UniProt functional annotation for P35236

UniProt code: P35236.

Organism: Homo sapiens (Human).
Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Function: Protein phosphatase that acts preferentially on tyrosine-phosphorylated MAPK1. Plays a role in the regulation of T and B-lymphocyte development and signal transduction. {ECO:0000269|PubMed:10206983, ECO:0000269|PubMed:10559944, ECO:0000269|PubMed:10702794, ECO:0000269|PubMed:1510684, ECO:0000269|PubMed:1530918, ECO:0000269|PubMed:9624114}.
Catalytic activity: Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
Enzyme regulation: Inhibited in cells after FCER1A triggering. {ECO:0000250}.
Subunit: Monomer. Interacts with MAPK1, MAPK3 and several other MAP kinases. {ECO:0000269|PubMed:10206983, ECO:0000269|PubMed:10559944, ECO:0000269|PubMed:10702794, ECO:0000269|PubMed:16226275, ECO:0000269|PubMed:16441242, ECO:0000269|PubMed:16765894, ECO:0000269|PubMed:9624114}.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14613483}. Cytoplasm, cytoskeleton {ECO:0000250}.
Tissue specificity: Expressed exclusively in thymus and spleen. {ECO:0000269|PubMed:1510684, ECO:0000269|PubMed:1530918}.
Ptm: Phosphorylated on serine residues in resting T-cells. Phosphorylation increases upon exposure to stimuli that increase intracellular cAMP levels. Phosphorylation leads to dissociation of bound MAP kinases. {ECO:0000269|PubMed:10206983, ECO:0000269|PubMed:10559944, ECO:0000269|PubMed:14613483}.
Ptm: Oxidized at active site cysteine. Treatment with pervanadate (vanadate and H(2)O(2)) or with antigen enhanced oxidation of active site cysteine (By similarity). {ECO:0000250}.
Similarity: Belongs to the protein-tyrosine phosphatase family. Non-receptor class subfamily. {ECO:0000305}.
Sequence caution: Sequence=AAA59531.1; Type=Frameshift; Positions=5; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.