<http://linkedlifedata.com/resource/#_513959364636002E> <http://www.w3.org/1999/02/22-rdf-syntax-ns#type> <http://www.w3.org/1999/02/22-rdf-syntax-ns#Statement> .
<http://linkedlifedata.com/resource/#_513959364636002E> <http://purl.uniprot.org/core/attribution> <http://linkedlifedata.com/resource/#_513959364636001F> .
<http://linkedlifedata.com/resource/#_513959364636002E> <http://www.w3.org/1999/02/22-rdf-syntax-ns#subject> <http://purl.uniprot.org/SHA-384/11F8FD8DEA14A8011356A9A743DC88D4E1F3BBE534C938AD6F454142F7B2A023CD18EDC73A7EB3E861CA94CF4DD74E39> .
<http://linkedlifedata.com/resource/#_513959364636002E> <http://www.w3.org/1999/02/22-rdf-syntax-ns#predicate> <http://www.w3.org/2000/01/rdf-schema#comment> .
<http://linkedlifedata.com/resource/#_513959364636002E> <http://www.w3.org/1999/02/22-rdf-syntax-ns#object> "Phosphorylated by PRKG1/cGKI-beta; Ser-367 showed constitutive phosphorylation in platelets Whereas Ser-657 is only phosphorylated in presence of cGMP and nitric oxide (NO); Ser-670 is phosphorylated in resting platelets but increases in presence of cGMP and NO. PRKG1 inhibitor prevents phosphorylation of Ser-657 and Ser-670 in response to NO and cGMP." .