PTPN13 Gene

HGNC Family	Phosphatases
Name	protein tyrosine phosphatase, non-receptor type 13 (APO-1/CD95 (Fas)-associated phosphatase)
Description	The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP is a large intracellular protein. It has a catalytic PTP domain at its C-terminus and two major structural domains: a region with five PDZ domains and a FERM domain that binds to plasma membrane and cytoskeletal elements. This PTP was found to interact with, and dephosphorylate, Fas receptor and IkappaBalpha through the PDZ domains. This suggests it has a role in Fas mediated programmed cell death. This PTP was also shown to interact with GTPase-activating protein, and thus may function as a regulator of Rho signaling pathways. Four alternatively spliced transcript variants, which encode distinct proteins, have been reported. [provided by RefSeq, Oct 2008]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPTPN13, also known as FAP‐1 or PTPL1, plays a pivotal role in regulating apoptotic signals mediated by the Fas (CD95) pathway. In several studies, selective autophagic degradation of FAP‐1 was shown to promote Fas‐induced apoptosis in a context‐dependent manner"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": ", while loss of FAP‐1 activity—in part by miR‐200c targeting—sensitizes tumor cells to Fas ligand–induced cell death."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": " In addition, biochemical and cellular analyses demonstrated that FAP‐1 associates with the intracellular C terminus of Fas, restricting its export to the cell surface and thereby modulating apoptotic sensitivity."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": " Moreover, transcriptional repression by factors such as ICSBP/IRF8 results in downregulation of PTPN13, further affecting Fas-mediated cell death in myeloid cells."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its impact on death receptor signaling, PTPN13 exerts important regulatory functions in growth factor and oncogenic pathways. It interacts with components of the phosphatidylinositol 3‐kinase (PI3K) cascade by targeting free p85β for ubiquitination, and directly dephosphorylates insulin receptor substrate‐1 (IRS-1) to dampen PI3K/Akt signaling."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "6", "end_ref": "8"}]}, {"type": "t", "text": " In models of Her2‐overexpressing tumors, suppression of PTPN13 enhanced growth factor–induced Her2 phosphorylation, indicating that PTPN13 normally dephosphorylates the activated receptor"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "9"}]}, {"type": "t", "text": "; similarly, human papillomavirus–mediated degradation of PTPN13 results in enhanced MAP kinase signaling."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "10"}]}, {"type": "t", "text": " In breast cancers and other malignancies, reduced PTPN13 expression correlates with increased Src activation and tumor aggressiveness, whereas its intact activity can suppress oncogenic signals by directly dephosphorylating Src."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}]}, {"type": "t", "text": " Furthermore, interactions with signaling partners such as TAPP1 mediate its subcellular localization in response to phosphoinositide signals"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "13"}]}, {"type": "t", "text": ", and comprehensive reviews highlight the dual role of PTPN13 in counteracting oncogenic tyrosine kinases while modulating death receptor signaling."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nStructural studies have provided deeper insight into PTPN13’s function. High‐resolution NMR and X‐ray crystallographic analyses of its PDZ domains have delineated the expanded binding interfaces and allosteric features that govern the interaction with key partners such as RA-GEF2 and the Fas receptor."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "17"}]}, {"type": "t", "text": " These studies emphasize how the modular PDZ domains of PTPN13 contribute to substrate recognition and may fine-tune its phosphatase activity in various signaling contexts.\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAlterations in PTPN13 expression and function have significant translational implications. In Ewing’s sarcoma, for example, PTPN13 is transcriptionally activated by the EWS-FLI1 oncogene, and its inhibition reduces tumor growth and enhances apoptosis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "18"}]}, {"type": "t", "text": " Conversely, loss or mutation of PTPN13 has been implicated in hepatocellular carcinoma as well as in aggressive melanomas, where decreased expression contributes to enhanced invasiveness."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "19"}]}, {"type": "t", "text": " Additionally, in hepatitis C–related liver disease, elevated miR-200c downregulates PTPN13, leading to increased Src activation, which in turn promotes fibrogenic growth factor production."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "21"}]}, {"type": "t", "text": " \n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Jacob M Gump, Leah Staskiewicz, Michael J Morgan, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Autophagy variation within a cell population determines cell fate through selective degradation of Fap-1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Cell Biol (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ncb2886"}], "href": "https://doi.org/10.1038/ncb2886"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24316673"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24316673"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Robert Schickel, Sun-Mi Park, Andrea E Murmann, et al. "}, {"type": "b", "children": [{"type": "t", "text": "miR-200c regulates induction of apoptosis through CD95 by targeting FAP-1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2010.05.018"}], "href": "https://doi.org/10.1016/j.molcel.2010.05.018"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20620960"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20620960"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Vladimir N Ivanov, Pablo Lopez Bergami, Gabriel Maulit, et al. "}, {"type": "b", "children": [{"type": "t", "text": "FAP-1 association with Fas (Apo-1) inhibits Fas expression on the cell surface."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.23.10.3623-3635.2003"}], "href": "https://doi.org/10.1128/MCB.23.10.3623-3635.2003"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12724420"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12724420"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Vladimir N Ivanov, Ze'ev Ronai, Tom K Hei "}, {"type": "b", "children": [{"type": "t", "text": "Opposite roles of FAP-1 and dynamin in the regulation of Fas (CD95) translocation to the cell surface and susceptibility to Fas ligand-mediated apoptosis."}]}, {"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.M509866200"}], "href": "https://doi.org/10.1074/jbc.M509866200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16306044"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16306044"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Weiqi Huang, Chunliu Zhu, Hao Wang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The interferon consensus sequence-binding protein (ICSBP/IRF8) represses PTPN13 gene transcription in differentiating myeloid cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M706710200"}], "href": "https://doi.org/10.1074/jbc.M706710200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18195016"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18195016"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Shafi Kuchay, Shanshan Duan, Emily Schenkein, et al. "}, {"type": "b", "children": [{"type": "t", "text": "FBXL2- and PTPL1-mediated degradation of p110-free p85β regulatory subunit controls the PI(3)K signalling cascade."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Cell Biol (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ncb2731"}], "href": "https://doi.org/10.1038/ncb2731"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23604317"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23604317"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Mathilde Dromard, Guillaume Bompard, Murielle Glondu-Lassis, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The putative tumor suppressor gene PTPN13/PTPL1 induces apoptosis through insulin receptor substrate-1 dephosphorylation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Res (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1158/0008-5472.CAN-07-0513"}], "href": "https://doi.org/10.1158/0008-5472.CAN-07-0513"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17638892"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17638892"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Guillaume Bompard, Carole Puech, Christine Prébois, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein-tyrosine phosphatase PTPL1/FAP-1 triggers apoptosis in human breast cancer cells."}]}, {"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.M208950200"}], "href": "https://doi.org/10.1074/jbc.M208950200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12354757"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12354757"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "J-H Zhu, R Chen, W Yi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein tyrosine phosphatase PTPN13 negatively regulates Her2/ErbB2 malignant signaling."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/sj.onc.1210922"}], "href": "https://doi.org/10.1038/sj.onc.1210922"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17982484"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17982484"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "A C Hoover, G L Strand, P N Nowicki, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Impaired PTPN13 phosphatase activity in spontaneous or HPV-induced squamous cell carcinomas potentiates oncogene signaling through the MAP kinase pathway."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/onc.2009.251"}], "href": "https://doi.org/10.1038/onc.2009.251"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19734941"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19734941"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Murielle Glondu-Lassis, Mathilde Dromard, Magali Lacroix-Triki, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PTPL1/PTPN13 regulates breast cancer cell aggressiveness through direct inactivation of Src kinase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Res (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1158/0008-5472.CAN-09-4368"}], "href": "https://doi.org/10.1158/0008-5472.CAN-09-4368"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20501847"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20501847"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Françoise Révillion, Carole Puech, Fanja Rabenoelina, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Expression of the putative tumor suppressor gene PTPN13/PTPL1 is an independent prognostic marker for overall survival in breast cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Int J Cancer (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/ijc.23989"}], "href": "https://doi.org/10.1002/ijc.23989"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19004008"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19004008"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Wendy A Kimber, Maria Deak, Alan R Prescott, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Interaction of the protein tyrosine phosphatase PTPL1 with the PtdIns(3,4)P2-binding adaptor protein TAPP1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem J (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1042/BJ20031154"}], "href": "https://doi.org/10.1042/BJ20031154"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14516276"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14516276"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Gilles Freiss, Dany Chalbos "}, {"type": "b", "children": [{"type": "t", "text": "PTPN13/PTPL1: an important regulator of tumor aggressiveness."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Anticancer Agents Med Chem (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.2174/187152011794941262"}], "href": "https://doi.org/10.2174/187152011794941262"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21235435"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21235435"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Guennadi Kozlov, Denis Banville, Kalle Gehring, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Solution structure of the PDZ2 domain from cytosolic human phosphatase hPTP1E complexed with a peptide reveals contribution of the beta2-beta3 loop to PDZ domain-ligand interactions."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Mol Biol (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/s0022-2836(02)00544-2"}], "href": "https://doi.org/10.1016/s0022-2836(02"}, {"type": "t", "text": "00544-2) PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12095257"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12095257"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Tine Walma, Christian A E M Spronk, Marco Tessari, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structure, dynamics and binding characteristics of the second PDZ domain of PTP-BL."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Mol Biol (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1006/jmbi.2002.5402"}], "href": "https://doi.org/10.1006/jmbi.2002.5402"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11884147"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11884147"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Jun Zhang, Paul J Sapienza, Hengming Ke, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "PTPL1 is a direct transcriptional target of EWS-FLI1 and modulates Ewing's Sarcoma tumorigenesis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/sj.onc.1208247"}], "href": "https://doi.org/10.1038/sj.onc.1208247"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15782144"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15782144"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Shiou-Hwei Yeh, Dai-Chen Wu, Ching-Yi Tsai, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Genetic characterization of fas-associated phosphatase-1 as a putative tumor suppressor gene on chromosome 4q21.3 in hepatocellular carcinoma."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Clin Cancer Res (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1158/1078-0432.CCR-05-1383"}], "href": "https://doi.org/10.1158/1078-0432.CCR-05-1383"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16489062"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16489062"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Byungho Lim, Chan Kim, Jeong-Hwan Kim, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Genetic alterations and their clinical implications in gastric cancer peritoneal carcinomatosis revealed by whole-exome sequencing of malignant ascites."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncotarget (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.18632/oncotarget.6977"}], "href": "https://doi.org/10.18632/oncotarget.6977"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26811494"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26811494"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Sabarinathan Ramachandran, Haseeb Ilias Basha, Nayan J Sarma, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Hepatitis C virus induced miR200c down modulates FAP-1, a negative regulator of Src signaling and promotes hepatic fibrosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS One (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pone.0070744"}], "href": "https://doi.org/10.1371/journal.pone.0070744"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23950995"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23950995"}]}]}]}
Synonyms	HPTP1E, PTPL1, FAP-1, PTP-BAS, PTP1E, PTP-BL, PTPLE, PNP1
Proteins	PTN13_HUMAN
NCBI Gene ID	5783
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

PTPN13 has 8,225 functional associations with biological entities spanning 9 categories (molecular profile, organism, functional term, phrase or reference, chemical, disease, phenotype or trait, structural feature, cell line, cell type or tissue, gene, protein or microRNA, sequence feature) extracted from 130 datasets.

Click the + buttons to view associations for PTPN13 from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

PTPN13 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 PTPN13 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 PTPN13 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 PTPN13 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 PTPN13 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 PTPN13 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 PTPN13 gene relative to other tissues from the Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles dataset.
	Biocarta Pathways	pathways involving PTPN13 protein from the Biocarta Pathways dataset.
	BioGPS Cell Line Gene Expression Profiles	cell lines with high or low expression of PTPN13 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 PTPN13 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 PTPN13 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 PTPN13 gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of PTPN13 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 PTPN13 gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with PTPN13 protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with PTPN13 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 PTPN13 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of PTPN13 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 PTPN13 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
	CMAP Signatures of Differentially Expressed Genes for Small Molecules	small molecule perturbations changing expression of PTPN13 gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing PTPN13 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing PTPN13 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores	cellular components co-occuring with PTPN13 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 PTPN13 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 PTPN13 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with PTPN13 gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with PTPN13 gene/protein from the curated CTD Gene-Disease Associations dataset.
	dbGAP Gene-Trait Associations	traits associated with PTPN13 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 PTPN13 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 PTPN13 gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with PTPN13 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 PTPN13 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 PTPN13 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with PTPN13 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 PTPN13 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 PTPN13 gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of PTPN13 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 PTPN13 from the ESCAPE Omics Signatures of Genes and Proteins for Stem Cells dataset.
	GAD Gene-Disease Associations	diseases associated with PTPN13 gene in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.
	GAD High Level Gene-Disease Associations	diseases associated with PTPN13 gene in GWAS and other genetic association datasets from the GAD High Level Gene-Disease Associations dataset.
	GDSC Cell Line Gene Expression Profiles	cell lines with high or low expression of PTPN13 gene relative to other cell lines from the GDSC Cell Line Gene Expression Profiles dataset.