| http://purl.uniprot.org/citations/10339589 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10339589 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10339589 | http://www.w3.org/2000/01/rdf-schema#comment | "Bruton's tyrosine kinase (Btk) is a cytoplasmic tyrosine kinase that is crucial for human and murine B cell development, and its deficiency causes human X-linked agammaglobulinemia and murine X-linked immunodeficiency. In this report, we describe the function of the Btk-binding protein Sab (SH3-domain binding protein that preferentially associates with Btk), which we reported previously as a newly identified Src homology 3 domain-binding protein. Sab was shown to inhibit the auto- and transphosphorylation activity of Btk, which prompted us to propose that Sab functions as a transregulator of Btk. Forced overexpression of Sab in B cells led to the reduction of B cell antigen receptor-induced tyrosine phosphorylation of Btk and significantly reduced both early and late B cell antigen receptor-mediated events, including calcium mobilization, inositol 1, 4,5-trisphosphate production, and apoptotic cell death, where the involvement of Btk activity has been demonstrated previously. Together, these results indicate the negative regulatory role of Sab in the B cell cytoplasmic tyrosine kinase pathway."xsd:string |
| http://purl.uniprot.org/citations/10339589 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.96.11.6341"xsd:string |
| http://purl.uniprot.org/citations/10339589 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.96.11.6341"xsd:string |
| http://purl.uniprot.org/citations/10339589 | http://purl.uniprot.org/core/author | "Baba Y."xsd:string |
| http://purl.uniprot.org/citations/10339589 | http://purl.uniprot.org/core/author | "Baba Y."xsd:string |
| http://purl.uniprot.org/citations/10339589 | http://purl.uniprot.org/core/author | "Hashimoto S."xsd:string |
| http://purl.uniprot.org/citations/10339589 | http://purl.uniprot.org/core/author | "Hashimoto S."xsd:string |
| http://purl.uniprot.org/citations/10339589 | http://purl.uniprot.org/core/author | "Kishimoto T."xsd:string |
| http://purl.uniprot.org/citations/10339589 | http://purl.uniprot.org/core/author | "Kishimoto T."xsd:string |
| http://purl.uniprot.org/citations/10339589 | http://purl.uniprot.org/core/author | "Kurosaki M."xsd:string |
| http://purl.uniprot.org/citations/10339589 | http://purl.uniprot.org/core/author | "Kurosaki M."xsd:string |
| http://purl.uniprot.org/citations/10339589 | http://purl.uniprot.org/core/author | "Kurosaki T."xsd:string |
| http://purl.uniprot.org/citations/10339589 | http://purl.uniprot.org/core/author | "Kurosaki T."xsd:string |
| http://purl.uniprot.org/citations/10339589 | http://purl.uniprot.org/core/author | "Mastushita M."xsd:string |
| http://purl.uniprot.org/citations/10339589 | http://purl.uniprot.org/core/author | "Mastushita M."xsd:string |
| http://purl.uniprot.org/citations/10339589 | http://purl.uniprot.org/core/author | "Tsukada S."xsd:string |
| http://purl.uniprot.org/citations/10339589 | http://purl.uniprot.org/core/author | "Tsukada S."xsd:string |
| http://purl.uniprot.org/citations/10339589 | http://purl.uniprot.org/core/author | "Yamadori T."xsd:string |
| http://purl.uniprot.org/citations/10339589 | http://purl.uniprot.org/core/author | "Yamadori T."xsd:string |
| http://purl.uniprot.org/citations/10339589 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10339589 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10339589 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/10339589 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |