CCS (gene)

Copper chaperone for superoxide dismutase

PDB rendering based on 1do5.

Available structures
PDB	1DO5, 2CRL

Identifiers

Symbols

CCS; MGC138260

External IDs

OMIM: 603864 MGI: 1333783 HomoloGene: 3762 GeneCards: CCS Gene

Gene Ontology
Molecular function	• superoxide dismutase activity • copper ion transmembrane transporter activity • copper ion binding • protein binding • zinc ion binding • superoxide dismutase copper chaperone activity • metal ion binding
Cellular component	• intracellular • intracellular • soluble fraction • nucleus • cytoplasm
Biological process	• superoxide metabolic process • intracellular copper ion transport • removal of superoxide radicals • metal ion transport • copper ion transmembrane transport • oxidation-reduction process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 11:
66.36 – 66.37 Mb

Chr 19:
4.83 – 4.84 Mb

PubMed search

[1]

[2]

Copper chaperone for superoxide dismutase is a metalloprotein that in humans is encoded by the CCS gene.^[1]^[2]

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.^[2]

Interactions

CCS (gene) has been shown to interact with SOD1^[3] and APBA1.^[4]

References

^ Culotta VC, Klomp LW, Strain J, Casareno RL, Krems B, Gitlin JD (Oct 1997). "The copper chaperone for superoxide dismutase". J Biol Chem 272 (38): 23469–72. doi:10.1074/jbc.272.38.23469. PMID 9295278.
^ ^a ^b "Entrez Gene: CCS copper chaperone for superoxide dismutase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9973.
^ Casareno, R L; Waggoner D, Gitlin J D (Sep. 1998). "The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase". J. Biol. Chem. (UNITED STATES) 273 (37): 23625–8. doi:10.1074/jbc.273.37.23625. ISSN 0021-9258. PMID 9726962.
^ McLoughlin, D M; Standen C L, Lau K F, Ackerley S, Bartnikas T P, Gitlin J D, Miller C C (Mar. 2001). "The neuronal adaptor protein X11alpha interacts with the copper chaperone for SOD1 and regulates SOD1 activity". J. Biol. Chem. (United States) 276 (12): 9303–7. doi:10.1074/jbc.M010023200. ISSN 0021-9258. PMID 11115513.

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. doi:10.1074/jbc.273.37.23625. PMID 9726962.
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. doi:10.1046/j.1471-4159.1999.0720422.x. PMID 9886096.
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. doi:10.1126/science.284.5415.805. PMID 10221913.
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. doi:10.1021/bi992822i. PMID 10677207.
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. doi:10.1159/000015480. PMID 10773661.
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. doi:10.1007/s003350010078. PMID 10790544.
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.
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.
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. doi:10.1186/1471-2156-3-5. PMC 107843. PMID 11991808. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=107843.
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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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.
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.
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. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
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.
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.
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.

PDB gallery

1do5: HUMAN COPPER CHAPERONE FOR SUPEROXIDE DISMUTASE DOMAIN II

2crl: The apo form of HMA domain of copper chaperone for superoxide dismutase

CCS (gene)

Interactions

References

Further reading