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Showing PTPRH — SAP-1 is a alias.

PTPRH

Receptor-type tyrosine-protein phosphatase H · UniProt Q9HD43

Length
1115 aa
Mass
122.4 kDa
Annotated
2026-06-10
46 papers in source corpus 14 papers cited in narrative 14 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 5/6 claims corpus-supported (83%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PTPRH (SAP-1) is a microvillus-specific receptor-type protein tyrosine phosphatase that negatively regulates adhesion- and growth-factor signaling in epithelial and immune cells by dephosphorylating key tyrosine-phosphorylated substrates (PMID:11278335, PMID:19170756). Using substrate trapping, it was established to dephosphorylate the focal-adhesion proteins p130cas, FAK, and p62dok, with its catalytic activity stimulated by cell-cell adhesion and its overexpression disrupting the actin cytoskeleton, cell spreading on fibronectin, and ERK2 activation (PMID:11278335). Its substrate repertoire extends to the T-cell kinase Lck, which it directly binds and inactivates to suppress TCR-proximal signaling (PMID:12837766), to c-Src (PMID:15850787), to the microvillus protein CEACAM20 — where loss of PTPRH-mediated dephosphorylation permits c-Src-driven CEACAM20–Syk association, NF-κB activation, and IL-8 production, and PTPRH deficiency aggravates colitis (PMID:26195794) — and to EGFR at Y1197, where catalytically intact PTPRH restrains EGFR phosphorylation in NSCLC and tumor-derived mutations (V483M) impair this function (PMID:36054194). PTPRH forms a redox-sensitive cysteine-bonded homodimer through its extracellular and transmembrane domains; monomerization increases catalytic activity, providing a mechanism for activity control (PMID:15850787). Consistent with a tumor-suppressive role, PTPRH ablation reduces intestinal tumorigenesis in APC-mutant mice (PMID:19170756) and its expression is epigenetically silenced by promoter DNA methylation and H3K27me3 in colorectal cancer (PMID:28713969). The timeline additionally documents an ELK4/SAP-1 transcription factor activity required for ERK-driven thymocyte positive selection through induction of immediate-early genes such as Egr1 (PMID:14770179, PMID:20554967), with Elk-1 functionally interchangeable in this role (PMID:20554967) and ELK4/ELK1 jointly restraining innate-like CD8+ T-cell generation (PMID:30068599).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2001 High

    Established PTPRH/SAP-1 as a catalytically active phosphatase acting on focal-adhesion signaling, answering what physiological substrates it targets and what cellular processes it controls.

    Evidence Substrate-trapping mutagenesis and immunocomplex phosphatase assays with cell spreading/colony formation readouts in intact cells

    PMID:11278335

    Open questions at the time
    • In vivo substrate relevance not yet tested
    • Did not address localization or upstream regulation of activity
  2. 2003 High

    Extended the substrate range to immune signaling by showing PTPRH directly binds and inactivates Lck, defining a role in dampening TCR-proximal phosphorylation.

    Evidence Direct binding and in vitro dephosphorylation assays plus catalytic-dead mutant overexpression in Jurkat T cells

    PMID:12837766

    Open questions at the time
    • Demonstrated in a cell line, not primary T cells in vivo
    • Stoichiometry and recruitment to the TCR complex unresolved
  3. 2004 High

    Identified an ELK4/SAP-1 transcription-factor activity downstream of ERK required for thymocyte positive selection, distinguishing it from the phosphatase function.

    Evidence SAP-1 knockout mice with TCR transgenes and target-gene expression analysis

    PMID:14770179

    Open questions at the time
    • Relationship between the phosphatase and transcription-factor activities not reconciled
    • Direct target genes beyond Egr1 not fully defined here
  4. 2005 Medium

    Revealed a redox-controlled dimerization mechanism for activity regulation, answering how PTPRH catalytic output is tuned at the membrane.

    Evidence Cross-linking, reciprocal Co-IP, reducing-agent treatment, and activity assay toward c-Src

    PMID:15850787

    Open questions at the time
    • Physiological trigger for redox-driven monomerization not identified
    • c-Src as substrate not validated in vivo
  5. 2007 Medium

    Delimited the ELK4 requirement by showing it is dispensable for Treg development and suppression, refining where the ERK-SAP-1 axis is essential.

    Evidence SAP-1 knockout mice with Treg marker analysis and in vitro/in vivo suppression assays

    PMID:17982074

    Open questions at the time
    • Negative/dissociation finding from a single lab
    • Mechanism of Egr1-independent Treg function not addressed
  6. 2009 Medium

    Localized PTPRH to gastrointestinal brush-border microvilli and linked it to intestinal tumor development, establishing tissue context and disease relevance.

    Evidence Immunofluorescence/fractionation for localization and SAP-1-deficient × APC-heterozygous mouse tumorigenesis readout

    PMID:19170756

    Open questions at the time
    • Substrate driving the tumor phenotype not identified in this study
    • Mechanism of microvillar targeting unknown
  7. 2010 High

    Defined Egr1 as the primary transcriptional effector of the ERK-SAP-1 axis and showed Elk-1 functional equivalence, clarifying the genetic logic of positive selection.

    Evidence SAP-1/Elk-1/Net knockout combinations, ectopic TCF and Egr1 rescue, and ChIP

    PMID:20554967

    Open questions at the time
    • Full set of in vivo SRE targets not enumerated
    • Does not connect to PTPRH phosphatase activity
  8. 2015 High

    Identified CEACAM20 as a microvillar substrate and built a mechanistic model linking loss of PTPRH activity to c-Src/Syk/NF-κB-driven intestinal inflammation.

    Evidence Reciprocal Co-IP, phosphorylation analysis in deficient epithelium, NF-κB reporter, and SAP-1/IL-10 double-knockout colitis model

    PMID:26195794

    Open questions at the time
    • Ectodomain interaction interface not structurally resolved
    • Direct in vitro dephosphorylation of CEACAM20 by PTPRH not isolated
  9. 2017 Medium

    Showed PTPRH is epigenetically silenced in colorectal cancer, providing a mechanism for loss of its tumor-suppressive activity.

    Evidence Promoter methylation pyrosequencing, 5-aza-deoxycytidine rescue, and ChIP for Pol II and H3K27me3

    PMID:28713969

    Open questions at the time
    • Causal link between silencing and tumor progression not tested functionally
    • Upstream signals driving methylation unknown
  10. 2017 Low

    Linked PTPRH loss to increased intestinal macromolecular permeability, implicating it in barrier/tight-junction regulation.

    Evidence SAP-1-deficient mouse everted ileal sac and colonic loop transport assays

    PMID:28431964

    Open questions at the time
    • No molecular mechanism for tight-junction regulation identified
    • No direct junctional substrate shown
  11. 2022 Medium

    Identified EGFR Y1197 as a PTPRH substrate in lung cancer and showed tumor-derived mutations impair this activity, extending the tumor-suppressor model to NSCLC.

    Evidence PTPRH knockout NSCLC cells with wild-type versus catalytic-dead rescue, pEGFR Western blot, and TCGA/IHC analysis

    PMID:36054194

    Open questions at the time
    • Direct (in vitro) EGFR dephosphorylation by PTPRH not demonstrated
    • Later evidence questions a direct PTPRH-EGFR interaction
  12. 2023 Low

    Connected PTPRH to glycolytic metabolism via PI3K/AKT/mTOR in NSCLC, broadening its cancer-relevant signaling output.

    Evidence PTPRH overexpression/knockdown with 18F-FDG uptake, lactate assays, pathway Western blots, PI3K inhibitor/agonist, and xenografts

    PMID:37974250

    Open questions at the time
    • No direct substrate linking PTPRH to PI3K/AKT identified
    • Correlative pharmacology rather than direct mechanism
  13. 2025 Low

    Challenged the direct PTPRH-EGFR model by showing no direct interaction but an NF-κB association and a broad interactome, reframing EGFR regulation as indirect.

    Evidence Co-IP and BioID proximity labeling, domain-deletion mutants, and RNA-seq in NSCLC cells (preprint)

    PMID:41383754

    Open questions at the time
    • Preprint; interactors (HELZ2, RFC2) not functionally validated
    • Indirect EGFR mechanism not resolved
    • Reconciliation with direct Y1197 dephosphorylation finding pending

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the membrane phosphatase activity (microvilli, substrate dephosphorylation) and the nuclear ELK4 transcription-factor activity are functionally and structurally reconciled within one gene product remains unresolved.
  • No structural model linking the two activities
  • No study addresses whether both functions derive from the same protein isoform
  • Mechanism of redox-regulated activity control in vivo unverified

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 4 GO:0016787 hydrolase activity 3 GO:0140110 transcription regulator activity 2
Localization
GO:0005634 nucleus 2 GO:0005886 plasma membrane 1
Pathway
R-HSA-162582 Signal Transduction 3 R-HSA-1643685 Disease 3 R-HSA-168256 Immune System 3
Partners
CEACAM20EGFRELK1LCKSRC

Evidence

Reading pass · 14 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2001 SAP-1 (PTPRH), using a substrate-trapping approach, was shown to dephosphorylate p130cas (a major focal adhesion-associated phosphotyrosyl protein) as a likely physiological substrate. Expression of recombinant SAP-1 induced dephosphorylation of p130cas, FAK, and p62dok in intact cells; a substrate-trapping mutant caused hyperphosphorylation (dominant negative effect). SAP-1 enzymatic activity was increased by cell-cell adhesion, and overexpression disrupted the actin cytoskeleton and inhibited cell spreading on fibronectin, ERK2 activation, and colony formation. Substrate-trapping mutagenesis, overexpression in intact cells, immunocomplex phosphatase assay, cell spreading/colony formation assays The Journal of biological chemistry High 11278335
2003 The cytoplasmic region of SAP-1 (PTPRH) directly binds and dephosphorylates the tyrosine kinase Lck in vitro. Overexpression of wild-type (but not catalytically inactive) SAP-1 inhibited basal and TCR-stimulated Lck activity in Jurkat T cells, reduced ZAP-70 and LAT tyrosine phosphorylation, attenuated MAP kinase activation, CD69 upregulation, p62dok phosphorylation, and cell migration. Direct binding assay, in vitro dephosphorylation assay, catalytically inactive mutant overexpression, TCR stimulation assays in Jurkat cells The Journal of biological chemistry High 12837766
2005 SAP-1/PTPRH forms a stable homodimer mediated by its extracellular and transmembrane domains (not the catalytic domain). Dimer formation/stabilization involves cysteine bonds, as reducing conditions reversibly disrupt the dimer. Monomerization is accompanied by increased catalytic activity; monomeric SAP-1 dephosphorylates and activates c-Src, identified as a novel substrate. Chemical cross-linking, co-immunoprecipitation, reducing agent treatment, catalytic activity assay toward c-Src Biochemical and biophysical research communications Medium 15850787
2009 SAP-1 (PTPRH) protein localizes specifically to the microvilli of the brush border in gastrointestinal epithelial cells. SAP-1 ablation in mice with heterozygous APC mutation inhibited intestinal tumorigenesis, establishing SAP-1 as a microvillus-specific RPTP that modulates intestinal tumor development. Immunofluorescence/subcellular fractionation for localization; SAP-1-deficient mouse crossed with APC heterozygous mouse for tumorigenesis readout Genes to cells : devoted to molecular & cellular mechanisms Medium 19170756
2015 SAP-1 (PTPRH) dephosphorylates CEACAM20 (a microvillus-specific transmembrane Ig superfamily protein) as a substrate; SAP-1 and CEACAM20 form a complex through interaction of their ectodomains. Tyrosine phosphorylation of CEACAM20 by c-Src, unopposed by SAP-1, promotes CEACAM20 association with Syk, activating NF-κB and IL-8 production. SAP-1-deficient mice on an IL-10-deficient background showed markedly increased colitis severity. Tyrosine phosphorylation analysis in SAP-1-deficient intestinal epithelium, co-immunoprecipitation of SAP-1 and CEACAM20, overexpression of c-Src and Syk in cultured cells, NF-κB reporter assay, SAP-1/IL-10 double-knockout mouse model Proceedings of the National Academy of Sciences of the United States of America High 26195794
2004 SAP-1 (ELK4) is required for ERK-mediated thymocyte positive selection. SAP-1-deficient mice showed severely reduced (80–90%) positive selection and impaired TCR-induced activation of target genes including Egr1 in double-positive thymocytes, despite normal ERK activation, positioning SAP-1 as a transcriptional effector directly downstream of ERK in the positive selection pathway. Negative selection was unimpaired. SAP-1 knockout mouse, TCR transgene analysis, RT-PCR/gene expression, ERK activation assays Nature immunology High 14770179
2010 SAP-1 and Elk-1 are functionally equivalent for thymocyte positive selection (Elk-1 ectopic expression rescues SAP-1-null positive selection defect; Net does not). Ectopic expression of the SAP-1/Elk-1 target gene Egr-1 alone restored positive selection in SAP-1-null thymocytes, establishing Egr-1 (and possibly other Egr family members) as the primary transcriptional effectors of the ERK–SAP-1 signaling axis in positive selection. SAP-1/Elk-1/Net genetic knockout mice, ectopic TCF expression rescue experiments, Egr-1 transgenic rescue, chromatin immunoprecipitation, array gene expression analysis Journal of immunology High 20554967
2007 SAP-1 (ELK4) is NOT required for regulatory T cell (Treg) development or suppressive function; SAP-1-deficient CD4+CD25+ Tregs still suppress T cell proliferation in vitro and in a colitis model in vivo, despite impaired Egr-1 induction after TCR crosslinking. SAP-1 knockout mouse, Foxp3/CD25/GITR/CTLA4 expression analysis, in vitro suppression assay, in vivo colitis model Journal of immunology Medium 17982074
2018 ELK4 (SAP-1) and ELK1 act cell-autonomously in the thymus to suppress the generation of innate-like αβ CD8+ T cells. In ELK4/ELK1 double-knockout mice, increased innate-like CD8+ T cell numbers were associated with reduced ERK-mediated activation of ELK4-SRF target genes, and ectopic EGR2 expression partially suppressed this phenotype. ELK4 and ELK1 single and double knockout mice, flow cytometry of CD8+ T cell populations, ectopic EGR2 expression rescue, ERK inhibition in peripheral CD8+ T cells Journal of immunology Medium 30068599
2022 PTPRH directly dephosphorylates EGFR at tyrosine Y1197 (Y1173). PTPRH knockout in NSCLC cells increased Y1197 EGFR phosphorylation; rescue with wild-type PTPRH restored basal phosphorylation levels, while rescue with catalytically dead PTPRH did not. PTPRH mutations found in NSCLC tumors (V483M) are inhibitory to PTPRH function, resulting in aberrant EGFR activity. PTPRH knockout NSCLC cell line, wild-type vs catalytically dead PTPRH rescue expression, Western blot for pEGFR Y1197, whole genome sequencing, TCGA data analysis, immunohistochemistry PLoS genetics Medium 36054194
2017 PTPRH expression in colorectal tumors is regulated epigenetically: DNA methylation of PTPRH promoter regions correlates with reduced PTPRH expression in CRC, and treatment with 5-aza-deoxycytidine restored PTPRH expression in methylated cell lines. H3K27 trimethylation in promoter/gene body and reduced RNA Pol II occupancy were also associated with silenced PTPRH. Pyrosequencing of promoter methylation, 5-aza-deoxycytidine demethylation treatment, chromatin immunoprecipitation (RNA Pol II, H3K27me3), qRT-PCR, immunohistochemistry International journal of oncology Medium 28713969
2017 SAP-1 (PTPRH) deficiency in mice increases paracellular transport of macromolecules (dextrans FD-4 and FD-10) across the intestinal epithelium, as measured in everted ileal sacs and colonic loop absorption assays, indicating SAP-1 contributes to regulation of tight junction permeability for macromolecules. SAP-1-deficient mouse, everted ileal sac transport assay, colonic loop absorption assay Journal of pharmaceutical sciences Low 28431964
2023 PTPRH promotes glycolysis in NSCLC cells via the PI3K/AKT/mTOR signaling pathway. Altering PTPRH expression changed 18F-FDG uptake, lactate production, and expression of glycolysis-related proteins; PI3K inhibitor (LY294002) or agonist (740Y-P) modulated these effects, consistent with PTPRH acting upstream of PI3K/AKT/mTOR in this context. PTPRH overexpression/knockdown in NSCLC cells, 18F-FDG uptake assay, lactate production assay, Western blot for glycolysis proteins and PI3K/AKT pathway, PI3K inhibitor/agonist treatment, xenograft tumor model Journal of translational medicine Low 37974250
2025 PTPRH does not directly interact with EGFR in NSCLC cells; instead PTPRH interacts with NF-κB (a transcription factor downstream of EGFR), as demonstrated by Co-IP and proximity-dependent biotinylation (BioID). BioID also identified 48 novel PTPRH interactors including HELZ2 and RFC2. Disruption of either extracellular or intracellular PTPRH domains leads to EGFR dephosphorylation, suggesting an indirect mechanism. PTPRH overexpression downregulates multiple oncogenic signature pathways and modulates expression of 34 protein tyrosine phosphatases and 45 tyrosine kinases. Co-immunoprecipitation, proximity-dependent biotinylation (BioID), PTPRH domain deletion mutants, RNA sequencing, PTPRH overexpression/knockout in NSCLC cells bioRxivpreprint Low 41383754

Source papers

Stage 0 corpus · 46 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1992 Characterization of SAP-1, a protein recruited by serum response factor to the c-fos serum response element. Cell 631 1339307
1988 Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus. Science (New York, N.Y.) 253 2842863
1984 Isolation and amino acid sequence of SAP-1, an acidic protein of human whole saliva, and sequence homology with human gamma-trace. Journal of biochemistry 99 6501254
1998 Structures of SAP-1 bound to DNA targets from the E74 and c-fos promoters: insights into DNA sequence discrimination by Ets proteins. Molecular cell 96 9734357
2001 The B-box dominates SAP-1-SRF interactions in the structure of the ternary complex. The EMBO journal 86 11406578
2001 Selective targeting of MAPKs to the ETS domain transcription factor SAP-1. The Journal of biological chemistry 78 11029469
1995 The ETS-domain transcription factors Elk-1 and SAP-1 exhibit differential DNA binding specificities. Nucleic acids research 77 8524663
1986 Biosynthesis of the sulfatide/GM1 activator protein (SAP-1) in control and mutant cultured skin fibroblasts. Biochimica et biophysica acta 64 3081038
1992 Additional biochemical findings in a patient and fetal sibling with a genetic defect in the sphingolipid activator protein (SAP) precursor, prosaposin. Evidence for a deficiency in SAP-1 and for a normal lysosomal neuraminidase. The Biochemical journal 61 1637339
1985 The gene coding for a sphingolipid activator protein, SAP-1, is on human chromosome 10. Human genetics 60 3980013
2004 Ternary complex factor SAP-1 is required for Erk-mediated thymocyte positive selection. Nature immunology 56 14770179
2001 Crystal structure of a ternary SAP-1/SRF/c-fos SRE DNA complex. Journal of molecular biology 56 11846562
1991 The mechanism for a 33-nucleotide insertion in mRNA causing sphingolipid activator protein (SAP-1)-deficient metachromatic leukodystrophy. Human genetics 46 2066109
2001 Inhibition of cell growth and spreading by stomach cancer-associated protein-tyrosine phosphatase-1 (SAP-1) through dephosphorylation of p130cas. The Journal of biological chemistry 43 11278335
2010 Ternary complex factors SAP-1 and Elk-1, but not net, are functionally equivalent in thymocyte development. Journal of immunology (Baltimore, Md. : 1950) 42 20554967
1984 Biochemical, immunological, and structural studies on a sphingolipid activator protein (SAP-1). Archives of biochemistry and biophysics 42 6435528
1997 Overexpression of SAP-1, a transmembrane-type protein tyrosine phosphatase, in human colorectal cancers. Biochemical and biophysical research communications 37 9070877
2023 PTPRH promotes the progression of non-small cell lung cancer via glycolysis mediated by the PI3K/AKT/mTOR signaling pathway. Journal of translational medicine 36 37974250
2009 SAP-1 is a microvillus-specific protein tyrosine phosphatase that modulates intestinal tumorigenesis. Genes to cells : devoted to molecular & cellular mechanisms 35 19170756
1986 Molecular cloning of the sphingolipid activator protein-1 (SAP-1), the sulfatide sulfatase activator. Biochemical and biophysical research communications 33 2868718
2015 Protein tyrosine phosphatase SAP-1 protects against colitis through regulation of CEACAM20 in the intestinal epithelium. Proceedings of the National Academy of Sciences of the United States of America 28 26195794
2005 Sap-1/PTPRH activity is regulated by reversible dimerization. Biochemical and biophysical research communications 28 15850787
1992 Molecular characterization of a JC virus (Sap-1) clone derived from a cerebellar form of progressive multifocal leukoencephalopathy. Acta neuropathologica 25 1313631
2003 Downregulation of stomach cancer-associated protein tyrosine phosphatase-1 (SAP-1) in advanced human hepatocellular carcinoma. Oncogene 24 12879010
1986 A triple-binding-domain model explains the specificity of the interaction of a sphingolipid activator protein (SAP-1) with sulphatide, GM1-ganglioside and globotriaosylceramide. The Biochemical journal 22 3827882
2018 ERK Signaling Controls Innate-like CD8+ T Cell Differentiation via the ELK4 (SAP-1) and ELK1 Transcription Factors. Journal of immunology (Baltimore, Md. : 1950) 20 30068599
2007 Raf signaling but not the ERK effector SAP-1 is required for regulatory T cell development. Journal of immunology (Baltimore, Md. : 1950) 18 17982074
1996 Analysis of SRF, SAP-1 and ELK-1 transcripts and proteins in human cell lines. FEBS letters 17 8764983
1993 Transcriptional activation domains of elk-1, delta elk-1 and SAP-1 proteins. Oncogene 17 8247551
1987 Regional localization of the gene coding for sphingolipid activator protein SAP-1 on human chromosome 10. Somatic cell and molecular genetics 17 3478817
1988 Complete amino-acid sequence of the naturally occurring A2 activator protein for enzymic sphingomyelin degradation: identity to the sulfatide activator protein (SAP-1). Biological chemistry Hoppe-Seyler 14 3242555
1992 Correction of sulfatide metabolism after transfer of prosaposin cDNA to cultured cells from a patient with SAP-1 deficiency. American journal of human genetics 10 1350885
2022 Elevated phosphorylation of EGFR in NSCLC due to mutations in PTPRH. PLoS genetics 9 36054194
2016 Characterization and vaccine potential of Fasciola gigantica saposin-like protein 1 (SAP-1). Veterinary parasitology 9 28043381
1994 The role of regulated phosphorylation in the biological activity of transcription factors SRF and Elk-1/SAP-1. Anticancer research 9 7847828
2017 Downregulation of PTPRH (Sap-1) in colorectal tumors. International journal of oncology 8 28713969
2003 Interaction of SAP-1, a transmembrane-type protein-tyrosine phosphatase, with the tyrosine kinase Lck. Roles in regulation of T cell function. The Journal of biological chemistry 8 12837766
2022 Geoalkalibacter halelectricus SAP-1 sp. nov. possessing extracellular electron transfer and mineral-reducing capabilities from a haloalkaline environment. Environmental microbiology 7 36066180
2001 Gene for the human transmembrane-type protein tyrosine phosphatase H (PTPRH): genomic structure, fine-mapping and its exclusion as a candidate for Peutz-Jeghers syndrome. Cytogenetics and cell genetics 5 11435690
2022 PTPRH Alleviates Airway Obstruction and Th2 Inflammation in Asthma as a Protective Factor. Journal of asthma and allergy 3 35140475
2014 Structural and binding studies of SAP-1 protein with heparin. Chemical biology & drug design 3 25147059
2017 Microvillus-Specific Protein Tyrosine Phosphatase SAP-1 Plays a Role in Regulating the Intestinal Paracellular Transport of Macromolecules. Journal of pharmaceutical sciences 1 28431964
2013 Studies on the interactions of SAP-1 (an N-terminal truncated form of cystatin S) with its binding partners by CD-spectroscopic and molecular docking methods. Journal of biomolecular structure & dynamics 1 24261636
2026 Functional impact assessment of tissue-specific missense variants in the PTPRH gene using a multi-tool computational framework. Cancer genetics 0 41570449
2026 RBM15/IGF2BP2-PTPRH m6A regulatory axis in non-small cell lung cancer. Cellular oncology (Dordrecht, Netherlands) 0 42113318
2025 Unraveling the role of receptor-like protein tyrosine phosphatase PTPRH in cell signaling regulation and biological processes of non-small cell lung cancer. bioRxiv : the preprint server for biology 0 41383754

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