PTPRU

PTPRU is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region, a single transmembrane region, and two tandem intracellular catalytic domains, and thus represents a receptor-type PTP. The extracellular region contains a meprin-A5 antigen-PTP (MAM) domain, Ig-like and fibronectin type III-like repeats. This PTP was thought to play roles in cell-cell recognition and adhesion.

Protein tyrosine phosphatase, receptor type U

Tyrosine-protein phosphatase which dephosphorylates CTNNB1. Regulates CTNNB1 function both in cell adhesion and signaling. May function in cell proliferation and migration and play a role in the maintenance of epithelial integrity. May play a role in megakaryocytopoiesis.

Animal organ regenerationIEA:Ensembl
Cell adhesion1 PublicationNAS:UniProtKB
Cell differentiationIEA:UniProtKB-KW
Homotypic cell-cell adhesionIEA:Ensembl
Negative regulation of canonical Wnt signaling pathwayManual Assertion Based On ExperimentIDA:UniProtKB
Negative regulation of cell migrationManual Assertion Based On ExperimentIDA:UniProtKB
Negative regulation of cell population proliferationManual Assertion Based On ExperimentIDA:UniProtKB
Positive regulation of cell-cell adhesion mediated by cadherinManual Assertion Based On ExperimentIDA:UniProtKB
Protein dephosphorylationManual Assertion Based On ExperimentIDA:UniProtKB
Protein localization to cell surfaceManual Assertion Based On ExperimentIDA:UniProtKB
Response to glucocorticoidIEA:Ensembl
Transmembrane receptor protein tyrosine phosphatase signaling pathway1 PublicationNAS:UniProtKB

Cell junction
Cell membrane

Extracellular: 19-749
Helical: 750-770
Cytoplasmic: 771-1446

The extracellular domain is proteolytically processed through cleavage within the fibronectin type-III 4 domain (By similarity).
In addition to the 190 kDa full-length protein, proteolytic products of 100 kDa, 80 kDa and 73 kDa are observed.
N-glycosylated.
Phosphorylated on tyrosine residues upon activation of KIT with stem cell factor (SCF). The 73 kDa proteolytic product is not phosphorylated.