked glycosylation of DPP10 plays an important role in modulating Kv4.3 channel/KCHIP2 complex activities."
xsd:string
http://purl.uniprot.org/uniprot/#_FEEF8DBE10A283006BFA19F56343C36B1C0399E011C84767E758636D826D536C66E2C4C25D961907F83B9EBC78FBDE1A
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/D3BF64D8CAE2CF192D12A9276ADED534E8A3F10FEEFD2CBB1AC4B0BC4D5D78C51BE768DAE314A353ABF6AA0A00C603AB
http://purl.uniprot.org/uniprot/Q9UK17
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/D3BF64D8CAE2CF192D12A9276ADED534E8A3F10FEEFD2CBB1AC4B0BC4D5D78C51BE768DAE314A353ABF6AA0A00C603AB
http://purl.uniprot.org/uniprot/#_Q9UK17-mappedCitation-20354865
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/D3BF64D8CAE2CF192D12A9276ADED534E8A3F10FEEFD2CBB1AC4B0BC4D5D78C51BE768DAE314A353ABF6AA0A00C603AB