PTPRS Gene

HGNC Family	Immunoglobulin superfamily domain containing, Fibronectin type III domain containing, Phosphatases
Name	protein tyrosine phosphatase, receptor type, S
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 contains an extracellular region, a single transmembrane segment and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. The extracellular region of this protein is composed of multiple Ig-like and fibronectin type III-like domains. Studies of the similar gene in mice suggested that this PTP may be involved in cell-cell interaction, primary axonogenesis, and axon guidance during embryogenesis. This PTP has been also implicated in the molecular control of adult nerve repair. Four alternatively spliced transcript variants, which encode distinct proteins, have been reported. [provided by RefSeq, Jul 2008]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPTPRS (also known as receptor protein tyrosine phosphatase σ) plays a central role in neural development by modulating neuronal extension and synapse formation. In response to extracellular cues, such as chondroitin sulfate and heparan sulfate proteoglycans, PTPRS undergoes ligand‐induced conformational changes and oligomerization to switch between inhibitory and growth‐promoting functions. These dynamic interactions regulate trans-synaptic adhesion and synaptic vesicle accumulation via partnerships with cell adhesion molecules (e.g., NGL-3, TrkC, and other LAR family members), thereby fine-tuning neurite outgrowth and circuit assembly."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its neural roles, alterations in PTPRS are implicated in oncogenic signaling. In several cancers—including head and neck, lung, colorectal, hepatocellular, and bile duct carcinomas—loss of PTPRS function (via microdeletions, down-regulation, or inactivating mutations) disrupts its normal suppression of growth factor pathways. This leads to hyperactivation of EGFR/PI3K/RAS/ERK cascades and aberrant STAT3 phosphorylation, thereby promoting cellular proliferation, invasion, and metastasis. These findings position PTPRS as a tumor suppressor whose genetic and epigenetic alterations bear significant prognostic implications."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPTPRS also exerts important functions in immune regulation, autophagy, and metabolic homeostasis. In immune cells such as plasmacytoid dendritic cells, it serves as an inhibitory receptor that dampens type I interferon production, while its altered expression is linked to inflammatory bowel disease and rheumatoid arthritis through dysregulation of adherens junction proteins. Moreover, loss of PTPRS activity increases phosphatidylinositol-3-phosphate levels, thereby hyperactivating autophagy. Genetic variants and alternative splicing events in the PTPRS gene further influence susceptibility to type 2 diabetes and may contribute to epigenetic changes associated with early-life obesity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "14", "end_ref": "19"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAt the mechanistic level, detailed structural studies have revealed that PTPRS is comprised of tandem phosphatase domains whose intramolecular interactions are critical for regulating catalytic activity and substrate specificity. Crystallographic analyses comparing mouse and human proteins highlight differences in domain conformation and substrate preference, while proximity-labeling proteomic approaches have uncovered a network of interacting proteins—including cortactin—that likely mediate its diverse biological functions. In addition, alternative splicing generates receptor variants with differential responses to ligands such as α-latrotoxin, further emphasizing the nuanced regulation of its signaling output."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "20", "end_ref": "23"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nEmerging evidence also indicates a neuroprotective role for PTPRS in neurodegenerative disease. Specific genetic variants of the PTPRS gene are associated with higher transcript abundance and preservation of synaptic integrity, which correlate with lower levels of phosphorylated tau and delayed onset of Alzheimer’s disease. These findings underscore the potential of targeting PTPRS-mediated pathways to mitigate synaptic degeneration and neurotoxicity."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "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": 2, "children": [{"type": "t", "text": "Yuntao Duan, Roman J Giger "}, {"type": "b", "children": [{"type": "t", "text": "A new role for RPTPsigma in spinal cord injury: signaling chondroitin sulfate proteoglycan inhibition."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Signal (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1126/scisignal.3110pe6"}], "href": "https://doi.org/10.1126/scisignal.3110pe6"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20179269"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20179269"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Charlotte H Coles, Yingjie Shen, Alan P Tenney, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Proteoglycan-specific molecular switch for RPTPσ clustering and neuronal extension."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Science (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1126/science.1200840"}], "href": "https://doi.org/10.1126/science.1200840"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21454754"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21454754"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Xigui Chen, Tomoyuki Yoshida, Hiroshi Sagara, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein tyrosine phosphatase σ regulates the synapse number of zebrafish olfactory sensory neurons."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Neurochem (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/j.1471-4159.2011.07411.x"}], "href": "https://doi.org/10.1111/j.1471-4159.2011.07411.x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21812780"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21812780"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Charlotte H Coles, Nikolaos Mitakidis, Peng Zhang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structural basis for extracellular cis and trans RPTPσ signal competition in synaptogenesis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ncomms6209"}], "href": "https://doi.org/10.1038/ncomms6209"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25385546"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25385546"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Kouki Tadai, Tatsumasa Shioiri, Jun Tsuchimoto, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Interaction of receptor type of protein tyrosine phosphatase sigma (RPTPσ) with a glycosaminoglycan library."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biochem (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/jb/mvy027"}], "href": "https://doi.org/10.1093/jb/mvy027"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29420785"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29420785"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Sebastian Korff, Stefan M Woerner, Yan P Yuan, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Frameshift mutations in coding repeats of protein tyrosine phosphatase genes in colorectal tumors with microsatellite instability."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "BMC Cancer (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/1471-2407-8-329"}], "href": "https://doi.org/10.1186/1471-2407-8-329"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19000305"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19000305"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Luc G T Morris, Barry S Taylor, Trever G Bivona, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Genomic dissection of the epidermal growth factor receptor (EGFR)/PI3K pathway reveals frequent deletion of the EGFR phosphatase PTPRS in head and neck cancers."}]}, {"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.1111963108"}], "href": "https://doi.org/10.1073/pnas.1111963108"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22065749"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22065749"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Guoliang Zhang, Xinyang Liu, Jingjing Wu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Expression and clinical relations of protein tyrosine phosphatase receptor type S in esophageal squamous cell carcinoma."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Histol Histopathol (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.14670/HH-18-002"}], "href": "https://doi.org/10.14670/HH-18-002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29745967"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29745967"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Thomas B Davis, Mingli Yang, Michael J Schell, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PTPRS Regulates Colorectal Cancer RAS Pathway Activity by Inactivating Erk and Preventing Its Nuclear Translocation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41598-018-27584-x"}], "href": "https://doi.org/10.1038/s41598-018-27584-x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29915291"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29915291"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Yan-Mei Yuan, Ning Ma, Er-Bin Zhang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "BMP10 suppresses hepatocellular carcinoma progression via PTPRS-STAT3 axis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41388-019-0943-y"}], "href": "https://doi.org/10.1038/s41388-019-0943-y"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31417183"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31417183"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Muntinee Lertpanprom, Atit Silsirivanit, Patcharaporn Tippayawat, et al. "}, {"type": "b", "children": [{"type": "t", "text": "High expression of protein tyrosine phosphatase receptor S (PTPRS) is an independent prognostic marker for cholangiocarcinoma."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Front Public Health (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3389/fpubh.2022.835914"}], "href": "https://doi.org/10.3389/fpubh.2022.835914"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35991009"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35991009"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Yuehua Li, Jun Liu, Jingxuan Huang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Reduced PTPRS expression promotes epithelial-mesenchymal transition of Schwann cells in NF1-related plexiform neurofibromas."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Lett (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.canlet.2024.217151"}], "href": "https://doi.org/10.1016/j.canlet.2024.217151"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "39094827"}], "href": "https://pubmed.ncbi.nlm.nih.gov/39094827"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Aleixo M Muise, Thomas Walters, Eytan Wine, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein-tyrosine phosphatase sigma is associated with ulcerative colitis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Curr Biol (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cub.2007.06.013"}], "href": "https://doi.org/10.1016/j.cub.2007.06.013"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17614280"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17614280"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Ewa-Carin Långberg, Harvest F Gu, Sofia Nordman, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Genetic variation in receptor protein tyrosine phosphatase sigma is associated with type 2 diabetes in Swedish Caucasians."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Eur J Endocrinol (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1530/EJE-07-0114"}], "href": "https://doi.org/10.1530/EJE-07-0114"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17893260"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17893260"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Katie R Martin, Yong Xu, Brendan D Looyenga, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Identification of PTPsigma as an autophagic phosphatase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.080341"}], "href": "https://doi.org/10.1242/jcs.080341"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21303930"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21303930"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Karen M Doody, Stephanie M Stanford, Cristiano Sacchetti, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Targeting phosphatase-dependent proteoglycan switch for rheumatoid arthritis therapy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Transl Med (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1126/scitranslmed.aaa4616"}], "href": "https://doi.org/10.1126/scitranslmed.aaa4616"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25995222"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25995222"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Anna Bunin, Vanja Sisirak, Hiyaa S Ghosh, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein Tyrosine Phosphatase PTPRS Is an Inhibitory Receptor on Human and Murine Plasmacytoid Dendritic Cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Immunity (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.immuni.2015.07.009"}], "href": "https://doi.org/10.1016/j.immuni.2015.07.009"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26231120"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26231120"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "M Samblas, F I Milagro, M L Mansego, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PTPRS and PER3 methylation levels are associated with childhood obesity: results from a genome-wide methylation analysis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Pediatr Obes (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/ijpo.12224"}], "href": "https://doi.org/10.1111/ijpo.12224"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28614626"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28614626"}]}, {"type": "r", "ref": 20, "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": 21, "children": [{"type": "t", "text": "Sophie Lajus, Jochen Lang "}, {"type": "b", "children": [{"type": "t", "text": "Splice variant 3, but not 2 of receptor protein-tyrosine phosphatase sigma can mediate stimulation of insulin-secretion by alpha-latrotoxin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Biochem (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/jcb.20871"}], "href": "https://doi.org/10.1002/jcb.20871"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16552719"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16552719"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Li Hou, Jianchuan Wang, Yueyang Zhou, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structural insights into the homology and differences between mouse protein tyrosine phosphatase-sigma and human protein tyrosine phosphatase-sigma."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Acta Biochim Biophys Sin (Shanghai) (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/abbs/gmr095"}], "href": "https://doi.org/10.1093/abbs/gmr095"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22027896"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22027896"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "Yuanhao Gong, Shaniya Abudureyimu, Kenji Kadomatsu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Identification of PTPRσ-interacting proteins by proximity-labelling assay."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biochem (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/jb/mvaa141"}], "href": "https://doi.org/10.1093/jb/mvaa141"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33313879"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33313879"}]}, {"type": "r", "ref": 24, "children": [{"type": "t", "text": "Alexandre Poirier, Cynthia Picard, Anne Labonté, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PTPRS is a novel marker for early Tau pathology and synaptic integrity in Alzheimer's disease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41598-024-65104-2"}], "href": "https://doi.org/10.1038/s41598-024-65104-2"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "38926456"}], "href": "https://pubmed.ncbi.nlm.nih.gov/38926456"}]}]}]}
Synonyms	R-PTP-sigma, R-PTP-S, PTPSIGMA
Proteins	PTPRS_HUMAN
NCBI Gene ID	5802
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

PTPRS has 7,404 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 127 datasets.

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

If available, associations are ranked by standardized value

Harmonizome 3.0

PTPRS Gene

Functional Associations

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

	Dataset	Summary
	Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of PTPRS 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 PTPRS 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 PTPRS 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 PTPRS 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 PTPRS 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 PTPRS 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 PTPRS 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 PTPRS 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 PTPRS 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 PTPRS gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of PTPRS 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 PTPRS gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with PTPRS protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with PTPRS 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 PTPRS gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of PTPRS 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 PTPRS gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
	CM4AI U2OS Cell Map Protein Localization Assemblies	assemblies containing PTPRS 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 PTPRS gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing PTPRS protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing PTPRS protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores 2025	cellular components containing PTPRS 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 PTPRS 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 PTPRS protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with PTPRS gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with PTPRS gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with PTPRS gene/protein from the curated CTD Gene-Disease Associations dataset.
	dbGAP Gene-Trait Associations	traits associated with PTPRS 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 PTPRS 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 PTPRS gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores 2025	diseases associated with PTPRS 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 PTPRS 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 PTPRS 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 PTPRS gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with PTPRS gene in GWAS and other genetic association datasets from the DisGeNET Gene-Phenoptype Associations dataset.
	DrugBank Drug Targets	interacting drugs for PTPRS protein from the curated DrugBank Drug Targets dataset.
	ENCODE Histone Modification Site Profiles	histone modification site profiles with high histone modification abundance at PTPRS 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 PTPRS gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of PTPRS 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 PTPRS from the ESCAPE Omics Signatures of Genes and Proteins for Stem Cells dataset.