Copper chaperone for superoxide dismutase

NameCopper chaperone for superoxide dismutase
Synonyms
  • Superoxide dismutase copper chaperone
Gene NameCCS
OrganismHuman
Amino acid sequence
>lcl|BSEQ0013944|Copper chaperone for superoxide dismutase
MASDSGNQGTLCTLEFAVQMTCQSCVDAVRKSLQGVAGVQDVEVHLEDQMVLVHTTLPSQ
EVQALLEGTGRQAVLKGMGSGQLQNLGAAVAILGGPGTVQGVVRFLQLTPERCLIEGTID
GLEPGLHGLHVHQYGDLTNNCNSCGNHFNPDGASHGGPQDSDRHRGDLGNVRADADGRAI
FRMEDEQLKVWDVIGRSLIIDEGEDDLGRGGHPLSKITGNSGERLACGIIARSAGLFQNP
KQICSCDGLTIWEERGRPIAGKGRKESAQPPAHL
Number of residues274
Molecular Weight29040.445
Theoretical pINot Available
GO Classification
Functions
  • copper ion binding
  • protein disulfide oxidoreductase activity
  • superoxide dismutase activity
  • superoxide dismutase copper chaperone activity
  • zinc ion binding
Processes
  • removal of superoxide radicals
  • positive regulation of oxidoreductase activity
  • response to reactive oxygen species
  • intracellular copper ion transport
  • superoxide metabolic process
Components
  • cytoplasm
  • nucleus
  • cytosol
General FunctionZinc ion binding
Specific FunctionDelivers copper to copper zinc superoxide dismutase (SOD1).
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein IDNot Available
UniProtKB IDO14618
UniProtKB Entry NameCCS_HUMAN
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0013945|Copper chaperone for superoxide dismutase (CCS)
ATGGCTTCGGATTCGGGGAACCAGGGGACCCTCTGCACGTTGGAGTTCGCGGTGCAGATG
ACCTGTCAGAGCTGTGTGGACGCGGTGCGCAAATCCCTGCAAGGGGTGGCAGGTGTCCAG
GATGTGGAGGTGCACTTGGAGGACCAGATGGTCTTGGTACACACCACTCTACCCAGCCAG
GAGGTGCAGGCTCTCCTGGAAGGCACGGGGCGGCAGGCGGTACTCAAGGGCATGGGCAGC
GGCCAGTTGCAGAATCTGGGGGCAGCAGTGGCCATCCTGGGGGGGCCTGGCACCGTGCAG
GGGGTGGTGCGCTTCCTACAGCTGACCCCTGAGCGCTGCCTCATCGAGGGAACTATTGAC
GGCCTGGAGCCTGGGCTGCATGGACTCCACGTCCATCAGTACGGGGACCTTACAAACAAC
TGCAACAGCTGTGGGAATCACTTTAACCCTGATGGAGCATCTCATGGGGGCCCCCAGGAC
TCTGACCGGCACCGCGGAGACCTGGGCAATGTCCGTGCTGATGCTGACGGCCGCGCCATC
TTCAGAATGGAGGATGAGCAGCTGAAGGTGTGGGATGTGATTGGCCGCAGCCTGATTATT
GATGAGGGAGAAGATGACCTGGGCCGGGGAGGCCATCCCTTATCCAAGATCACAGGGAAC
TCCGGGGAGAGGTTGGCCTGTGGCATCATTGCACGCTCCGCTGGCCTTTTCCAGAACCCC
AAGCAGATCTGCTCTTGCGATGGCCTCACCATCTGGGAGGAGCGAGGCCGGCCCATCGCT
GGCAAGGGCCGAAAGGAGTCAGCGCAGCCCCCTGCCCACCTTTGA
GenBank Gene IDNot Available
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDHGNC:1613
Chromosome Location11
LocusNot Available
References
  1. Culotta VC, Klomp LW, Strain J, Casareno RL, Krems B, Gitlin JD: The copper chaperone for superoxide dismutase. J Biol Chem. 1997 Sep 19;272(38):23469-72. 9295278
  2. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. 21269460
  3. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. 24275569
  4. Banci L, Cantini F, Kozyreva T, Rubino JT: Mechanistic aspects of hSOD1 maturation from the solution structure of Cu(I) -loaded hCCS domain 1 and analysis of disulfide-free hSOD1 mutants. Chembiochem. 2013 Sep 23;14(14):1839-44. doi: 10.1002/cbic.201300042. Epub 2013 Apr 26. 23625804
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  6. Casareno RL, Waggoner D, Gitlin JD: The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase. J Biol Chem. 1998 Sep 11;273(37):23625-8. 9726962
  7. Stasser JP, Eisses JF, Barry AN, Kaplan JH, Blackburn NJ: Cysteine-to-serine mutants of the human copper chaperone for superoxide dismutase reveal a copper cluster at a domain III dimer interface. Biochemistry. 2005 Mar 8;44(9):3143-52. 15736924
  8. Vonk WI, Wijmenga C, Berger R, van de Sluis B, Klomp LW: Cu,Zn superoxide dismutase maturation and activity are regulated by COMMD1. J Biol Chem. 2010 Sep 10;285(37):28991-9000. doi: 10.1074/jbc.M110.101477. Epub 2010 Jul 1. 20595380
  9. Brady GF, Galban S, Liu X, Basrur V, Gitlin JD, Elenitoba-Johnson KS, Wilson TE, Duckett CS: Regulation of the copper chaperone CCS by XIAP-mediated ubiquitination. Mol Cell Biol. 2010 Apr;30(8):1923-36. doi: 10.1128/MCB.00900-09. Epub 2010 Feb 12. 20154138
  10. Huppke P, Brendel C, Korenke GC, Marquardt I, Donsante A, Yi L, Hicks JD, Steinbach PJ, Wilson C, Elpeleg O, Moller LB, Christodoulou J, Kaler SG, Gartner J: Molecular and biochemical characterization of a unique mutation in CCS, the human copper chaperone to superoxide dismutase. Hum Mutat. 2012 Aug;33(8):1207-15. doi: 10.1002/humu.22099. Epub 2012 May 16. 22508683
  11. Lamb AL, Wernimont AK, Pufahl RA, O'Halloran TV, Rosenzweig AC: Crystal structure of the second domain of the human copper chaperone for superoxide dismutase. Biochemistry. 2000 Feb 22;39(7):1589-95. 10677207