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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: Coiled-coil domain-containing protein 22

UniprotKB/SwissProt ID: O60826 (O60826)

Gene Name: CCDC22

Organism: Homo sapiens (Human)

Function: Component of the commander complex that is essential for endosomal recycling of transmembrane cargos; the Commander complex is composed of composed of the CCC subcomplex and the retriever subcomplex (PubMed:37172566, PubMed:38459129). Component of the CCC complex, which is involved in the regulation of endosomal recycling of surface proteins, including integrins, signaling receptor and channels (PubMed:37172566, PubMed:38459129). Involved in regulation of NF-kappa-B signaling (PubMed:23563313). Promotes ubiquitination of I-kappa-B-kinase subunit IKBKB and its subsequent proteasomal degradation leading to NF-kappa-B activation; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex (PubMed:23563313). May down-regulate NF-kappa-B activity via association with COMMD1 and involving a CUL2-dependent E3 ubiquitin ligase complex. Regulates the cellular localization of COMM domain-containing proteins, such as COMMD1 and COMMD10 (PubMed:23563313). Component of the CCC complex, which is involved in the regulation of endosomal recycling of surface proteins, including integrins, signaling receptor and channels. The CCC complex associates with SNX17, retriever and WASH complexes to prevent lysosomal degradation and promote cell surface recycling of numerous cargos such as integrins ITGA5:ITGB1 (PubMed:25355947, PubMed:28892079). Plays a role in copper ion homeostasis (PubMed:25355947). Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes (PubMed:25355947) (Microbial infection) The CCC complex, in collaboration with the heterotrimeric retriever complex, mediates the exit of human papillomavirus to the cell surface

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Endosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR008530 CCDC22
IPR048348 CCDC22_CC
IPR048349 CCDC22_N

The S-nitrosylation sites of O60826

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 369 GVSFVQAESE C RHSKLSTAER