MBTPS1 Gene

Name	membrane-bound transcription factor peptidase, site 1
Description	This gene encodes a member of the subtilisin-like proprotein convertase family, which includes proteases that process protein and peptide precursors trafficking through regulated or constitutive branches of the secretory pathway. The encoded protein undergoes an initial autocatalytic processing event in the ER to generate a heterodimer which exits the ER and sorts to the cis/medial-Golgi where a second autocatalytic event takes place and the catalytic activity is acquired. It encodes a type 1 membrane bound protease which is ubiquitously expressed and regulates cholesterol or lipid homeostasis via cleavage of substrates at non-basic residues. Mutations in this gene may be associated with lysosomal dysfunction. [provided by RefSeq, Feb 2014]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMBTPS1, also known as the site‐1 protease (S1P), is an essential membrane‐bound protease that activates key transcription factors and enzymes by cleaving their precursor forms. It initiates the proteolytic cascades required for lysosome biogenesis by processing the α/β‐subunit precursor of N‐acetylglucosamine-1-phosphotransferase, ensuring proper mannose 6-phosphate tagging of lysosomal enzymes (see."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " MBTPS1 also cleaves the endoplasmic reticulum (ER) membrane-anchored transcription factor ATF6 during the unfolded protein response, a necessary step in relieving ER stress (see"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": "and."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": " In parallel, it is central to cholesterol and fatty acid homeostasis by activating sterol regulatory element-binding proteins (SREBPs), as highlighted by studies demonstrating its crucial role in maintaining cellular lipid balance and lysosomal function (see"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": "and."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": "."}, {"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": "\nIn addition to its role in cellular homeostasis, MBTPS1 is harnessed by various pathogens and cellular substrates alike. It processes viral envelope glycoprotein precursors in hemorrhagic fever viruses such as Crimean-Congo hemorrhagic fever virus and arenaviruses, ensuring proper virus assembly and infectivity (see"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": "and."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": " It is also involved in the sequential processing of the (pro)renin receptor to generate soluble forms that may serve as biomarkers (see"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": ", and in the proteolytic activation of secreted protein kinases like Fam20C, which in turn influence osteoblast differentiation and biomineralization (see."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "9"}]}, {"type": "t", "text": " Moreover, MBTPS1-mediated substrate processing displays a remarkable dependency on the structural features of the substrate, which is exemplified by its extended binding pocket required for efficient viral glycoprotein cleavage (see."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "10"}]}, {"type": "t", "text": "."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}, {"type": "fg_f", "ref": "6"}, {"type": "fg_f", "ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nThe activation and substrate selectivity of MBTPS1 are finely tuned by its own autoproteolytic processing and modular prodomain organization. Detailed biochemical analyses have revealed that its zymogen maturation, which involves sequential autocatalytic cleavages, is essential for full catalytic activity and substrate specificity (see"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}]}, {"type": "t", "text": ", and."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "13"}]}, {"type": "t", "text": " Clinically, disruptive variants in MBTPS1 can underlie rare skeletal dysplasias accompanied by aberrant lysosomal enzyme profiles (see"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "14"}]}, {"type": "t", "text": ", and genetic studies have linked its locus with variations in plasma plasminogen activator inhibitor-1 levels (see."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "15"}]}, {"type": "t", "text": " Furthermore, MBTPS1 facilitates the cleavage of the (pro)renin receptor to form its soluble counterpart, indicating a role in diverse signaling events (see."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "16"}]}, {"type": "t", "text": " Its regulation of SREBP processing by responding to substrate binding has even been exploited to modulate pathways like glycogenesis, with UDP-glucose binding directly to MBTPS1 to prevent SREBP activation and hepatic lipogenesis (see"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "17"}]}, {"type": "t", "text": "and."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "18"}]}, {"type": "t", "text": " Lastly, emerging studies point to MBTPS1 as a therapeutic target, with inhibition strategies showing promise in reducing melanoma cell proliferation and ameliorating cystic fibrosis–related defects by modulating ATF6 cleavage (see"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "19"}]}, {"type": "t", "text": ", and."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "21"}]}, {"type": "t", "text": "."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}, {"type": "fg_f", "ref": "14"}, {"type": "fg_f", "ref": "12"}, {"type": "fg_fs", "start_ref": "15", "end_ref": "21"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Katrin Marschner, Katrin Kollmann, Michaela Schweizer, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A key enzyme in the biogenesis of lysosomes is a protease that regulates cholesterol metabolism."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Science (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1126/science.1205677"}], "href": "https://doi.org/10.1126/science.1205677"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21719679"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21719679"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Jingshi Shen, Ron Prywes "}, {"type": "b", "children": [{"type": "t", "text": "Dependence of site-2 protease cleavage of ATF6 on prior site-1 protease digestion is determined by the size of the luminal domain of ATF6."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M408466200"}], "href": "https://doi.org/10.1074/jbc.M408466200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15299016"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15299016"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Muna Al-Maskari, Matthew A Care, Emily Robinson, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Site-1 protease function is essential for the generation of antibody secreting cells and reprogramming for secretory activity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41598-018-32705-7"}], "href": "https://doi.org/10.1038/s41598-018-32705-7"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30254311"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30254311"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Renata Voltolini Velho, Raffaella De Pace, Sarah Klünder, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Site-1 protease and lysosomal homeostasis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochim Biophys Acta Mol Cell Res (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbamcr.2017.06.023"}], "href": "https://doi.org/10.1016/j.bbamcr.2017.06.023"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28693924"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28693924"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Aloys De Windt, Myriam Rai, Lise Bernier, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Gene set enrichment analysis reveals several globally affected pathways due to SKI-1/S1P inhibition in HepG2 cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "DNA Cell Biol (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1089/dna.2007.0624"}], "href": "https://doi.org/10.1089/dna.2007.0624"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17867930"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17867930"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Eric Bergeron, Martin J Vincent, Stuart T Nichol "}, {"type": "b", "children": [{"type": "t", "text": "Crimean-Congo hemorrhagic fever virus glycoprotein processing by the endoprotease SKI-1/S1P is critical for virus infectivity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Virol (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/JVI.01647-07"}], "href": "https://doi.org/10.1128/JVI.01647-07"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17898072"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17898072"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Jillian M Rojek, Andrew M Lee, NgocThao Nguyen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Site 1 protease is required for proteolytic processing of the glycoproteins of the South American hemorrhagic fever viruses Junin, Machupo, and Guanarito."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Virol (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/JVI.02392-07"}], "href": "https://doi.org/10.1128/JVI.02392-07"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18400865"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18400865"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Tsutomu Nakagawa, Chiharu Suzuki-Nakagawa, Akiko Watanabe, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Site-1 protease is required for the generation of soluble (pro)renin receptor."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biochem (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/jb/mvw080"}], "href": "https://doi.org/10.1093/jb/mvw080"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28013223"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28013223"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Xinxin Chen, Jianchao Zhang, Pulan Liu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Proteolytic processing of secretory pathway kinase Fam20C by site-1 protease promotes biomineralization."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.2100133118"}], "href": "https://doi.org/10.1073/pnas.2100133118"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34349020"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34349020"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Dominique J Burri, Joel Ramos da Palma, Nabil G Seidah, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Differential recognition of Old World and New World arenavirus envelope glycoproteins by subtilisin kexin isozyme 1 (SKI-1)/site 1 protease (S1P)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Virol (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/JVI.00072-13"}], "href": "https://doi.org/10.1128/JVI.00072-13"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23536681"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23536681"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Joel Ramos da Palma, Dominique Julien Burri, Joël Oppliger, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Zymogen activation and subcellular activity of subtilisin kexin isozyme 1/site 1 protease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M114.588525"}], "href": "https://doi.org/10.1074/jbc.M114.588525"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25378398"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25378398"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Kristofer Bodvard, Johanna Mohlin, Wolfgang Knecht "}, {"type": "b", "children": [{"type": "t", "text": "Recombinant expression, purification, and kinetic and inhibitor characterisation of human site-1-protease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Protein Expr Purif (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.pep.2006.07.015"}], "href": "https://doi.org/10.1016/j.pep.2006.07.015"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16973377"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16973377"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Joel Ramos da Palma, Laura Cendron, Nabil Georges Seidah, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mechanism of Folding and Activation of Subtilisin Kexin Isozyme-1 (SKI-1)/Site-1 Protease (S1P)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M115.677757"}], "href": "https://doi.org/10.1074/jbc.M115.677757"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26645686"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26645686"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Daniel R Carvalho, Carlos E Speck-Martins, Jaime M Brum, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Spondyloepimetaphyseal dysplasia with elevated plasma lysosomal enzymes caused by homozygous variant in MBTPS1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Med Genet A (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/ajmg.a.61614"}], "href": "https://doi.org/10.1002/ajmg.a.61614"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32420688"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32420688"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Matthew B Lanktree, Christopher T Johansen, Sonia S Anand, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Genetic variation in hyaluronan metabolism loci is associated with plasma plasminogen activator inhibitor-1 concentration."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Blood (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1182/blood-2010-02-269902"}], "href": "https://doi.org/10.1182/blood-2010-02-269902"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20558613"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20558613"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Saije K Morosin, Sarah J Delforce, Eugenie R Lumbers, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cleavage of the soluble (pro)renin receptor (sATP6AP2) in the placenta."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Placenta (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.placenta.2020.08.019"}], "href": "https://doi.org/10.1016/j.placenta.2020.08.019"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32920451"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32920451"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Jie Chen, Yabo Zhou, Zhuohang Liu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Hepatic glycogenesis antagonizes lipogenesis by blocking S1P via UDPG."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Science (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1126/science.adi3332"}], "href": "https://doi.org/10.1126/science.adi3332"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "38359126"}], "href": "https://pubmed.ncbi.nlm.nih.gov/38359126"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Sarah Klünder, Jörg Heeren, Sandra Markmann, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Novel circular, cyclic and acyclic Ψ(CH(2)O) containing peptide inhibitors of SKI-1/S1P: synthesis, kinetic and biochemical evaluations."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Curr Med Chem (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.2174/092986711796011265"}], "href": "https://doi.org/10.2174/092986711796011265"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21568902"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21568902"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Raphaël Santinelli, Nathalie Benz, Julie Guellec, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The Inhibition of the Membrane-Bound Transcription Factor Site-1 Protease (MBTP1) Alleviates the p.Phe508del-Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) Defects in Cystic Fibrosis Cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cells (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3390/cells13020185"}], "href": "https://doi.org/10.3390/cells13020185"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "38247876"}], "href": "https://pubmed.ncbi.nlm.nih.gov/38247876"}]}]}]}
Synonyms	PCSK8, S1P, SKI-1
Proteins	MBTP1_HUMAN
NCBI Gene ID	8720
API
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Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

MBTPS1 has 7,957 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 119 datasets.

Click the + buttons to view associations for MBTPS1 from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

MBTPS1 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 MBTPS1 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 MBTPS1 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 MBTPS1 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 MBTPS1 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 MBTPS1 gene relative to other tissues from the Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles dataset.
	Biocarta Pathways	pathways involving MBTPS1 protein from the Biocarta Pathways dataset.
	BioGPS Cell Line Gene Expression Profiles	cell lines with high or low expression of MBTPS1 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 MBTPS1 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 MBTPS1 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 MBTPS1 gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of MBTPS1 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 MBTPS1 gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with MBTPS1 protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with MBTPS1 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 MBTPS1 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of MBTPS1 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 MBTPS1 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 MBTPS1 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 MBTPS1 gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing MBTPS1 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing MBTPS1 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores	cellular components co-occuring with MBTPS1 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 MBTPS1 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 MBTPS1 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Disease Associations	diseases associated with MBTPS1 gene/protein from the curated CTD Gene-Disease Associations dataset.
	DeepCoverMOA Drug Mechanisms of Action	small molecule perturbations with high or low expression of MBTPS1 protein relative to other small molecule perturbations from the DeepCoverMOA Drug Mechanisms of Action dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with MBTPS1 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 MBTPS1 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 MBTPS1 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with MBTPS1 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 MBTPS1 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 MBTPS1 gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of MBTPS1 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 MBTPS1 from the ESCAPE Omics Signatures of Genes and Proteins for Stem Cells dataset.
	GAD High Level Gene-Disease Associations	diseases associated with MBTPS1 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 MBTPS1 gene relative to other cell lines from the GDSC Cell Line Gene Expression Profiles dataset.
	GeneRIF Biological Term Annotations	biological terms co-occuring with MBTPS1 gene in literature-supported statements describing functions of genes from the GeneRIF Biological Term Annotations dataset.
	GeneSigDB Published Gene Signatures	PubMedIDs of publications reporting gene signatures containing MBTPS1 from the GeneSigDB Published Gene Signatures dataset.
	GEO Signatures of Differentially Expressed Genes for Diseases	disease perturbations changing expression of MBTPS1 gene from the GEO Signatures of Differentially Expressed Genes for Diseases dataset.
	GEO Signatures of Differentially Expressed Genes for Gene Perturbations	gene perturbations changing expression of MBTPS1 gene from the GEO Signatures of Differentially Expressed Genes for Gene Perturbations dataset.