PTPRF Gene

HGNC Family	Immunoglobulin superfamily domain containing, Phosphatases, Fibronectin type III domain containing
Name	protein tyrosine phosphatase, receptor type, F
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 intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. The extracellular region contains three Ig-like domains, and nine non-Ig like domains similar to that of neural-cell adhesion molecule. This PTP was shown to function in the regulation of epithelial cell-cell contacts at adherents junctions, as well as in the control of beta-catenin signaling. An increased expression level of this protein was found in the insulin-responsive tissue of obese, insulin-resistant individuals, and may contribute to the pathogenesis of insulin resistance. Two alternatively spliced transcript variants of this gene, which encode distinct proteins, have been reported. [provided by RefSeq, Jul 2008]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPTPRF, also known as the leukocyte common antigen‐related (LAR) protein, is a receptor-type protein tyrosine phosphatase that plays multifaceted roles in neural development and synapse formation. It mediates trans‐synaptic adhesion by interacting with ligands such as NGL-3 and netrin-G1, and its extracellular region undergoes sequential proteolytic processing that modulates its association with adhesion molecules like β-catenin—thereby influencing synaptic differentiation and neuronal network assembly. This dynamic interplay between ligand binding, proteolytic cleavage, and subsequent intracellular signaling helps couple initial axo–dendritic adhesion to the induction of presynaptic differentiation."}, {"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 addition to its neuronal functions, PTPRF is a key regulator of cell signaling in metabolic and immune contexts. Its expression is regulated in a cell-density–dependent manner through E-cadherin–mediated adhesion, which impacts contact inhibition and proper T cell development via dephosphorylation of Src family kinases such as Lck and Fyn. Moreover, PTPRF modulates insulin receptor signaling by attenuating downstream pathways—affecting both insulin sensitivity and adipogenesis—where reduced PTPRF activity has been linked to post-receptor insulin resistance and altered adipocyte differentiation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPTPRF’s signaling versatility is further underscored by its involvement in tumorigenesis and cancer progression. In various tumor models, altered levels or post-translational modifications of PTPRF affect key oncogenic pathways such as those driven by the Wnt/β-catenin cascade, with its promoter also being responsive to PPARγ. In liver and colorectal cancers, modulation of PTPRF expression—whether through microRNA-mediated suppression or interactions with cell-surface proteins like TM4SF5 and CD133—can yield either tumor suppressive or oncogenic outcomes. Additionally, structural studies have revealed that PTPRF can bind ligands such as heparin and promote the formation of actin-based protrusions (cytonemes), implicating it in the regulation of cell motility and intercellular communication."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "19"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Jens E Ruhe, Sylvia Streit, Stefan Hart, et al. "}, {"type": "b", "children": [{"type": "t", "text": "EGFR signaling leads to downregulation of PTP-LAR via TACE-mediated proteolytic processing."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Signal (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cellsig.2005.12.003"}], "href": "https://doi.org/10.1016/j.cellsig.2005.12.003"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16478662"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16478662"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Annakaisa Haapasalo, Doo Yeon Kim, Bryce W Carey, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Presenilin/gamma-secretase-mediated cleavage regulates association of leukocyte-common antigen-related (LAR) receptor tyrosine phosphatase with beta-catenin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M611324200"}], "href": "https://doi.org/10.1074/jbc.M611324200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17259169"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17259169"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Seok-Kyu Kwon, Jooyeon Woo, Soo-Young Kim, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Trans-synaptic adhesions between netrin-G ligand-3 (NGL-3) and receptor tyrosine phosphatases LAR, protein-tyrosine phosphatase delta (PTPdelta), and PTPsigma via specific domains regulate excitatory synapse formation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M109.061127"}], "href": "https://doi.org/10.1074/jbc.M109.061127"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20139422"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20139422"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Yoo Sung Song, Hye-Jin Lee, Pavel Prosselkov, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Trans-induced cis interaction in the tripartite NGL-1, netrin-G1 and LAR adhesion complex promotes development of excitatory synapses."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.129718"}], "href": "https://doi.org/10.1242/jcs.129718"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23986473"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23986473"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Javelle R Symons, Charles M LeVea, Robert A Mooney "}, {"type": "b", "children": [{"type": "t", "text": "Expression of the leucocyte common antigen-related (LAR) tyrosine phosphatase is regulated by cell density through functional E-cadherin complexes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem J (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1042/BJ20020381"}], "href": "https://doi.org/10.1042/BJ20020381"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12095414"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12095414"}]}, {"type": "r", "ref": 6, "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": 7, "children": [{"type": "t", "text": "Kazutake Tsujikawa, Tomoko Ichijo, Kazuki Moriyama, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Regulation of Lck and Fyn tyrosine kinase activities by transmembrane protein tyrosine phosphatase leukocyte common antigen-related molecule."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cancer Res (2002)"}]}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12496362"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12496362"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Giuseppe Miscio, Vittorio Tassi, Angelo Coco, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The allelic variant of LAR gene promoter -127 bp T-->A is associated with reduced risk of obesity and other features related to insulin resistance."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Mol Med (Berl) (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s00109-004-0544-1"}], "href": "https://doi.org/10.1007/s00109-004-0544-1"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15150650"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15150650"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Ann Mander, Conrad P Hodgkinson, Graham J Sale "}, {"type": "b", "children": [{"type": "t", "text": "Knock-down of LAR protein tyrosine phosphatase induces insulin resistance."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS Lett (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.febslet.2005.04.057"}], "href": "https://doi.org/10.1016/j.febslet.2005.04.057"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15896785"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15896785"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "N Seki, S Yagi, Y Suzuki, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein tyrosine phosphatase regulation in fibroblasts from patients with an insulin receptor gene mutation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Horm Metab Res (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1055/s-0028-1082082"}], "href": "https://doi.org/10.1055/s-0028-1082082"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18925540"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18925540"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Won-Kon Kim, Hyeyun Jung, Do-Hyung Kim, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Regulation of adipogenic differentiation by LAR tyrosine phosphatase in human mesenchymal stem cells and 3T3-L1 preadipocytes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.053009"}], "href": "https://doi.org/10.1242/jcs.053009"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19910497"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19910497"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Rabindranath Bera, Chih-Yung Chiou, Ming-Chin Yu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Functional genomics identified a novel protein tyrosine phosphatase receptor type F-mediated growth inhibition in hepatocarcinogenesis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hepatology (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/hep.27030"}], "href": "https://doi.org/10.1002/hep.27030"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24470239"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24470239"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Denis Soulières, Fred R Hirsch, Frances A Shepherd, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PTPRF Expression as a Potential Prognostic/Predictive Marker for Treatment with Erlotinib in Non-Small-Cell Lung Cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Thorac Oncol (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1097/JTO.0000000000000624"}], "href": "https://doi.org/10.1097/JTO.0000000000000624"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26291013"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26291013"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Qi Gao, Jeong-Yeh Yang, Kelley W Moremen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structural Characterization of a Heparan Sulfate Pentamer Interacting with LAR-Ig1-2."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochemistry (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/acs.biochem.8b00241"}], "href": "https://doi.org/10.1021/acs.biochem.8b00241"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29570275"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29570275"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Somi Kim, Chang Yun Cho, Doohyung Lee, et al. "}, {"type": "b", "children": [{"type": "t", "text": "CD133-induced TM4SF5 expression promotes sphere growth via recruitment and blocking of protein tyrosine phosphatase receptor type F (PTPRF)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Lett (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.canlet.2018.09.009"}], "href": "https://doi.org/10.1016/j.canlet.2018.09.009"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30217560"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30217560"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Y-Y Xu, H Liu, L Su, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PPARγ inhibits breast cancer progression by upregulating PTPRF expression."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Eur Rev Med Pharmacol Sci (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.26355/eurrev_201911_19563"}], "href": "https://doi.org/10.26355/eurrev_201911_19563"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31799666"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31799666"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Tong Gan, Ashley T Stevens, Xiaopeng Xiong, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Inhibition of protein tyrosine phosphatase receptor type F suppresses Wnt signaling in colorectal cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41388-020-01472-z"}], "href": "https://doi.org/10.1038/s41388-020-01472-z"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32973331"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32973331"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Xiangyang Ye, Rongxian Qiu, Xiongzhi He, et al. "}, {"type": "b", "children": [{"type": "t", "text": "miR-647 inhibits hepatocellular carcinoma cell progression by targeting protein tyrosine phosphatase receptor type F."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Bioengineered (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1080/21655979.2021.2017628"}], "href": "https://doi.org/10.1080/21655979.2021.2017628"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34969357"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34969357"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Mai Quynh Nguyen, Manabu Taniguchi, Misato Yasumura, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cytoneme-like protrusion formation induced by LAR is promoted by receptor dimerization."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biol Open (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/bio.059024"}], "href": "https://doi.org/10.1242/bio.059024"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35735010"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35735010"}]}]}]}
Synonyms	LAR, BNAH2
Proteins	PTPRF_HUMAN
NCBI Gene ID	5792
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

PTPRF has 9,786 functional associations with biological entities spanning 9 categories (molecular profile, organism, chemical, disease, phenotype or trait, functional term, phrase or reference, structural feature, cell line, cell type or tissue, gene, protein or microRNA, sequence feature) extracted from 135 datasets.

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

If available, associations are ranked by standardized value

Harmonizome 3.0

PTPRF 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 PTPRF 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 PTPRF gene relative to other tissues from the Allen Brain Atlas Adult Human 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 PTPRF 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 PTPRF 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 PTPRF 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 PTPRF 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 PTPRF 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 PTPRF 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 PTPRF 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 PTPRF gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of PTPRF 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 PTPRF gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with PTPRF protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with PTPRF 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 PTPRF gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of PTPRF 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 PTPRF gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
	ClinVar Gene-Phenotype Associations 2025	phenotypes associated with PTPRF gene from the curated ClinVar Gene-Phenotype Associations 2025 dataset.
	CMAP Signatures of Differentially Expressed Genes for Small Molecules	small molecule perturbations changing expression of PTPRF gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing PTPRF protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores	cellular components containing PTPRF protein in low- or high-throughput protein localization assays from the COMPARTMENTS Experimental Protein Localization Evidence Scores dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores 2025	cellular components containing PTPRF protein in low- or high-throughput protein localization assays from the COMPARTMENTS Experimental Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores	cellular components co-occuring with PTPRF 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 PTPRF 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 PTPRF gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with PTPRF gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with PTPRF gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with PTPRF gene/protein from the curated CTD Gene-Disease Associations dataset.
	DeepCoverMOA Drug Mechanisms of Action	small molecule perturbations with high or low expression of PTPRF 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 PTPRF gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DEPOD Substrates of Phosphatases	phosphatases that dephosphorylate PTPRF protein from the curated DEPOD Substrates of Phosphatases dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores	diseases associated with PTPRF gene in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores 2025	diseases associated with PTPRF gene in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores 2025 dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with PTPRF 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 PTPRF 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 PTPRF gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with PTPRF 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 PTPRF 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 PTPRF gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of PTPRF gene in ChIP-seq datasets from the ENCODE Transcription Factor Targets dataset.