Protein Tyrosine Phosphatase Receptor Type E (PTPRE)

PTPR-E; HPTPE; PTPE; R-PTP-EPSILON; Receptor-type tyrosine-protein phosphatase epsilon

SPN	T183
HGNC	9669
MGI	97813
PubMed	8697801
RGD	620771
UniProt	P23469
Wiki	PTPRE

PTPRE 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. Two alternatively spliced transcript variants of this gene have been reported, one of which encodes a receptor-type PTP that possesses a short extracellular domain, a single transmembrane region, and two tandem intracytoplasmic catalytic domains; Another one encodes a PTP that contains a distinct hydrophilic N-terminus, and thus represents a nonreceptor-type isoform of this PTP. Studies of the similar gene in mice suggested the regulatory roles of this PTP in RAS related signal transduction pathways, cytokines induced SATA signaling, as well as the activation of voltage-gated K+ channels.

Reference

"Structural diversity and evolution of human receptor-like protein tyrosine phosphatases."
EMBO J. 9:3241-3252(1990) [PubMed] [Europe PMC] [Abstract]

"Expression of human protein tyrosine phosphatase epsilon in leucocytes: a potential ERK pathway-regulating phosphatase."
Scand. J. Immunol. 56:195-203(2002) [PubMed] [Europe PMC] [Abstract]

"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]

"The DNA sequence and comparative analysis of human chromosome 10."
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Identification of a cytoplasmic, phorbol ester-inducible isoform of protein tyrosine phosphatase epsilon."
Proc. Natl. Acad. Sci. U.S.A. 92:12235-12239(1995) [PubMed] [Europe PMC] [Abstract]

"Protein-tyrosine phosphatase activity regulates osteoclast formation and function: inhibition by alendronate."
Proc. Natl. Acad. Sci. U.S.A. 93:3068-3073(1996) [PubMed] [Europe PMC] [Abstract]

"Distinct promoters control transmembrane and cytosolic protein tyrosine phosphatase epsilon expression during macrophage differentiation."
Eur. J. Biochem. 259:46-54(1999) [PubMed] [Europe PMC] [Abstract]

"Generation of novel cytoplasmic forms of protein tyrosine phosphatase epsilon by proteolytic processing and translational control."
Oncogene 19:4375-4384(2000) [PubMed] [Europe PMC] [Abstract]

"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]

"Large-scale structural analysis of the classical human protein tyrosine phosphatome."
Cell 136:352-363(2009) [PubMed] [Europe PMC] [Abstract]