PPME1 Gene

Name	protein phosphatase methylesterase 1
Description	This gene encodes a protein phosphatase methylesterase localized to the nucleus. The encoded protein acts on the protein phosphatase-2A catalytic subunit and supports the ERK pathway through dephosphorylation of regulatory proteins. It plays a role in malignant glioma progression. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Oct 2012]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nProtein phosphatase methylesterase‐1 (PME‐1) is a critical regulator of protein phosphatase 2A (PP2A) activity. It catalyzes the demethylation of PP2A’s catalytic subunit at its carboxy‐terminal leucine residue, a modification that is essential for proper holoenzyme assembly and the prevention of premature phosphatase activity. In addition, PME‐1 exhibits a distinct subcellular localization—it is predominantly nuclear—which enables precise spatial control over PP2A demethylation and the stabilization of an inactive PP2A pool."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its core enzymatic function, PME‐1 modulates multiple intracellular signaling pathways. Its demethylating activity contributes to maintaining basal ERK/MAPK pathway signaling, while influencing downstream cascades including AKT, Wnt, and Ca²⁺/calmodulin‐dependent kinase pathways. This modulation has been linked to oncogenic events in several contexts. Moreover, PME‐1 itself is subject to regulation by upstream kinases such as GSK‑3β and CHK1, and its interactions with partners like SIK2 further dictate its association with PP2A. Inhibitor screens have uncovered selective covalent agents that target PME‐1, supporting its emerging role in chemical biology, and β‑catenin-dependent transcription further regulates its expression."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "3", "end_ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nImportantly, aberrant PME‐1 expression and activity are increasingly recognized as critical contributors to human malignancies. In certain cancers such as glioblastoma, endometrial, and prostate tumors, PME‐1 overexpression or gene amplification sustains oncogenic MAPK/ERK and AKT signaling and promotes cellular resistance to apoptosis (e.g., anoikis). Furthermore, PME‐1 dysregulation perturbs mitotic spindle dynamics and modulates cellular responses to oxidative and metabolic stress. Cutting‐edge phosphoproteomic analyses have revealed that PME‐1 regulates unique subsets of phosphorylation sites, distinct from other PP2A modulators, thereby reinforcing its nonredundant role in cellular signaling. These insights have spurred the development of novel inhibitors and provided a rationale for targeting PME‐1 in combination therapeutic strategies."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "17"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Sari Longin, Karen Zwaenepoel, Ellen Martens, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Spatial control of protein phosphatase 2A (de)methylation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Exp Cell Res (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.yexcr.2007.07.030"}], "href": "https://doi.org/10.1016/j.yexcr.2007.07.030"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17803990"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17803990"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Ward Sents, Elitsa Ivanova, Caroline Lambrecht, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The biogenesis of active protein phosphatase 2A holoenzymes: a tightly regulated process creating phosphatase specificity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS J (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/j.1742-4658.2012.08579.x"}], "href": "https://doi.org/10.1111/j.1742-4658.2012.08579.x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22443683"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22443683"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Pietri Puustinen, Melissa R Junttila, Sari Vanhatupa, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PME-1 protects extracellular signal-regulated kinase pathway activity from protein phosphatase 2A-mediated inactivation in human malignant glioma."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Res (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1158/0008-5472.CAN-08-2760"}], "href": "https://doi.org/10.1158/0008-5472.CAN-08-2760"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19293187"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19293187"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Daniel A Bachovchin, Justin T Mohr, Anna E Speers, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Academic cross-fertilization by public screening yields a remarkable class of protein phosphatase methylesterase-1 inhibitors."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.1015248108"}], "href": "https://doi.org/10.1073/pnas.1015248108"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21398589"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21398589"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Xiu-Qing Yao, Xia-Chun Li, Xiao-Xue Zhang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Glycogen synthase kinase-3β regulates leucine-309 demethylation of protein phosphatase-2A via PPMT1 and PME-1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS Lett (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.febslet.2012.06.018"}], "href": "https://doi.org/10.1016/j.febslet.2012.06.018"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22732552"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22732552"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Chia-Wei Lee, Fu-Chia Yang, Hsin-Yun Chang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Interaction between salt-inducible kinase 2 and protein phosphatase 2A regulates the activity of calcium/calmodulin-dependent protein kinase I and protein phosphatase methylesterase-1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M113.540229"}], "href": "https://doi.org/10.1074/jbc.M113.540229"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24841198"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24841198"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Nana Jin, Ruirui Shi, Yanli Jiang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Glycogen synthase kinase-3β suppresses the expression of protein phosphatase methylesterase-1 through β-catenin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Aging (Albany NY) (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.18632/aging.102413"}], "href": "https://doi.org/10.18632/aging.102413"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31714894"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31714894"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Sana Ando, Keiko Tanaka, Maharu Matsumoto, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The luciferase-based in vivo protein-protein interaction assay revealed that CHK1 promotes PP2A and PME-1 interaction."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.jbc.2024.107277"}], "href": "https://doi.org/10.1016/j.jbc.2024.107277"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "38588804"}], "href": "https://pubmed.ncbi.nlm.nih.gov/38588804"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Jing Li, Sufang Han, Ziliang Qian, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Genetic amplification of PPME1 in gastric and lung cancer and its potential as a novel therapeutic target."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Biol Ther (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.4161/cbt.27146"}], "href": "https://doi.org/10.4161/cbt.27146"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24253382"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24253382"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Xiaoyu Xia, Ankur Gholkar, Silvia Senese, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A LCMT1-PME-1 methylation equilibrium controls mitotic spindle size."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Cycle (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1080/15384101.2015.1026487"}], "href": "https://doi.org/10.1080/15384101.2015.1026487"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25839665"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25839665"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Michelle Pusey, Sophie Bail, Yan Xu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Inhibition of protein methylesterase 1 decreased cancerous phenotypes in endometrial adenocarcinoma cell lines and xenograft tumor models."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Tumour Biol (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s13277-016-5036-8"}], "href": "https://doi.org/10.1007/s13277-016-5036-8"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27048286"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27048286"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Kamalakannan Palanichamy, Suman Kanji, Nicolaus Gordon, et al. "}, {"type": "b", "children": [{"type": "t", "text": "NNMT Silencing Activates Tumor Suppressor PP2A, Inactivates Oncogenic STKs, and Inhibits Tumor Forming Ability."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Clin Cancer Res (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1158/1078-0432.CCR-16-1323"}], "href": "https://doi.org/10.1158/1078-0432.CCR-16-1323"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27810903"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27810903"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Amanpreet Kaur, Jukka Westermarck "}, {"type": "b", "children": [{"type": "t", "text": "Regulation of protein phosphatase 2A (PP2A) tumor suppressor function by PME-1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Soc Trans (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1042/BST20160161"}], "href": "https://doi.org/10.1042/BST20160161"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27913678"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27913678"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Soo-Yeon Kim, Jihye Choi, Da-Hye Lee, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PME-1 is regulated by USP36 in ERK and Akt signaling pathways."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS Lett (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/1873-3468.13039"}], "href": "https://doi.org/10.1002/1873-3468.13039"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29577269"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29577269"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Shen Tang, Cailing Lu, Laiming Mo, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Hydrogen peroxide redistributes the localization of protein phosphatase methylesterase 1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Life Sci (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.lfs.2018.10.029"}], "href": "https://doi.org/10.1016/j.lfs.2018.10.029"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30340029"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30340029"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Otto Kauko, Susumu Y Imanishi, Evgeny Kulesskiy, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Phosphoproteome and drug-response effects mediated by the three protein phosphatase 2A inhibitor proteins CIP2A, SET, and PME-1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.RA119.011265"}], "href": "https://doi.org/10.1074/jbc.RA119.011265"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32071079"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32071079"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Anna Aakula, Aleksi Isomursu, Christian Rupp, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PP2A methylesterase PME-1 suppresses anoikis and is associated with therapy relapse of PTEN-deficient prostate cancers."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Oncol (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/1878-0261.13353"}], "href": "https://doi.org/10.1002/1878-0261.13353"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36461911"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36461911"}]}]}]}
Synonyms	PME-1
Proteins	PPME1_HUMAN
NCBI Gene ID	51400
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

PPME1 has 7,659 functional associations with biological entities spanning 9 categories (molecular profile, organism, chemical, functional term, phrase or reference, disease, phenotype or trait, structural feature, cell line, cell type or tissue, gene, protein or microRNA, sequence feature) extracted from 123 datasets.

Click the + buttons to view associations for PPME1 from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

PPME1 Gene

Functional Associations

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

	Dataset	Summary
	Achilles Cell Line Gene Essentiality Profiles	cell lines with fitness changed by PPME1 gene knockdown relative to other cell lines from the Achilles Cell Line Gene Essentiality Profiles dataset.
	Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of PPME1 gene relative to other tissues from the Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles dataset.
	Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles	tissues with high or low expression of PPME1 gene relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.
	Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles	tissue samples with high or low expression of PPME1 gene relative to other tissue samples from the Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles dataset.
	Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by Microarray	tissue samples with high or low expression of PPME1 gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by Microarray dataset.
	Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq	tissue samples with high or low expression of PPME1 gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq dataset.
	Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of PPME1 gene relative to other tissues from the Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles dataset.
	BioGPS Cell Line Gene Expression Profiles	cell lines with high or low expression of PPME1 gene relative to other cell lines from the BioGPS Cell Line Gene Expression Profiles dataset.
	BioGPS Human Cell Type and Tissue Gene Expression Profiles	cell types and tissues with high or low expression of PPME1 gene relative to other cell types and tissues from the BioGPS Human Cell Type and Tissue Gene Expression Profiles dataset.
	BioGPS Mouse Cell Type and Tissue Gene Expression Profiles	cell types and tissues with high or low expression of PPME1 gene relative to other cell types and tissues from the BioGPS Mouse Cell Type and Tissue Gene Expression Profiles dataset.
	Carcinogenome Chemical Perturbation Carcinogenicity Signatures	small molecule perturbations changing expression of PPME1 gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of PPME1 gene relative to other cell lines from the CCLE Cell Line Gene CNV Profiles dataset.
	CCLE Cell Line Gene Expression Profiles	cell lines with high or low expression of PPME1 gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with PPME1 protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with PPME1 gene from the CellMarker Gene-Cell Type Associations dataset.
	ChEA Transcription Factor Binding Site Profiles	transcription factor binding site profiles with transcription factor binding evidence at the promoter of PPME1 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of PPME1 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets dataset.
	ChEA Transcription Factor Targets 2022	transcription factors binding the promoter of PPME1 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
	CM4AI KOLF21J CRISPRi Gene Perturbation Atlas	gene perturbations changing expression of PPME1 gene from the CM4AI KOLF21J CRISPRi Gene Perturbation Atlas dataset.
	CM4AI U2OS Cell Map Protein Localization Assemblies	assemblies containing PPME1 protein from integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.
	CMAP Signatures of Differentially Expressed Genes for Small Molecules	small molecule perturbations changing expression of PPME1 gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores	cellular components containing PPME1 protein in low- or high-throughput protein localization assays from the COMPARTMENTS Experimental Protein Localization Evidence Scores dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores	cellular components co-occuring with PPME1 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025	cellular components co-occuring with PPME1 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
	CORUM Protein Complexes	protein complexs containing PPME1 protein from the CORUM Protein Complexes dataset.
	COSMIC Cell Line Gene CNV Profiles	cell lines with high or low copy number of PPME1 gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with PPME1 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with PPME1 gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with PPME1 gene/protein from the curated CTD Gene-Disease Associations dataset.
	dbGAP Gene-Trait Associations	traits associated with PPME1 gene in GWAS and other genetic association datasets from the dbGAP Gene-Trait Associations dataset.
	DeepCoverMOA Drug Mechanisms of Action	small molecule perturbations with high or low expression of PPME1 protein relative to other small molecule perturbations from the DeepCoverMOA Drug Mechanisms of Action dataset.
	DepMap CRISPR Gene Dependency	cell lines with fitness changed by PPME1 gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DGIdb Drug Targets 2026	interacting drugs for PPME1 protein from the DGIdb Drug Targets 2026 dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with PPME1 gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores 2025	diseases co-occuring with PPME1 gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.
	DisGeNET Gene-Disease Associations	diseases associated with PPME1 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	ENCODE Histone Modification Site Profiles	histone modification site profiles with high histone modification abundance at PPME1 gene from the ENCODE Histone Modification Site Profiles dataset.
	ENCODE Transcription Factor Binding Site Profiles	transcription factor binding site profiles with transcription factor binding evidence at the promoter of PPME1 gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of PPME1 gene in ChIP-seq datasets from the ENCODE Transcription Factor Targets dataset.
	ESCAPE Omics Signatures of Genes and Proteins for Stem Cells	PubMedIDs of publications reporting gene signatures containing PPME1 from the ESCAPE Omics Signatures of Genes and Proteins for Stem Cells dataset.