ERAP1 Gene

HGNC Family	Minor histocompatibility antigens, Aminopeptidases
Name	endoplasmic reticulum aminopeptidase 1
Description	The protein encoded by this gene is an aminopeptidase involved in trimming HLA class I-binding precursors so that they can be presented on MHC class I molecules. The encoded protein acts as a monomer or as a heterodimer with ERAP2. This protein may also be involved in blood pressure regulation by inactivation of angiotensin II. Three transcript variants encoding two different isoforms have been found for this gene.[provided by RefSeq, Oct 2010]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n Endoplasmic reticulum aminopeptidase 1 (ERAP1), also known as ARTS‐1, is a multifunctional zinc‐dependent metallopeptidase that plays a pivotal role in antigen processing within the endoplasmic reticulum by trimming N‐extended peptide precursors to generate optimally sized epitopes for binding to major histocompatibility complex (MHC) class I molecules."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": " By employing a “molecular ruler” mechanism, ERAP1 preferentially processes substrates that are 9–16 amino acids in length—efficiently converting longer precursors into mature peptides while sparing those already at the optimal size."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}, {"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n In doing so, ERAP1 not only shapes the peptide repertoire available for MHC class I presentation but also strongly influences the magnitude and hierarchy of CD8<sup>+</sup> T cell responses."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": " Structural studies have revealed that ERAP1 contains a large internal cavity and undergoes substantial conformational (domain) movements that facilitate substrate binding and catalysis; furthermore, naturally occurring polymorphisms can alter its catalytic kinetics and substrate specificity."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}, {"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n In addition to its canonical role in peptide trimming, ERAP1 (ARTS‐1) has been implicated in the modulation of immune receptor activity by promoting the shedding of cell surface receptors such as tumor necrosis factor receptor 1 (TNFR1) and interleukin‐6 receptor alpha (IL-6Rα), processes that contribute to the regulation of inflammatory signaling."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Moreover, ERAP1 acts in concert with its homolog ERAP2; the complementary and sometimes cooperative trimming activities of these two enzymes ensure the proper processing of a wide variety of antigenic peptides."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "10"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Importantly, genetic polymorphisms in ERAP1 have been robustly associated with several immune-mediated diseases—including ankylosing spondylitis, psoriasis, Behçet’s disease, and type 1 diabetes—highlighting the critical role of precise peptide trimming in immune surveillance and disease susceptibility."}, {"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": "\n Overall, ERAP1 is integral not only to the generation of a correctly sized antigenic peptide repertoire for MHC class I presentation but also to broader immunoregulatory processes through its influence on receptor shedding and cooperative action with ERAP2, thereby linking antigen processing with downstream adaptive and inflammatory responses.\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Thomas Serwold, Federico Gonzalez, Jennifer Kim, et al. "}, {"type": "b", "children": [{"type": "t", "text": "ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nature (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nature01074"}], "href": "https://doi.org/10.1038/nature01074"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12368856"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12368856"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Ian A York, Shih-Chung Chang, Tomo Saric, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Immunol (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ni860"}], "href": "https://doi.org/10.1038/ni860"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12436110"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12436110"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Tina T Nguyen, Shih-Chung Chang, Irini Evnouchidou, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structural basis for antigenic peptide precursor processing by the endoplasmic reticulum aminopeptidase ERAP1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Struct Mol Biol (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nsmb.2021"}], "href": "https://doi.org/10.1038/nsmb.2021"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21478864"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21478864"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Shih-Chung Chang, Frank Momburg, Nidhi Bhutani, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The ER aminopeptidase, ERAP1, trims precursors to lengths of MHC class I peptides by a \"molecular ruler\" mechanism."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0500721102"}], "href": "https://doi.org/10.1073/pnas.0500721102"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16286653"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16286653"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Ian A York, Michael A Brehm, Sophia Zendzian, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Endoplasmic reticulum aminopeptidase 1 (ERAP1) trims MHC class I-presented peptides in vivo and plays an important role in immunodominance."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0603095103"}], "href": "https://doi.org/10.1073/pnas.0603095103"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16754858"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16754858"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Grazyna Kochan, Tobias Krojer, David Harvey, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Crystal structures of the endoplasmic reticulum aminopeptidase-1 (ERAP1) reveal the molecular basis for N-terminal peptide trimming."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.1101262108"}], "href": "https://doi.org/10.1073/pnas.1101262108"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21508329"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21508329"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Arron Hearn, Ian A York, Kenneth L Rock "}, {"type": "b", "children": [{"type": "t", "text": "The specificity of trimming of MHC class I-presented peptides in the endoplasmic reticulum."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Immunol (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.4049/jimmunol.0803663"}], "href": "https://doi.org/10.4049/jimmunol.0803663"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19828632"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19828632"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Xinle Cui, Feras Hawari, Sura Alsaaty, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Identification of ARTS-1 as a novel TNFR1-binding protein that promotes TNFR1 ectodomain shedding."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Clin Invest (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1172/JCI13847"}], "href": "https://doi.org/10.1172/JCI13847"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12189246"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12189246"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Xinle Cui, Farshid N Rouhani, Feras Hawari, et al. "}, {"type": "b", "children": [{"type": "t", "text": "An aminopeptidase, ARTS-1, is required for interleukin-6 receptor shedding."}]}, {"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.M300456200"}], "href": "https://doi.org/10.1074/jbc.M300456200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12748171"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12748171"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Loredana Saveanu, Oliver Carroll, Vivian Lindo, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Concerted peptide trimming by human ERAP1 and ERAP2 aminopeptidase complexes in the endoplasmic reticulum."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Immunol (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ni1208"}], "href": "https://doi.org/10.1038/ni1208"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15908954"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15908954"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "James R Birtley, Emmanuel Saridakis, Efstratios Stratikos, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The crystal structure of human endoplasmic reticulum aminopeptidase 2 reveals the atomic basis for distinct roles in antigen processing."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochemistry (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/bi201230p"}], "href": "https://doi.org/10.1021/bi201230p"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22106953"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22106953"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Amy Strange, Francesca Capon, Chris C A Spencer, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A genome-wide association study identifies new psoriasis susceptibility loci and an interaction between HLA-C and ERAP1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Genet (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ng.694"}], "href": "https://doi.org/10.1038/ng.694"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20953190"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20953190"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Yohei Kirino, George Bertsias, Yoshiaki Ishigatsubo, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Genome-wide association analysis identifies new susceptibility loci for Behçet's disease and epistasis between HLA-B*51 and ERAP1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Genet (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ng.2520"}], "href": "https://doi.org/10.1038/ng.2520"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23291587"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23291587"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Patrick Danoy, Karena Pryce, Johanna Hadler, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Association of variants at 1q32 and STAT3 with ankylosing spondylitis suggests genetic overlap with Crohn's disease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS Genet (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pgen.1001195"}], "href": "https://doi.org/10.1371/journal.pgen.1001195"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21152001"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21152001"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "John D Reveille, Anne-Marie Sims, Patrick Danoy, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Genome-wide association study of ankylosing spondylitis identifies non-MHC susceptibility loci."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Genet (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ng.513"}], "href": "https://doi.org/10.1038/ng.513"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20062062"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20062062"}]}]}]}
Synonyms	A-LAP, ERAAP, PILSAP, ALAP, ARTS-1, ARTS1, APPILS, ERAAP1, PILS-AP
Proteins	ERAP1_HUMAN
NCBI Gene ID	51752
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

ERAP1 has 8,700 functional associations with biological entities spanning 9 categories (molecular profile, organism, chemical, functional term, phrase or reference, disease, phenotype or trait, structural feature, cell line, cell type or tissue, gene, protein or microRNA, sequence feature) extracted from 126 datasets.

Click the + buttons to view associations for ERAP1 from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

ERAP1 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 ERAP1 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 ERAP1 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 ERAP1 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 ERAP1 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 ERAP1 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 ERAP1 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 ERAP1 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 ERAP1 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 ERAP1 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 ERAP1 gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of ERAP1 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 ERAP1 gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with ERAP1 protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with ERAP1 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 ERAP1 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of ERAP1 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 ERAP1 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
	CM4AI U2OS Cell Map Protein Localization Assemblies	assemblies containing ERAP1 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 ERAP1 gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing ERAP1 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing ERAP1 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores	cellular components containing ERAP1 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 ERAP1 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 ERAP1 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 ERAP1 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
	CORUM Protein Complexes	protein complexs containing ERAP1 protein from the CORUM Protein Complexes dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with ERAP1 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with ERAP1 gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with ERAP1 gene/protein from the curated CTD Gene-Disease Associations dataset.
	dbGAP Gene-Trait Associations	traits associated with ERAP1 gene in GWAS and other genetic association datasets from the dbGAP Gene-Trait Associations dataset.
	DeepCoverMOA Drug Mechanisms of Action	small molecule perturbations with high or low expression of ERAP1 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 ERAP1 gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DISEASES Curated Gene-Disease Association Evidence Scores	diseases involving ERAP1 gene from the DISEASES Curated Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Curated Gene-Disease Association Evidence Scores 2025	diseases involving ERAP1 gene from the DISEASES Curated Gene-Disease Association Evidence Scores 2025 dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores	diseases associated with ERAP1 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 ERAP1 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 ERAP1 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 ERAP1 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 ERAP1 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with ERAP1 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Phenoptype Associations dataset.