Ptpre protein tyrosine phosphatase receptor type E [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Ptpreprovided by MGI
Official Full Name: protein tyrosine phosphatase receptor type Eprovided by MGI
Primary source: MGI:MGI:97813
See related: Ensembl:ENSMUSG00000041836 AllianceGenome:MGI:97813
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: PTPe; PTPepsilon; RPTPepsilon
Summary: Enables identical protein binding activity and protein tyrosine phosphatase activity. Involved in negative regulation of insulin receptor signaling pathway and regulation of mast cell activation. Acts upstream of or within cell surface receptor protein tyrosine phosphatase signaling pathway. Located in cytoplasm and plasma membrane. Is expressed in midbrain and superior colliculus. Orthologous to human PTPRE (protein tyrosine phosphatase receptor type E). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Ubiquitous expression in lung adult (RPKM 7.9), thymus adult (RPKM 6.2) and 27 other tissues See more
Orthologs: human all
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Genomic context

Location:: 7 F3; 7 81.27 cM

Exon count:: 24

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	7	NC_000073.7 (135139195..135288023)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	7	NC_000073.6 (135537824..135686294)

Chromosome 7 - NC_000073.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

We describe a new regulatory mechanism, where an unreported lncRNA, PTPRE-AS1, targets receptor-type tyrosine protein phosphatase epsilon (PTPRE) to regulate macrophage activation.
Title: LncRNA PTPRE-AS1 modulates M2 macrophage activation and inflammatory diseases by epigenetic promotion of PTPRE.
GRB2 physically links cyt-PTPe with Src and enables cyt-PTPe to activate Src downstream of activated integrins in osteoclast-like cells.
Title: Adaptor protein GRB2 promotes Src tyrosine kinase activation and podosomal organization by protein-tyrosine phosphatase ϵ in osteoclasts.
PTPs alpha and epsilon play distinct roles in osteoclasts.
Title: Protein tyrosine phosphatases ε and α perform nonredundant roles in osteoclasts.
Multifaceted modulation of K+ channels by protein-tyrosine phosphatase epsilon tunes neuronal excitability.
Title: Multifaceted modulation of K+ channels by protein-tyrosine phosphatase ε tunes neuronal excitability.
Integrin activation regulates cyt-PTPe via Src-dependent Y638 phosphorylation. cyt-PTPe affects osteoclast podosome stability by a feedback loop ensuring proper Src activation downstream of integrins, linking their signaling with Src activation.
Title: Protein tyrosine phosphatase epsilon regulates integrin-mediated podosome stability in osteoclasts by activating Src.
Findings demonstrate that PTPalpha is a critical regulator of Fyn activation and of specific Fyn signaling events during differentiation, and is essential for promoting OPC differentiation and central nervous system myelination.
Title: Protein-tyrosine phosphatase alpha acts as an upstream regulator of Fyn signaling to promote oligodendrocyte differentiation and myelination.
Data suggest that PTPepsilon negatively regulates FcepsilonRI-mediated signalling pathways and thus constitutes a novel target for ameliorating allergic conditions.
Title: Protein tyrosine phosphatase epsilon is a negative regulator of FcepsilonRI-mediated mast cell responses.
findings show that PTPe is expressed in erythrocytes & is involved in red cell signaling networks
Title: PTPepsilon has a critical role in signaling transduction pathways and phosphoprotein network topology in red cells.
Protein-tyrosine phosphatase epsilon regulates Shc signaling in a kinase-specific manner: increasing coherence in tyrosine phosphatase signaling
Title: Protein-tyrosine phosphatase epsilon regulates Shc signaling in a kinase-specific manner: increasing coherence in tyrosine phosphatase signaling.
cytosolic PTPepsilon serves as another major candidate negative regulator of insulin receptor signaling in skeletal muscle
Title: Cytosolic protein tyrosine phosphatase-epsilon is a negative regulator of insulin signaling in skeletal muscle.

Submit: New GeneRIF Correction See all GeneRIFs (17)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (3)
Targeted (1) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

D7Mit13 (e-PCR), detects polymorphism
- UniSTS:116745

Ptpre (e-PCR), detects polymorphism
- UniSTS:536487

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables histone H2AXY142 phosphatase activity	IEA Inferred from Electronic Annotation more info
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables non-membrane spanning protein tyrosine phosphatase activity	IEA Inferred from Electronic Annotation more info
enables protein tyrosine phosphatase activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein tyrosine phosphatase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein tyrosine phosphatase activity, metal-dependent	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
acts_upstream_of_or_within cell surface receptor protein tyrosine phosphatase signaling pathway	IDA Inferred from Direct Assay more info	PubMed
involved_in chromatin remodeling	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of insulin receptor signaling pathway	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of insulin receptor signaling pathway	ISO Inferred from Sequence Orthology more info
involved_in regulation of mast cell activation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in signal transduction	IBA Inferred from Biological aspect of Ancestor more info

Component	Evidence Code	Pubs
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
located_in nucleus	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed
located_in plasma membrane	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: receptor-type tyrosine-protein phosphatase epsilon

Names: R-PTP-epsilon; protein-tyrosine phosphatase epsilon

NP_001303607.1

EC 3.1.3.48

NP_001303608.1

EC 3.1.3.48

NP_001303609.1

EC 3.1.3.48

NP_001303610.1

EC 3.1.3.48

NP_035342.3

EC 3.1.3.48

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001316678.1 → NP_001303607.1 receptor-type tyrosine-protein phosphatase epsilon isoform a precursor

Status: VALIDATED

Description

Transcript Variant: This variant (1) encodes the longest isoform (a).

Source sequence(s)

AC123047, AK004602, AK132455, U40280

Consensus CDS

CCDS85444.1

UniProtKB/TrEMBL

A0A1B0GRT6, Q3V1H5

Related

ENSMUSP00000147656.2, ENSMUST00000209256.2

Conserved Domains (2) summary

smart00194
Location:154 → 412

PTPc; Protein tyrosine phosphatase, catalytic domain

cd00047
Location:180 → 412

PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...
NM_001316679.1 → NP_001303608.1 receptor-type tyrosine-protein phosphatase epsilon isoform b precursor

Status: VALIDATED

Description

Transcript Variant: This variant (3) contains an alternate exon in place of the first exon compared to variant 1. The resulting isoform (b) is shorter at the N-terminus compared to isoform a. Variants 2 and 3 both encode the same isoform (b).

Source sequence(s)

AC123047, U40280

Consensus CDS

CCDS21944.1

UniProtKB/Swiss-Prot

P49446, Q3U369, Q60986, Q61042, Q62134, Q62444, Q64496

UniProtKB/TrEMBL

Q3V1H5

Related

ENSMUSP00000147313.2, ENSMUST00000210833.2

Conserved Domains (2) summary

smart00194
Location:134 → 392

PTPc; Protein tyrosine phosphatase, catalytic domain

cd00047
Location:160 → 392

PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...
NM_001316680.1 → NP_001303609.1 receptor-type tyrosine-protein phosphatase epsilon isoform c precursor

Status: VALIDATED

Description

Transcript Variant: This variant (4) contains two alternate exons in place of the first exon compared to variant 1. The resulting isoform (c) has a shorter and distinct N-terminus compared to isoform a.

Source sequence(s)

AC123047, AC151841, BC053408, U40280

Consensus CDS

CCDS85445.1

UniProtKB/TrEMBL

A0A1B0GRH2, Q3V1H5

Related

ENSMUSP00000147524.2, ENSMUST00000211788.2

Conserved Domains (2) summary

smart00194
Location:147 → 405

PTPc; Protein tyrosine phosphatase, catalytic domain

cd00047
Location:173 → 405

PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...
NM_001316681.1 → NP_001303610.1 receptor-type tyrosine-protein phosphatase epsilon isoform d

Status: VALIDATED

Description

Transcript Variant: This variant (5) contains an alternate exon in place of the first exon compared to variant 1. The resulting isoform (d) has a shorter and distinct N-terminus compared to isoform a.

Source sequence(s)

AC123047, AK132455, BY210317, U40280

Consensus CDS

CCDS85446.1

UniProtKB/TrEMBL

Q3V1H5

Related

ENSMUSP00000147613.2, ENSMUST00000209979.2

Conserved Domains (2) summary

smart00194
Location:77 → 335

PTPc; Protein tyrosine phosphatase, catalytic domain

cd00047
Location:103 → 335

PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...
NM_011212.3 → NP_035342.3 receptor-type tyrosine-protein phosphatase epsilon isoform b precursor

See identical proteins and their annotated locations for NP_035342.3

Status: VALIDATED

Description

Transcript Variant: This variant (2) contains an alternate exon in the 5' end compared to variant 1. The resulting isoform (b) is shorter at the N-terminus compared to isoform a. Variants 2 and 3 both encode the same isoform (b).

Source sequence(s)

AC123047, AC151838, AC151841

Consensus CDS

CCDS21944.1

UniProtKB/Swiss-Prot

P49446, Q3U369, Q60986, Q61042, Q62134, Q62444, Q64496

UniProtKB/TrEMBL

Q3V1H5

Related

ENSMUSP00000073616.7, ENSMUST00000073961.8

Conserved Domains (2) summary

smart00194
Location:134 → 392

PTPc; Protein tyrosine phosphatase, catalytic domain

cd00047
Location:160 → 392

PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...