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Showing PTPN13 — PTPL1 is a alias.

PTPN13

Tyrosine-protein phosphatase non-receptor type 13 · UniProt Q12923

Length
2485 aa
Mass
276.9 kDa
Annotated
2026-06-10
95 papers in source corpus 42 papers cited in narrative 42 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PTPN13 (PTPL1/PTP-BL/FAP-1) is a large cytoplasmic protein tyrosine phosphatase that integrates an N-terminal FERM domain, five PDZ domains, and a C-terminal PTP catalytic domain to act as a membrane-anchored scaffold and negative regulator of tyrosine-kinase signaling (PMID:7929060, PMID:15611135). Its FERM domain binds PtdIns(4,5)P2 directly and is necessary and sufficient to target the protein to the apical plasma membrane and dorsal microvilli of epithelial cells, while a TAPP1/PtdIns(3,4)P2-dependent route mediates inducible membrane recruitment upon oxidative stimulation (PMID:12766187, PMID:14516276). The tandem PDZ array assembles multiprotein complexes through C-terminal-motif recognition, with binding specificity tuned by alternative splicing and intramolecular PDZ1–PDZ2 allostery (PMID:9261095, PMID:10951583, PMID:14596806, PMID:17979300). Through these PDZ-anchored complexes and its catalytic domain, PTPN13 dephosphorylates a broad set of phosphotyrosine substrates—including ephrinB, IRS-1, Her2/ErbB2, Src at the activating Tyr419, TRIP6 at Tyr55, the PI3K regulatory subunit p85β at Tyr655, STAT family proteins, and c-Abl—thereby restraining PI3K/Akt, Ras/RAF/MEK/ERK, Src/FAK, and STAT signaling and promoting apoptosis while suppressing tumor cell invasion and migration (PMID:11983165, PMID:12354757, PMID:17638892, PMID:17982484, PMID:17591779, PMID:19734941, PMID:20501847, PMID:23604317, PMID:17306571, PMID:28924170, PMID:31938048). Beyond catalysis, PTPN13 also functions as a phosphatase-independent scaffold: it anchors PTEN at the apical membrane and competitively sequesters IGF2BP1 to destabilize c-Myc mRNA (PMID:29581186, PMID:33051595). PTPN13 localizes to the centrosome, spindle midzone, and midbody, where its activity is required for faithful cytokinesis (PMID:12529439, PMID:23108400). By dephosphorylating STAT1, PTPN13 suppresses interferon-stimulated MHC class I antigen presentation and CD8+ T cell infiltration, a circuit engaged by APC loss in colorectal cancer (PMID:41486293). Pathogenic PTPN13 mutations in families with ALL/anemia/inherited bone marrow failure impair the PTPN13–β-catenin interaction and BCR-driven BTK/β-catenin signaling, linking the gene to lymphoid homeostasis (PMID:41422331).

Mechanistic history

Synthesis pass · year-by-year structured walk · 21 steps
  1. 1994 High

    Establishing that PTPN13 is a bona fide tyrosine phosphatase with a distinctive multidomain architecture defined the gene as a candidate scaffolding phosphatase rather than a simple enzyme.

    Evidence PCR cloning, immunoprecipitation, and in vitro phosphatase assay on 32P-myelin basic protein

    PMID:7929060

    Open questions at the time
    • No physiological substrate identified at this stage
    • Roles of the FERM, PDZ, and leucine-zipper modules unassigned
  2. 1997 High

    Mapping PDZ2/PDZ4 binding to the Fas/CD95 C-terminus and PDZ4 to the RhoGAP PARG1 showed PTPN13 selects partners via C-terminal motifs, framing it as a multi-complex organizer.

    Evidence Peptide binding/affinity assays for Fas; yeast two-hybrid and in vitro GAP assay for PARG1

    PMID:9261095 PMID:9305890

    Open questions at the time
    • Functional consequence of Fas binding not resolved here
    • PARG1 complex link to Rho signaling inferred from in vitro GAP, not cellular readout
  3. 1998 High

    Identifying RIL as both a PDZ-binding partner and an in vitro substrate connected PTPN13's scaffolding and catalytic functions at actin-based structures.

    Evidence Yeast two-hybrid, in vitro kinase/phosphatase assays, colocalization

    PMID:9487134

    Open questions at the time
    • Physiological relevance of RIL dephosphorylation in cells not established
    • Cellular pathway controlled by RIL phosphorylation unknown
  4. 1999 High

    Demonstrating that the FERM domain alone targets PTPN13 to the apical membrane, and IκBα binds PDZ1, defined how the phosphatase is positioned and added an NF-κB-regulatory link.

    Evidence Modular domain expression, immuno-EM, FRAP for localization; yeast two-hybrid, Co-IP, dominant-negative for IκBα

    PMID:10504335 PMID:9882613

    Open questions at the time
    • Direct molecular driver of FERM targeting not yet identified (resolved later)
    • IκBα as a direct substrate inferred from dominant-negative, not in vitro dephosphorylation
  5. 2000 High

    Quantifying high-affinity PDZ2 binding to the APC tumor suppressor and its abolition by a 5-residue splice insertion revealed splicing as a switch controlling PTPN13 partner selection.

    Evidence Yeast two-hybrid, surface plasmon resonance, co-precipitation, colocalization; additional TRIP6 PDZ2 mapping

    PMID:10826496 PMID:10951583

    Open questions at the time
    • Functional output of the PTPN13-APC complex not defined here
    • Physiological regulation of the splicing switch unknown
  6. 2002 High

    Defining ephrinB dephosphorylation downstream of Src family kinases, and solving the PDZ2 structure, established PTPN13 as a temporally-controlled signaling switch with structurally rationalized specificity.

    Evidence Reciprocal Co-IP and temporal phosphorylation assays (ephrinB); NMR structure with peptide binding (PDZ2); FEBS PRK2 PDZ3 interaction mapping

    PMID:11356191 PMID:11884147 PMID:11983165

    Open questions at the time
    • Species-specific PDZ2 recognition complicates extrapolation across organisms
    • In vivo ephrinB regulation by endogenous PTPN13 not tested
  7. 2002 High

    Showing PTPN13 localizes to centrosome, midzone, and midbody and its overexpression causes multinucleation established a direct role in cytokinesis.

    Evidence Immunofluorescence of endogenous protein, domain co-sedimentation with actin/microtubules, overexpression phenotype

    PMID:12529439

    Open questions at the time
    • Substrate dephosphorylated during cytokinesis not identified
    • Mechanism linking phosphatase activity to abscission unclear
  8. 2003 High

    Identifying the FERM–PtdIns(4,5)P2 interaction and TAPP1/PtdIns(3,4)P2-dependent recruitment defined the lipid logic of constitutive versus stimulus-induced membrane targeting.

    Evidence Mutagenesis of PIP2-binding motifs, protein-lipid overlay, fractionation (FERM); endogenous Co-IP, GST pull-down, RNAi, lipid binding (TAPP1)

    PMID:12766187 PMID:14516276

    Open questions at the time
    • How membrane recruitment is coupled to substrate access not resolved
    • Relative contribution of constitutive vs inducible routes in vivo unknown
  9. 2004 High

    The catalytic domain crystal structure and the spliced PDZ2b NMR structure provided atomic-level explanations for substrate preference and splice-dependent specificity loss.

    Evidence X-ray crystallography of PTP domain with bis-phospho-peptide assay; NMR of PDZ2b with binding studies

    PMID:14596806 PMID:15611135

    Open questions at the time
    • Physiological bis-phosphorylated substrates not identified
    • Functional consequence of PDZ2b lipid binding in cells untested
  10. 2007 High

    A burst of substrate-identification studies established PTPN13 as a broad negative regulator of growth/survival signaling and immune differentiation by directly dephosphorylating IRS-1, Her2, TRIP6, STATs, and regulating TRPM2.

    Evidence In vitro phosphatase assays, Co-IP, dominant-negative/RNAi, knockout mouse (STATs), substrate-site mapping (TRIP6 Tyr55), Ca2+/viability assays (TRPM2)

    PMID:17251321 PMID:17306571 PMID:17591779 PMID:17638892 PMID:17982484

    Open questions at the time
    • Hierarchy/coordination among multiple substrates within a single cell unresolved
    • Determinants of substrate selection by individual PDZ domains incompletely mapped
  11. 2007 High

    Discovering an allosteric PDZ1–PDZ2 interaction and transcriptional repression by ICSBP/IRF8 revealed both intramolecular and gene-expression-level control of PTPN13 function.

    Evidence Phage display, NMR (PDZ1-PDZ2 allostery); ChIP, luciferase reporters, phospho-mutants (ICSBP)

    PMID:17979300 PMID:18195016

    Open questions at the time
    • In vivo relevance of allosteric specificity modulation unknown
    • Signals controlling ICSBP-mediated repression beyond myeloid differentiation unclear
  12. 2009 High

    Placing PTPN13 phosphatase activity upstream of Ras/RAF/MEK/ERK extended its tumor-suppressive scope to a major mitogenic cascade and linked cancer-associated catalytic mutations to pathway dysregulation.

    Evidence Co-transfection with catalytic mutants, ERK phosphorylation assays, MEK-inhibitor epistasis, anchorage-independent growth in HNSCC

    PMID:19734941

    Open questions at the time
    • Direct ERK-pathway substrate not pinpointed in this study
    • Mechanism connecting PTPN13 to upstream receptors incompletely defined
  13. 2010 High

    Substrate-trapping identification of Src Tyr419 as a direct target established PTPN13 as the first phosphatase shown to directly inactivate Src in intact cells, with strong tumor-suppressive consequences.

    Evidence Substrate-trapping catalytic mutant, RNAi, downstream FAK/p130cas readouts, in vivo tumor growth/invasion

    PMID:20501847

    Open questions at the time
    • Spatial coupling of PTPN13 to Src pools not defined
    • Whether membrane anchoring is required for Src dephosphorylation untested
  14. 2012 High

    Defining an ICSBP–Tel–HDAC3 repressor complex at the PTPN13 promoter and its disruption by Tel-PdgfRβ, plus the SDCCAG3 cytokinesis link, connected PTPN13 regulation to leukemogenesis and trafficking.

    Evidence ChIP, reporter assays, Tel/HDAC3 knockdown, complex Co-IP (transcription); Co-IP, colocalization, knockdown (SDCCAG3)

    PMID:22262849 PMID:23108400

    Open questions at the time
    • How increased PTPN13 confers Fas-resistance mechanistically unresolved
    • SDCCAG3-GIT1 endosomal contribution to cytokinesis defined only by Co-IP and phenotype
  15. 2013 High

    Identifying p85β Tyr655 dephosphorylation that triggers SCF-FBXL2-mediated p85β degradation revealed an indirect route by which PTPN13 tunes PI3K subunit stoichiometry.

    Evidence FBXL2 complex purification, Co-IP, ubiquitylation assays, phospho-site mutants, PI3K signaling readouts

    PMID:23604317

    Open questions at the time
    • Integration with direct IRS-1 dephosphorylation in regulating PI3K not fully reconciled
    • Cell-type dependence of the p85β degradation axis unknown
  16. 2014 Medium

    Demonstrating PTEN binding to PDZ2 and PTPN13 control of β-catenin phosphorylation/stability expanded the scaffolding and Wnt-linked functions of the protein.

    Evidence Yeast two-hybrid/GST pull-down with PTEN PDZ-BM mutagenesis; Co-IP, RNAi, differentiation/stability assays (β-catenin)

    PMID:25193362 PMID:25448478

    Open questions at the time
    • PTEN interaction shown without functional consequence in this study
    • Whether β-catenin is a direct substrate not demonstrated
  17. 2017 High

    Showing calpain-2 cleaves and inactivates PTPN13, de-repressing c-Abl and driving tau pathology after TBI, revealed regulated proteolysis as an off-switch with neuropathological consequence.

    Evidence PDZ partner ID, Co-IP, in vitro cleavage and phosphatase assays, c-Abl substrate identification, in vivo calpain-2 inhibitor

    PMID:28924170

    Open questions at the time
    • Generalizability of the calpain-PTPN13-cAbl-tau axis beyond TBI unclear
    • Other substrates de-repressed by PTPN13 cleavage not catalogued
  18. 2018 High

    CRISPR knockout established PTPN13 as a phosphatase-independent scaffold required for apical PTEN enrichment, and PDZ3 structure with PRK2 refined ligand-recognition rules.

    Evidence CRISPR/Cas9 KO with brush-border phenotype, catalytically-dead rescue, Co-IP (PTEN); NMR of PDZ3-PRK2 complex

    PMID:29581186 PMID:30189200

    Open questions at the time
    • How PTEN anchoring is coordinated with PTPN13 catalytic substrates unknown
    • Functional output of the PDZ3-PRK2 interaction in cells not defined
  19. 2020 High

    Catalytic-activity-dependent suppression of breast cancer motility/invasion and phosphatase-independent IGF2BP1/c-Myc control demonstrated that PTPN13 acts both enzymatically and as a scaffold to restrain tumor progression.

    Evidence Transgenic mouse, isogenic WT vs catalytic-dead clones, phosphoproteomics (invasion); Co-IP/competitive binding, c-Myc mRNA stability, ChIP/DNMT3A (IGF2BP1)

    PMID:31938048 PMID:33051595

    Open questions at the time
    • Direct junction-protein substrates not individually validated
    • Coordination between catalytic and scaffolding tumor-suppressive arms unresolved
  20. 2022 Medium

    Epistasis placing PTPN13 upstream of Src/ERK/YAP1 and counteraction of TGF-β1/Smad/p38 EMT signaling consolidated its role as a brake on multiple oncogenic cascades in lung cancer.

    Evidence shRNA/siRNA knockdown, double-knockdown epistasis, Co-IP (p38), EMT marker and xenograft assays

    PMID:33536603 PMID:36193770

    Open questions at the time
    • p38 MAPK as a direct substrate rests on a single Co-IP
    • Direct vs indirect control of YAP1 not distinguished
  21. 2025 High

    Identifying STAT1 dephosphorylation as the basis of APC-loss-driven immune evasion, PDLIM4 as a STAT-recruiting adaptor, and β-catenin-linked pathogenic mutations integrated PTPN13 into antigen presentation, T-cell differentiation, and inherited hematologic disease.

    Evidence APC-KO models, Co-IP, APC11 peptide competition, immune-infiltration/anti-PD1 assays (STAT1); Co-IP, PDLIM4-deficient T cells, nsSNP binding (adaptor); Co-IP, silencing, BCR-activation/surface markers (β-catenin/BTK in ALL/IBMF families)

    PMID:41422331 PMID:41486293 PMID:42028851

    Open questions at the time
    • β-catenin pathogenic-mutation study (Medium) does not directly demonstrate dephosphorylation mechanism
    • How PDLIM4-recruited STAT dephosphorylation integrates with direct STAT1/4/6 substrate activity unresolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • How PTPN13's distinct PDZ-anchored complexes, lipid-dependent membrane targeting, and broad substrate set are coordinated within a single cell to produce context-specific outcomes remains unresolved.
  • No integrated model of substrate prioritization across tissues
  • In vivo phenotypes of full-length human PTPN13 loss incompletely mapped
  • Relationship between scaffolding and catalytic functions not unified

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 10 GO:0060090 molecular adaptor activity 5 GO:0008289 lipid binding 3 GO:0008092 cytoskeletal protein binding 2 GO:0016787 hydrolase activity 2
Localization
GO:0005886 plasma membrane 4 GO:0005829 cytosol 3 GO:0005856 cytoskeleton 2 GO:0005815 microtubule organizing center 1
Pathway
R-HSA-162582 Signal Transduction 6 R-HSA-1643685 Disease 4 R-HSA-5357801 Programmed Cell Death 4 R-HSA-168256 Immune System 3 R-HSA-1640170 Cell Cycle 2
Partners
APCFASIGF2BP1PRK2PTENSDCCAG3TAPP1TRIP6
Complex memberships
PTPN13-PDLIM4-STAT complexPTPN13-TAPP1 complexSCF-FBXL2 (functional partner in p85β degradation)

Evidence

Reading pass · 42 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1994 PTPN13/PTPL1 is a large cytoplasmic protein tyrosine phosphatase (270 kDa) with a PTP domain at the C-terminus, a band 4.1/FERM domain, five PDZ (GLGF repeat) domains, and a leucine zipper motif; it dephosphorylates 32P-labeled myelin basic protein in vitro, establishing its phosphatase activity. PCR-based cloning, peptide antisera immunoprecipitation, in vitro phosphatase assay with 32P-labeled substrate The Journal of biological chemistry High 7929060
1997 PDZ domains 2 and 4 of PTPN13/PTPL1 interact with high affinity with the C-terminal tail of Fas/CD95; the three C-terminal residues (SLV) of Fas are necessary and sufficient for binding, with specific contributions from residues at positions -2, -3, -4, and -5. Peptide binding assay, affinity measurements The Journal of biological chemistry High 9261095
1997 The fourth PDZ domain of PTPN13/PTPL1 interacts with the C-terminal four residues of PARG1, a novel 150 kDa RhoGAP protein; PARG1 shows GAP activity toward Rho, Rac, and Cdc42 in vitro with preference for Rho, suggesting a PTPN13-PARG1 complex as a dual negative regulator of Rho signaling. Yeast two-hybrid, in vitro GAP assay The Journal of biological chemistry Medium 9305890
1998 PDZ domains 2 and 4 of PTPN13/PTP-BL bind the LIM domain of RIL; the RIL LIM domain can be phosphorylated on tyrosine in vitro and in vivo and is dephosphorylated in vitro by the PTPase domain of PTP-BL, placing RIL as a substrate. Yeast two-hybrid, in vitro kinase and phosphatase assays, immunohistochemistry for colocalization Molecular biology of the cell High 9487134
1999 The FERM domain of PTP-BL/PTPN13 is necessary and sufficient for targeting the protein to the apical side of epithelial MDCK cells; the protein shows a submembranous localization ~10-15 nm from the plasma membrane as shown by immuno-electron microscopy, and FRAP experiments show dynamic redistribution via a cytosolic pool. The PTP domains mediate homotypic interactions. Transient expression of modular domains, immuno-electron microscopy, immunofluorescence, FRAP, yeast two-hybrid Journal of cell science High 10504335
1999 The PDZ1 domain of PTPN13/PTP-BAS interacts with IκBα through the N-terminal three ankyrin repeats of IκBα; this interaction was confirmed by co-immunoprecipitation in HeLa cells. Dominant-negative PTP-BAS caused tyrosine phosphorylation of IκBα, suggesting PTPN13 dephosphorylates IκBα to regulate NF-κB activation. Yeast two-hybrid, co-immunoprecipitation, dominant-negative mutant expression The Biochemical journal Medium 9882613
2000 PTPN13/PTP-BL PDZ2 domain (specifically the non-spliced variant PDZ2a) binds the extreme C-terminus of the tumor suppressor APC with a dissociation constant of 8.1×10⁻⁹ M; a naturally occurring 5-amino acid splice insertion (PDZ2b) abolishes this binding. Interaction confirmed by co-precipitation in COS cells and colocalization in epithelial cells. Yeast two-hybrid, surface plasmon resonance, co-precipitation in transfected COS cells, immunofluorescence colocalization Oncogene High 10951583
2000 PTPN13/PTP-BL PDZ2 domain interacts with the third LIM domain (including the C-terminus) of TRIP6; both proteins colocalize in transfected epithelial cells at F-actin structures, placing PTPN13 in a multiprotein complex with RIL and TRIP6 at actin-based structures. Yeast two-hybrid, co-precipitation from transfected cells, immunofluorescence colocalization European journal of cell biology Medium 10826496
2001 The PDZ3 domain of PTPN13/PTP-BL interacts with the extreme C-terminus of PRK2 (protein kinase C-related kinase 2), a Rho effector serine/threonine kinase; a conserved C-terminal cysteine of PRK2 is indispensable for this interaction. Both proteins colocalize in lamellipodia-like structures in HeLa cells. Yeast two-hybrid, co-immunoprecipitation from transfected HeLa cells, site-directed mutagenesis, immunofluorescence colocalization FEBS letters Medium 11356191
2002 PTPN13/PTP-BL is recruited to ephrinB expression domains with delayed kinetics after EphB receptor engagement and mediates dephosphorylation of ephrinB, acting downstream of Src family kinases which phosphorylate ephrinB. This defines a switch from phosphotyrosine/SFK-dependent signaling to PDZ-dependent signaling. Co-immunoprecipitation, cell biology/signaling assays, phosphorylation analysis Molecular cell High 11983165
2002 NMR solution structure of PDZ2 of PTP-BL/PTPN13 reveals a compact canonical PDZ fold with six β-strands and two α-helices, with a unique flexible L1 loop. PDZ2 binds C-termini of human Fas/CD95 and RIL (including non-canonical E-x-V motif), but murine PDZ2 does not bind murine Fas/CD95, suggesting species-specific differences in substrate recognition. NMR structure determination, 15N relaxation analysis, peptide binding studies Journal of molecular biology High 11884147
2002 PTPN13/PTPL1/FAP-1 promotes apoptosis in MCF7 breast cancer cells by inhibiting the IRS-1/PI3K/Akt pathway; antisense abrogation of PTPL1 expression abolished tamoxifen-induced apoptosis, and PTPL1 expression reduced IRS-1 tyrosine phosphorylation by 65%, PI3K activity by 80%, and Akt activation by 55%. Antisense stable transfection, PI3K activity assay, Akt phosphorylation assay, TUNEL/nucleosome ELISA apoptosis assay The Journal of biological chemistry High 12354757
2003 The FERM domain of PTPN13/PTPL1 is necessary and sufficient for membrane targeting to the apical plasma membrane enriched in dorsal microvilli; two PtdIns(4,5)P2-binding motifs within the FERM domain are required—mutation of both abolishes membrane localization. Direct interaction of the FERM domain with PtdIns(4,5)P2 was demonstrated by protein-lipid overlay assay. Live imaging of domain constructs in HeLa cells, site-directed mutagenesis of PIP2-binding motifs, protein-lipid overlay, cell fractionation, neomycin treatment Journal of cell science High 12766187
2003 Endogenous PTPN13/PTPL1 constitutively associates with TAPP1 (a PtdIns(3,4)P2-binding adaptor) primarily through its first PDZ domain; this complex enables PTPN13 association with PtdIns(3,4)P2 in vitro. TAPP1 binding maintains PTPN13 in the cytoplasm; upon H2O2 stimulation (which produces PtdIns(3,4)P2), the PTPN13-TAPP1 complex translocates to the plasma membrane. Co-immunoprecipitation of endogenous proteins, GST pull-down, RNA interference, lipid binding assay, subcellular fractionation The Biochemical journal High 14516276
2003 PTPN13/PTP-BL localizes to centrosomes during inter- and metaphase, the spindle midzone during anaphase, and concentrates at the midbody during cytokinesis. Targeting to midbody/centrosome requires a specific N-terminal splicing variant (182 aa insertion). The FERM domain associates with the contractile ring and co-sediments with F-actin; the N-terminus co-sediments with microtubules. Overexpression of wild-type or phosphatase-dead PTPN13 causes cytokinesis defects and multinucleate cells. Immunofluorescence localization of endogenous protein, domain deletion constructs, actin/microtubule co-sedimentation, overexpression functional assay Molecular biology of the cell High 12529439
2004 Crystal structure of the PTPN13/PTPL1 catalytic domain at 1.8 Å resolution reveals the standard PTP fold with an additional N-terminal helix and an ordered phosphate in the active site. A second positively charged pocket near the active site resembles the second phosphotyrosine-binding site of PTP1B; consistent with this, PTPL1 dephosphorylates a bis-phosphorylated insulin receptor peptide more efficiently than monophosphorylated peptides. Four of five colorectal cancer mutations map to solvent-exposed regions remote from the active site; the fifth (Met2307Thr) is near the active-site cysteine and significantly decreases activity. X-ray crystallography (1.8 Å), in vitro phosphatase assay with bis- vs mono-phosphorylated peptides, mutant activity assays The Journal of biological chemistry High 15611135
2004 NMR structure of the alternatively spliced PDZ2b (with 5-residue insertion) of PTP-BL/PTPN13 reveals that the insert causes reorientation of a loop that closes the binding site (Lys32 side chain occludes the pocket) and repositions α-helix 2, rendering the binding pocket unable to accommodate APC C-terminus; PDZ2b binds PIP2 and PIP3 with KD ~230 μM via a groove overlapping the APC binding site. NMR structure determination, NMR titration binding studies, high-affinity chromatography for lipid binding Journal of molecular biology High 14596806
2007 PTPN13/PTPL1 directly dephosphorylates IRS-1 (insulin receptor substrate-1) in vitro and in cells; this is confirmed by dominant-negative mutant and RNAi approaches. PTPN13 expression blocks the IRS-1/PI3K/Akt pathway, inhibits IGF-I-induced cell survival, and induces apoptosis. In vitro phosphatase assay, co-immunoprecipitation, dominant-negative mutant, RNA interference, PI3K/Akt pathway assays, cell survival assays Cancer research High 17638892
2007 PTPN13 negatively regulates Her2/ErbB2 signaling by dephosphorylating the Her2 signaling domain; siRNA knockdown of PTPN13 augmented Her2 phosphorylation and promoted cancer cell invasiveness. Growth factor-induced phosphorylation of PTPN13 is required for its ability to dephosphorylate Her2, suggesting a negative feedback mechanism. PTPN13 mutations found in human tumors reduced phosphatase activity. siRNA phosphatase library screen, phosphorylation assays, cell invasion assays, mutant phosphatase activity assays Oncogene High 17982484
2007 PTPN13/PTP-BL dephosphorylates STAT proteins (STAT4, STAT6 confirmed) in vitro and in vivo, attenuating STAT-mediated gene activation. In CD4+ T cells, PTP-BL deficiency leads to increased and prolonged activation of STAT4 and STAT6, and consequently enhanced Th1 and Th2 cell differentiation. In vitro phosphatase assay, PTP-BL-deficient mouse model, T cell differentiation assays, STAT phosphorylation measurements Immunity High 17306571
2007 PTPN13/PTPL1 dephosphorylates phosphotyrosine-55 of TRIP6 in vitro, inhibiting LPA-induced tyrosine phosphorylation of TRIP6 in cells. This negative regulation requires direct protein-protein interaction and phosphatase activity of PTPL1, preventing TRIP6 turnover at adhesion sites and inhibiting LPA-induced Crk recruitment and cell migration. In vitro phosphatase assay, co-immunoprecipitation, phosphatase-dead mutant, cell migration/morphology assays The Journal of biological chemistry High 17591779
2007 PTPN13/PTPL1 interacts with the TRP channel TRPM2 (confirmed by co-IP and GST pull-down); PTPL1 co-expression reduces TRPM2 tyrosine phosphorylation and inhibits H2O2/TNFα-induced Ca2+ influx and cell death. PTPL1 knockdown increases TRPM2 tyrosine phosphorylation, Ca2+ influx, and cell death susceptibility. Endogenous TRPM2-PTPL1 association confirmed in U937 cells. PDZ array blot, co-immunoprecipitation, GST pull-down, siRNA knockdown, Ca2+ imaging, cell viability assay American journal of physiology. Cell physiology High 17251321
2007 An allosteric intramolecular PDZ1-PDZ2 interaction within PTPN13/PTP-BL modulates PDZ2 binding specificity; structural studies revealed PDZ1 directly contacts a surface on PDZ2 opposite the peptide binding groove, causing long-range allosteric changes in the PDZ2 binding pocket. Phage display library screening, NMR structural studies, binding specificity assays Biochemistry High 17979300
2008 ICSBP/IRF8 represses PTPN13 gene transcription by binding to a cis element in the proximal PTPN13 promoter in differentiating myeloid cells; this repression is regulated by phosphorylation of conserved tyrosine residues in the ICSBP IRF domain and increases during myeloid differentiation. ICSBP influences Fas-induced apoptosis in a FAP-1/PTPN13-dependent manner. CpG island microarray with chromatin immunoprecipitation, luciferase reporter assays, ChIP, phosphorylation mutants, Fas-apoptosis assays The Journal of biological chemistry High 18195016
2009 PTPN13 phosphatase activity inhibits Ras/RAF/MEK/Erk signaling downstream of ErbB2, EGFR, and H-RasV12; co-transfection of wild-type but not enzymatically inactive PTPN13 inhibited this pathway. HPV-negative HNSCCs with PTPN13 phosphatase mutations showed impaired Ras/RAF/MEK/Erk inhibition. MEK inhibitor U0126 blocked anchorage-independent growth in PTPN13-deficient cells, placing PTPN13 upstream of ERK signaling. Co-transfection assays, phosphatase activity mutants, ERK phosphorylation assays, MEK inhibitor epistasis, anchorage-independent growth assay Oncogene High 19734941
2010 PTPN13/PTPL1 directly dephosphorylates Src at tyrosine 419 (the activating phosphorylation site) as shown by substrate-trapping experiments; PTPL1 knockdown increases Src-Y419 phosphorylation and activates downstream Fak and p130cas. PTPL1 inhibition dramatically increased tumor growth and invasion, identifying PTPL1 as the first phosphatase shown to directly inhibit Src in intact cells. Substrate-trapping with catalytic mutant, phosphorylation assays, RNA interference, in vivo tumor growth assay, invasion assay Cancer research High 20501847
2012 PTPN13/PTPL1 is a direct transcriptional target of ICSBP; repression requires cooperation of ICSBP with Tel and HDAC3 forming a multiprotein complex at the PTPN13 cis element. The leukemia fusion protein Tel-PdgfRβ disrupts this repressive complex by competing with the Tel component, resulting in increased PTPN13 expression and Fas-resistance. ChIP, promoter reporter assays, knockdown of Tel/HDAC3, co-immunoprecipitation of repressor complex The Journal of biological chemistry High 22262849
2012 SDCCAG3 forms a complex with PTPN13 (co-immunoprecipitation) and both colocalize at the midbody during cytokinesis; SDCCAG3 is an endosomal protein (early/recycling endosome) that interacts with the ArfGAP GIT1. Overexpression or downregulation of SDCCAG3 causes multinucleate cells, linking PTPN13's cytokinesis function to endosomal trafficking via SDCCAG3-GIT1. Co-immunoprecipitation, immunofluorescence colocalization, overexpression/knockdown functional assays Oncogene Medium 23108400
2013 PTPN13/PTPL1 dephosphorylates p85β (PI3K regulatory subunit) at Tyr-655, which stimulates p85β binding to and degradation through the SCF-FBXL2 ubiquitin ligase complex; this controls PI3K signaling by reducing the pool of free p85β that competes with p85-p110 heterodimers for IRS1. Protein purification (FBXL2 complex), co-immunoprecipitation, ubiquitylation assays, phosphorylation site mutants, PI3K signaling assays Nature cell biology High 23604317
2014 PTEN binds to PDZ2 of PTPN13 in a manner dependent on the PTEN PDZ-binding motif and the specific PDZ domain arrangement including the PDZ1-PDZ2 interdomain region; this was shown by yeast two-hybrid and GST pull-down with mutational analysis of the PTEN PDZ-BM. Yeast two-hybrid, GST pull-down, site-directed mutagenesis of PTEN PDZ-BM Methods (San Diego, Calif.) Medium 25448478
2014 PTPN13 co-immunoprecipitates and colocalizes with β-catenin; PTPN13 regulates β-catenin phosphorylation, stability, and transcriptional activity during megakaryocytic differentiation. PTPN13 is stabilized upon Wnt signaling, and its silencing triggers megakaryocytic differentiation through effects on ERK and STAT signaling and β-catenin. Co-immunoprecipitation, colocalization, siRNA silencing, differentiation assays, phosphorylation/stability assays Biochimica et biophysica acta Medium 25193362
2017 PTPN13/FAP-1 is a PDZ-domain-mediated binding partner of calpain-2; PTPN13 is cleaved by calpain-2, which inactivates its phosphatase activity and generates stable breakdown products (P13BPs). PTPN13 dephosphorylates and inhibits c-Abl; after TBI, calpain-2-mediated PTPN13 cleavage activates c-Abl and triggers tau tyrosine phosphorylation and oligomer accumulation. Post-TBI calpain-2 inhibitor treatment prevented this cascade. PDZ binding partner identification, co-immunoprecipitation, in vitro cleavage and phosphatase activity assays, calpain-2 selective inhibitor in vivo Scientific reports High 28924170
2018 PTPN13/PTPL1 interacts with PTEN, and this interaction is necessary for apical membrane enrichment of PTEN in polarized epithelial cells; PTPL1 depletion (CRISPR/Cas9) causes enlarged brush border similar to PTEN loss. PTPL1 functions as a scaffolding anchor for PTEN in this process—its phosphatase activity is NOT required. CRISPR/Cas9 knockout, live imaging of brush border formation, co-immunoprecipitation, domain mapping Molecular and cellular biology High 29581186
2018 NMR solution structures of the PDZ3 domain of murine PTPN13 in apo form and in complex with the C-terminal peptide of PRK2 reveal classical compact globular fold; PRK2 binds via an elongated peptide in the canonical groove between β-strand and α-helix, with P0 cysteine and P-2 aspartate facing the groove (class III ligand recognition). Multidimensional NMR spectroscopy, structure determination Journal of molecular biology High 30189200
2019 The tandem PDZ2/3 domain of PTPN13 shows allosterically modulated binding to APC; PDZ3 presence alters PDZ2 binding affinity for APC, and PRK2 is identified as a weak binding partner of PDZ2. HADDOCK molecular modeling and NMR spectroscopy support an allosteric effect from PDZ3 on PDZ2's ligand binding site. NMR spectroscopy, HADDOCK molecular modeling, binding affinity measurements of isolated vs tandem domains BMC molecular and cell biology Medium 31286859
2020 PTPN13 phosphatase activity is required to inhibit breast cancer cell motility and invasion; PTPN13 overexpression in MDA-MB-231 cells inhibited invasion and induced mesenchymal-to-epithelial transition in vivo. Phosphoproteomic and GO analyses revealed a role for PTPN13 in regulation of intercellular junction proteins; PTPN13 stabilizes intercellular adhesion and promotes desmosome formation. Transgenic mouse crossing (HER2×PTPN13-ΔP), isogenic cell clones with WT vs catalytically inactive PTPN13, phosphoproteomics, wound healing, Boyden chamber, videomicroscopy, immunofluorescence Theranostics High 31938048
2020 PTPN13 competitively binds IGF2BP1 to decrease functional IGF2BP1 levels, thereby promoting c-Myc mRNA degradation and suppressing metabolic reprogramming; this function is independent of PTPN13 phosphatase activity. HBx inhibits PTPN13 expression by upregulating DNMT3A, which binds the PTPN13 promoter (-343 to -313 bp) and increases DNA methylation to suppress transcription. Co-immunoprecipitation, competitive binding assays, c-Myc mRNA stability assays, ChIP on PTPN13 promoter, DNMT3A knockdown Oncogene Medium 33051595
2021 PTPN13/PTPL1 suppresses TGF-β1-induced EMT in lung cancer cells by counteracting activation of canonical Smad2/3 and non-canonical p38 MAPK signaling pathways; immunoprecipitation demonstrated direct binding of PTPL1 to p38 MAPK, suggesting p38 MAPK as a direct substrate. siRNA knockdown, immunoprecipitation for PTPL1-p38 MAPK interaction, EMT marker analysis, Smad2/3 and p38 phosphorylation assays, xenograft model Acta pharmacologica Sinica Medium 33536603
2022 PTPL1/PTPN13 suppresses lung cancer cell proliferation by counteracting the Src/ERK pathway; PTPL1 knockdown induced activation of Src/ERK signaling and promoted YAP1 nuclear translocation and activation. YAP1 co-knockdown reversed the proliferation increase caused by PTPL1 knockdown, placing PTPL1 upstream of Src/ERK/YAP1. shRNA knockdown, signaling pathway assays, xenograft model, double knockdown epistasis Thoracic cancer Medium 36193770
2025 PTPN13 directly dephosphorylates STAT1, suppressing interferon-stimulated MHC class I antigen presentation and CD8+ T cell infiltration; peptides containing the last 11 C-terminal residues of APC (APC11) bind directly to PTPN13, block PTPN13-STAT1 interaction, restore STAT1 phosphorylation and IRF1 expression, and enhance anti-tumor immunity in CRC. APC loss thus drives immune evasion via PTPN13-dependent STAT1 dephosphorylation independently of β-catenin. APC knockout models, Co-immunoprecipitation for PTPN13-STAT1 interaction, STAT1 phosphorylation assays, APC11 peptide competition assay, in vivo tumor/immune infiltration assays, anti-PD1 combination experiments Cell research High 41486293
2025 PDLIM4 acts as an adaptor that recruits PTP-BL/PTPN13 through its LIM domain to facilitate dephosphorylation of STAT3, STAT4, and STAT6; a disease-associated PDLIM4 nsSNP in the LIM domain reduces PTP-BL binding and impairs STAT3 dephosphorylation, linking this complex to regulation of Th1, Th2, and Th17 differentiation. Co-immunoprecipitation, STAT phosphorylation assays, PDLIM4-deficient T cells, LIM domain nsSNP mutant binding assay International immunology High 42028851
2025 PTPN13 pathogenic mutations (identified in ALL/anemia/IBMF families) impair the PTPN13-β-catenin interaction; PTPN13 silencing reduces Bruton's tyrosine kinase (BTK) activation and β-catenin levels after B-cell receptor (BCR) stimulation, indicating PTPN13 modulates BCR signaling and lymphoid cell homeostasis through β-catenin. Co-immunoprecipitation of endogenous proteins, PTPN13 silencing with BCR activation assays, surface marker analysis (CD25, CD38) Scientific reports Medium 41422331

Source papers

Stage 0 corpus · 95 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2002 EphrinB phosphorylation and reverse signaling: regulation by Src kinases and PTP-BL phosphatase. Molecular cell 260 11983165
1998 PDZ motifs in PTP-BL and RIL bind to internal protein segments in the LIM domain protein RIL. Molecular biology of the cell 131 9487134
1997 A novel GTPase-activating protein for Rho interacts with a PDZ domain of the protein-tyrosine phosphatase PTPL1. The Journal of biological chemistry 116 9305890
2007 The PDZ binding motif of human papillomavirus type 16 E6 induces PTPN13 loss, which allows anchorage-independent growth and synergizes with ras for invasive growth. Journal of virology 113 18160445
2013 FBXL2- and PTPL1-mediated degradation of p110-free p85β regulatory subunit controls the PI(3)K signalling cascade. Nature cell biology 109 23604317
1994 Cloning and characterization of PTPL1, a protein tyrosine phosphatase with similarities to cytoskeletal-associated proteins. The Journal of biological chemistry 93 7929060
2011 Curcumin suppresses human papillomavirus oncoproteins, restores p53, Rb, and PTPN13 proteins and inhibits benzo[a]pyrene-induced upregulation of HPV E7. Molecular carcinogenesis 89 21061268
2000 The Adenomatous Polyposis Coli-protein (APC) interacts with the protein tyrosine phosphatase PTP-BL via an alternatively spliced PDZ domain. Oncogene 74 10951583
2002 Structure, dynamics and binding characteristics of the second PDZ domain of PTP-BL. Journal of molecular biology 66 11884147
2000 The zyxin-related protein TRIP6 interacts with PDZ motifs in the adaptor protein RIL and the protein tyrosine phosphatase PTP-BL. European journal of cell biology 64 10826496
2009 Impaired PTPN13 phosphatase activity in spontaneous or HPV-induced squamous cell carcinomas potentiates oncogene signaling through the MAP kinase pathway. Oncogene 60 19734941
2007 Protein tyrosine phosphatase PTPN13 negatively regulates Her2/ErbB2 malignant signaling. Oncogene 60 17982484
2005 PTPL1 is a direct transcriptional target of EWS-FLI1 and modulates Ewing's Sarcoma tumorigenesis. Oncogene 60 15782144
2007 The putative tumor suppressor gene PTPN13/PTPL1 induces apoptosis through insulin receptor substrate-1 dephosphorylation. Cancer research 59 17638892
2002 Protein-tyrosine phosphatase PTPL1/FAP-1 triggers apoptosis in human breast cancer cells. The Journal of biological chemistry 56 12354757
2012 The nonreceptor-type tyrosine phosphatase PTPN13 is a tumor suppressor gene in non-small cell lung cancer. The American journal of pathology 54 22245727
2008 PTPL1: a large phosphatase with a split personality. Cancer metastasis reviews 54 18265946
1999 Association of protein-tyrosine phosphatase PTP-BAS with the transcription-factor-inhibitory protein IkappaBalpha through interaction between the PDZ1 domain and ankyrin repeats. The Biochemical journal 53 9882613
2008 The interferon consensus sequence-binding protein (ICSBP/IRF8) represses PTPN13 gene transcription in differentiating myeloid cells. The Journal of biological chemistry 52 18195016
2007 Regulation of signal transducer and activator of transcription signaling by the tyrosine phosphatase PTP-BL. Immunity 49 17306571
2003 Membrane targeting of protein tyrosine phosphatase PTPL1 through its FERM domain via binding to phosphatidylinositol 4,5-biphosphate. Journal of cell science 49 12766187
2011 PTPN13/PTPL1: an important regulator of tumor aggressiveness. Anti-cancer agents in medicinal chemistry 48 21235435
2007 An allosteric intramolecular PDZ-PDZ interaction modulates PTP-BL PDZ2 binding specificity. Biochemistry 48 17979300
2005 Kinetic folding mechanism of PDZ2 from PTP-BL. Protein engineering, design & selection : PEDS 48 16043447
1999 A FERM domain governs apical confinement of PTP-BL in epithelial cells. Journal of cell science 48 10504335
2010 PTPL1/PTPN13 regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. Cancer research 46 20501847
1997 Characterization of the interactions between PDZ domains of the protein-tyrosine phosphatase PTPL1 and the carboxyl-terminal tail of Fas. The Journal of biological chemistry 46 9261095
2003 The protein tyrosine phosphatase PTP-BL associates with the midbody and is involved in the regulation of cytokinesis. Molecular biology of the cell 45 12529439
2003 Interaction of the protein tyrosine phosphatase PTPL1 with the PtdIns(3,4)P2-binding adaptor protein TAPP1. The Biochemical journal 45 14516276
2001 The protein kinase C-related kinase PRK2 interacts with the protein tyrosine phosphatase PTP-BL via a novel PDZ domain binding motif. FEBS letters 42 11356191
2007 Regulation of TRP channel TRPM2 by the tyrosine phosphatase PTPL1. American journal of physiology. Cell physiology 40 17251321
2020 Anti-oncogene PTPN13 inactivation by hepatitis B virus X protein counteracts IGF2BP1 to promote hepatocellular carcinoma progression. Oncogene 36 33051595
2009 Missense polymorphisms of PTPRJ and PTPN13 genes affect susceptibility to a variety of human cancers. Journal of cancer research and clinical oncology 36 19672627
2004 Crystal structure of the PTPL1/FAP-1 human tyrosine phosphatase mutated in colorectal cancer: evidence for a second phosphotyrosine substrate recognition pocket. The Journal of biological chemistry 35 15611135
2004 Mild impairment of motor nerve repair in mice lacking PTP-BL tyrosine phosphatase activity. Physiological genomics 33 15226483
2020 Dual Role of the PTPN13 Tyrosine Phosphatase in Cancer. Biomolecules 31 33322542
2012 The serologically defined colon cancer antigen-3 interacts with the protein tyrosine phosphatase PTPN13 and is involved in the regulation of cytokinesis. Oncogene 29 23108400
1996 PTPN13, a fas-associated protein tyrosine phosphatase, is located on the long arm of chromosome 4 at band q21.3. Genomics 29 8824809
2007 PTPL1/FAP-1 negatively regulates TRIP6 function in lysophosphatidic acid-induced cell migration. The Journal of biological chemistry 27 17591779
2003 Cloning and characterization of mCRIP2, a mouse LIM-only protein that interacts with PDZ domain IV of PTP-BL. Genes to cells : devoted to molecular & cellular mechanisms 27 12839623
2003 Structure determination and ligand interactions of the PDZ2b domain of PTP-Bas (hPTP1E): splicing-induced modulation of ligand specificity. Journal of molecular biology 27 14596806
2014 PTEN-PDZ domain interactions: binding of PTEN to PDZ domains of PTPN13. Methods (San Diego, Calif.) 26 25448478
2021 PTPL1 suppresses lung cancer cell migration via inhibiting TGF-β1-induced activation of p38 MAPK and Smad 2/3 pathways and EMT. Acta pharmacologica Sinica 24 33536603
2017 The tyrosine phosphatase PTPN13/FAP-1 links calpain-2, TBI and tau tyrosine phosphorylation. Scientific reports 24 28924170
2016 miR-26a desensitizes non-small cell lung cancer cells to tyrosine kinase inhibitors by targeting PTPN13. Oncotarget 24 27285768
2012 ErbB2, EphrinB1, Src kinase and PTPN13 signaling complex regulates MAP kinase signaling in human cancers. PloS one 24 22279592
2012 Accurate prediction of the dynamical changes within the second PDZ domain of PTP1e. PLoS computational biology 24 23209399
2009 Genetic polymorphisms in the PTPN13 gene and risk of squamous cell carcinoma of head and neck. Carcinogenesis 24 19892796
2017 Characterization and Functional Analysis of the Poplar Pectate Lyase-Like Gene PtPL1-18 Reveal Its Role in the Development of Vascular Tissues. Frontiers in plant science 23 28702042
2004 A closed binding pocket and global destabilization modify the binding properties of an alternatively spliced form of the second PDZ domain of PTP-BL. Structure (London, England : 1993) 23 14725761
2016 Tumour-suppressive role of PTPN13 in hepatocellular carcinoma and its clinical significance. Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine 21 26801674
2014 PTPN13 regulates cellular signalling and β-catenin function during megakaryocytic differentiation. Biochimica et biophysica acta 19 25193362
2009 Downregulation of protein tyrosine phosphatase PTP-BL represses adipogenesis. The international journal of biochemistry & cell biology 19 19782949
2005 Effects of LAR and PTP-BL phosphatase deficiency on adult mouse retinal cells activated by lens injury. The European journal of neuroscience 19 15932596
2012 Downregulation of protein tyrosine phosphatase PTPL1 alters cell cycle and upregulates invasion-related genes in prostate cancer cells. Clinical & experimental metastasis 18 22274591
2020 PTPN13 induces cell junction stabilization and inhibits mammary tumor invasiveness. Theranostics 17 31938048
2015 PTPN13 and β-Catenin Regulate the Quiescence of Hematopoietic Stem Cells and Their Interaction with the Bone Marrow Niche. Stem cell reports 16 26344907
2020 Cancer-derived IgG involved in cisplatin resistance through PTP-BAS/Src/PDK1/AKT signaling pathway. Oral diseases 15 32730654
2013 PTPL1 and PKCδ contribute to proapoptotic signalling in prostate cancer cells. Cell death & disease 15 23559010
2013 The role of PTPN13 in invasion and metastasis of lung squamous cell carcinoma. Experimental and molecular pathology 15 23906871
2015 Promoter hypermethylation of PTPL1, PTPN6, DAPK, p16 and 5-azacitidine inhibits growth in DLBCL. Oncology reports 12 26498513
2004 The interaction of PTP-BL PDZ domains with RIL: an enigmatic role for the RIL LIM domain. Molecular biology reports 12 15663004
2024 METTL1/FOXM1 promotes lung adenocarcinoma progression and gefitinib resistance by inhibiting PTPN13 expression. Cancer medicine 11 38967523
2020 PTPN13 acts as a tumor suppressor in clear cell renal cell carcinoma by inactivating Akt signaling. Experimental cell research 10 32919955
2012 Valosin containing protein (VCP/p97) is a novel substrate for the protein tyrosine phosphatase PTPL1. Experimental cell research 10 23018179
2005 Redox-regulated affinity of the third PDZ domain in the phosphotyrosine phosphatase PTP-BL for cysteine-containing target peptides. The FEBS journal 10 15978037
2017 High PTPN13 expression in high grade serous ovarian carcinoma is associated with a better patient outcome. Oncotarget 9 29221157
2013 Stat3 inhibits PTPN13 expression in squamous cell lung carcinoma through recruitment of HDAC5. BioMed research international 9 24191246
2018 The Phosphatase PTPL1 Is Required for PTEN-Mediated Regulation of Apical Membrane Size. Molecular and cellular biology 8 29581186
2012 The leukemia-associated fusion protein Tel-platelet-derived growth factor receptor β (Tel-PdgfRβ) inhibits transcriptional repression of PTPN13 gene by interferon consensus sequence binding protein (Icsbp). The Journal of biological chemistry 8 22262849
2015 5-Azacitidine induces demethylation of PTPL1 and inhibits growth in non-Hodgkin lymphoma. International journal of molecular medicine 7 26133246
2008 Mutational analysis of FLASH and PTPN13 genes in colorectal carcinomas. Pathology 7 18038312
1996 The gene (PTPN13) encoding the protein tyrosine phosphatase PTP-BL/PTP-BAS is located in mouse chromosome region 5E/F and human chromosome region 4q21. Cytogenetics and cell genetics 7 8893825
2022 Protein tyrosine phosphatase PTPL1 suppresses lung cancer through Src/ERK/YAP1 signaling. Thoracic cancer 6 36193770
2021 Transcriptional regulation of miR-30a by YAP impacts PTPN13 and KLF9 levels and Schwann cell proliferation. The Journal of biological chemistry 6 34265306
2023 PTPN13 Participates in the Regulation of Epithelial-Mesenchymal Transition and Platinum Sensitivity in High-Grade Serous Ovarian Carcinoma Cells. International journal of molecular sciences 5 37895093
2022 miR-200b, ZEB2 and PTPN13 Are Downregulated in Colorectal Carcinoma with Serosal Invasion. Biomedicines 5 36140249
2019 The binding affinity of PTPN13's tandem PDZ2/3 domain is allosterically modulated. BMC molecular and cell biology 5 31286859
2018 Molecular Basis of Class III Ligand Recognition by PDZ3 in Murine Protein Tyrosine Phosphatase PTPN13. Journal of molecular biology 5 30189200
2017 The PTPN13 Y2081D (T>G) (rs989902) polymorphism is associated with an increased risk of sporadic colorectal cancer. Colorectal disease : the official journal of the Association of Coloproctology of Great Britain and Ireland 5 28504867
2005 Subcellular localization and differentiation-induced redistribution of the protein tyrosine phosphatase PTP-BL in Neuroblastoma cells. Cellular and molecular neurobiology 4 16388334
2004 [PTPL1, a proapoptotic protein tyrosine phosphatase in breast cancers]. Bulletin du cancer 4 15242314
2023 Comprehensive analysis of the PTPN13 expression and its clinical implication in breast cancer. Neoplasma 3 36812232
2007 Sequence-specific (1)H, (13)C, and (15)N backbone assignment of the 28 kDa PDZ2/PDZ3 tandem domain of the protein tyrosine phosphatase PTP-BL. Biomolecular NMR assignments 3 19636852
2010 Sequence-specific 1H, 13C, and 15N assignment of the extended PDZ3 domain of the protein tyrosine phosphatase basophil-like PTP-BL. Biomolecular NMR assignments 2 20563762
2026 Targeting PTPN13 with 11-amino-acid peptides of C-terminal APC prevents immune evasion of colorectal cancer. Cell research 1 41486293
2025 Combined exome and RNA-seq analysis in patients with rare non-syndromic inherited brain arteriovenous malformation suggests a novel function for PTPN13 in arterial specification. Thrombosis research 1 41418676
2024 Arsenic disulfide promoted the demethylation of PTPL1 in diffuse large B cell lymphoma cells. PeerJ 1 38766487
2023 PTPN13 rs989902 and CHEK2 rs738722 are associated with esophageal cancer. Annals of medicine 1 38039548
2016 High-resolution crystal structure of the PDZ1 domain of human protein tyrosine phosphatase PTP-Bas. Biochemical and biophysical research communications 1 27544031
2026 PDLIM4 promotes dephosphorylation of STAT transcription factors by recruiting PTP-BL and inhibits Th1, Th2, and Th17 cell differentiation. International immunology 0 42028851
2026 Anti-SIA-cIgG enhances chemotherapy effectiveness through PTPN13-regulated tumor stemness in head and neck squamous cell carcinoma. Journal of translational internal medicine 0 42046805
2025 Altered PTPN13-β-catenin interaction by pathogenic mutations and involvement of this axis in B-cell receptor signalling. Scientific reports 0 41422331
2015 [Methylation Status of PTPL1 Gene in Non-Hodgkin's Lymphoma Cells]. Zhongguo shi yan xue ye xue za zhi 0 26708878
2014 [Expression and Significance of PTPL1 in Hematological Malignancies]. Zhongguo shi yan xue ye xue za zhi 0 25543508

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