| UniProt functional annotation for P29074 | |||
| UniProt code: P29074. |
| Organism: | Homo sapiens (Human). | |
| Taxonomy: | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. | |
| Function: | Phosphatase that plays a role in immunity, learning, synaptic plasticity or cell homeostasis (PubMed:25825441, PubMed:27246854). Regulates neuronal cell homeostasis by protecting neurons against apoptosis (PubMed:20086240). Negatively regulates TLR4-induced interferon beta production by dephosphorylating adapter TICAM2 and inhibiting subsequent TRAM-TRIF interaction (PubMed:25825441). Dephosphorylates also the immunoreceptor tyrosine-based activation motifs/ITAMs of the TCR zeta subunit and thereby negatively regulates TCR-mediated signaling pathway (By similarity). May act at junctions between the membrane and the cytoskeleton. {ECO:0000250, ECO:0000250|UniProtKB:Q9WU22, ECO:0000269|PubMed:20086240, ECO:0000269|PubMed:25825441, ECO:0000269|PubMed:27246854}. | |
| Catalytic activity: | Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE- ProRule:PRU10044}; | |
| Subunit: | Interacts with MAPK12 (via C-terminus); this interaction abolishes PTPN4 catalytic autoinhibition and thus activates the phosphatase activity. {ECO:0000269|PubMed:27246854}. | |
| Subunit: | (Microbial infection) Interacts with attenuated rabies virus protein G; this interaction is required for virally-induced apoptosis. {ECO:0000269|PubMed:20086240}. | |
| Subcellular location: | Cell membrane {ECO:0000269|PubMed:8910369}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:8910369}. Cytoplasm {ECO:0000269|PubMed:20086240, ECO:0000269|PubMed:8910369}. | |
| Ptm: | Highly phosphorylated on serine and threonine residues but not on tyrosines. {ECO:0000269|PubMed:8910369}. | |
| Ptm: | Cleaved and activated by calpain I/CAPN1. {ECO:0000269|PubMed:8910369}. | |
| Similarity: | Belongs to the protein-tyrosine phosphatase family. Non- receptor class subfamily. {ECO:0000305}. | |
Annotations taken from UniProtKB at the EBI.