Alternative titles; symbols
HGNC Approved Gene Symbol: PTPRB
Cytogenetic location: 12q15 Genomic coordinates (GRCh38): 12:70,515,870-70,637,429 (from NCBI)
For background information on protein-tyrosine phosphatases (PTPases), see 176884.
By screening a human brainstem cDNA library with a leukocyte common antigen (LCA, or PTPRC; 151460) probe spanning both conserved cytoplasmic domains, Kaplan et al. (1990) isolated clones encoding the alpha polypeptide (PTPRA; 176884) of the receptor-type PTPases, as well as partial clones for 2 other tyrosine phosphatases, beta (PTPRB) and gamma (PTPRG; 176886).
By screening a human placenta cDNA library with Drosophila Ptp, Krueger et al. (1990) cloned several PTPases, including PTPRB, which they called PTP-beta. The deduced 1,997-amino acid protein has an N-terminal signal peptide, followed by an extracellular receptor-like domain, a transmembrane segment, and a cytoplasmic region containing a characteristic PTPase domain. The extracellular region contains 16 repeated fibronectin (FN1; 135600) type III domains of about 90 amino acids each, followed by a putative proline-rich hinge region before the transmembrane segment. Krueger et al. (1990) also identified a PTP-beta splice variant predicted to alter the extracellular region of the protein.
Using the cytoplasmic segment of human PTP-beta expressed in E. coli, Krueger et al. (1990) confirmed that PTP-beta had robust PTPase activity against phosphorylated test substrates.
Using a cDNA probe for in situ hybridization, Harder et al. (1992) mapped the PTPRB gene to chromosome 12q15-q21.
Dominguez et al. (2007) replaced mouse Veptp with a reporter gene and found that Veptp was expressed in endothelium and in the developing outflow tract of the heart, with later expression in developing heart valves. Embryonic Veptp-null mice died due to a variety of angiogenic defects in the embryo and yolk sac, including failure of remodeling of the vascular plexus into large veins and branched vascular networks. Dominguez et al. (2007) concluded that VEPTP is essential for cardiovascular development and proposed that its continued expression in adult mouse suggests that it may have a role in vascular homeostasis and may be involved in pathologic angiogenesis of tumors.
Dominguez, M. G., Hughes, V. C., Pan, L., Simmons, M., Daly, C., Anderson, K., Noguera-Troise, I., Murphy, A. J., Valenzuela, D. M., Davis, S., Thurston, G., Yancopoulos, G. D., Gale, N. W. Vascular endothelial tyrosine phosphatase (VE-PTP)-null mice undergo vasculogenesis but die embryonically because of defects in angiogenesis. Proc. Nat. Acad. Sci. 104: 3243-3248, 2007. [PubMed: 17360632] [Full Text: https://doi.org/10.1073/pnas.0611510104]
Harder, K. W., Anderson, L. L., Duncan, A. M. V., Jirik, F. R. The gene for receptor-like protein tyrosine phosphatase (PTPRB) is assigned to chromosome 12q15-q21. Cytogenet. Cell Genet. 61: 269-270, 1992. [PubMed: 1486802] [Full Text: https://doi.org/10.1159/000133419]
Kaplan, R., Morse, B., Huebner, K., Croce, C., Howk, R., Ravera, M., Ricca, G., Jaye, M., Schlessinger, J. Cloning of three human tyrosine phosphatases reveals a multigene family of receptor-linked protein-tyrosine-phosphatases expressed in brain. Proc. Nat. Acad. Sci. 87: 7000-7004, 1990. [PubMed: 2169617] [Full Text: https://doi.org/10.1073/pnas.87.18.7000]
Krueger, N. X., Streuli, M., Saito, H. Structural diversity and evolution of human receptor-like protein tyrosine phosphatases. EMBO J. 9: 3241-3252, 1990. [PubMed: 2170109] [Full Text: https://doi.org/10.1002/j.1460-2075.1990.tb07523.x]