PTPRE Gene

HGNC Family	Phosphatases
Name	protein tyrosine phosphatase, receptor type, E
Description	The protein encoded by this gene 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. Several alternatively spliced transcript variants of this gene have been reported, at least two of which encode 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, cytokine-induced SATA signaling, as well as the activation of voltage-gated K+ channels. [provided by RefSeq, Oct 2015]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nProtein tyrosine phosphatase receptor type epsilon (PTPRE) is expressed as multiple isoforms – including transmembrane (RPTPε) and cytoplasmic forms – that play central roles in modulating tyrosine phosphorylation‐dependent signaling. Studies have shown that the catalytic domains of these isoforms interact in complex manners, with mechanisms such as dimerization (often enhanced by oxidative stress) and regulation by ancillary domains determining their substrate specificity and overall activity. Such regulatory processes have been detailed by analyses of the domain interactions and the formation of receptor complexes, highlighting the contribution of distinct terminal regions in maintaining functional control of phosphatase action."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": "\n\nIn addition to these regulatory mechanisms, PTPRE has been shown to critically impact mitogen-activated protein kinase (MAPK) signaling pathways. It can function as a physiological inhibitor of ERK1/2 activity by reducing their phosphorylation, a process that may occur directly or indirectly—via dephosphorylation of adaptor proteins such as Shc. Paradoxically, in certain oncogenic contexts (for example, under Neu-induced conditions), PTPRE may also contribute to Src activation, thereby facilitating mitogenic responses and cell survival, as observed in human breast cancer cell lines."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "7"}]}, {"type": "t", "text": "\n\nBeyond its role in regulating kinase cascades, PTPRE is also implicated in several physiological and pathological contexts. In the immune system, for instance, a hepatitis C virus (HCV)-derived small RNA has been shown to reduce PTPRE expression, thereby impairing T cell receptor (TCR) signaling and potentially contributing to viral persistence. Moreover, genetic association studies have linked certain PTPRE polymorphisms to a protective effect in allergic asthma and atopy. In addition, distinct PTPRE isoforms have been found to mediate leukotriene-dependent migration of monocyte-derived macrophages, to influence oligodendrocyte differentiation and optic nerve myelination, and have been implicated in the progression of thyroid carcinoma."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "T Wabakken, H Hauge, E F Finne, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Expression of human protein tyrosine phosphatase epsilon in leucocytes: a potential ERK pathway-regulating phosphatase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Scand J Immunol (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1046/j.1365-3083.2002.01126.x"}], "href": "https://doi.org/10.1046/j.1365-3083.2002.01126.x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12121439"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12121439"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "T Wabakken, H Hauge, S Funderud, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Characterization, expression and functional aspects of a novel protein tyrosine phosphatase epsilon isoform."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Scand J Immunol (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1046/j.1365-3083.2002.01127.x"}], "href": "https://doi.org/10.1046/j.1365-3083.2002.01127.x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12193229"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12193229"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Christophe Blanchetot, Leon G Tertoolen, John Overvoorde, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M205810200"}], "href": "https://doi.org/10.1074/jbc.M205810200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12376545"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12376545"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Hila Toledano-Katchalski, Zohar Tiran, Tal Sines, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Dimerization in vivo and inhibition of the nonreceptor form of protein tyrosine phosphatase epsilon."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.23.15.5460-5471.2003"}], "href": "https://doi.org/10.1128/MCB.23.15.5460-5471.2003"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12861030"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12861030"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Hila Toledano-Katchalski, Judith Kraut, Tal Sines, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein tyrosine phosphatase epsilon inhibits signaling by mitogen-activated protein kinases."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cancer Res (2003)"}]}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12754301"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12754301"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Judith Kraut-Cohen, William J Muller, Ari Elson "}, {"type": "b", "children": [{"type": "t", "text": "Protein-tyrosine phosphatase epsilon regulates Shc signaling in a kinase-specific manner: increasing coherence in tyrosine phosphatase signaling."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M708822200"}], "href": "https://doi.org/10.1074/jbc.M708822200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18093973"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18093973"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Caroline E Nunes-Xavier, Ari Elson, Rafael Pulido "}, {"type": "b", "children": [{"type": "t", "text": "Epidermal growth factor receptor (EGFR)-mediated positive feedback of protein-tyrosine phosphatase epsilon (PTPepsilon) on ERK1/2 and AKT protein pathways is required for survival of human breast cancer cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M111.293928"}], "href": "https://doi.org/10.1074/jbc.M111.293928"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22117074"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22117074"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Karine Tremblay, Mathieu Lemire, Camille Potvin, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Genes to diseases (G2D) computational method to identify asthma candidate genes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS One (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pone.0002907"}], "href": "https://doi.org/10.1371/journal.pone.0002907"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18682798"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18682798"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "William Murk, Kyle Walsh, Ling-I Hsu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Attempted replication of 50 reported asthma risk genes identifies a SNP in RAD50 as associated with childhood atopic asthma."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hum Hered (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1159/000319536"}], "href": "https://doi.org/10.1159/000319536"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21734400"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21734400"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Nirjal Bhattarai, James H McLinden, Jinhua Xiang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Hepatitis C virus infection inhibits a Src-kinase regulatory phosphatase and reduces T cell activation in vivo."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS Pathog (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.ppat.1006232"}], "href": "https://doi.org/10.1371/journal.ppat.1006232"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28235043"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28235043"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Fanny Lapointe, Sylvie Turcotte, Joanny Roy, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RPTPε promotes M2-polarized macrophage migration through ROCK2 signaling and podosome formation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.234641"}], "href": "https://doi.org/10.1242/jcs.234641"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31722979"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31722979"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Naser Muja, Gabor Lovas, Elena Romm, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Expression of a catalytically inactive transmembrane protein tyrosine phosphatase epsilon (tm-PTP epsilon) delays optic nerve myelination."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Glia (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/glia.20078"}], "href": "https://doi.org/10.1002/glia.20078"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15390114"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15390114"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Chen Peng, Chunming Zhang, Wenjie Yu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Receptor Type Protein Tyrosine Phosphatase Epsilon (PTPRE) Plays an Oncogenic Role in Thyroid Carcinoma by Activating the AKT and ERK1/2 Signaling Pathway."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Curr Cancer Drug Targets (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.2174/1568009623666230118111745"}], "href": "https://doi.org/10.2174/1568009623666230118111745"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36654463"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36654463"}]}]}]}
Synonyms	HPTPE, R-PTP-EPSILON, PTPE
Proteins	PTPRE_HUMAN
NCBI Gene ID	5791
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

PTPRE has 7,577 functional associations with biological entities spanning 8 categories (molecular profile, organism, chemical, functional term, phrase or reference, disease, phenotype or trait, structural feature, cell line, cell type or tissue, gene, protein or microRNA) extracted from 125 datasets.

Click the + buttons to view associations for PTPRE from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

PTPRE Gene

Functional Associations

Please acknowledge the Harmonizome in your publications by citing the following reference(s):

	Dataset	Summary
	Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of PTPRE gene relative to other tissues from the Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles dataset.
	Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles	tissues with high or low expression of PTPRE gene relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.
	Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles	tissue samples with high or low expression of PTPRE gene relative to other tissue samples from the Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles dataset.
	Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by Microarray	tissue samples with high or low expression of PTPRE gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by Microarray dataset.
	Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq	tissue samples with high or low expression of PTPRE gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq dataset.
	Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of PTPRE gene relative to other tissues from the Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles dataset.
	BioGPS Cell Line Gene Expression Profiles	cell lines with high or low expression of PTPRE gene relative to other cell lines from the BioGPS Cell Line Gene Expression Profiles dataset.
	BioGPS Human Cell Type and Tissue Gene Expression Profiles	cell types and tissues with high or low expression of PTPRE gene relative to other cell types and tissues from the BioGPS Human Cell Type and Tissue Gene Expression Profiles dataset.
	BioGPS Mouse Cell Type and Tissue Gene Expression Profiles	cell types and tissues with high or low expression of PTPRE gene relative to other cell types and tissues from the BioGPS Mouse Cell Type and Tissue Gene Expression Profiles dataset.
	Carcinogenome Chemical Perturbation Carcinogenicity Signatures	small molecule perturbations changing expression of PTPRE gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of PTPRE gene relative to other cell lines from the CCLE Cell Line Gene CNV Profiles dataset.
	CCLE Cell Line Gene Expression Profiles	cell lines with high or low expression of PTPRE gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with PTPRE protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with PTPRE gene from the CellMarker Gene-Cell Type Associations dataset.
	ChEA Transcription Factor Binding Site Profiles	transcription factor binding site profiles with transcription factor binding evidence at the promoter of PTPRE gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of PTPRE gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets dataset.
	ChEA Transcription Factor Targets 2022	transcription factors binding the promoter of PTPRE gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
	CM4AI U2OS Cell Map Protein Localization Assemblies	assemblies containing PTPRE protein from integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.
	CMAP Signatures of Differentially Expressed Genes for Small Molecules	small molecule perturbations changing expression of PTPRE gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing PTPRE protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing PTPRE protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores	cellular components containing PTPRE protein in low- or high-throughput protein localization assays from the COMPARTMENTS Experimental Protein Localization Evidence Scores dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores 2025	cellular components containing PTPRE protein in low- or high-throughput protein localization assays from the COMPARTMENTS Experimental Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores	cellular components co-occuring with PTPRE protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025	cellular components co-occuring with PTPRE protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
	COSMIC Cell Line Gene CNV Profiles	cell lines with high or low copy number of PTPRE gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with PTPRE gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with PTPRE gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with PTPRE gene/protein from the curated CTD Gene-Disease Associations dataset.
	dbGAP Gene-Trait Associations	traits associated with PTPRE gene in GWAS and other genetic association datasets from the dbGAP Gene-Trait Associations dataset.
	DeepCoverMOA Drug Mechanisms of Action	small molecule perturbations with high or low expression of PTPRE protein relative to other small molecule perturbations from the DeepCoverMOA Drug Mechanisms of Action dataset.
	DepMap CRISPR Gene Dependency	cell lines with fitness changed by PTPRE gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with PTPRE gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores 2025	diseases co-occuring with PTPRE gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.
	DisGeNET Gene-Disease Associations	diseases associated with PTPRE gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DrugBank Drug Targets	interacting drugs for PTPRE protein from the curated DrugBank Drug Targets dataset.
	ENCODE Histone Modification Site Profiles	histone modification site profiles with high histone modification abundance at PTPRE gene from the ENCODE Histone Modification Site Profiles dataset.
	ENCODE Transcription Factor Binding Site Profiles	transcription factor binding site profiles with transcription factor binding evidence at the promoter of PTPRE gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of PTPRE gene in ChIP-seq datasets from the ENCODE Transcription Factor Targets dataset.
	ESCAPE Omics Signatures of Genes and Proteins for Stem Cells	PubMedIDs of publications reporting gene signatures containing PTPRE from the ESCAPE Omics Signatures of Genes and Proteins for Stem Cells dataset.