CCS (gene)

Copper chaperone for superoxide dismutase
PDB rendering based on 1do5.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1do5​, 2crl​
Identifiers
Symbols	CCS ; MGC138260
External IDs	Template:OMIM5 Template:MGI HomoloGene: 3762
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Copper chaperone for superoxide dismutase, also known as CCS, is a human gene.

Copper chaperone for superoxide dismutase specifically delivers Cu to copper/zinc superoxide dismutase and may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.

Further reading

• Culotta VC, Klomp LW, Strain J; et al. (1997). "The copper chaperone for superoxide dismutase". J. Biol. Chem. 272 (38): 23469–72. PMID 9295278.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Casareno RL, Waggoner D, Gitlin JD (1998). "The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase". J. Biol. Chem. 273 (37): 23625–8. PMID 9726962.CS1 maint: Multiple names: authors list (link)
• Rothstein JD, Dykes-Hoberg M, Corson LB; et al. (1999). "The copper chaperone CCS is abundant in neurons and astrocytes in human and rodent brain". J. Neurochem. 72 (1): 422–9. PMID 9886096.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Rae TD, Schmidt PJ, Pufahl RA; et al. (1999). "Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase". Science. 284 (5415): 805–8. PMID 10221913.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Lamb AL, Wernimont AK, Pufahl RA; et al. (2000). "Crystal structure of the second domain of the human copper chaperone for superoxide dismutase". Biochemistry. 39 (7): 1589–95. PMID 10677207.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Moore SD, Chen MM, Cox DW (2000). "Cloning and mapping of murine superoxide dismutase copper chaperone (Ccsd) and mapping of the human ortholog". Cytogenet. Cell Genet. 88 (1–2): 35–7. PMID 10773661.CS1 maint: Multiple names: authors list (link)
• Bartnikas TB, Waggoner DJ, Casareno RL; et al. (2000). "Chromosomal localization of CCS, the copper chaperone for Cu/Zn superoxide dismutase". Mamm. Genome. 11 (5): 409–11. PMID 10790544.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Rae TD, Torres AS, Pufahl RA, O'Halloran TV (2001). "Mechanism of Cu,Zn-superoxide dismutase activation by the human metallochaperone hCCS". J. Biol. Chem. 276 (7): 5166–76. doi:10.1074/jbc.M008005200. PMID 11018045.CS1 maint: Multiple names: authors list (link)
• McLoughlin DM, Standen CL, Lau KF; et al. (2001). "The neuronal adaptor protein X11alpha interacts with the copper chaperone for SOD1 and regulates SOD1 activity". J. Biol. Chem. 276 (12): 9303–7. doi:10.1074/jbc.M010023200. PMID 11115513.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Silahtaroglu AN, Brondum-Nielsen K, Gredal O; et al. (2002). "Human CCS gene: genomic organization and exclusion as a candidate for amyotrophic lateral sclerosis (ALS)". BMC Genet. 3: 5. PMID 11991808.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Bertinato J, L'Abbé MR (2003). "Copper modulates the degradation of copper chaperone for Cu,Zn superoxide dismutase by the 26 S proteosome". J. Biol. Chem. 278 (37): 35071–8. doi:10.1074/jbc.M302242200. PMID 12832419.
• Silahtaroglu AN, Jensen LR, Harboe TL; et al. (2004). "Sequencing and mapping of the porcine CCS gene". Anim. Genet. 35 (4): 353–4. doi:10.1111/j.1365-2052.2004.01150.x. PMID 15265083.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Jin J, Smith FD, Stark C; et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Stasser JP, Eisses JF, Barry AN; et al. (2005). "Cysteine-to-serine mutants of the human copper chaperone for superoxide dismutase reveal a copper cluster at a domain III dimer interface". Biochemistry. 44 (9): 3143–52. doi:10.1021/bi0478392. PMID 15736924.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Duquesne AE, Ruijter M, Brouwer J; et al. (2005). "Solution structure of the second PDZ domain of the neuronal adaptor X11alpha and its interaction with the C-terminal peptide of the human copper chaperone for superoxide dismutase". J. Biomol. NMR. 32 (3): 209–18. doi:10.1007/s10858-005-7333-1. PMID 16132821.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Caruano-Yzermans AL, Bartnikas TB, Gitlin JD (2006). "Mechanisms of the copper-dependent turnover of the copper chaperone for superoxide dismutase". J. Biol. Chem. 281 (19): 13581–7. doi:10.1074/jbc.M601580200. PMID 16531609.CS1 maint: Multiple names: authors list (link)