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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Endoplasmic reticulum aminopeptidase 1

UniprotKB/SwissProt ID: Q9JJ22 (Q9JJ22)

Gene Name: Erap1

Organism: Rattus norvegicus (Rat)

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 (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Endoplasmic reticulum membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR045357 Aminopeptidase_N-like_N
IPR042097 Aminopeptidase_N-like_N_sf
IPR024571 ERAP1-like_C_dom
IPR034016 M1_APN-typ
IPR001930 Peptidase_M1
IPR050344 Peptidase_M1_aminopeptidases
IPR014782 Peptidase_M1_dom
IPR027268 Peptidase_M4/M1_CTD_sf