Details for: CCS

Gene ID: 9973

Symbol: CCS

Ensembl ID: ENSG00000173992

Description: copper chaperone for superoxide dismutase

Associated with

Other Information

Genular Protein ID: 1156289490

Symbol: CCS_HUMAN

Name: Superoxide dismutase copper chaperone

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 9295278

Title: The copper chaperone for superoxide dismutase.

PubMed ID: 9295278

DOI: 10.1074/jbc.272.38.23469

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 31292775

Title: Copper-zinc superoxide dismutase (Sod1) activation terminates interaction between its copper chaperone (Ccs) and the cytosolic metal-binding domain of the copper importer Ctr1.

PubMed ID: 31292775

DOI: 10.1007/s10534-019-00206-3

PubMed ID: 23625804

Title: Mechanistic aspects of hSOD1 maturation from the solution structure of Cu(I) -loaded hCCS domain 1 and analysis of disulfide-free hSOD1 mutants.

PubMed ID: 23625804

DOI: 10.1002/cbic.201300042

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 9726962

Title: The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase.

PubMed ID: 9726962

DOI: 10.1074/jbc.273.37.23625

PubMed ID: 15736924

Title: Cysteine-to-serine mutants of the human copper chaperone for superoxide dismutase reveal a copper cluster at a domain III dimer interface.

PubMed ID: 15736924

DOI: 10.1021/bi0478392

PubMed ID: 20595380

Title: Cu,Zn superoxide dismutase maturation and activity are regulated by COMMD1.

PubMed ID: 20595380

DOI: 10.1074/jbc.m110.101477

PubMed ID: 20154138

Title: Regulation of the copper chaperone CCS by XIAP-mediated ubiquitination.

PubMed ID: 20154138

DOI: 10.1128/mcb.00900-09

PubMed ID: 22508683

Title: Molecular and biochemical characterization of a unique mutation in CCS, the human copper chaperone to superoxide dismutase.

PubMed ID: 22508683

DOI: 10.1002/humu.22099

PubMed ID: 10677207

Title: Crystal structure of the second domain of the human copper chaperone for superoxide dismutase.

PubMed ID: 10677207

DOI: 10.1021/bi992822i

Sequence Information:

  • Length: 274
  • Mass: 29041
  • Checksum: A392432954B65760
  • Sequence:
  • MASDSGNQGT LCTLEFAVQM TCQSCVDAVR KSLQGVAGVQ DVEVHLEDQM VLVHTTLPSQ 
    EVQALLEGTG RQAVLKGMGS GQLQNLGAAV AILGGPGTVQ GVVRFLQLTP ERCLIEGTID 
    GLEPGLHGLH VHQYGDLTNN CNSCGNHFNP DGASHGGPQD SDRHRGDLGN VRADADGRAI 
    FRMEDEQLKV WDVIGRSLII DEGEDDLGRG GHPLSKITGN SGERLACGII ARSAGLFQNP 
    KQICSCDGLT IWEERGRPIA GKGRKESAQP PAHL

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.