Receptor-type tyrosine-protein phosphatase U-like, Fn3 domain
IPR057598
Definition
This entry represents the fourth divergent fibronectin type 3 domain found in a group of Receptor-type tyrosine-protein phosphatases (PTPR) including PTPR U, kappa, mu, T and related proteins. This domain is closest to the transmembrane α-helix. PTPRU, also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs). It regulates CTNNB1 function both in cell adhesion and signalling. It may function in cell proliferation and migration and play a role in the maintenance of epithelial integrity. May play a role in megakaryocytopoiesis [[cite:PMID:10397721], [cite:PMID:12501215], [cite:PMID:16574648]]. Protein tyrosine (pTyr) phosphorylation is a common post-translational modification which can create novel recognition motifs for protein interactions and cellular localisation, affect protein stability, and regulate enzyme activity. Consequently, maintaining an appropriate level of protein tyrosine phosphorylation is essential for many cellular functions. Tyrosine-specific protein phosphatases (PTPase; [ec:3.1.3.48]) catalyse the removal of a phosphate group attached to a tyrosine residue, using a cysteinyl-phosphate enzyme intermediate. These enzymes are key regulatory components in signal transduction pathways (such as the MAP kinase pathway) and cell cycle control, and are important in the control of cell growth, proliferation, differentiation and transformation [[cite:PMID:9818190], [cite:PMID:14625689]]. The PTP superfamily can be divided into four subfamilies PMID:12678841: (1) pTyr-specific phosphatases (2) dual specificity phosphatases (dTyr and dSer/dThr) (3) Cdc25 phosphatases (dTyr and/or dThr) (4) LMW (low molecular weight) phosphatases Based on their cellular localisation, PTPases are also classified as: Receptor-like, which are transmembrane receptors that contain PTPase domains PMID:16672235 Non-receptor (intracellular) PTPases PMID:8948575 All PTPases carry the highly conserved active site motif C(X)5R (PTP signature motif), employ a common catalytic mechanism, and share a similar core structure made of a central parallel β-sheet with flanking α-helices containing a β-loop-α-loop that encompasses the PTP signature motif PMID:9646865. Functional diversity between PTPases is endowed by regulatory domains and subunits.
5 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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