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DESCRIBE <http://purl.uniprot.org/SHA-384/D22A5B06384325721148B01F203FBC536BE4B1DE73D9FF1B18F106443D65E9619CCFE4FC19978A0B5B536D2B9129206B>
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http://purl.uniprot.org/SHA-384/D22A5B06384325721148B01F203FBC536BE4B1DE73D9FF1B18F106443D65E9619CCFE4FC19978A0B5B536D2B9129206B
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/D22A5B06384325721148B01F203FBC536BE4B1DE73D9FF1B18F106443D65E9619CCFE4FC19978A0B5B536D2B9129206B
http://www.w3.org/2000/01/rdf-schema#comment
"Lac1 and Lag1 are direct targets for CK2 and that phosphorylation at conserved positions within the C-terminal cytoplasmic domain of each protein is required for optimal CerS activity"
xsd:string
http://purl.uniprot.org/uniprot/#_937367C7A33CD24CCC5368F39B2186482048FE19AA62FFC3D12328FAFEFB88C76C139B9E6169CA4F65E90E3A70F4B76E
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/D22A5B06384325721148B01F203FBC536BE4B1DE73D9FF1B18F106443D65E9619CCFE4FC19978A0B5B536D2B9129206B
http://purl.uniprot.org/uniprot/A0A6A5PS36
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/D22A5B06384325721148B01F203FBC536BE4B1DE73D9FF1B18F106443D65E9619CCFE4FC19978A0B5B536D2B9129206B
http://purl.uniprot.org/uniprot/#_A0A6A5PS36-mappedCitation-25429105
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/D22A5B06384325721148B01F203FBC536BE4B1DE73D9FF1B18F106443D65E9619CCFE4FC19978A0B5B536D2B9129206B