PTPRM Gene

HGNC Family	Immunoglobulin superfamily domain containing, Fibronectin type III domain containing, Phosphatases
Name	protein tyrosine phosphatase, receptor type, M
Description	The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region, a single transmembrane region, and two tandem catalytic domains, and thus represents a receptor-type PTP. The extracellular region contains a meprin-A5 antigen-PTP mu (MAM) domain, an Ig-like domain and four fibronectin type III-like repeats. This PTP has been shown to mediate cell-cell aggregation through the interaction with another molecule of this PTP on an adjacent cell. This PTP can interact with scaffolding protein RACK1/GNB2L1, which may be necessary for the downstream signaling in response to cell-cell adhesion. Alternative splicing results in multiple transcripts encoding distinct isoforms. [provided by RefSeq, Jul 2008]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nReceptor protein tyrosine phosphatase mu (PTPRM) is a transmembrane signaling molecule characterized by an extracellular region that mediates homophilic cell–cell adhesion and an intracellular segment harboring dual phosphatase domains. Structural and biochemical studies have revealed that the extended, rigid ectodomain of PTPRM acts as a molecular “distance gauge” at sites of cell‐cell contact, while interactions between its membrane–proximal and distally located PTP domains contribute to binding specificity and regulation of adjacent receptor complexes. In vivo expression analyses further demonstrate that PTPRM is localized not only to neuronal and glial cells but also to arterial endothelial cells, underscoring its versatile roles in tissue organization and intercellular adhesion."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the nervous system, PTPRM is instrumental in transducing adhesion‐mediated signals that regulate neurite outgrowth, axonal guidance, and cadherin-dependent cell–cell adhesion. Its direct association with intracellular effectors—including regulators of Rho GTPases such as IQGAP1 and BCCIP—further refines cytoskeletal dynamics and directional signaling during neuronal development."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAbnormal regulation of PTPRM is a recurring theme in cancer, particularly in aggressive gliomas. In these malignancies, full-length PTPRM is frequently lost through downregulation by microRNAs or proteolytic cleavage, leading to the accumulation of intracellular phosphatase fragments. Such alterations correlate with increased tumor cell migration, enhanced anchorage-independent growth, and greater dispersal of glioma cells. Moreover, post-translational modifications such as aberrant glycosylation further diminish its catalytic activity, collectively tipping the balance toward oncogene-driven signaling and tumor progression."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond gliomas, PTPRM also plays critical roles in other cancer types by modulating key tyrosine phosphorylation events. In lung epithelia, for instance, PTPRM dephosphorylates specific residues on the epidermal growth factor receptor (EGFR), thereby tempering downstream pathways that drive cell migration. In breast cancer, its expression is linked to the regulation of intercellular adhesion, and in cervical cancer, elevated levels of PTPRM have been associated with enhanced proliferation, epithelial–mesenchymal transition, and lymph node metastasis—processes that are mediated, in part, through the Src–AKT and STAT3 signaling cascades."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Christophe Blanchetot, Leon G Tertoolen, John Overvoorde, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M205810200"}], "href": "https://doi.org/10.1074/jbc.M205810200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12376545"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12376545"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Elianne A Koop, Susana M Chuva de Sousa Lopes, Elles Feiken, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Receptor protein tyrosine phosphatase mu expression as a marker for endothelial cell heterogeneity; analysis of RPTPmu gene expression using LacZ knock-in mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Int J Dev Biol (2003)"}]}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12895029"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12895029"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "A Radu Aricescu, Christian Siebold, Kaushik Choudhuri, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structure of a tyrosine phosphatase adhesive interaction reveals a spacer-clamp mechanism."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Science (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1126/science.1144646"}], "href": "https://doi.org/10.1126/science.1144646"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17761881"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17761881"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Iain M Hay, Maria Shamin, Eve R Caroe, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Determinants of receptor tyrosine phosphatase homophilic adhesion: Structural comparison of PTPRK and PTPRM extracellular domains."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.jbc.2022.102750"}], "href": "https://doi.org/10.1016/j.jbc.2022.102750"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36436563"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36436563"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Polly J Phillips-Mason, Theresa J Gates, Denice L Major, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The receptor protein-tyrosine phosphatase PTPmu interacts with IQGAP1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M506414200"}], "href": "https://doi.org/10.1074/jbc.M506414200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16380380"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16380380"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Polly J Phillips-Mason, Tracy Mourton, Denice L Major, et al. "}, {"type": "b", "children": [{"type": "t", "text": "BCCIP associates with the receptor protein tyrosine phosphatase PTPmu."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Biochem (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/jcb.21907"}], "href": "https://doi.org/10.1002/jcb.21907"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18773424"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18773424"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Adam M Burgoyne, Juan M Palomo, Polly J Phillips-Mason, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PTPmu suppresses glioma cell migration and dispersal."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Neuro Oncol (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1215/15228517-2009-019"}], "href": "https://doi.org/10.1215/15228517-2009-019"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19304959"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19304959"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Adam M Burgoyne, Polly J Phillips-Mason, Susan M Burden-Gulley, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Proteolytic cleavage of protein tyrosine phosphatase mu regulates glioblastoma cell migration."}]}, {"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-09-0863"}], "href": "https://doi.org/10.1158/0008-5472.CAN-09-0863"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19690139"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19690139"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "C Quintavalle, M Garofalo, C Zanca, et al. "}, {"type": "b", "children": [{"type": "t", "text": "miR-221/222 overexpession in human glioblastoma increases invasiveness by targeting the protein phosphate PTPμ."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/onc.2011.280"}], "href": "https://doi.org/10.1038/onc.2011.280"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21743492"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21743492"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Harpreet Kaur, Susan M Burden-Gulley, Polly J Phillips-Mason, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein tyrosine phosphatase mu regulates glioblastoma cell growth and survival in vivo."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Neuro Oncol (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/neuonc/nos066"}], "href": "https://doi.org/10.1093/neuonc/nos066"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22505657"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22505657"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Polly J Phillips-Mason, Sonya E L Craig, Susann M Brady-Kalnay "}, {"type": "b", "children": [{"type": "t", "text": "A protease storm cleaves a cell-cell adhesion molecule in cancer: multiple proteases converge to regulate PTPmu in glioma cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Biochem (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/jcb.24824"}], "href": "https://doi.org/10.1002/jcb.24824"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24771611"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24771611"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Yan Gao, Fuming Yang, Zuopeng Su, et al. "}, {"type": "b", "children": [{"type": "t", "text": "β1,6 GlcNAc branches-modified protein tyrosine phosphatase Mu attenuates its tyrosine phosphatase activity and promotes glioma cell migration through PLCγ-PKC pathways."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2018.09.150"}], "href": "https://doi.org/10.1016/j.bbrc.2018.09.150"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30274773"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30274773"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Sang W Hyun, Ian E Anglin, Anguo Liu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Diverse injurious stimuli reduce protein tyrosine phosphatase-μ expression and enhance epidermal growth factor receptor signaling in human airway epithelia."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Exp Lung Res (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3109/01902148.2011.566673"}], "href": "https://doi.org/10.3109/01902148.2011.566673"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21649524"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21649524"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Ping-Hui Sun, Lin Ye, Malcolm D Mason, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein tyrosine phosphatase µ (PTP µ or PTPRM), a negative regulator of proliferation and invasion of breast cancer cells, is associated with disease prognosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS One (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pone.0050183"}], "href": "https://doi.org/10.1371/journal.pone.0050183"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23185569"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23185569"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Pan Liu, Chunyu Zhang, Yuandong Liao, et al. "}, {"type": "b", "children": [{"type": "t", "text": "High expression of PTPRM predicts poor prognosis and promotes tumor growth and lymph node metastasis in cervical cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Death Dis (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41419-020-02826-x"}], "href": "https://doi.org/10.1038/s41419-020-02826-x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32826853"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32826853"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Jian Song, Di Zhao, Guozhu Sun, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PTPRM methylation induced by FN1 promotes the development of glioblastoma by activating STAT3 signalling."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Pharm Biol (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1080/13880209.2021.1944220"}], "href": "https://doi.org/10.1080/13880209.2021.1944220"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34225581"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34225581"}]}]}]}
Synonyms	HR-PTPU, RPTPM, PTPRL1, RPTPU, R-PTP-MU
Proteins	PTPRM_HUMAN
NCBI Gene ID	5797
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

PTPRM has 9,759 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 129 datasets.

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

If available, associations are ranked by standardized value

Harmonizome 3.0

PTPRM 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 PTPRM 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 PTPRM 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 PTPRM 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 PTPRM 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 PTPRM 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 PTPRM 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 PTPRM 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 PTPRM 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 PTPRM 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 PTPRM 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 PTPRM gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of PTPRM 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 PTPRM gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with PTPRM protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with PTPRM 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 PTPRM gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of PTPRM 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 PTPRM 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 PTPRM gene from the CM4AI KOLF21J CRISPRi Gene Perturbation Atlas dataset.
	CM4AI U2OS Cell Map Protein Localization Assemblies	assemblies containing PTPRM 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 PTPRM gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing PTPRM protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing PTPRM protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores	cellular components co-occuring with PTPRM 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 PTPRM protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
	COSMIC Cell Line Gene CNV Profiles	cell lines with high or low copy number of PTPRM gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with PTPRM gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with PTPRM gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with PTPRM gene/protein from the curated CTD Gene-Disease Associations dataset.
	dbGAP Gene-Trait Associations	traits associated with PTPRM gene in GWAS and other genetic association datasets from the dbGAP Gene-Trait Associations dataset.
	DepMap CRISPR Gene Dependency	cell lines with fitness changed by PTPRM gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DGIdb Drug Targets 2026	interacting drugs for PTPRM protein from the DGIdb Drug Targets 2026 dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores	diseases associated with PTPRM gene in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with PTPRM 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 PTPRM 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 PTPRM gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with PTPRM gene in GWAS and other genetic association datasets from the DisGeNET Gene-Phenoptype Associations dataset.
	ENCODE Histone Modification Site Profiles	histone modification site profiles with high histone modification abundance at PTPRM 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 PTPRM gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of PTPRM gene in ChIP-seq datasets from the ENCODE Transcription Factor Targets dataset.