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FLASH GENE
Symbol ERAP1 contributors: mct/pgu - updated : 16-04-2017
HGNC name endoplasmic reticulum aminopeptidase 1
HGNC id 18173
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • N terminal signal peptide
  • five potential N glycosylation sites
  • one potential membrane spanning domain
  • one zinc finger binding motif
  • mono polymer monomer
    HOMOLOGY
    interspecies homolog to murine Erap1 (85.7pc)
    homolog to rattus Erap1 (84.8pc)
    intraspecies paralog to ERAP2
    Homologene
    FAMILY
  • M1 family of zinc metallopeptidase
  • CATEGORY enzyme
    SUBCELLULAR LOCALIZATION extracellular
    intracellular,cytoplasm,organelle,membrane
    intracellular,cytoplasm,organelle,endoplasmic reticulum
    intracellular,cytoplasm,cytosolic
    basic FUNCTION
  • playing a role in the regulation of blood pressure through inactivation of angiotensin 2 and/or generation of bradykinin in the kidney
  • NUCB2/ERAP1 complexes, which associate with TNFRSF1A play an important role in mediating TNFRSF1A release to the extracellular compartment
  • a multifunctional aminopeptidase that may modulate inflammatory events by promoting IL6Ralpha and TNFR1 shedding
  • IFN-gamma-induced aminopeptidase that trims longer precursors to the antigenic peptides presented on MHC class I molecules to facilitates antigen presentation
  • major enzyme that trims precursor peptides in the endoplasmic reticulum and, in this process, can generate or destroy antigenic peptides (trims MHC class I-presented peptides and plays an important role in immunodominance)
  • having function in the cleavage of cell-surface cytokine receptors (e.g. TNFR1) and peptide binding to MHC class I molecules in the ER
  • play a role in blood pressure regulation and essential hypertension in addition to innate immune and inflammatory responses
  • ERAP1, ERAP2, LNPEP play critical roles in the generation of antigenic peptides
  • trims antigen precursors to fit into MHC class I proteins, through a generic aminopeptidase structure adapted for the specialized function of trimming antigenic precursors
  • endoplasmic reticulum aminopeptidase involved in peptide trimming before HLA class I presentation
  • ERAP1 and ERAP2 cooperate to trim antigenic peptide precursors for loading onto MHC class I molecules and help regulate the adaptive immune response
  • ERAP1 and ERAP2 might play an important role in shaping the MHC class I-presented peptide repertoire
  • ERAP1 and ERAP2 are two multifunctional enzymes playing an important role in the biological processes requiring trimming of substrates, including the generation of major histocompatibility complex (MHC) class I binding peptide
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
  • NUCB2/ERAP1 complexes
  • INTERACTION
    DNA
    RNA
    small molecule metal binding,
  • zinc ion
  • protein
  • interacting with NUCB2 (via its helix-loop-helix domains, binds the ERAP1 extracellular domain)
  • ERP44 controls the release of ERAP1 in a redox-dependent manner to control blood pressure
  • plays a central role as a "molecular ruler", proteolyzing of N-terminal of the antigenic peptides before their loading onto HLA-I molecules for antigen presentation in the Endoplasmic Reticulum (ER)
  • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Susceptibility
  • to ankylosing spondylitis (AS), in HLA-B27-positive individuals
  • to preeclampsia
  • Variant & Polymorphism SNP , other
  • snp ERAP1-56 and ERAP1-127 significantly associated with clinical outcome in cervical carcinoma
  • rs27434, rs27689 and rs27043 strongly associated to AS
  • polymorphisms of ERAP1 increasing the risk of ankylosing spondylitis (AS), in HLA-B27-positive individuals (
  • associated with preeclampsia
  • Candidate gene
    Marker
    Therapy target
    ANIMAL & CELL MODELS
    healthy mice Erap1-/-. MHC class I levels were reduced in Erap1 -/- splenocytes, but not fibroblasts, and peptide trimming in Erap1 -/- fibroblasts was reduced. The immune response in Erap1 -/- mice to some viral peptides was altered due to lack of the trimming enzyme