\
logo
  Home | Contact us | Browse | Quick Search by UniProtKB ID, Keyword, PDBID

Menu:

Latest news:

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.

Read more...


Protein Name: Chloride intracellular channel protein 5

UniprotKB/SwissProt ID: Q9NZA1 (Q9NZA1)

Gene Name: CLIC5

Organism: Homo sapiens (Human)

Function: In the soluble state, catalyzes glutaredoxin-like thiol disulfide exchange reactions with reduced glutathione as electron donor (By similarity). Can insert into membranes and form non-selective ion channels almost equally permeable to Na(+), K(+) and Cl(-) (PubMed:15184393, PubMed:18028448). Required for normal hearing (PubMed:24781754). It is necessary for the formation of stereocilia in the inner ear and normal development of the organ of Corti (By similarity). May play a role in the regulation of transepithelial ion absorption and secretion. Is required for the development and/or maintenance of the proper glomerular endothelial cell and podocyte architecture (PubMed:15184393, PubMed:18028448, PubMed:20335315). Plays a role in formation of the lens suture in the eye, which is important for normal optical properties of the lens (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Membrane. Apical cell membrane. Cytoplasm. Mitochondrion. Cell projection, stereocilium. Golgi apparatus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR002946 CLIC
IPR042069 CLIC5_C_GST
IPR053823 CLIC_N
IPR010987 Glutathione-S-Trfase_C-like
IPR036282 Glutathione-S-Trfase_C_sf
IPR040079 Glutathione_S-Trfase
IPR036249 Thioredoxin-like_sf

The S-nitrosylation sites of Q9NZA1

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 191 AGIDGESIGN C PFSQRLFMIL