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DESCRIBE <http://purl.uniprot.org/SHA-384/DADDA4131650E2F388B80495E9EEF0322FD40126DF3955B2509CC898F799C53FE66D7CD1CF53429F0798E6C6E799E0E8>
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http://purl.uniprot.org/SHA-384/DADDA4131650E2F388B80495E9EEF0322FD40126DF3955B2509CC898F799C53FE66D7CD1CF53429F0798E6C6E799E0E8
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/DADDA4131650E2F388B80495E9EEF0322FD40126DF3955B2509CC898F799C53FE66D7CD1CF53429F0798E6C6E799E0E8
http://www.w3.org/2000/01/rdf-schema#comment
"Cdk1-mediated phosphorylation of DIAPH1 stably maintains cortical tension after rounding and inactivates the spindle assembly checkpoint (SAC). Cdk1 phosphorylates DIAPH1 preventing profilin1 binding to maintain cortical tension."
xsd:string
http://purl.uniprot.org/uniprot/#_88CE123E72C3DCEA2EED625B85D5117AD49133B279F19BD1A51A54CA0635705EE925C465F427C95600BC907169502DB7
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/DADDA4131650E2F388B80495E9EEF0322FD40126DF3955B2509CC898F799C53FE66D7CD1CF53429F0798E6C6E799E0E8
http://purl.uniprot.org/uniprot/A0A1E1ERW3
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/DADDA4131650E2F388B80495E9EEF0322FD40126DF3955B2509CC898F799C53FE66D7CD1CF53429F0798E6C6E799E0E8
http://purl.uniprot.org/uniprot/#_A0A1E1ERW3-mappedCitation-30816115
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/DADDA4131650E2F388B80495E9EEF0322FD40126DF3955B2509CC898F799C53FE66D7CD1CF53429F0798E6C6E799E0E8