\
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: Cysteine and histidine-rich domain-containing protein 1

UniprotKB/SwissProt ID: Q9UHD1 (Q9UHD1)

Gene Name: CHORDC1

Organism: Homo sapiens (Human)

Function: Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2 (PubMed:20230755). Proposed to act as co-chaperone for HSP90 (PubMed:20230755). May play a role in the regulation of NOD1 via a HSP90 chaperone complex (PubMed:20230755). 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 (PubMed:32053105). Involved in stress response (PubMed:20230755). Prevents tumorigenesis (PubMed:20230755)

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 Q9UHD1

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 157 DNDEIKIGTS C KNGGCSKTYQ   
2 176 YQGLESLEEV C VYHSGVPIFH   
3 195 FHEGMKYWSC C RRKTSDFNTF   
4 211 DFNTFLAQEG C TKGKHMWTKK   
5 230 KKDAGKKVVP C RHDWHQTGGE   
6 24 FDPETNSDDA C TYHPGVPVFH   
7 42 VFHDALKGWS C CKRRTTDFSD   
8 5 ------MALL C YNRGCGQRFD   
9 59 DFSDFLSIVG C TKGRHNSEKP   
10 86 EVKTTEKKEL C ELKPKFQEHI