Protein Variants | Comment | Organism |
---|---|---|
C453S | a catalytically inactive, dominant negative mutant of SHP-1 | Mus musculus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytoplasm | - |
Mus musculus | 5737 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
female wild-type C57BL/6 mice | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | SHP-1 has a C-terminal tail containing at least two tyrosine phosphorylation sites | Mus musculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
hematopoietic cell | primary | Mus musculus | - |
macrophage | bone-marrow-derived | Mus musculus | - |
Subunits | Comment | Organism |
---|---|---|
More | SHP-1 has two SH2 domains at its N terminus and a C-terminal tail containing at least two tyrosine phosphorylation sites | Mus musculus |
Synonyms | Comment | Organism |
---|---|---|
More | SHP-1 is a member of SH2 domain-containing PTP subfamily | Mus musculus |
protein tyrosine phosphatase | - |
Mus musculus |
SHP-1 | - |
Mus musculus |
General Information | Comment | Organism |
---|---|---|
malfunction | bone marrow-derived macrophages lacking significant SHP-1 activity display a profound defect in interleukin-12p40 synthesis in response to lipopolysaccharide, peptidoglycan, and synthetic Toll-like receptor ligands, while producing normal amounts of other proinflammatory cytokines, such as TNFalpha and interleukin-6 | Mus musculus |
physiological function | SHP-1 plays critical roles in regulation of many receptor-mediated signaling cascades in the immune system, and it represents a mechanism for host regulation of a specific proinflammatory cytokine important in both innate and adaptive immunity. It is required for SHP-1 in interleukin-12/23 p40 production in response to Toll-like receptor stimulation in macrophages. SHP-1 regulation of interleukin-12p40 transcription requires both its catalytic activity and phosphotyrosine binding by its N-terminal SH2 domain and is mediated via repression of, and interaction with, phosphatidylinositol 3-kinase, without affecting c-Rel activation, overview | Mus musculus |