LYN
Gene Ontology Biological Process
- B cell homeostasis [ISS]
- Fc receptor mediated inhibitory signaling pathway [ISS]
- Fc receptor mediated stimulatory signaling pathway [IBA, ISS]
- Fc-epsilon receptor signaling pathway [TAS]
- Fc-gamma receptor signaling pathway involved in phagocytosis [TAS]
- JAK-STAT cascade involved in growth hormone signaling pathway [TAS]
- T cell costimulation [TAS]
- blood coagulation [TAS]
- cellular response to DNA damage stimulus [IDA]
- cellular response to peptide hormone stimulus [IBA]
- cellular response to retinoic acid [IMP]
- central nervous system development [IBA]
- dendritic cell differentiation [IBA, ISS]
- erythrocyte differentiation [ISS]
- immune response-regulating cell surface receptor signaling pathway [ISS, TAS]
- inflammatory response [IBA]
- innate immune response [IBA, TAS]
- leukocyte migration [TAS]
- lipopolysaccharide-mediated signaling pathway [ISS]
- negative regulation of B cell proliferation [IBA]
- negative regulation of ERK1 and ERK2 cascade [ISS]
- negative regulation of MAP kinase activity [ISS]
- negative regulation of cell proliferation [IMP]
- negative regulation of immune response [TAS]
- negative regulation of intracellular signal transduction [ISS]
- negative regulation of mast cell proliferation [IBA, ISS]
- negative regulation of protein phosphorylation [ISS]
- negative regulation of toll-like receptor 2 signaling pathway [ISS]
- negative regulation of toll-like receptor 4 signaling pathway [ISS]
- peptidyl-tyrosine autophosphorylation [IBA]
- peptidyl-tyrosine phosphorylation [IDA]
- platelet activation [TAS]
- platelet degranulation [IBA, ISS]
- positive regulation of cell proliferation [ISS]
- positive regulation of cellular component movement [IDA]
- positive regulation of dendritic cell apoptotic process [IBA, ISS]
- positive regulation of mast cell proliferation [IMP]
- positive regulation of neuron projection development [IMP]
- positive regulation of stress-activated protein kinase signaling cascade [IDA]
- positive regulation of tyrosine phosphorylation of STAT protein [ISS]
- protein autophosphorylation [IDA]
- protein phosphorylation [IDA]
- regulation of B cell apoptotic process [IBA]
- regulation of B cell receptor signaling pathway [IBA, ISS]
- regulation of ERK1 and ERK2 cascade [ISS]
- regulation of cell adhesion mediated by integrin [IMP]
- regulation of cytokine production [ISS]
- regulation of erythrocyte differentiation [ISS]
- regulation of mast cell activation [ISS]
- regulation of mast cell degranulation [IBA, ISS]
- regulation of monocyte chemotaxis [IMP]
- regulation of platelet aggregation [IBA, ISS]
- regulation of protein phosphorylation [TAS]
- response to hormone [ISS]
- signal transduction [TAS]
- signal transduction by phosphorylation [TAS]
- tolerance induction to self antigen [IBA, ISS, TAS]
- transmembrane receptor protein tyrosine kinase signaling pathway [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
PPP1R8
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Biochemical Activity (Phosphorylation)
An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.
Publication
The C-terminus of NIPP1 (nuclear inhibitor of protein phosphatase-1) contains a novel binding site for protein phosphatase-1 that is controlled by tyrosine phosphorylation and RNA binding.
Nuclear inhibitor of protein phosphatase-1 (NIPP1; 351 residues) is a nuclear RNA-binding protein that also contains in its central domain two contiguous sites of interaction with the catalytic subunit of protein phosphatase-1 (PP1(C)). We show here that mutation of these phosphatase-interaction sites did not completely abolish the ability of NIPP1 to bind and inhibit PP1(C). This could be accounted for ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID