ERAP1 — Endoplasmic reticulum aminopeptidase 1
ERAP1 belongs to a gene co-expression module in 3 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.
ERAP1's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| Gamma-delta T cells | ER Antigen Processing Protein processing & ER | ACLY, ATL3, ATR, CANX, DCTN1, DDB1, FOXJ3, ITCH +9 more | |
| Macrophages | Myeloid Differentiation Identity Developmental | ADCK2, ALOX5, ATP2C1, CCDC6, CDK6, CMTM7, DEF6, EEF2K +21 more | View in SCUBA |
| Mucosal-associated invariant T cell | SWI/SNF Chromatin Remodeling DNA/chromatin regulation | ARCN1, ATL3, CASP8, CYFIP2, DENND4C, DIDO1, DPP4, NFATC3 +8 more |
About the gene
| Synonyms | A-LAP, ARTS-1, ERAAP1, KIAA0525, PILS-AP |
|---|---|
| Chromosome | 5: 96760810-96808100 |
| Predicted location | Intracellular, Secreted |
| Essential gene | No |
| Protein class | Enzymes, Plasma proteins, Predicted intracellular proteins, Predicted secreted proteins |
| Molecular function | Aminopeptidase, Hydrolase, Metalloprotease, Protease |
| Biological process | Adaptive immunity, Immunity |
Function
Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney.
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.