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DESCRIBE <http://purl.uniprot.org/SHA-384/387401628DCBD1456B9BE6B280E160A13B4845470ACEB1E3F7E6DE770FEE4197D5A27B08D3352BE28E7F2276E0A6A87D>
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http://purl.uniprot.org/SHA-384/387401628DCBD1456B9BE6B280E160A13B4845470ACEB1E3F7E6DE770FEE4197D5A27B08D3352BE28E7F2276E0A6A87D
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/387401628DCBD1456B9BE6B280E160A13B4845470ACEB1E3F7E6DE770FEE4197D5A27B08D3352BE28E7F2276E0A6A87D
http://www.w3.org/2000/01/rdf-schema#comment
"both TNF-R and nucleotide-binding oligomerization domain stimulation promote ATG16L1 stabilization via IKKalpha-dependent phosphorylation of ATG16L1 at Ser278."
xsd:string
http://purl.uniprot.org/uniprot/#_BEC5C9B7E7D3E91CFC84D73C96028278B08DADBC7539E5AB5934F1DD25FF33F949668BEF727A4E0B155D1FC91F40BCA2
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/387401628DCBD1456B9BE6B280E160A13B4845470ACEB1E3F7E6DE770FEE4197D5A27B08D3352BE28E7F2276E0A6A87D
http://purl.uniprot.org/uniprot/Q8C0J2
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/387401628DCBD1456B9BE6B280E160A13B4845470ACEB1E3F7E6DE770FEE4197D5A27B08D3352BE28E7F2276E0A6A87D
http://purl.uniprot.org/uniprot/#_Q8C0J2-mappedCitation-28082356
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/387401628DCBD1456B9BE6B280E160A13B4845470ACEB1E3F7E6DE770FEE4197D5A27B08D3352BE28E7F2276E0A6A87D