LRP2 Gene

HGNC Family	Low density lipoprotein receptors
Name	low density lipoprotein receptor-related protein 2
Description	The protein encoded by this gene, low density lipoprotein-related protein 2 (LRP2) or megalin, is a multi-ligand endocytic receptor that is expressed in many different tissues but primarily in absorptive epithilial tissues such as the kidney. This glycoprotein has a large amino-terminal extracellular domain, a single transmembrane domain, and a short carboxy-terminal cytoplasmic tail. The extracellular ligand-binding-domains bind diverse macromolecules including albumin, apolipoproteins B and E, and lipoprotein lipase. The LRP2 protein is critical for the reuptake of numerous ligands, including lipoproteins, sterols, vitamin-binding proteins, and hormones. This protein also has a role in cell-signaling; extracellular ligands include parathyroid horomones and the morphogen sonic hedgehog while cytosolic ligands include MAP kinase scaffold proteins and JNK interacting proteins. Recycling of this membrane receptor is regulated by phosphorylation of its cytoplasmic domain. Mutations in this gene cause Donnai-Barrow syndrome (DBS) and facio-oculoacoustico-renal syndrome (FOAR).[provided by RefSeq, Aug 2009]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nLRP2, which encodes the multiligand endocytic receptor megalin, is central to the selective uptake of diverse circulating compounds. Working in concert with cubilin, megalin mediates the internalization of nutrients, hormones, and other ligands, and its trafficking is finely regulated—for example, by phosphorylation events that modulate receptor recycling. This basic endocytic function is critical for maintaining normal cellular homeostasis and has implications in several pathological states."}, {"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": "\nDuring embryogenesis and in specialized tissues, megalin’s role extends to processes essential for development and hormone processing. In the thyroid, for example, it mediates the transcytosis of thyroglobulin—a process critical for effective hormone release—while its expression in the yolk sac and placental villi underscores a key function in maternal–fetal nutrient transfer."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the kidney, megalin is predominantly expressed by proximal tubular epithelial cells where it is responsible for the reabsorption of filtered proteins including light chains, vitamin D–binding protein, and various toxins. Altered megalin function or diminished expression contributes to renal pathologies such as diabetic nephropathy, acute kidney injury, and cisplatin-induced ototoxicity. Detailed structural studies even reveal its direct interactions with compounds like gentamicin, further emphasizing its importance in drug handling and toxicity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMegalin also participates in extra‐renal functions. In the prostate, it facilitates the internalization of androgen–protein complexes, thereby influencing local hormone availability. Furthermore, megalin has emerged as a player in neuroendocrine regulation; its interaction with ligands such as clusterin appears to modulate hypothalamic feeding circuits, and genetic polymorphisms in megalin have been linked to alterations in vitamin D metabolism and potentially in cognitive status."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "14", "end_ref": "17"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Erik Ilsø Christensen, Henrik Birn "}, {"type": "b", "children": [{"type": "t", "text": "Megalin and cubilin: multifunctional endocytic receptors."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Rev Mol Cell Biol (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nrm778"}], "href": "https://doi.org/10.1038/nrm778"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11994745"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11994745"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Vibeke Hvidberg, Christian Jacobsen, Roland K Strong, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The endocytic receptor megalin binds the iron transporting neutrophil-gelatinase-associated lipocalin with high affinity and mediates its cellular uptake."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS Lett (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.febslet.2004.12.031"}], "href": "https://doi.org/10.1016/j.febslet.2004.12.031"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15670845"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15670845"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "María Isabel Yuseff, Pamela Farfan, Guojun Bu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A cytoplasmic PPPSP motif determines megalin's phosphorylation and regulates receptor's recycling and surface expression."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Traffic (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/j.1600-0854.2007.00601.x"}], "href": "https://doi.org/10.1111/j.1600-0854.2007.00601.x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17555532"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17555532"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Sibel Kantarci, Lihadh Al-Gazali, R Sean Hill, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mutations in LRP2, which encodes the multiligand receptor megalin, cause Donnai-Barrow and facio-oculo-acoustico-renal syndromes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Genet (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ng2063"}], "href": "https://doi.org/10.1038/ng2063"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17632512"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17632512"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Simonetta Lisi, Aldo Pinchera, Robert T McCluskey, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Preferential megalin-mediated transcytosis of low-hormonogenic thyroglobulin: a control mechanism for thyroid hormone release."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.2432267100"}], "href": "https://doi.org/10.1073/pnas.2432267100"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14657389"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14657389"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Carolyn E Fisher, Sarah E M Howie "}, {"type": "b", "children": [{"type": "t", "text": "The role of megalin (LRP-2/Gp330) during development."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Dev Biol (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.ydbio.2006.06.007"}], "href": "https://doi.org/10.1016/j.ydbio.2006.06.007"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16828734"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16828734"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "K A Burke, E Jauniaux, G J Burton, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Expression and immunolocalisation of the endocytic receptors megalin and cubilin in the human yolk sac and placenta across gestation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Placenta (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.placenta.2013.08.003"}], "href": "https://doi.org/10.1016/j.placenta.2013.08.003"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23978537"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23978537"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "L Riedemann, C Lanvers, D Deuster, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Megalin genetic polymorphisms and individual sensitivity to the ototoxic effect of cisplatin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Pharmacogenomics J (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/sj.tpj.6500455"}], "href": "https://doi.org/10.1038/sj.tpj.6500455"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17457342"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17457342"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Min Li, Saravanan Balamuthusamy, Eric E Simon, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Silencing megalin and cubilin genes inhibits myeloma light chain endocytosis and ameliorates toxicity in human renal proximal tubule epithelial cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Physiol Renal Physiol (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1152/ajprenal.00091.2008"}], "href": "https://doi.org/10.1152/ajprenal.00091.2008"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18448595"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18448595"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Andrea Schreiber, Franziska Theilig, Frank Schweda, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Acute endotoxemia in mice induces downregulation of megalin and cubilin in the kidney."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Kidney Int (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ki.2012.62"}], "href": "https://doi.org/10.1038/ki.2012.62"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22437417"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22437417"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Robert Dagil, Charlotte O'Shea, Anders Nykjær, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Gentamicin binds to the megalin receptor as a competitive inhibitor using the common ligand binding motif of complement type repeats: insight from the nmr structure of the 10th complement type repeat domain alone and in complex with gentamicin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M112.434159"}], "href": "https://doi.org/10.1074/jbc.M112.434159"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23275343"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23275343"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Ravikiran Mahadevappa, Rikke Nielsen, Erik Ilsø Christensen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Megalin in acute kidney injury: foe and friend."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Physiol Renal Physiol (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1152/ajprenal.00378.2013"}], "href": "https://doi.org/10.1152/ajprenal.00378.2013"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24197071"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24197071"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Shankhajit De, Shoji Kuwahara, Michihiro Hosojima, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Exocytosis-Mediated Urinary Full-Length Megalin Excretion Is Linked With the Pathogenesis of Diabetic Nephropathy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Diabetes (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.2337/db16-1031"}], "href": "https://doi.org/10.2337/db16-1031"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28289043"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28289043"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Sarah K Holt, Danielle M Karyadi, Erika M Kwon, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Association of megalin genetic polymorphisms with prostate cancer risk and prognosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Clin Cancer Res (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1158/1078-0432.CCR-07-4566"}], "href": "https://doi.org/10.1158/1078-0432.CCR-07-4566"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18559602"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18559602"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "May A Beydoun, Eric L Ding, Hind A Beydoun, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Vitamin D receptor and megalin gene polymorphisms and their associations with longitudinal cognitive change in US adults."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Clin Nutr (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3945/ajcn.111.017137"}], "href": "https://doi.org/10.3945/ajcn.111.017137"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22170372"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22170372"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Iuliana Ionita-Laza, Vlad Makarov, Joseph D Buxbaum "}, {"type": "b", "children": [{"type": "t", "text": "Scan-statistic approach identifies clusters of rare disease variants in LRP2, a gene linked and associated with autism spectrum disorders, in three datasets."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Hum Genet (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.ajhg.2012.04.010"}], "href": "https://doi.org/10.1016/j.ajhg.2012.04.010"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22578327"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22578327"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "So Young Gil, Byung-Soo Youn, Kyunghee Byun, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Clusterin and LRP2 are critical components of the hypothalamic feeding regulatory pathway."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ncomms2896"}], "href": "https://doi.org/10.1038/ncomms2896"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23673647"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23673647"}]}]}]}
Synonyms	DBS, GP330, LRP-2
Proteins	LRP2_HUMAN
NCBI Gene ID	4036
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

LRP2 has 8,231 functional associations with biological entities spanning 8 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) extracted from 134 datasets.

Click the + buttons to view associations for LRP2 from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

LRP2 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 LRP2 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 LRP2 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 LRP2 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 LRP2 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 LRP2 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 LRP2 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 LRP2 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 LRP2 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 LRP2 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 LRP2 gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of LRP2 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 LRP2 gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Gene Mutation Profiles	cell lines with LRP2 gene mutations from the CCLE Cell Line Gene Mutation Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with LRP2 protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with LRP2 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 LRP2 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of LRP2 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 LRP2 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 LRP2 gene from the curated ClinVar Gene-Phenotype Associations dataset.
	ClinVar Gene-Phenotype Associations 2025	phenotypes associated with LRP2 gene from the curated ClinVar Gene-Phenotype Associations 2025 dataset.
	CM4AI U2OS Cell Map Protein Localization Assemblies	assemblies containing LRP2 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 LRP2 gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing LRP2 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing LRP2 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores	cellular components containing LRP2 protein in low- or high-throughput protein localization assays from the COMPARTMENTS Experimental Protein Localization Evidence Scores dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores 2025	cellular components containing LRP2 protein in low- or high-throughput protein localization assays from the COMPARTMENTS Experimental Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores	cellular components co-occuring with LRP2 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 LRP2 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 LRP2 gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with LRP2 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with LRP2 gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with LRP2 gene/protein from the curated CTD Gene-Disease Associations dataset.
	dbGAP Gene-Trait Associations	traits associated with LRP2 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 LRP2 gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DISEASES Curated Gene-Disease Association Evidence Scores 2025	diseases involving LRP2 gene from the DISEASES Curated Gene-Disease Association Evidence Scores 2025 dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores	diseases associated with LRP2 gene in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores 2025	diseases associated with LRP2 gene in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores 2025 dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with LRP2 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 LRP2 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 LRP2 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.