ABCC2 Gene

HGNC Family	ATP binding cassette transporters (ABC)
Name	ATP-binding cassette, sub-family C (CFTR/MRP), member 2
Description	The protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the MRP subfamily which is involved in multi-drug resistance. This protein is expressed in the canalicular (apical) part of the hepatocyte and functions in biliary transport. Substrates include anticancer drugs such as vinblastine; therefore, this protein appears to contribute to drug resistance in mammalian cells. Several different mutations in this gene have been observed in patients with Dubin-Johnson syndrome (DJS), an autosomal recessive disorder characterized by conjugated hyperbilirubinemia. [provided by RefSeq, Jul 2008]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nABCC2 (also known as MRP2 or canalicular multispecific organic anion transporter) is an ATP‐driven efflux protein that plays an essential role in the elimination of a wide range of endogenous and exogenous anionic compounds. In the liver its predominant localization to the apical (canalicular) membrane of hepatocytes facilitates the biliary excretion of conjugated metabolites—such as bilirubin glucuronides, bile acids, and folate derivatives—and thereby helps maintain systemic detoxification and homeostasis. Furthermore, ABCC2 is expressed in renal epithelial cells, enterocytes, and even certain hematopoietic cells, where its activity contributes to drug resistance and the clearance of anticancer drugs. Defective expression or mutations in this transporter are associated with disorders like Dubin–Johnson syndrome and may affect overall drug disposition in vivo."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMechanistic studies using vesicle transport assays and polarized cell models have shown that ABCC2 exhibits substrate‐dependent kinetic properties including homotropic cooperativity with substrates such as estradiol-17β-glucuronide and methotrexate. Its activity is modulated allosterically by compounds like indomethacin and sulfanitran, which enhance substrate affinity and can shift cooperative kinetics toward more hyperbolic behavior. Moreover, specific structural determinants—such as sequences within its C-terminal domain—are critical for apical sorting, with deletions or missense mutations resulting in improper localization and loss of function."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "15"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nGenetic studies have further underscored the clinical importance of ABCC2 function. Multiple missense mutations and polymorphisms have been identified that impair protein maturation, proper membrane targeting, or substrate-induced ATP hydrolysis; such defects contribute directly to conditions like Dubin–Johnson syndrome. In addition, variants in ABCC2 have been investigated for their impact on the pharmacokinetics of drugs including pravastatin, irinotecan, and antifolate agents, as well as on the cellular retention of natural folates—findings that bear implications for drug resistance and even developmental disorders (e.g. neural tube defects). Although some studies report no significant associations between ABCC2 polymorphisms and drug exposure, the collective evidence highlights ABCC2’s pivotal role in modulating both endogenous metabolite and xenobiotic efflux, thereby influencing oral bioavailability and therapeutic outcomes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "16", "end_ref": "19"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "R Mor-Cohen, A Zivelin, N Rosenberg, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Identification and functional analysis of two novel mutations in the multidrug resistance protein 2 gene in Israeli patients with Dubin-Johnson syndrome."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2001)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M105047200"}], "href": "https://doi.org/10.1074/jbc.M105047200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11477083"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11477083"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Yoshimune Sakaki, Kenji Terashi, Akihiko Yamaguchi, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Structural requirements for the apical sorting of human multidrug resistance protein 2 (ABCC2)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Eur J Biochem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1046/j.1432-1033.2002.02832.x"}], "href": "https://doi.org/10.1046/j.1432-1033.2002.02832.x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11952788"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11952788"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Verena Keitel, Anne T Nies, Manuela Brom, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A common Dubin-Johnson syndrome mutation impairs protein maturation and transport activity of MRP2 (ABCC2)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Physiol Gastrointest Liver Physiol (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1152/ajpgi.00362.2002"}], "href": "https://doi.org/10.1152/ajpgi.00362.2002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12388192"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12388192"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Kenkichi Hashimoto, Takeshi Uchiumi, Toshikazu Konno, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Trafficking and functional defects by mutations of the ATP-binding domains in MRP2 in patients with Dubin-Johnson syndrome."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hepatology (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1053/jhep.2002.36368"}], "href": "https://doi.org/10.1053/jhep.2002.36368"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12395335"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12395335"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Herman Burger, John A Foekens, Maxime P Look, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "The role of multidrug resistance proteins MRP1, MRP2 and MRP3 in cellular folate homeostasis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Pharmacol (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/s0006-2952(02)01615-5"}], "href": "https://doi.org/10.1016/s0006-2952(02"}, {"type": "t", "text": "01615-5) PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12628490"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12628490"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Adrienn Bodo, Eva Bakos, Flora Szeri, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Differential modulation of the human liver conjugate transporters MRP2 and MRP3 by bile acids and organic anions."}]}, {"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.M303515200"}], "href": "https://doi.org/10.1074/jbc.M303515200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12704183"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12704183"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Hideyuki Kojima, Anne T Nies, Jörg König, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Changes in the expression and localization of hepatocellular transporters and radixin in primary biliary cirrhosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Hepatol (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/s0168-8278(03)00410-0"}], "href": "https://doi.org/10.1016/s0168-8278(03"}, {"type": "t", "text": "00410-0) PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14568249"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14568249"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Christoph G Dietrich, Andreas Geier, Nina Salein, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Consequences of bile duct obstruction on intestinal expression and function of multidrug resistance-associated protein 2."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Gastroenterology (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1053/j.gastro.2003.12.046"}], "href": "https://doi.org/10.1053/j.gastro.2003.12.046"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15057744"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15057744"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Ichiro Ieiri, Hiroshi Suzuki, Miyuki Kimura, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Influence of common variants in the pharmacokinetic genes (OATP-C, UGT1A1, and MRP2) on serum bilirubin levels in healthy subjects."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hepatol Res (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.hepres.2004.07.005"}], "href": "https://doi.org/10.1016/j.hepres.2004.07.005"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15519273"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15519273"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Noam Zelcer, Maarten T Huisman, Glen Reid, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Evidence for two interacting ligand binding sites in human multidrug resistance protein 2 (ATP binding cassette C2)."}]}, {"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.M303504200"}], "href": "https://doi.org/10.1074/jbc.M303504200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12702717"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12702717"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Kersti Oselin, Przemyslaw M Mrozikiewicz, Rein Pähkla, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Quantitative determination of the human MRP1 and MRP2 mRNA expression in FACS-sorted peripheral blood CD4+, CD8+, CD19+, and CD56+ cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Eur J Haematol (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1034/j.1600-0609.2003.00100.x"}], "href": "https://doi.org/10.1034/j.1600-0609.2003.00100.x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12890151"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12890151"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Verena Materna, Hermann Lage "}, {"type": "b", "children": [{"type": "t", "text": "Homozygous mutation Arg768Trp in the ABC-transporter encoding gene MRP2/cMOAT/ABCC2 causes Dubin-Johnson syndrome in a Caucasian patient."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Hum Genet (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s10038-003-0057-8"}], "href": "https://doi.org/10.1007/s10038-003-0057-8"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12942343"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12942343"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Ron H J Mathijssen, Sharon Marsh, Mats O Karlsson, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Irinotecan pathway genotype analysis to predict pharmacokinetics."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Clin Cancer Res (2003)"}]}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12960109"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12960109"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Liselotte E Jensen, Amelia M Wall, Michelle Cook, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A common ABCC2 promoter polymorphism is not a determinant of the risk of spina bifida."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Birth Defects Res A Clin Mol Teratol (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/bdra.20023"}], "href": "https://doi.org/10.1002/bdra.20023"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15211708"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15211708"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Mikko Niemi, Elke Schaeffeler, Thomas Lang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "High plasma pravastatin concentrations are associated with single nucleotide polymorphisms and haplotypes of organic anion transporting polypeptide-C (OATP-C, SLCO1B1)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Pharmacogenetics (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1097/01.fpc.0000114750.08559.32"}], "href": "https://doi.org/10.1097/01.fpc.0000114750.08559.32"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15226675"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15226675"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Qingyu Zhou, Alex Sparreboom, Eng-Huat Tan, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Pharmacogenetic profiling across the irinotecan pathway in Asian patients with cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Br J Clin Pharmacol (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/j.1365-2125.2004.02330.x"}], "href": "https://doi.org/10.1111/j.1365-2125.2004.02330.x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15801936"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15801936"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Hannah Prime-Chapman, Vanessa Moore, Barry H Hirst "}, {"type": "b", "children": [{"type": "t", "text": "Antibiotic exposure does not influence MRP2 functional expression in Caco-2 cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Drug Target (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1080/10611860400015944"}], "href": "https://doi.org/10.1080/10611860400015944"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15848949"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15848949"}]}]}]}
Synonyms	CMOAT, CMRP, DJS, ABC30
Proteins	MRP2_HUMAN
NCBI Gene ID	1244
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

ABCC2 has 9,385 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 122 datasets.

Click the + buttons to view associations for ABCC2 from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

ABCC2 Gene

Functional Associations

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

	Dataset	Summary
	Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles	tissues with high or low expression of ABCC2 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 ABCC2 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 ABCC2 gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by Microarray dataset.
	Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of ABCC2 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 ABCC2 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 ABCC2 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 ABCC2 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 ABCC2 gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of ABCC2 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 ABCC2 gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with ABCC2 protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with ABCC2 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 ABCC2 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of ABCC2 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 ABCC2 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 ABCC2 gene from the curated ClinVar Gene-Phenotype Associations dataset.
	ClinVar Gene-Phenotype Associations 2025	phenotypes associated with ABCC2 gene from the curated ClinVar Gene-Phenotype Associations 2025 dataset.
	CM4AI KOLF21J CRISPRi Gene Perturbation Atlas	gene perturbations changing expression of ABCC2 gene from the CM4AI KOLF21J CRISPRi Gene Perturbation Atlas dataset.
	CMAP Signatures of Differentially Expressed Genes for Small Molecules	small molecule perturbations changing expression of ABCC2 gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing ABCC2 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing ABCC2 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores	cellular components co-occuring with ABCC2 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 ABCC2 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 ABCC2 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with ABCC2 gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with ABCC2 gene/protein from the curated CTD Gene-Disease Associations dataset.
	DeepCoverMOA Drug Mechanisms of Action	small molecule perturbations with high or low expression of ABCC2 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 ABCC2 gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DGIdb Drug Targets 2026	interacting drugs for ABCC2 protein from the DGIdb Drug Targets 2026 dataset.
	DISEASES Curated Gene-Disease Association Evidence Scores	diseases involving ABCC2 gene from the DISEASES Curated Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Curated Gene-Disease Association Evidence Scores 2025	diseases involving ABCC2 gene from the DISEASES Curated Gene-Disease Association Evidence Scores 2025 dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores 2025	diseases associated with ABCC2 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 ABCC2 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 ABCC2 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 ABCC2 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with ABCC2 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Phenoptype Associations dataset.
	DrugBank Drug Targets	interacting drugs for ABCC2 protein from the curated DrugBank Drug Targets dataset.
	ENCODE Histone Modification Site Profiles	histone modification site profiles with high histone modification abundance at ABCC2 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 ABCC2 gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of ABCC2 gene in ChIP-seq datasets from the ENCODE Transcription Factor Targets dataset.