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DESCRIBE <http://purl.uniprot.org/SHA-384/D028957FA9BE44F9EED36A484C86AD9D30B51A57500FA2EF28ABBD72B7B243B7B28A12D703C67E5133B65C0B76C53796>
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http://purl.uniprot.org/SHA-384/D028957FA9BE44F9EED36A484C86AD9D30B51A57500FA2EF28ABBD72B7B243B7B28A12D703C67E5133B65C0B76C53796
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/D028957FA9BE44F9EED36A484C86AD9D30B51A57500FA2EF28ABBD72B7B243B7B28A12D703C67E5133B65C0B76C53796
http://www.w3.org/2000/01/rdf-schema#comment
"Our findings revealed an intriguing mechanism of regulating USP1 activity that combines phosphorylation of a key serine residue in USP1 and the specific interaction of USP1 with a WD40-repeat protein UAF1"
xsd:string
http://purl.uniprot.org/uniprot/#_7F95762ECE3A66276F9575B6ECF796BBBE30EEC1B53F78EAE9B80B62E435FF95AC74371DC01EA689AC00AF29BD68C91C
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/D028957FA9BE44F9EED36A484C86AD9D30B51A57500FA2EF28ABBD72B7B243B7B28A12D703C67E5133B65C0B76C53796
http://purl.uniprot.org/uniprot/A0A024R2L1
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/D028957FA9BE44F9EED36A484C86AD9D30B51A57500FA2EF28ABBD72B7B243B7B28A12D703C67E5133B65C0B76C53796
http://purl.uniprot.org/uniprot/#_A0A024R2L1-mappedCitation-23116119
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/D028957FA9BE44F9EED36A484C86AD9D30B51A57500FA2EF28ABBD72B7B243B7B28A12D703C67E5133B65C0B76C53796