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DESCRIBE <http://purl.uniprot.org/SHA-384/0CD012CD7A211A8CC5367167F749E9E069245DDEFED390337FB892413D8C6CBEF5956B59E31E33E4D6946F5F94A4841F>
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http://purl.uniprot.org/SHA-384/0CD012CD7A211A8CC5367167F749E9E069245DDEFED390337FB892413D8C6CBEF5956B59E31E33E4D6946F5F94A4841F
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/0CD012CD7A211A8CC5367167F749E9E069245DDEFED390337FB892413D8C6CBEF5956B59E31E33E4D6946F5F94A4841F
http://www.w3.org/2000/01/rdf-schema#comment
"Through a comprehensive set of biochemical biophysical mutational and structural studies we quantitatively assess how phosphorylation of MOB1A regulates its interaction with both MST kinases and LATS/NDR family kinases in vitro."
xsd:string
http://purl.uniprot.org/uniprot/#_A9FE5C4A24B618506DB2342EF9D9FF87B57CFC2E58A9650E8508A7B435D3467965324D0FDDA816718D3A1859FA4CAFE9
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/0CD012CD7A211A8CC5367167F749E9E069245DDEFED390337FB892413D8C6CBEF5956B59E31E33E4D6946F5F94A4841F
http://purl.uniprot.org/uniprot/A0A087WVN8
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/0CD012CD7A211A8CC5367167F749E9E069245DDEFED390337FB892413D8C6CBEF5956B59E31E33E4D6946F5F94A4841F
http://purl.uniprot.org/uniprot/#_A0A087WVN8-mappedCitation-28373297
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/0CD012CD7A211A8CC5367167F749E9E069245DDEFED390337FB892413D8C6CBEF5956B59E31E33E4D6946F5F94A4841F