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DESCRIBE <http://purl.uniprot.org/SHA-384/D9F920F49639151565CF930034EB48967F32F36BF9658167558118DACDBAEBB0D84BC6D5610C14565A1B5AB2136F7AF2>
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http://purl.uniprot.org/SHA-384/D9F920F49639151565CF930034EB48967F32F36BF9658167558118DACDBAEBB0D84BC6D5610C14565A1B5AB2136F7AF2
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/D9F920F49639151565CF930034EB48967F32F36BF9658167558118DACDBAEBB0D84BC6D5610C14565A1B5AB2136F7AF2
http://www.w3.org/2000/01/rdf-schema#comment
"In the resting state the BTK PH domain binds to the activation loop face of the kinase domain and allosterically alters key sites within the kinase domain."
xsd:string
http://purl.uniprot.org/uniprot/#_7B5928B7E87103DD60624C54BE5FBB129FA3260117F9BA98E9D2CE5FD193E856F7369153C4039606B2B7EBD7C17728A1
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/D9F920F49639151565CF930034EB48967F32F36BF9658167558118DACDBAEBB0D84BC6D5610C14565A1B5AB2136F7AF2
http://purl.uniprot.org/uniprot/Q572P3
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/D9F920F49639151565CF930034EB48967F32F36BF9658167558118DACDBAEBB0D84BC6D5610C14565A1B5AB2136F7AF2
http://purl.uniprot.org/uniprot/#_Q572P3-mappedCitation-31591208
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/D9F920F49639151565CF930034EB48967F32F36BF9658167558118DACDBAEBB0D84BC6D5610C14565A1B5AB2136F7AF2