UniProt functional annotation for P29350

UniProt code: P29350.

Organism: Homo sapiens (Human).
Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
 
Function: Modulates signaling by tyrosine phosphorylated cell surface receptors such as KIT and the EGF receptor/EGFR. The SH2 regions may interact with other cellular components to modulate its own phosphatase activity against interacting substrates. Together with MTUS1, induces UBE2V2 expression upon angiotensin II stimulation. Plays a key role in hematopoiesis. {ECO:0000269|PubMed:11266449}.
 
Catalytic activity: Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
Subunit: Monomer. Interacts with MTUS1 (By similarity). Interacts with MILR1 (tyrosine-phosphorylated). Interacts with KIT (By similarity). Binds PTPNS1, LILRB1 and LILRB2. Interacts with FCRL2, FCRL3, FCRL4, CD300LF, CDK2 and CD84. Interacts with KIR2DL1; the interaction is enhanced by ARRB2. Interacts (via SH2 1 domain) with ROS1; the interaction is direct and promotes ROS1 dephosphorylation. Interacts with EGFR; inhibits EGFR-dependent activation of MAPK/ERK. Interacts with LYN. Interacts with the tyrosine phosphorylated form of PDPK1. {ECO:0000250, ECO:0000269|PubMed:10574931, ECO:0000269|PubMed:11162587, ECO:0000269|PubMed:11266449, ECO:0000269|PubMed:11414741, ECO:0000269|PubMed:14597715, ECO:0000269|PubMed:15184070, ECO:0000269|PubMed:18604210, ECO:0000269|PubMed:19591923, ECO:0000269|PubMed:21262353, ECO:0000269|PubMed:9285411, ECO:0000269|PubMed:9712903, ECO:0000269|PubMed:9842885}.
Subcellular location: Cytoplasm. Nucleus. Note=In neurons, translocates into the nucleus after treatment with angiotensin II (By similarity). Shuttles between the cytoplasm and nucleus via its association with PDPK1. {ECO:0000250}.
Tissue specificity: Isoform 1 is expressed in hematopoietic cells. Isoform 2 is expressed in non-hematopoietic cells.
Domain: The N-terminal SH2 domain functions as an auto-inhibitory domain, blocking the catalytic domain in the ligand-free close conformation. {ECO:0000269|PubMed:12482860, ECO:0000269|PubMed:21465528}.
Ptm: Phosphorylated on tyrosine residues. Binding of KITLG/SCF to KIT increases tyrosine phosphorylation (By similarity). Phosphorylation at Tyr-564 enhances phosphatase activity. {ECO:0000250, ECO:0000269|PubMed:10574931, ECO:0000269|PubMed:19690332, ECO:0000269|PubMed:7781604}.
Similarity: Belongs to the protein-tyrosine phosphatase family. Non-receptor class 2 subfamily. {ECO:0000305}.
Similarity: Contains 2 SH2 domains. {ECO:0000255|PROSITE- ProRule:PRU00191}.
Similarity: Contains 1 tyrosine-protein phosphatase domain. {ECO:0000255|PROSITE-ProRule:PRU00160}.

Annotations taken from UniProtKB at the EBI.