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http://purl.uniprot.org/citations/9353338http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9353338http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9353338http://www.w3.org/2000/01/rdf-schema#comment"We cloned and characterized a novel human member of the STE20 serine/threonine protein kinase family named mst-3. Based on its domain structure, mst-3 belongs to the SPS1 subgroup of STE20-like proteins, which includes germinal center (GC) kinase, hematopoietic progenitor kinase (HPK), kinase homologous to STE20/SPS-1 (KHS), kinases responsive to stress (KRS1/2), the mammalian STE20-like kinases (mst1/2), and the recently published STE20/oxidant stress response kinase SOK-1. mst-3 is most closely related to SOK-1, with 88% amino acid similarity in the kinase domain. The similarity of the mst-3 kinase domain to STE20 is 42%. The mst-3 transcript is ubiquitously expressed, and the protein was found in all human, mouse, and monkey cell lines tested. An in vitro kinase assay showed that mst-3 can phosphorylate basic exogenous substrates as well as itself. Interestingly, mst-3 prefers Mn2+ to Mg2+ as a divalent cation and can use both GTP and ATP as phosphate donors. Like SOK-1, mst-3 is activated by autophosphorylation. However, a physiological stimulus of mst-3 activity was not identified. mst-3 activity does not change upon exposure to several mitogenic and stress stimuli. Overexpression of mst-3 wild-type or kinase dead protein affects neither the extracellular signal-regulated kinases (ERK1/2 or ERK6), c-Jun N-terminal kinase (JNK), p38, nor pp70S6 kinase, suggesting that mst-3 is part of a novel signaling pathway."xsd:string
http://purl.uniprot.org/citations/9353338http://purl.org/dc/terms/identifier"doi:10.1074/jbc.272.45.28695"xsd:string
http://purl.uniprot.org/citations/9353338http://purl.org/dc/terms/identifier"doi:10.1074/jbc.272.45.28695"xsd:string
http://purl.uniprot.org/citations/9353338http://purl.uniprot.org/core/author"Blenis J."xsd:string
http://purl.uniprot.org/citations/9353338http://purl.uniprot.org/core/author"Blenis J."xsd:string
http://purl.uniprot.org/citations/9353338http://purl.uniprot.org/core/author"Schinkmann K."xsd:string
http://purl.uniprot.org/citations/9353338http://purl.uniprot.org/core/author"Schinkmann K."xsd:string
http://purl.uniprot.org/citations/9353338http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9353338http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9353338http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9353338http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9353338http://purl.uniprot.org/core/pages"28695-28703"xsd:string
http://purl.uniprot.org/citations/9353338http://purl.uniprot.org/core/pages"28695-28703"xsd:string
http://purl.uniprot.org/citations/9353338http://purl.uniprot.org/core/title"Cloning and characterization of a human STE20-like protein kinase with unusual cofactor requirements."xsd:string
http://purl.uniprot.org/citations/9353338http://purl.uniprot.org/core/title"Cloning and characterization of a human STE20-like protein kinase with unusual cofactor requirements."xsd:string
http://purl.uniprot.org/citations/9353338http://purl.uniprot.org/core/volume"272"xsd:string
http://purl.uniprot.org/citations/9353338http://purl.uniprot.org/core/volume"272"xsd:string
http://purl.uniprot.org/citations/9353338http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9353338
http://purl.uniprot.org/citations/9353338http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9353338
http://purl.uniprot.org/citations/9353338http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9353338
http://purl.uniprot.org/citations/9353338http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9353338
http://purl.uniprot.org/uniprot/Q9Y6E0http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9353338
http://purl.uniprot.org/uniprot/Q9Y6E0#attribution-A39DBF0C73C1E32873B114CE6D11B939http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/9353338