PPT1 Gene

Name	palmitoyl-protein thioesterase 1
Description	The protein encoded by this gene is a small glycoprotein involved in the catabolism of lipid-modified proteins during lysosomal degradation. The encoded enzyme removes thioester-linked fatty acyl groups such as palmitate from cysteine residues. Defects in this gene are a cause of infantile neuronal ceroid lipofuscinosis 1 (CLN1, or INCL) and neuronal ceroid lipofuscinosis 4 (CLN4). Two transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Dec 2008]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPalmitoyl‐protein thioesterase 1 (PPT1) is a lysosomal enzyme that catalyzes the removal of long‐chain fatty acyl (predominantly palmitoyl) moieties from cysteine residues in lipid‐modified proteins, thereby facilitating their degradation and recycling in the lysosome. This depalmitoylation reaction is crucial for normal protein turnover and lysosomal function, as evidenced by early biochemical studies and structural comparisons that distinguish PPT1 from related hydrolases."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDefects in PPT1 activity, whether through genetic mutations or deficiency in enzyme function, result in the accumulation of palmitoylated proteins and storage material—a pathological hallmark of neuronal ceroid lipofuscinoses (NCLs). PPT1 deficiency disrupts critical neuronal processes such as synaptic vesicle recycling, leading to persistent membrane association of palmitoylated proteins, aberrant neurotransmission, and early neurodegeneration. Moreover, improper PPT1 function has been implicated in triggering ER stress, oxidative damage, and dysregulated apoptotic signaling, which further contribute to disease progression in infantile and variant late‐infantile NCL."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its well‐established role in neurodegeneration, PPT1 has recently emerged as a critical regulator in cancer cell physiology. Studies using chloroquine derivatives and novel dimeric antimalarials have identified PPT1 as a lysosomal target whose inhibition deacidifies lysosomes, disrupts autophagic flux, and concurrently impairs mTOR signaling. These effects not only suppress autophagy-dependent survival pathways in tumor cells but also correlate with reduced tumor growth and poorer patient survival when PPT1 expression is elevated, highlighting its promise as a therapeutic cancer target."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its canonical lysosomal role, PPT1 contributes to cellular lipid metabolism and intracellular signaling. In monocytes and macrophages, PPT1 participates in the hydrolysis of lipid messengers such as 2-arachidonoylglycerol and prostaglandin glyceryl esters, implicating it in endocannabinoid turnover. Moreover, emerging evidence indicates that PPT1 itself can be palmitoylated by enzymes such as DHHC3 and DHHC7—a modification that attenuates its depalmitoylation activity and may establish a positive feedback loop exacerbating palmitoylated protein accumulation. Abnormal PPT1 function also appears connected to defects in ciliary organization and protein trafficking, thereby broadening its influence on cellular homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "17", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nTherapeutic strategies aimed at modulating PPT1 function hold promise both for treating neurodegenerative lysosomal storage disorders and for targeting cancer. In neuronal models, pharmacological agents like PTC124 have been shown to induce residual PPT1 activity in cells harboring nonsense mutations, while the absence of effective small-molecule therapies underscores the need for novel treatment approaches. Further, structural analyses of PPT1 mutations help guide the design of targeted interventions that could restore enzyme function or exploit its inhibition to suppress tumor growth."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "J Y Lu, L A Verkruyse, S L Hofmann "}, {"type": "b", "children": [{"type": "t", "text": "Lipid thioesters derived from acylated proteins accumulate in infantile neuronal ceroid lipofuscinosis: correction of the defect in lymphoblasts by recombinant palmitoyl-protein thioesterase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (1996)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.93.19.10046"}], "href": "https://doi.org/10.1073/pnas.93.19.10046"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "8816748"}], "href": "https://pubmed.ncbi.nlm.nih.gov/8816748"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Jill M Weimer, Elizabeth Kriscenski-Perry, Yasser Elshatory, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The neuronal ceroid lipofuscinoses: mutations in different proteins result in similar disease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Neuromolecular Med (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1385/NMM:1:2:111"}], "href": "https://doi.org/10.1385/NMM:1:2:111"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12025857"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12025857"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Sandra L Hofmann, Armita Atashband, Steve K Cho, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Neuronal ceroid lipofuscinoses caused by defects in soluble lysosomal enzymes (CLN1 and CLN2)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Curr Mol Med (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.2174/1566524023362294"}], "href": "https://doi.org/10.2174/1566524023362294"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12125808"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12125808"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Guillermo Calero, Praveena Gupta, M Cristina Nonato, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The crystal structure of palmitoyl protein thioesterase-2 (PPT2) reveals the basis for divergent substrate specificities of the two lysosomal thioesterases, PPT1 and PPT2."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M301225200"}], "href": "https://doi.org/10.1074/jbc.M301225200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12855696"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12855696"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Toshihiko Tsukamoto, Juri Iida, Yoh Dobashi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Overexpression in colorectal carcinoma of two lysosomal enzymes, CLN2 and CLN1, involved in neuronal ceroid lipofuscinosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/cncr.21764"}], "href": "https://doi.org/10.1002/cncr.21764"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16518810"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16518810"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Laura Ahtiainen, Kaisu Luiro, Maria Kauppi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Palmitoyl protein thioesterase 1 (PPT1) deficiency causes endocytic defects connected to abnormal saposin processing."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Exp Cell Res (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.yexcr.2006.01.034"}], "href": "https://doi.org/10.1016/j.yexcr.2006.01.034"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16542649"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16542649"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Sung-Jo Kim, Zhongjian Zhang, Yi-Ching Lee, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Palmitoyl-protein thioesterase-1 deficiency leads to the activation of caspase-9 and contributes to rapid neurodegeneration in INCL."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hum Mol Genet (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/hmg/ddl078"}], "href": "https://doi.org/10.1093/hmg/ddl078"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16571600"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16571600"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Sung-Jo Kim, Zhongjian Zhang, Chinmoy Sarkar, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Palmitoyl protein thioesterase-1 deficiency impairs synaptic vesicle recycling at nerve terminals, contributing to neuropathology in humans and mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Clin Invest (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1172/JCI33482"}], "href": "https://doi.org/10.1172/JCI33482"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18704195"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18704195"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Maria Kousi, Eija Siintola, Lenka Dvorakova, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mutations in CLN7/MFSD8 are a common cause of variant late-infantile neuronal ceroid lipofuscinosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Brain (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/brain/awn366"}], "href": "https://doi.org/10.1093/brain/awn366"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19201763"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19201763"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Alessandro Simonati, Alessandra Tessa, Bernardo Dalla Bernardina, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Variant late infantile neuronal ceroid lipofuscinosis because of CLN1 mutations."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Pediatr Neurol (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.pediatrneurol.2008.10.018"}], "href": "https://doi.org/10.1016/j.pediatrneurol.2008.10.018"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19302939"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19302939"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Jayesh Sheth, Mehul Mistri, Riddhi Bhavsar, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Batten disease: biochemical and molecular characterization revealing novel PPT1 and TPP1 gene mutations in Indian patients."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "BMC Neurol (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/s12883-018-1206-1"}], "href": "https://doi.org/10.1186/s12883-018-1206-1"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30541466"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30541466"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Bailey Balouch, Halle Nagorsky, Truc Pham, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Human INCL fibroblasts display abnormal mitochondrial and lysosomal networks and heightened susceptibility to ROS-induced cell death."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS One (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pone.0239689"}], "href": "https://doi.org/10.1371/journal.pone.0239689"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33561134"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33561134"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Vito W Rebecca, Michael C Nicastri, Noel McLaughlin, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A Unified Approach to Targeting the Lysosome's Degradative and Growth Signaling Roles."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Discov (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1158/2159-8290.CD-17-0741"}], "href": "https://doi.org/10.1158/2159-8290.CD-17-0741"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28899863"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28899863"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Young-Kyoung Lee, Jin J Lim, Un-Woo Jeoun, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Lactate-mediated mitoribosomal defects impair mitochondrial oxidative phosphorylation and promote hepatoma cell invasiveness."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M117.809012"}], "href": "https://doi.org/10.1074/jbc.M117.809012"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28978646"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28978646"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Vito W Rebecca, Michael C Nicastri, Colin Fennelly, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PPT1 Promotes Tumor Growth and Is the Molecular Target of Chloroquine Derivatives in Cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Discov (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1158/2159-8290.CD-18-0706"}], "href": "https://doi.org/10.1158/2159-8290.CD-18-0706"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30442709"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30442709"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Wei Tian, Chenyu Li, Jiaqi Ren, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Identification of PPT1 as a lysosomal core gene with prognostic value in hepatocellular carcinoma."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biosci Rep (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1042/BSR20230067"}], "href": "https://doi.org/10.1042/BSR20230067"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "37103469"}], "href": "https://pubmed.ncbi.nlm.nih.gov/37103469"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Ran Wang, Abdolsamad Borazjani, Anberitha T Matthews, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Identification of palmitoyl protein thioesterase 1 in human THP1 monocytes and macrophages and characterization of unique biochemical activities for this enzyme."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochemistry (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/bi401138s"}], "href": "https://doi.org/10.1021/bi401138s"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24083319"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24083319"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Enzo Scifo, Agnieszka Szwajda, Rabah Soliymani, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Proteomic analysis of the palmitoyl protein thioesterase 1 interactome in SH-SY5Y human neuroblastoma cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Proteomics (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.jprot.2015.03.038"}], "href": "https://doi.org/10.1016/j.jprot.2015.03.038"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25865307"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25865307"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Michal Segal-Salto, Karin Hansson, Tamar Sapir, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Proteomics insights into infantile neuronal ceroid lipofuscinosis (CLN1) point to the involvement of cilia pathology in the disease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hum Mol Genet (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/hmg/ddx074"}], "href": "https://doi.org/10.1093/hmg/ddx074"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28334871"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28334871"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Qingqiong Luo, Sheng Hu, Yijie Tang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PPT1 Promotes Growth and Inhibits Ferroptosis of Oral Squamous Cell Carcinoma Cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Curr Cancer Drug Targets (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.2174/0115680096294098240123104657"}], "href": "https://doi.org/10.2174/0115680096294098240123104657"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "38299399"}], "href": "https://pubmed.ncbi.nlm.nih.gov/38299399"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Chinmoy Sarkar, Zhongjian Zhang, Anil B Mukherjee "}, {"type": "b", "children": [{"type": "t", "text": "Stop codon read-through with PTC124 induces palmitoyl-protein thioesterase-1 activity, reduces thioester load and suppresses apoptosis in cultured cells from INCL patients."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Genet Metab (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.ymgme.2011.05.021"}], "href": "https://doi.org/10.1016/j.ymgme.2011.05.021"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21704547"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21704547"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Charles Shyng, Mark S Sands "}, {"type": "b", "children": [{"type": "t", "text": "Astrocytosis in infantile neuronal ceroid lipofuscinosis: friend or foe?"}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Soc Trans (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1042/BST20140188"}], "href": "https://doi.org/10.1042/BST20140188"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25233404"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25233404"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "Ni Sima, Rong Li, Wei Huang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Neural stem cells for disease modeling and evaluation of therapeutics for infantile (CLN1/PPT1) and late infantile (CLN2/TPP1) neuronal ceroid lipofuscinoses."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Orphanet J Rare Dis (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/s13023-018-0798-2"}], "href": "https://doi.org/10.1186/s13023-018-0798-2"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29631617"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29631617"}]}, {"type": "r", "ref": 24, "children": [{"type": "t", "text": "D Thirumal Kumar, Nishaat Shaikh, S Udhaya Kumar, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Computational and structural investigation of Palmitoyl-Protein Thioesterase 1 (PPT1) protein causing Neuronal Ceroid Lipofuscinoses (NCL)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Adv Protein Chem Struct Biol (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/bs.apcsb.2022.07.002"}], "href": "https://doi.org/10.1016/bs.apcsb.2022.07.002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36088080"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36088080"}]}]}]}
Synonyms	CLN1, INCL
Proteins	PPT1_HUMAN
NCBI Gene ID	5538
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

PPT1 has 10,162 functional associations with biological entities spanning 9 categories (molecular profile, organism, chemical, disease, phenotype or trait, functional term, phrase or reference, structural feature, cell line, cell type or tissue, gene, protein or microRNA, sequence feature) extracted from 134 datasets.

Click the + buttons to view associations for PPT1 from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

PPT1 Gene

Functional Associations

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

	Dataset	Summary
	Achilles Cell Line Gene Essentiality Profiles	cell lines with fitness changed by PPT1 gene knockdown relative to other cell lines from the Achilles Cell Line Gene Essentiality Profiles dataset.
	Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of PPT1 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 PPT1 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 PPT1 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 PPT1 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 PPT1 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 PPT1 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 PPT1 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 PPT1 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 PPT1 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 PPT1 gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of PPT1 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 PPT1 gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with PPT1 protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with PPT1 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 PPT1 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of PPT1 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 PPT1 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
	ClinVar Gene-Phenotype Associations	phenotypes associated with PPT1 gene from the curated ClinVar Gene-Phenotype Associations dataset.
	ClinVar Gene-Phenotype Associations 2025	phenotypes associated with PPT1 gene from the curated ClinVar Gene-Phenotype Associations 2025 dataset.
	CM4AI U2OS Cell Map Protein Localization Assemblies	assemblies containing PPT1 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 PPT1 gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing PPT1 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing PPT1 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores	cellular components co-occuring with PPT1 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 PPT1 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
	COSMIC Cell Line Gene CNV Profiles	cell lines with high or low copy number of PPT1 gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with PPT1 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with PPT1 gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with PPT1 gene/protein from the curated CTD Gene-Disease Associations dataset.
	DeepCoverMOA Drug Mechanisms of Action	small molecule perturbations with high or low expression of PPT1 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 PPT1 gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DISEASES Curated Gene-Disease Association Evidence Scores	diseases involving PPT1 gene from the DISEASES Curated Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Curated Gene-Disease Association Evidence Scores 2025	diseases involving PPT1 gene from the DISEASES Curated Gene-Disease Association Evidence Scores 2025 dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with PPT1 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 PPT1 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 PPT1 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with PPT1 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Phenoptype Associations dataset.
	DrugBank Drug Targets	interacting drugs for PPT1 protein from the curated DrugBank Drug Targets dataset.
	ENCODE Histone Modification Site Profiles	histone modification site profiles with high histone modification abundance at PPT1 gene from the ENCODE Histone Modification Site Profiles dataset.