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DESCRIBE <http://purl.uniprot.org/SHA-384/7027FE03ADB19FFEDB49A90ED8BF1DE485710970396A5FF266CE67670AFF284BCA1F0B4E5661D0B45337088B7A6F784E>
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http://purl.uniprot.org/SHA-384/7027FE03ADB19FFEDB49A90ED8BF1DE485710970396A5FF266CE67670AFF284BCA1F0B4E5661D0B45337088B7A6F784E
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/7027FE03ADB19FFEDB49A90ED8BF1DE485710970396A5FF266CE67670AFF284BCA1F0B4E5661D0B45337088B7A6F784E
http://www.w3.org/2000/01/rdf-schema#comment
"the 1.75 A resolution crystal structure of the N-terminal domain of mouse LIS1 shows that the LisH motif is a novel thermodynamically very stable dimerization domain"
xsd:string
http://purl.uniprot.org/uniprot/#_AA2FB6DD68A0C4E97D19C33F96F81E7C408B146E68F3C6AA1F2A557B01CD9AD9110FCB401CC172FB13FC429943913156
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/7027FE03ADB19FFEDB49A90ED8BF1DE485710970396A5FF266CE67670AFF284BCA1F0B4E5661D0B45337088B7A6F784E
http://purl.uniprot.org/uniprot/Q3UHM0
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/7027FE03ADB19FFEDB49A90ED8BF1DE485710970396A5FF266CE67670AFF284BCA1F0B4E5661D0B45337088B7A6F784E
http://purl.uniprot.org/uniprot/#_Q3UHM0-mappedCitation-15274919
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/7027FE03ADB19FFEDB49A90ED8BF1DE485710970396A5FF266CE67670AFF284BCA1F0B4E5661D0B45337088B7A6F784E