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| http://purl.uniprot.org/keywords/1126 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/keywords/1090 |
| http://purl.uniprot.org/keywords/1126 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/keywords/899 |
| http://purl.uniprot.org/keywords/1126 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/keywords/922 |
| http://purl.uniprot.org/keywords/1126 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/keywords/1114 |
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| http://purl.uniprot.org/keywords/1126 | http://www.w3.org/2000/01/rdf-schema#comment | "Protein phosphatase-1 (PP1) is a member of the Serine/Threonine phosphatases. The enzyme regulates many important physiological processes, including gene transcription, translation, metabolism, cell growth and division. Different viruses including asfivirus, herpes simplex virus or papillomavirus interact with and modulate PPP1 phosphatase activity to dephosphorylate specific cellular substrates including EIF2S1. Upon viral infection, the host PKR/EIF2AK2 triggers the phosphorylation of EIF2S1 leading to a complete translational shut-off. By dephosphroylating EIF2S1 with PPP1CA, viruses manage to circumvent this antiviral response and prevent translational shut-off."xsd:string |
| http://purl.uniprot.org/keywords/1126 | http://www.w3.org/2000/01/rdf-schema#seeAlso | http://purl.obolibrary.org/obo/GO_0004865 |
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| http://purl.uniprot.org/keywords/1126 | http://www.w3.org/2004/02/skos/core#prefLabel | "Modulation of host PP1 activity by virus"xsd:string |
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