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DESCRIBE <http://purl.uniprot.org/SHA-384/6B9B08E7980ABF1E4B1A9CCBEC1967D2B8A05B762D4FA9F7DA7902618442F79A54EC01A26ABA8B1E35A0A6A94839DA96>
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http://purl.uniprot.org/SHA-384/6B9B08E7980ABF1E4B1A9CCBEC1967D2B8A05B762D4FA9F7DA7902618442F79A54EC01A26ABA8B1E35A0A6A94839DA96
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/6B9B08E7980ABF1E4B1A9CCBEC1967D2B8A05B762D4FA9F7DA7902618442F79A54EC01A26ABA8B1E35A0A6A94839DA96
http://www.w3.org/2000/01/rdf-schema#comment
"During fasting desmin phosphorylation increases and enhances Trim32-mediated degradation of the desmin cytoskeleton which appears to facilitate the breakdown of Z-bands and thin filaments."
xsd:string
http://purl.uniprot.org/uniprot/#_2A44CE07C16B32DEB01A027F47E1E8AA2C169A5269272E8F266FB4F4914B865B845290303F5A720D79C9529E65B99B42
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/6B9B08E7980ABF1E4B1A9CCBEC1967D2B8A05B762D4FA9F7DA7902618442F79A54EC01A26ABA8B1E35A0A6A94839DA96
http://purl.uniprot.org/uniprot/Q3TLR3
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/6B9B08E7980ABF1E4B1A9CCBEC1967D2B8A05B762D4FA9F7DA7902618442F79A54EC01A26ABA8B1E35A0A6A94839DA96
http://purl.uniprot.org/uniprot/#_Q3TLR3-mappedCitation-22908310
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/6B9B08E7980ABF1E4B1A9CCBEC1967D2B8A05B762D4FA9F7DA7902618442F79A54EC01A26ABA8B1E35A0A6A94839DA96