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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: Cysteine and histidine-rich domain-containing protein 1

UniprotKB/SwissProt ID: Q9D1P4 (Q9D1P4)

Gene Name: Chordc1

Organism: Mus musculus (Mouse)

Function: Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2 (PubMed:20230755). Proposed to act as co-chaperone for HSP90 (PubMed:16083881). May play a role in the regulation of NOD1 via a HSP90 chaperone complex (PubMed:16083881). In vitro, has intrinsic chaperone activity (PubMed:20230755). This function may be achieved by inhibiting association of ROCK2 with NPM1 (PubMed:20230755). Plays a role in ensuring the localization of the tyrosine kinase receptor EGFR to the plasma membrane, and thus ensures the subsequent regulation of EGFR activity and EGF-induced actin cytoskeleton remodeling (By similarity). Involved in stress response (PubMed:20493909). Prevents tumorigenesis (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization:

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR007051 CHORD_dom
IPR039790 CHRD1
IPR007052 CS_dom
IPR008978 HSP20-like_chaperone

The S-nitrosylation sites of Q9D1P4

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 211 DFNTFLAQEG C TRGKHVWTKK  CCEEECCCCC C CCCCCCCCCC  2%
2 59 DFSDFLSIVG C TKGRHNSEKP  CCEEECCCCC C CCCCCCCCCC  2.17% 21278135