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http://www.tkuhn.ch/bel2nanopub/RAAKT9qQvnvt7E0L7jHv5Fckv1Eh3zZmd0QDiHkUUVN60#_1
http://semanticscience.org/resource/SIO_000139
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http://amigo.geneontology.org/amigo/term/GO:0016301
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http://purl.obolibrary.org/obo/RO_0002204
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http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI_36080
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http://www.ebi.ac.uk/ontology-lookup/?termId=MOD:00000
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http://www.ebi.ac.uk/ontology-lookup/?termId=MOD:00696
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http://purl.obolibrary.org/obo/BFO_0000066
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http://www.w3.org/2000/01/rdf-schema#label
kin(p(HGNC:MAPK9)) -> p(HGNC:JUN,pmod(P,S,73))
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http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel
http://purl.org/dc/elements/1.1/description
Approximately 61,000 statements.
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Copyright (c) 2011-2012, Selventa. All rights reserved.
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http://purl.org/dc/elements/1.1/title
BEL Framework Large Corpus Document
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http://purl.org/pav/authoredBy
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Phosphorylation of c-jun at serines 63 and 73 has also been reported to be involved in mammalian stress responses (45,46). As shown in Figure 9D , c-jun protein levels remained fairly constant after treatment of HME87 cells with BPDE, but highly increased phosphorylation of both Ser63 and Ser73 of c-jun was detected beginning 30 min after BPDE treatment. Phosphorylation at these residues remained higher than control levels for at least 10 h. Phosphorylation of these residues is known to be controlled by the stress activated protein kinases (SAPK), in particular by the jun N-terminal kinase (JNK)
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http://www.w3.org/ns/prov#wasQuotedFrom
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Selventa
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http://www.w3.org/ns/prov#hadPrimarySource
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2014-07-03T14:31:58.884+02:00
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http://orcid.org/0000-0001-6818-334X
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http://purl.org/pav/createdBy
http://orcid.org/0000-0002-1267-0234