CHORDC1 Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis. Underexpressed in many breast and lung cancers. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: Calcium-binding
Chromosomal Location of mouse Ortholog: 9|9 A2
Cellular Component: 
Molecular Function:  ADP binding; ATP binding; Hsp90 protein binding; metal ion binding; protein binding; zinc ion binding
Biological Process:  chaperone-mediated protein folding; negative regulation of Rho-dependent protein serine/threonine kinase activity; regulation of cellular response to heat; regulation of centrosome duplication
Reference #:  Q9D1P4 (UniProtKB)
Alt. Names/Synonyms: 1110001O09Rik; AA409036; CHORD domain-containing protein 1; CHORD-containing protein 1; Chordc1; Chp-; Chp-1; Chp1; CHRD1; cysteine and histidine-rich domain (CHORD)-containing, zinc-binding protein 1; Cysteine and histidine-rich domain-containing protein 1; Morgana; Protein morgana
Gene Symbols: Chordc1
Molecular weight: 37,351 Da
Basal Isoelectric point: 8.13  Predict pI for various phosphorylation states
Select Structure to View Below


Protein Structure Not Found.

Cross-references to other databases:  AlphaFold  |  STRING  |  BioGPS  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene