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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: Insulin-degrading enzyme

UniprotKB/SwissProt ID: P35559 (P35559)

Gene Name: Ide

Organism: Rattus norvegicus (Rat)

Function: Plays a role in the cellular breakdown of insulin, APP peptides, IAPP peptides, natriuretic peptides, glucagon, bradykinin, kallidin, and other peptides, and thereby plays a role in intercellular peptide signaling (PubMed:10684867, PubMed:12941771, PubMed:1445854, PubMed:14527953, PubMed:1836994, PubMed:22049080). Substrate binding induces important conformation changes, making it possible to bind and degrade larger substrates, such as insulin (By similarity). Contributes to the regulation of peptide hormone signaling cascades and regulation of blood glucose homeostasis via its role in the degradation of insulin, glucagon and IAPP (By similarity). Plays a role in the degradation and clearance of APP-derived amyloidogenic peptides that are secreted by neurons and microglia (PubMed:10684867). Degrades the natriuretic peptides ANP, BNP and CNP, inactivating their ability to raise intracellular cGMP (By similarity). Also degrades an aberrant frameshifted 40-residue form of NPPA (fsNPPA) which is associated with familial atrial fibrillation in heterozygous patients (By similarity). Involved in antigen processing. Produces both the N terminus and the C terminus of MAGEA3-derived antigenic peptide (EVDPIGHLY) that is presented to cytotoxic T lymphocytes by MHC class I

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm, cytosol. Cell membrane. Secreted

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR011249 Metalloenz_LuxS/M16
IPR011765 Pept_M16_N
IPR001431 Pept_M16_Zn_BS
IPR050626 Peptidase_M16
IPR007863 Peptidase_M16_C
IPR032632 Peptidase_M16_M
IPR054734 PqqF-like_C_4

The S-nitrosylation sites of P35559

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 171 ALDRFAQFFL C PLFDASCKDR