TPP2 Gene

Name	tripeptidyl peptidase II
Description	This gene encodes a mammalian peptidase that, at neutral pH, removes tripeptides from the N terminus of longer peptides. The protein has a specialized function that is essential for some MHC class I antigen presentation. The protein is a high molecular mass serine exopeptidase; the amino acid sequence surrounding the serine residue at the active site is similar to the peptidases of the subtilisin class rather than the trypsin class. [provided by RefSeq, Jul 2008]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTripeptidyl peptidase II (TPP2) is a large, multifunctional serine protease that plays a pivotal role in intracellular protein degradation. By removing tripeptides from proteasome‐generated substrates, it contributes both to the recycling of amino acids and to the processing of antigenic peptides for MHC class I presentation. In certain contexts, such as dendritic cell cross‐presentation of tumor antigens, TPP2 is essential for liberating epitopes in a proteasome‐independent manner, while in other models—such as muscle disuse—it remains relatively unaltered despite changes in other proteolytic enzyme transcripts."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "5"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nTPP2 also exerts a significant influence on immune regulation and cellular metabolism. Its deficiency in both mice and humans has been linked to immunosenescence, autoimmunity, and primary immunodeficiency, with compensatory increases in lysosomal activity that can disrupt metabolic pathways such as glycolysis. In addition, under conditions in which the proteasome is inhibited, TPP2 can serve as an alternate proteolytic route that sustains viral propagation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "6", "end_ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn cancer and proliferative contexts, TPP2 function appears to be a double‐edged sword. Overexpression of TPP2 is associated with accelerated cell cycle progression, evasion of mitotic checkpoints, and genetic instability, all of which may promote malignant growth. Moreover, TPP2 engages in protein–protein interactions with key regulators such as p53, SIRT7, MYBBP1A, and CDK2, and its altered expression has been observed in oral squamous cell carcinoma, underscoring its potential involvement in tumor biology."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDetailed structural and regulatory studies have further illuminated the multifaceted roles of TPP2. High‐resolution structural analyses reveal that TPP2 assembles into a gigantic, spindle‐like homo‐oligomer characterized by an elaborate network of internal cavities. Kinetic investigations show that its catalytic activity is modulated by pH, while transcriptional regulation studies have identified key promoter elements and transcription factors (e.g. NF-Y, USF-1, Oct-1) governing its expression. In addition, a marked reduction in TPP2 activity—mediated in part by the serine protease inhibitor serpinB2—in senescent cells triggers compensatory lysosome biogenesis, linking TPP2 to broader proteostatic and aging processes, as well as to growth factor–mediated ERK1/2 signaling in neuronal contexts."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Maarten D de Boer, Anna Selby, Philip Atherton, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The temporal responses of protein synthesis, gene expression and cell signalling in human quadriceps muscle and patellar tendon to disuse."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Physiol (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1113/jphysiol.2007.142828"}], "href": "https://doi.org/10.1113/jphysiol.2007.142828"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17901116"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17901116"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Max Schnurr, Martin Orban, Neil C Robson, et al. "}, {"type": "b", "children": [{"type": "t", "text": "ISCOMATRIX adjuvant induces efficient cross-presentation of tumor antigen by dendritic cells via rapid cytosolic antigen delivery and processing via tripeptidyl peptidase II."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Immunol (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.4049/jimmunol.182.3.1253"}], "href": "https://doi.org/10.4049/jimmunol.182.3.1253"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19155470"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19155470"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Ian A York, Nidhi Bhutani, Sophia Zendzian, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Tripeptidyl peptidase II is the major peptidase needed to trim long antigenic precursors, but is not required for most MHC class I antigen presentation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Immunol (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.4049/jimmunol.177.3.1434"}], "href": "https://doi.org/10.4049/jimmunol.177.3.1434"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16849449"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16849449"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Jan Diekmann, Eleni Adamopoulou, Olaf Beck, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Processing of two latent membrane protein 1 MHC class I epitopes requires tripeptidyl peptidase II involvement."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Immunol (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.4049/jimmunol.0803441"}], "href": "https://doi.org/10.4049/jimmunol.0803441"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19587004"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19587004"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Miguel Marcilla, Eugenia M Villasevil, José Antonio López de Castro "}, {"type": "b", "children": [{"type": "t", "text": "Tripeptidyl peptidase II is dispensable for the generation of both proteasome-dependent and proteasome-independent ligands of HLA-B27 and other class I molecules."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Eur J Immunol (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/eji.200737444"}], "href": "https://doi.org/10.1002/eji.200737444"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18286573"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18286573"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Polina Stepensky, Anne Rensing-Ehl, Ruth Gather, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Early-onset Evans syndrome, immunodeficiency, and premature immunosenescence associated with tripeptidyl-peptidase II deficiency."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Blood (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1182/blood-2014-08-593202"}], "href": "https://doi.org/10.1182/blood-2014-08-593202"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25414442"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25414442"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Wei Lu, Yu Zhang, David O McDonald, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Dual proteolytic pathways govern glycolysis and immune competence."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cell.2014.12.001"}], "href": "https://doi.org/10.1016/j.cell.2014.12.001"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25525876"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25525876"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Jingchun Zhang, Jerry Wong, Guang Gao, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Tripeptidyl peptidase II serves as an alternative to impaired proteasome to maintain viral growth in the host cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS Lett (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.febslet.2010.11.056"}], "href": "https://doi.org/10.1016/j.febslet.2010.11.056"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21134372"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21134372"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Isis Atallah, Mathieu Quinodoz, Belinda Campos-Xavier, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Immune deficiency, autoimmune disease and intellectual disability: A pleiotropic disorder caused by biallelic variants in the TPP2 gene."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Clin Genet (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/cge.13942"}], "href": "https://doi.org/10.1111/cge.13942"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33586135"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33586135"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Katsuya Usukura, Atsushi Kasamatsu, Atsushi Okamoto, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Tripeptidyl peptidase II in human oral squamous cell carcinoma."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cancer Res Clin Oncol (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s00432-012-1307-y"}], "href": "https://doi.org/10.1007/s00432-012-1307-y"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22986808"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22986808"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Beate Rockel, Klaus O Kopec, Andrei N Lupas, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structure and function of tripeptidyl peptidase II, a giant cytosolic protease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochim Biophys Acta (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbapap.2011.07.002"}], "href": "https://doi.org/10.1016/j.bbapap.2011.07.002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21771670"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21771670"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Jarmila Nahálková "}, {"type": "b", "children": [{"type": "t", "text": "Novel protein-protein interactions of TPPII, p53, and SIRT7."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biochem (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s11010-015-2507-y"}], "href": "https://doi.org/10.1007/s11010-015-2507-y"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26169984"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26169984"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Vaia Stavropoulou, Vanessa Vasquez, Biancastella Cereser, et al. "}, {"type": "b", "children": [{"type": "t", "text": "TPPII promotes genetic instability by allowing the escape from apoptosis of cells with activated mitotic checkpoints."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2006.05.141"}], "href": "https://doi.org/10.1016/j.bbrc.2006.05.141"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16762321"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16762321"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Jarmila Nahálková, Birgitta Tomkinson "}, {"type": "b", "children": [{"type": "t", "text": "TPPII, MYBBP1A and CDK2 form a protein-protein interaction network."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Arch Biochem Biophys (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.abb.2014.09.017"}], "href": "https://doi.org/10.1016/j.abb.2014.09.017"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25303791"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25303791"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Anne-Marie Schönegge, Elizabeth Villa, Friedrich Förster, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The structure of human tripeptidyl peptidase II as determined by a hybrid approach."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Structure (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.str.2012.01.025"}], "href": "https://doi.org/10.1016/j.str.2012.01.025"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22483107"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22483107"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Anne Wiemhoefer, Anita Stargardt, Wouter A van der Linden, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Tripeptidyl Peptidase II Mediates Levels of Nuclear Phosphorylated ERK1 and ERK2."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Proteomics (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/mcp.M114.043331"}], "href": "https://doi.org/10.1074/mcp.M114.043331"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26041847"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26041847"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Ann-Christin Lindås, Birgitta Tomkinson "}, {"type": "b", "children": [{"type": "t", "text": "Identification and characterization of the promoter for the gene encoding human tripeptidyl-peptidase II."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Gene (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.gene.2004.11.042"}], "href": "https://doi.org/10.1016/j.gene.2004.11.042"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15716107"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15716107"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Sandra Eklund, Ann-Christin Lindås, Emil Hamnevik, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Exploring the active site of tripeptidyl-peptidase II through studies of pH dependence of reaction kinetics."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochim Biophys Acta (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbapap.2012.01.004"}], "href": "https://doi.org/10.1016/j.bbapap.2012.01.004"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22266401"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22266401"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Ann-Christin Lindås, Birgitta Tomkinson "}, {"type": "b", "children": [{"type": "t", "text": "Characterization of the promoter of the gene encoding human tripeptidyl-peptidase II and identification of upstream silencer elements."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Gene (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.gene.2007.01.015"}], "href": "https://doi.org/10.1016/j.gene.2007.01.015"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17343995"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17343995"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Chia-Li Liao, Rong-Chi Hu, Min-Shiang Liao, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Unveiling a novel serpinB2-tripeptidyl peptidase II signaling axis during senescence."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.259513"}], "href": "https://doi.org/10.1242/jcs.259513"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35466366"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35466366"}]}]}]}
Synonyms	TPPII, TPP-2, TPP-II
Proteins	TPP2_HUMAN
NCBI Gene ID	7174
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

TPP2 has 5,930 functional associations with biological entities spanning 8 categories (molecular profile, organism, disease, phenotype or trait, functional term, phrase or reference, chemical, structural feature, cell line, cell type or tissue, gene, protein or microRNA) extracted from 118 datasets.

Click the + buttons to view associations for TPP2 from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

TPP2 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 TPP2 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 TPP2 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 TPP2 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 TPP2 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 TPP2 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 TPP2 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 TPP2 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 TPP2 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 TPP2 gene relative to other cell types and tissues from the BioGPS Mouse Cell Type and Tissue Gene Expression Profiles dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of TPP2 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 TPP2 gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with TPP2 protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with TPP2 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 TPP2 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of TPP2 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 TPP2 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 TPP2 gene from the curated ClinVar Gene-Phenotype Associations 2025 dataset.
	CM4AI U2OS Cell Map Protein Localization Assemblies	assemblies containing TPP2 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 TPP2 gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing TPP2 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing TPP2 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores	cellular components co-occuring with TPP2 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 TPP2 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
	CORUM Protein Complexes	protein complexs containing TPP2 protein from the CORUM Protein Complexes dataset.
	COSMIC Cell Line Gene CNV Profiles	cell lines with high or low copy number of TPP2 gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with TPP2 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with TPP2 gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with TPP2 gene/protein from the curated CTD Gene-Disease Associations dataset.
	dbGAP Gene-Trait Associations	traits associated with TPP2 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 TPP2 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 TPP2 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 TPP2 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 TPP2 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with TPP2 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 TPP2 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 TPP2 gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of TPP2 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 TPP2 from the ESCAPE Omics Signatures of Genes and Proteins for Stem Cells dataset.
	GAD Gene-Disease Associations	diseases associated with TPP2 gene in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.
	GAD High Level Gene-Disease Associations	diseases associated with TPP2 gene in GWAS and other genetic association datasets from the GAD High Level Gene-Disease Associations dataset.