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DESCRIBE <http://purl.uniprot.org/SHA-384/2BB303AEACEFD955F3E56CAE290A9B9766FC1BCE9FFC690DCA572EEEA4757FE98A72D975805AD0C6AEB59471EADDBDC5>
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http://purl.uniprot.org/SHA-384/2BB303AEACEFD955F3E56CAE290A9B9766FC1BCE9FFC690DCA572EEEA4757FE98A72D975805AD0C6AEB59471EADDBDC5
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/2BB303AEACEFD955F3E56CAE290A9B9766FC1BCE9FFC690DCA572EEEA4757FE98A72D975805AD0C6AEB59471EADDBDC5
http://www.w3.org/2000/01/rdf-schema#comment
"Results demonstrate that in concert with dynamin-1 self-assembly pleckstrin homology domain membrane insertion is essential for fission and vesicle release in vitro and for clathrin-mediated endocytosis in vivo."
xsd:string
http://purl.uniprot.org/uniprot/#_CAB76EE9F42C548B6B0765B300F481DEE5696436422A8CE7142ED8739A0A69475CFA5DF51D98EE6885AEECE473F6096B
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/2BB303AEACEFD955F3E56CAE290A9B9766FC1BCE9FFC690DCA572EEEA4757FE98A72D975805AD0C6AEB59471EADDBDC5
http://purl.uniprot.org/uniprot/B4DK06
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/2BB303AEACEFD955F3E56CAE290A9B9766FC1BCE9FFC690DCA572EEEA4757FE98A72D975805AD0C6AEB59471EADDBDC5
http://purl.uniprot.org/uniprot/#_B4DK06-mappedCitation-19776347
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/2BB303AEACEFD955F3E56CAE290A9B9766FC1BCE9FFC690DCA572EEEA4757FE98A72D975805AD0C6AEB59471EADDBDC5