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DESCRIBE <http://purl.uniprot.org/SHA-384/2B43A14BC262870BBA32A0B3794DF7139971723CF37DE45B9398D7D02118ACF501A7E1A470EBF41639404C2219073D81>
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http://purl.uniprot.org/SHA-384/2B43A14BC262870BBA32A0B3794DF7139971723CF37DE45B9398D7D02118ACF501A7E1A470EBF41639404C2219073D81
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/2B43A14BC262870BBA32A0B3794DF7139971723CF37DE45B9398D7D02118ACF501A7E1A470EBF41639404C2219073D81
http://www.w3.org/2000/01/rdf-schema#comment
"Data establish a role for the F-BAR domain of SRGP-1 in promoting rapid and robust cell adhesion during embryonic closure events independent of the Rho guanosine triphosphatase-activating protein domain."
xsd:string
http://purl.uniprot.org/uniprot/#_8DD135CF0B299E9DD8B3B920DF998DE2211962BF2DFA7A437A3D226362043673E3DDA347FF352A78B61D45A6CB34EBA2
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/2B43A14BC262870BBA32A0B3794DF7139971723CF37DE45B9398D7D02118ACF501A7E1A470EBF41639404C2219073D81
http://purl.uniprot.org/uniprot/Q19370
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/2B43A14BC262870BBA32A0B3794DF7139971723CF37DE45B9398D7D02118ACF501A7E1A470EBF41639404C2219073D81
http://purl.uniprot.org/uniprot/#_Q19370-mappedCitation-21059849
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/2B43A14BC262870BBA32A0B3794DF7139971723CF37DE45B9398D7D02118ACF501A7E1A470EBF41639404C2219073D81