ID:PTPRU_HUMAN DESCRIPTION: RecName: Full=Receptor-type tyrosine-protein phosphatase U; Short=R-PTP-U; EC=3.1.3.48; AltName: Full=Pancreatic carcinoma phosphatase 2; Short=PCP-2; AltName: Full=Protein-tyrosine phosphatase J; Short=PTP-J; Short=hPTP-J; AltName: Full=Protein-tyrosine phosphatase pi; Short=PTP pi; AltName: Full=Protein-tyrosine phosphatase receptor omicron; Short=PTP-RO; AltName: Full=Receptor-type protein-tyrosine phosphatase psi; Short=R-PTP-psi; Flags: Precursor; FUNCTION: 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. CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate. SUBUNIT: Forms homooligomeric complexes which mediate cell homotypic adhesion (Probable). Interacts (via the cytoplasmic juxtamembrane domain) with CTNNB1; may mediate interaction with the cadherin/catenin adhesion complex. Interacts with KIT. May interact with AP3B1. SUBCELLULAR LOCATION: Cell junction. Cell membrane; Single-pass type I membrane protein. TISSUE SPECIFICITY: High levels in brain, pancreas, and skeletal muscle; less in colon, kidney, liver, stomach, and uterus; not expressed in placenta and spleen. Also detected in heart, prostate, lung, thymus, testis and ovary. Ubiquitously expressed in brain. Expressed by hematopoietic stem cells. DEVELOPMENTAL STAGE: Expressed in fetal brain, lung and kidney. INDUCTION: Up-regulated upon cell contact (at protein level). Down-regulated by phorbol ester (at protein level) and calcium ionophore but up-regulated by phorbol ester in megakaryocytic cells (PubMed:10397721). PTM: The extracellular domain is proteolytically processed through cleavage within the fibronectin type-III 4 domain (By similarity). Beside the 190 kDa full-length protein, proteolytic products of 100 kDa, 80 kDa and 73 kDa are observed. PTM: N-glycosylated. PTM: Phosphorylated on tyrosine residues upon activation of KIT with stem cell factor (SCF). The 73 kDa proteolytic product is not phosphorylated. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Receptor class 2B subfamily. SIMILARITY: Contains 4 fibronectin type-III domains. SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like) domain. SIMILARITY: Contains 1 MAM domain. SIMILARITY: Contains 2 tyrosine-protein phosphatase domains. SEQUENCE CAUTION: Sequence=CAA65016.1; Type=Miscellaneous discrepancy; Note=Several sequencing problems; Sequence=CAA65832.1; Type=Miscellaneous discrepancy; Note=Several sequencing problems;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
Pfam Domains: PF00041 - Fibronectin type III domain PF00102 - Protein-tyrosine phosphatase PF00629 - MAM domain, meprin/A5/mu
SCOP Domains: 48726 - Immunoglobulin 49265 - Fibronectin type III 49899 - Concanavalin A-like lectins/glucanases 52799 - (Phosphotyrosine protein) phosphatases II
ModBase Predicted Comparative 3D Structure on Q92729
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
US Server
Sequence and Links to Tools and Databases 
Common Gene Haplotype Alleles 
