Copper chaperone for superoxide dismutase
Details
- Name
- Copper chaperone for superoxide dismutase
- Synonyms
- Superoxide dismutase copper chaperone
- Gene Name
- CCS
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0013944|Copper chaperone for superoxide dismutase MASDSGNQGTLCTLEFAVQMTCQSCVDAVRKSLQGVAGVQDVEVHLEDQMVLVHTTLPSQ EVQALLEGTGRQAVLKGMGSGQLQNLGAAVAILGGPGTVQGVVRFLQLTPERCLIEGTID GLEPGLHGLHVHQYGDLTNNCNSCGNHFNPDGASHGGPQDSDRHRGDLGNVRADADGRAI FRMEDEQLKVWDVIGRSLIIDEGEDDLGRGGHPLSKITGNSGERLACGIIARSAGLFQNP KQICSCDGLTIWEERGRPIAGKGRKESAQPPAHL
- Number of residues
- 274
- Molecular Weight
- 29040.445
- Theoretical pI
- Not Available
- GO Classification
- Functionscopper ion binding / protein disulfide oxidoreductase activity / superoxide dismutase activity / superoxide dismutase copper chaperone activity / zinc ion bindingProcessesintracellular copper ion transport / positive regulation of oxidoreductase activity / removal of superoxide radicals / response to reactive oxygen species / superoxide metabolic processComponentscytoplasm / cytosol / nucleus
- General Function
- Zinc ion binding
- Specific Function
- Delivers copper to copper zinc superoxide dismutase (SOD1).
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0013945|Copper chaperone for superoxide dismutase (CCS) ATGGCTTCGGATTCGGGGAACCAGGGGACCCTCTGCACGTTGGAGTTCGCGGTGCAGATG ACCTGTCAGAGCTGTGTGGACGCGGTGCGCAAATCCCTGCAAGGGGTGGCAGGTGTCCAG GATGTGGAGGTGCACTTGGAGGACCAGATGGTCTTGGTACACACCACTCTACCCAGCCAG GAGGTGCAGGCTCTCCTGGAAGGCACGGGGCGGCAGGCGGTACTCAAGGGCATGGGCAGC GGCCAGTTGCAGAATCTGGGGGCAGCAGTGGCCATCCTGGGGGGGCCTGGCACCGTGCAG GGGGTGGTGCGCTTCCTACAGCTGACCCCTGAGCGCTGCCTCATCGAGGGAACTATTGAC GGCCTGGAGCCTGGGCTGCATGGACTCCACGTCCATCAGTACGGGGACCTTACAAACAAC TGCAACAGCTGTGGGAATCACTTTAACCCTGATGGAGCATCTCATGGGGGCCCCCAGGAC TCTGACCGGCACCGCGGAGACCTGGGCAATGTCCGTGCTGATGCTGACGGCCGCGCCATC TTCAGAATGGAGGATGAGCAGCTGAAGGTGTGGGATGTGATTGGCCGCAGCCTGATTATT GATGAGGGAGAAGATGACCTGGGCCGGGGAGGCCATCCCTTATCCAAGATCACAGGGAAC TCCGGGGAGAGGTTGGCCTGTGGCATCATTGCACGCTCCGCTGGCCTTTTCCAGAACCCC AAGCAGATCTGCTCTTGCGATGGCCTCACCATCTGGGAGGAGCGAGGCCGGCCCATCGCT GGCAAGGGCCGAAAGGAGTCAGCGCAGCCCCCTGCCCACCTTTGA
- Chromosome Location
- 11
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID O14618 UniProtKB Entry Name CCS_HUMAN HGNC ID HGNC:1613 - General References
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB09130 Copper approved, investigational no binder Details DB01593 Zinc approved, investigational unknown Details DB14487 Zinc acetate approved, investigational unknown Details DB14533 Zinc chloride approved, investigational unknown cofactor Details DB14548 Zinc sulfate, unspecified form approved, experimental unknown cofactor Details