| http://purl.uniprot.org/citations/10585430 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10585430 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10585430 | http://www.w3.org/2000/01/rdf-schema#comment | "The inhibition of growth hormone (GH) signaling by five members of the GH-inducible suppressor of cytokine signaling (SOCS/CIS) family was investigated in transfected COS cells. Complete inhibition of GH activation of the signal transducer STAT5b and STAT5b-dependent transcriptional activity was observed upon expression of SOCS-1 or SOCS-3, while partial inhibition (CIS, SOCS-2) or no inhibition (SOCS-6) was seen with other SOCS/CIS family members. SOCS-1, SOCS-2, SOCS-3, and CIS each strongly inhibited the GH receptor (GHR)-dependent tyrosine phosphorylation of JAK2 seen at low levels of transfected JAK2; however, only SOCS-1 strongly inhibited the GHR-independent tyrosine phosphorylation of JAK2 seen at higher JAK2 levels. To probe for interactions with GHR, in vitro binding assays were carried out using glutathione S-transferase-GHR fusion proteins containing variable lengths of GHR's COOH-terminal cytoplasmic domain. CIS and SOCS-2 bound to fusions containing as few as 80 COOH-terminal GHR residues, provided the fusion protein was tyrosine-phosphorylated. By contrast, SOCS-3 binding required tyrosine-phosphorylated GHR membrane-proximal sequences, SOCS-1 binding was tyrosine phosphorylation-independent, and SOCS-6 did not bind the GHR fusion proteins at all. Mutation of GHR's membrane-proximal tyrosine residues 333 and 338 to phenylalanine suppressed the inhibition by SOCS-3, but not by CIS, of GH signaling to STAT5b. SOCS/CIS proteins can thus inhibit GH signaling to STAT5b by three distinct mechanisms, distinguished by their molecular targets within the GHR-JAK2 signaling complex, as exemplified by SOCS-1 (direct JAK2 kinase inhibition), SOCS-3 (inhibition of JAK2 signaling via membrane-proximal GHR tyrosines 333 and 338), and CIS and SOCS-2 (inhibition via membrane-distal tyrosine(s))."xsd:string |
| http://purl.uniprot.org/citations/10585430 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.274.50.35553"xsd:string |
| http://purl.uniprot.org/citations/10585430 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.274.50.35553"xsd:string |
| http://purl.uniprot.org/citations/10585430 | http://purl.uniprot.org/core/author | "Waxman D.J."xsd:string |
| http://purl.uniprot.org/citations/10585430 | http://purl.uniprot.org/core/author | "Waxman D.J."xsd:string |
| http://purl.uniprot.org/citations/10585430 | http://purl.uniprot.org/core/author | "Ram P.A."xsd:string |
| http://purl.uniprot.org/citations/10585430 | http://purl.uniprot.org/core/author | "Ram P.A."xsd:string |
| http://purl.uniprot.org/citations/10585430 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10585430 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10585430 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/10585430 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/10585430 | http://purl.uniprot.org/core/pages | "35553-35561"xsd:string |
| http://purl.uniprot.org/citations/10585430 | http://purl.uniprot.org/core/pages | "35553-35561"xsd:string |
| http://purl.uniprot.org/citations/10585430 | http://purl.uniprot.org/core/title | "SOCS/CIS protein inhibition of growth hormone-stimulated STAT5 signaling by multiple mechanisms."xsd:string |
| http://purl.uniprot.org/citations/10585430 | http://purl.uniprot.org/core/title | "SOCS/CIS protein inhibition of growth hormone-stimulated STAT5 signaling by multiple mechanisms."xsd:string |
| http://purl.uniprot.org/citations/10585430 | http://purl.uniprot.org/core/volume | "274"xsd:string |
| http://purl.uniprot.org/citations/10585430 | http://purl.uniprot.org/core/volume | "274"xsd:string |
| http://purl.uniprot.org/citations/10585430 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10585430 |
| http://purl.uniprot.org/citations/10585430 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10585430 |
| http://purl.uniprot.org/citations/10585430 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10585430 |
| http://purl.uniprot.org/citations/10585430 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10585430 |
| http://purl.uniprot.org/uniprot/P16310 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/10585430 |
| http://purl.uniprot.org/uniprot/#_P16310-citation-10585430 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/10585430 |