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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: Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3

UniprotKB/SwissProt ID: Q14573 (Q14573)

Gene Name: ITPR3

Organism: Homo sapiens (Human)

Function: Inositol 1,4,5-trisphosphate-gated calcium channel that, upon 1D-myo-inositol 1,4,5-trisphosphate binding, transports calcium from the endoplasmic reticulum lumen to cytoplasm, thus releasing the intracellular calcium and therefore participates in cellular calcium ion homeostasis (PubMed:32949214, PubMed:37898605, PubMed:8081734, PubMed:8288584). 1D-myo-inositol 1,4,5-trisphosphate binds to the ligand-free channel without altering its global conformation, yielding the low-energy resting state, then progresses through resting-to preactivated transitions to the higher energy preactivated state, which increases affinity for calcium, promoting binding of the low basal cytosolic calcium at the juxtamembrane domain (JD) site, favoring the transition through the ensemble of high-energy intermediate states along the trajectory to the fully-open activated state (PubMed:30013099, PubMed:35301323, PubMed:37898605). Upon opening, releases calcium in the cytosol where it can bind to the low-affinity cytoplasmic domain (CD) site and stabilizes the inhibited state to terminate calcium release (PubMed:30013099, PubMed:35301323, PubMed:37898605)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Endoplasmic reticulum membrane. Cytoplasmic vesicle, secretory vesicle membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR014821 Ins145_P3_rcpt
IPR000493 InsP3_rcpt
IPR005821 Ion_trans_dom
IPR036300 MIR_dom_sf
IPR016093 MIR_motif
IPR013662 RIH_assoc-dom
IPR000699 RIH_dom
IPR015925 Ryanodine_IP3_receptor
IPR035910 RyR/IP3R_RIH_dom_sf

The S-nitrosylation sites of Q14573

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 1525 QQQHKGSVEA C IRTLAMVAKG   
2 1638 FLEGSEAYQR C ESGGFLSKLI   
3 1726 PDWSAIAATQ C RLDKEGATKL   
4 1738 LDKEGATKLV C DLITSTKNEK   
5 2144 EQIVFPVPGI C QFLTEETKHR   
6 215 AGCKEVNSVN C NTSWKINLFM   
7 254 FHAEQEKFLT C DEYKGKLQVF   
8 2668 QRLGFVDVQN C ISR-------