Affinage

PTPN18

Tyrosine-protein phosphatase non-receptor type 18 · UniProt Q99952

Round 2 corrected
Length
460 aa
Mass
50.5 kDa
Annotated
2026-04-28
63 papers in source corpus 13 papers cited in narrative 13 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PTPN18 is a PEST-domain-containing non-receptor protein tyrosine phosphatase that serves as a negative regulator of receptor tyrosine kinase and Src-family kinase signaling, while also controlling protein stability through ubiquitin-dependent degradation mechanisms. Its catalytic domain selectively dephosphorylates HER2 at pY1112, pY1196, and pY1248 — with crystal structures defining substrate recognition — to attenuate MAPK and growth signaling, while its PEST domain independently promotes K48-linked ubiquitination and proteasomal destruction of HER2 (PMID:14660651, PMID:25081058). PTPN18 also cooperates with Csk to inactivate Src-family kinases by dephosphorylating their positive-regulatory tyrosine (PMID:11158295), dephosphorylates the transcription factor ETS1 in the nucleus (following MVP/importin-β2-mediated translocation) to suppress TGF-β-driven epithelial-to-mesenchymal transition (PMID:35982039), and dephosphorylates fibrillarin at Y313 to regulate rRNA 2′-O-methylation and MAPK signaling (PMID:41559020). In hematopoietic progenitors, EPO-induced phosphorylation of PTPN18 at Y389 converts it into a positive regulator of JAK2/STAT5/ERK signaling and cell survival (PMID:32027948).

Mechanistic history

Synthesis pass · year-by-year structured walk · 10 steps
  1. 1996 Medium

    Identification of PTPN18 as an active non-receptor PTPase with a PEST motif established a new PEST-family phosphatase capable of dephosphorylating autophosphorylated tyrosine kinases overrepresented in tumors.

    Evidence PCR cloning and phosphatase assay in transfected 293 cells

    PMID:8950995

    Open questions at the time
    • Physiological substrates not identified
    • In vivo relevance not tested
    • Single-lab characterization
  2. 2001 High

    Demonstration that PTPN18 physically associates with Csk via SH2-domain interactions and synergizes with it to inactivate Src-family kinases established PTPN18 as a scaffold-dependent negative regulator of Src signaling.

    Evidence Yeast two-hybrid, co-immunoprecipitation in mammalian and hematopoietic cells, domain-mapping functional assays

    PMID:11158295

    Open questions at the time
    • Identity of the specific Src-family member(s) dephosphorylated in vivo unclear
    • Structural basis of Csk–PTPN18 interface not resolved
  3. 2003 High

    Gain- and loss-of-function experiments showed PTPN18 selectively dephosphorylates HER2 (not EGFR) and attenuates downstream Gab1/MAPK signaling, defining PTPN18 as a specific negative regulator of the HER2 axis.

    Evidence Overexpression and siRNA knockdown in breast cancer cells, phosphorylation-state immunoblotting

    PMID:14660651

    Open questions at the time
    • Specific HER2 phosphotyrosine sites not yet mapped
    • Mechanism of substrate selectivity for HER2 over EGFR unknown
  4. 2014 High

    Crystal structures of PTPN18 bound to HER2 phosphopeptides revealed the molecular basis of site-selective dephosphorylation (pY1112, pY1196, pY1248), while a distinct PEST-domain-mediated K48-ubiquitination mechanism for HER2 degradation was uncovered, showing that catalytic and non-catalytic domains impose distinct signaling barcodes on HER2.

    Evidence X-ray crystallography (three complexes), in vitro enzymology, mutagenesis, ubiquitination assays, cell growth/migration assays

    PMID:25081058

    Open questions at the time
    • E3 ligase recruited by the PEST domain not identified
    • In vivo confirmation of dual-mechanism regulation lacking
  5. 2020 Medium

    Discovery that EPO-induced Y389 phosphorylation converts PTPN18 into a positive regulator of JAK2/STAT5/ERK signaling in hematopoietic progenitors revealed context-dependent signaling roles beyond its canonical tumor-suppressive functions.

    Evidence Phosphoproteomics, phospho-site mutants, proliferation/survival assays in hematopoietic cells

    PMID:32027948

    Open questions at the time
    • Direct substrate in EPO pathway not identified (RHEX dephosphorylation implied but not proven direct)
    • Single cell-line system
    • Kinase responsible for Y389 phosphorylation not definitively confirmed
  6. 2020 Medium

    Co-immunoprecipitation linked PTPN18 to MYC protein stabilization and CDK4 activation in colorectal cancer, suggesting an oncogenic role in certain tissue contexts.

    Evidence Co-IP, overexpression/knockdown in CRC cells, xenograft assay

    PMID:34522712

    Open questions at the time
    • Single Co-IP without reciprocal validation or domain-mapping
    • Whether PTPN18 dephosphorylates MYC directly or acts indirectly not resolved
    • Mechanism of MYC stabilization not defined
  7. 2022 Medium

    Identification of MVP/importin-β2-mediated nuclear translocation of PTPN18 and its dephosphorylation of ETS1 to suppress TGF-β/EMT showed that subcellular compartmentalization determines PTPN18's functional output, with nuclear localization essential for anti-metastatic activity.

    Evidence Subcellular fractionation, nuclear/cytoplasmic mutant constructs, ETS1 phosphorylation/degradation assays, migration/invasion assays in breast cancer cells

    PMID:35982039

    Open questions at the time
    • ETS1 phosphosite targeted by PTPN18 not mapped
    • Whether MVP-dependent transport is regulated by signaling cues unknown
    • Single-lab finding
  8. 2024 Medium

    Phosphoproteomic screening in hepatocellular carcinoma cells placed PTPN18 as an activator of p53 and a suppressor of AKT/FOXO1 signaling, and identified HBx-driven miR-128-3p upregulation as a mechanism of PTPN18 silencing during HBV infection.

    Evidence Phospho-protein microarray, western blot validation, miRNA and PTPN18 overexpression/knockdown in HCC cells

    PMID:38787319

    Open questions at the time
    • Direct PTPN18 substrates in the p53 and AKT pathways not identified
    • In vivo HBV context not tested
  9. 2026 High

    Mass spectrometry interactome analysis and mutagenesis defined fibrillarin (FBL) as a direct PTPN18 substrate dephosphorylated at Y313, linking PTPN18 to rRNA 2′-O-methylation, histone H2AQ104 methylation, and MAPK signaling — extending its catalytic activity to nucleolar RNA-processing machinery.

    Evidence MS interactome, peptide mapping, co-IP, R451A mutagenesis, phosphatase assay for FBL-Y313, ubiquitination assay, methylation readouts

    PMID:41559020

    Open questions at the time
    • Physiological conditions triggering PTPN18–FBL interaction not defined
    • Impact on ribosome biogenesis and translation not directly measured
  10. 2026 Medium

    PTPN18 was shown to bind cyclin E1 specifically and promote its proteasomal degradation, causing cell cycle arrest and regulating p21/p27 through PI3K/AKT signaling in breast cancer cells.

    Evidence Co-immunoprecipitation, ubiquitin-proteasome pathway assay, cell cycle analysis, PI3K/AKT inhibitor rescue

    PMID:41480706

    Open questions at the time
    • Whether PTPN18 dephosphorylates cyclin E1 directly or acts as a scaffold for an E3 ligase not resolved
    • Single-lab finding

Open questions

Synthesis pass · forward-looking unresolved questions
  • The E3 ubiquitin ligase(s) recruited by the PTPN18 PEST domain to promote K48-ubiquitination of HER2 (and potentially other substrates) remain unidentified, and the regulatory signals that switch PTPN18 between tumor-suppressive and context-dependent pro-proliferative roles are not understood.
  • E3 ligase partner for PEST-domain-mediated ubiquitination unknown
  • Structural basis for nuclear vs. cytoplasmic substrate selectivity unresolved
  • No knockout mouse phenotype reported

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 6 GO:0098772 molecular function regulator activity 4
Localization
GO:0005829 cytosol 3 GO:0005634 nucleus 2
Pathway
R-HSA-162582 Signal Transduction 5 R-HSA-392499 Metabolism of proteins 3 R-HSA-1640170 Cell Cycle 1
Partners
CCNE1CSKERBB2ETS1FBLMVPMYC

Evidence

Reading pass · 13 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1996 PTPN18 (originally named BDP1/Brain Derived Phosphatase) was identified as a functional protein tyrosine phosphatase with a PEST motif, classified in the PTP-PEST family. It lacks a transmembrane domain, has a calculated molecular weight of ~50 kDa, and was shown to hydrolyze p-Nitrophenylphosphate when expressed in 293 cells, confirming PTPase activity. It was found to differentially dephosphorylate autophosphorylated tyrosine kinases overexpressed in tumor tissues. PCR cloning, transient expression in 293 cells, enzymatic phosphatase assay, northern blot Oncogene Medium 8950995
2001 PTPN18 (PTP-HSCF) interacts with the SH2 domain of Csk via two putative tyrosine phosphorylation sites in its non-catalytic region. Csk and PTPN18 synergize to inhibit Src family kinase signaling, and this cooperativity depends on the domains mediating their association. PTPN18 inactivates Src-related PTKs by selectively dephosphorylating the positive regulatory tyrosine in their kinase domain. Modified yeast two-hybrid screen, co-immunoprecipitation in mammalian cells and hematopoietic cells, transfection/overexpression functional assays Molecular and cellular biology High 11158295
2003 PTPN18 (BDP1) negatively regulates HER2 signaling. Overexpression of PTPN18 inhibited ligand-induced HER2 phosphorylation but not EGFR phosphorylation, demonstrating substrate specificity. Suppression of endogenous PTPN18 increased HER2 phosphorylation. PTPN18 also inhibited phosphorylation of the adaptor protein Gab1 and reduced MAPK activation downstream of HER2. Overexpression and siRNA knockdown in breast cancer cells, immunoprecipitation/western blot for phosphorylation states The Journal of biological chemistry High 14660651
2014 PTPN18 regulates HER2 through two distinct mechanisms: (1) The catalytic domain dephosphorylates HER2 at specific phosphorylation sites (pY1112, pY1196, pY1248), with crystal structures of PTPN18 in complex with HER2 phospho-peptides revealing molecular basis for substrate recognition in two distinct conformations; dephosphorylation of pY1112 blocks lysosomal routing and delays HER2 degradation. (2) The PEST domain of PTPN18 promotes K48-linked ubiquitination of HER2 and its rapid proteasomal destruction via a negative feedback loop, independent of catalytic activity. These two mechanisms define distinct HER2 phosphorylation and ubiquitination barcodes controlling cell growth and migration. X-ray crystallography (3 crystal structures of PTPN18–HER2 phosphopeptide complexes), in vitro enzymology, site-directed mutagenesis, cell-based ubiquitination assays, cell growth/migration assays, co-immunoprecipitation Cell research High 25081058
2020 PTPN18 acts as a positive regulator of EPO/EPOR/JAK2 signaling in hematopoietic progenitor cells. EPO induces phosphorylation of PTPN18 at Y389, modulated by JAK2 inhibitors. Ectopic expression of wild-type PTPN18 (but not a Y389 mutant) promoted EPO dose-dependent cell proliferation and survival, sustained activation of ERK1/2, AKT, STAT5, and JAK2, increased high-molecular-weight EPOR forms, and sharply inhibited EPO-induced phosphorylation of the adaptor RHEX at Y141. Phospho-tyrosine PTM proteomics, ectopic expression with phospho-site mutants, western blot for pathway activation, cell proliferation/survival assays Cellular signalling Medium 32027948
2020 PTPN18 promotes colorectal cancer cell growth by stabilizing the MYC protein, which in turn activates CDK4 expression. MYC was found to interact with PTPN18 by co-immunoprecipitation. PTPN18 overexpression increased MYC protein levels and activated MYC-CDK4 signaling; PTPN18 deficiency had the opposite effect both in vitro and in xenograft assays. Co-immunoprecipitation, overexpression and knockdown in CRC cells, xenograft assay, western blot for pathway components Genes & diseases Medium 34522712
2021 Molecular dynamics simulations revealed that PTPN18 binds HER2 phospho-peptides with differential affinity (pY1248 > pY1196 > pY1112), and binding induces WPD-loop closure through new hydrogen bond and hydrophobic interactions involving residues Tyr62, Asp64, Val65, Ala231, Arg235, and Ala273. Allosteric communication networks from the pY binding loop to the WPD loop were identified, explaining substrate specificity at the atomic level. Molecular dynamics simulations, free energy calculations (MM/GBSA), correlation analysis of allosteric networks Journal of molecular recognition Low 33620127
2021 Silencing of PTPN18 in endometrial cancer cells (KLE) induced ferroptosis, increased intracellular ROS levels, downregulated GPX4 and xCT expression, and induced expression of phospho-p38. This places PTPN18 upstream of the p-p38/GPX4/xCT axis in regulating ferroptosis resistance. Lentiviral shRNA knockdown, ELISA for ROS, western blot for GPX4/xCT/p-p38 Cancer management and research Low 33642877
2022 PTPN18 is translocated from the cytoplasm to the nucleus by MVP (major vault protein) and importin β2 in breast cancer cells. Nuclear PTPN18 dephosphorylates ETS1 transcription factor and promotes its degradation, thereby suppressing TGF-β signaling and epithelial-to-mesenchymal transition. Cytoplasmic PTPN18 does not suppress metastasis, establishing nuclear localization as essential for the anti-metastatic function. Subcellular fractionation, co-immunoprecipitation, ectopic expression with nuclear/cytoplasmic mutants, western blot for ETS1 phosphorylation/degradation, migration/invasion assays, TGF-β signaling readouts Cell death & disease Medium 35982039
2024 HBx protein of hepatitis B virus represses PTPN18 expression by upregulating miR-128-3p. PTPN18 activates the p53 signaling pathway and suppresses the AKT/FOXO1 signaling cascade in hepatocellular carcinoma cells, as identified by phospho-protein microarray screening and validation experiments. Phospho-protein microarray, western blot validation, miRNA overexpression, PTPN18 overexpression/knockdown functional assays Molecular cancer research Medium 38787319
2024 PTPN18 knockdown in endometrial cancer cells suppressed aerobic glycolysis (reduced glucose consumption, lactate production, ATP levels, and glycolysis proteins HIF-1α, PKM2, LDHA), migration, and invasion by inhibiting the MYC/PI3K/AKT pathway. MYC overexpression partially rescued the effects of PTPN18 knockdown, placing PTPN18 upstream of MYC in this pathway. shRNA knockdown, Transwell assay, metabolic assays (glucose consumption, lactate, ATP), western blot, rescue experiment with MYC overexpression Histology and histopathology Medium 38855855
2026 PTPN18 interacts with fibrillarin (FBL) via its R451 residue (with FBL's V187 site being critical on the other side), as identified by mass spectrometry and confirmed by peptide mapping and co-immunoprecipitation. PTPN18 dephosphorylates FBL at Y313 and promotes FBL degradation via the ubiquitin-proteasome pathway. Through FBL regulation, PTPN18 affects MAPK signaling, rRNA 2'-O-methylation, histone H2AQ104 methylation, and RNA synthesis. The PTPN18 R451A mutant loses these activities. Mass spectrometry interactome, peptide mapping, co-immunoprecipitation, site-directed mutagenesis (R451A), phosphatase assay for FBL-Y313, ubiquitination assay, downstream methylation and signaling readouts Cell death & disease High 41559020
2026 PTPN18 binds cyclin E1 (by co-immunoprecipitation) and promotes its degradation via the ubiquitin-proteasome pathway, leading to cell cycle arrest in breast cancer cells. PTPN18 also regulates CDK inhibitors p21 (CDKN1A) and p27 (CDKN1B) through the PI3K/AKT signaling pathway. Cyclin E2 addition did not displace PTPN18 binding to cyclin E1, indicating specificity. Co-immunoprecipitation, ubiquitin-proteasome pathway assay, western blot, cell cycle analysis, PI3K/AKT inhibitor experiments International journal of oncology Medium 41480706

Source papers

Stage 0 corpus · 63 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2012 Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 1718 22658674
2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America 1479 12477932
2021 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. Cell 705 33961781
2011 Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Briefings in bioinformatics 656 21873635
2005 Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Molecular & cellular proteomics : MCP 434 15951569
2002 Mutations in CD2BP1 disrupt binding to PTP PEST and are responsible for PAPA syndrome, an autoinflammatory disorder. Human molecular genetics 341 11971877
2017 Genome-wide CRISPR screen identifies HNRNPL as a prostate cancer dependency regulating RNA splicing. Proceedings of the National Academy of Sciences of the United States of America 282 28611215
2005 Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry. Nature methods 243 16094384
2011 Selected reaction monitoring mass spectrometry reveals the dynamics of signaling through the GRB2 adaptor. Nature biotechnology 172 21706016
2005 Substrate-trapping techniques in the identification of cellular PTP targets. Methods (San Diego, Calif.) 146 15588985
1997 PSTPIP: a tyrosine phosphorylated cleavage furrow-associated protein that is a substrate for a PEST tyrosine phosphatase. The Journal of cell biology 141 9265651
2014 The mammalian-membrane two-hybrid assay (MaMTH) for probing membrane-protein interactions in human cells. Nature methods 131 24658140
2014 In silico prediction of physical protein interactions and characterization of interactome orphans. Nature methods 112 25402006
2000 Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation. Molecular cell 105 11163214
2017 A Global Analysis of the Receptor Tyrosine Kinase-Protein Phosphatase Interactome. Molecular cell 102 28065597
2014 The catalytic region and PEST domain of PTPN18 distinctly regulate the HER2 phosphorylation and ubiquitination barcodes. Cell research 75 25081058
2016 Phenotypic and Interaction Profiling of the Human Phosphatases Identifies Diverse Mitotic Regulators. Cell reports 72 27880917
1998 PSTPIP 2, a second tyrosine phosphorylated, cytoskeletal-associated protein that binds a PEST-type protein-tyrosine phosphatase. The Journal of biological chemistry 66 9804817
2011 The TFIIF-like Rpc37/53 dimer lies at the center of a protein network to connect TFIIIC, Bdp1, and the RNA polymerase III active center. Molecular and cellular biology 62 21536656
2004 CK2 phosphorylation of Bdp1 executes cell cycle-specific RNA polymerase III transcription repression. Molecular cell 53 15469824
2001 SH2 domain-mediated interaction of inhibitory protein tyrosine kinase Csk with protein tyrosine phosphatase-HSCF. Molecular and cellular biology 51 11158295
2020 RIG-I regulates myeloid differentiation by promoting TRIM25-mediated ISGylation. Proceedings of the National Academy of Sciences of the United States of America 47 32513696
2017 Molecular mechanisms of Bdp1 in TFIIIB assembly and RNA polymerase III transcription initiation. Nature communications 46 28743884
2013 Linkage study and exome sequencing identify a BDP1 mutation associated with hereditary hearing loss. PloS one 46 24312468
2003 Negative regulation of HER2 signaling by the PEST-type protein-tyrosine phosphatase BDP1. The Journal of biological chemistry 46 14660651
2002 Essential roles of Bdp1, a subunit of RNA polymerase III initiation factor TFIIIB, in transcription and tRNA processing. Molecular and cellular biology 41 11971960
2021 Silencing of PTPN18 Induced Ferroptosis in Endometrial Cancer Cells Through p-P38-Mediated GPX4/xCT Down-Regulation. Cancer management and research 36 33642877
2016 Defining the Protein-Protein Interaction Network of the Human Protein Tyrosine Phosphatase Family. Molecular & cellular proteomics : MCP 36 27432908
2022 Quantitative fragmentomics allow affinity mapping of interactomes. Nature communications 33 36115835
2003 Protein tyrosine phosphatase PTP20 induces actin cytoskeleton reorganization by dephosphorylating p190 RhoGAP in rat ovarian granulosa cells stimulated with follicle-stimulating hormone. Molecular endocrinology (Baltimore, Md.) 31 12554790
1998 Identification of a novel polyproline recognition site in the cytoskeletal associated protein, proline serine threonine phosphatase interacting protein. The Journal of biological chemistry 27 9422760
2022 Nuclear import of PTPN18 inhibits breast cancer metastasis mediated by MVP and importin β2. Cell death & disease 25 35982039
2005 Transcriptome analysis of human gastric cancer. Mammalian genome : official journal of the International Mammalian Genome Society 24 16341674
1996 Characterization of the PEST family protein tyrosine phosphatase BDP1. Oncogene 23 8950995
2018 Prognostic Value of Phosphotyrosine Phosphatases in Hepatocellular Carcinoma. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology 22 29742497
2024 Rapid iPSC inclusionopathy models shed light on formation, consequence, and molecular subtype of α-synuclein inclusions. Neuron 20 39079530
2019 Downregulation of PTPN18 can inhibit proliferation and metastasis and promote apoptosis of endometrial cancer. Clinical and experimental pharmacology & physiology 20 31034093
2006 Mapping the principal interaction site of the Brf1 and Bdp1 subunits of Saccharomyces cerevisiae TFIIIB. The Journal of biological chemistry 20 16551611
2017 A Human Tyrosine Phosphatase Interactome Mapped by Proteomic Profiling. Journal of proteome research 19 28675297
2003 The Brf1 and Bdp1 subunits of transcription factor TFIIIB bind to overlapping sites in the tetratricopeptide repeats of Tfc4. The Journal of biological chemistry 17 12930823
2020 PTPN18 promotes colorectal cancer progression by regulating the c-MYC-CDK4 axis. Genes & diseases 16 34522712
2015 A Region of Bdp1 Necessary for Transcription Initiation That Is Located within the RNA Polymerase III Active Site Cleft. Molecular and cellular biology 15 26055328
2021 CNKSR1 serves as a scaffold to activate an EGFR phosphatase via exclusive interaction with RhoB-GTP. Life science alliance 14 34187934
2022 PSTPIP1-LYP phosphatase interaction: structural basis and implications for autoinflammatory disorders. Cellular and molecular life sciences : CMLS 10 35152348
2020 Phospho-PTM proteomic discovery of novel EPO- modulated kinases and phosphatases, including PTPN18 as a positive regulator of EPOR/JAK2 Signaling. Cellular signalling 10 32027948
2025 The solute carrier superfamily interactome. Molecular systems biology 9 40355756
2022 Structural insights into acetylated histone ligand recognition by the BDP1 bromodomain of Plasmodium falciparum. International journal of biological macromolecules 9 36328269
2008 Structural characterization of the interaction between TFIIIB components Bdp1 and Brf1. Biochemistry 8 19086269
2018 Bdp1 interacts with SNAPc bound to a U6, but not U1, snRNA gene promoter element to establish a stable protein-DNA complex. FEBS letters 7 29932462
2022 BDP1 Alterations Correlate with Clinical Outcomes in Breast Cancer. Cancers 6 35406430
2021 Molecular dynamics simulation studies on the specific regulation of PTPN18 to the HER2 phospho-peptides. Journal of molecular recognition : JMR 6 33620127
2019 TFIIIB Subunit Bdp1 Participates in RNA Polymerase III Transcription in the Protozoan Parasite Leishmania major. BioMed research international 6 31058184
2022 BDP1 as a biomarker in serous ovarian cancer. Cancer medicine 5 36305848
2020 Assembly of SNAPc, Bdp1, and TBP on the U6 snRNA Gene Promoter in Drosophila melanogaster. Molecular and cellular biology 5 32253345
2006 The zinc finger protein ZNF297B interacts with BDP1, a subunit of TFIIIB. Biological chemistry 4 16542149
2024 Hepatitis B Virus X Protein Represses Expression of Tumor Suppressor PTPN18 in Hepatocellular Carcinoma. Molecular cancer research : MCR 3 38787319
2006 The Saccharomyces cerevisiae RNA polymerase III recruitment factor subunits Brf1 and Bdp1 impose a strict sequence preference for the downstream half of the TATA box. Nucleic acids research 3 17028095
2003 A gene-specific effect of an internal deletion in the Bdp1 subunit of the RNA polymerase III transcription initiation factor TFIIIB. FEBS letters 3 12885403
2024 Mechanism of PTPN18 for regulating the migration and invasion of endometrial cancer cells via the MYC/PI3K/AKT pathway. Histology and histopathology 2 38855855
2023 PTPN18 Serves as a Potential Oncogene for Glioblastoma by Enhancing Immune Suppression. Oxidative medicine and cellular longevity 2 36846716
2022 PTPN18 Stimulates the Development of Ovarian Cancer by Activating the PI3K/AKT Signaling. Evidence-based complementary and alternative medicine : eCAM 2 35310041
2026 PTPN18 functions as a tumor suppressor in breast cancer by negatively regulating cyclin E. International journal of oncology 0 41480706
2026 The R451 site is critical for PTPN18 to exert tumor suppressive effects in breast cancer through the negative regulatory interacting protein fibrillarin. Cell death & disease 0 41559020