PTPRB

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 contains an extracellular domain, a single transmembrane segment and one intracytoplasmic catalytic domain, thus belongs to receptor type PTP. The extracellular region of this PTP is composed of multiple fibronectin type_III repeats, which was shown to interact with neuronal receptor and cell adhesion molecules, such as contactin and tenascin C. This protein was also found to interact with sodium channels, and thus may regulate sodium channels by altering tyrosine phosphorylation status. The functions of the interaction partners of this protein implicate the roles of this PTP in cell adhesion, neurite growth, and neuronal differentiation.

Full Name

Protein tyrosine phosphatase, receptor type B

Function

Plays an important role in blood vessel remodeling and angiogenesis. Not necessary for the initial formation of blood vessels, but is essential for their maintenance and remodeling. Can induce dephosphorylation of TEK/TIE2, CDH5/VE-cadherin and KDR/VEGFR-2. Regulates angiopoietin-TIE2 signaling in endothelial cells. Acts as a negative regulator of TIE2, and controls TIE2 driven endothelial cell proliferation, which in turn affects blood vessel remodeling during embryonic development and determines blood vessel size during perinatal growth. Essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells and this requires the presence of plakoglobin (By similarity).

Biological Process

AngiogenesisManual Assertion Based On ExperimentIBA:GO_Central
DephosphorylationManual Assertion Based On ExperimentIDA:UniProtKB
Glial cell migrationIEA:Ensembl
Peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activityManual Assertion Based On ExperimentIBA:GO_Central
Phosphate-containing compound metabolic processManual Assertion Based On ExperimentTAS:ProtInc
Protein dephosphorylationManual Assertion Based On ExperimentTAS:ProtInc

Cellular Location

Membrane

Topology

Extracellular: 23-1621
Helical: 1622-1642
Cytoplasmic: 1643-1997