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Identification
HMDB Protein ID HMDBP08238
Secondary Accession Numbers
  • 13950
Name Copper chaperone for superoxide dismutase
Synonyms
  1. Superoxide dismutase copper chaperone
Gene Name CCS
Protein Type Unknown
Biological Properties
General Function Involved in metal ion binding
Specific Function Delivers copper to copper zinc superoxide dismutase (SOD1)
Pathways Not Available
Reactions Not Available
GO Classification
Function
ion binding
cation binding
metal ion binding
binding
Process
metabolic process
establishment of localization
transport
cellular metabolic process
oxidation reduction
oxygen and reactive oxygen species metabolic process
superoxide metabolic process
ion transport
cation transport
metal ion transport
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location Chromosome:1
Locus 11q13
SNPs CCS
Gene Sequence
>825 bp
ATGGCTTCGGATTCGGGGAACCAGGGGACCCTCTGCACGTTGGAGTTCGCGGTGCAGATG
ACCTGTCAGAGCTGTGTGGACGCGGTGCGCAAATCCCTGCAAGGGGTGGCAGGTGTCCAG
GATGTGGAGGTGCACTTGGAGGACCAGATGGTCTTGGTACACACCACTCTACCCAGCCAG
GAGGTGCAGGCTCTCCTGGAAGGCACGGGGCGGCAGGCGGTACTCAAGGGCATGGGCAGC
GGCCAGTTGCAGAATCTGGGGGCAGCAGTGGCCATCCTGGGGGGGCCTGGCACCGTGCAG
GGGGTGGTGCGCTTCCTACAGCTGACCCCTGAGCGCTGCCTCATCGAGGGAACTATTGAC
GGCCTGGAGCCTGGGCTGCATGGACTCCACGTCCATCAGTACGGGGACCTTACAAACAAC
TGCAACAGCTGTGGGAATCACTTTAACCCTGATGGAGCATCTCATGGGGGCCCCCAGGAC
TCTGACCGGCACCGCGGAGACCTGGGCAATGTCCGTGCTGATGCTGACGGCCGCGCCATC
TTCAGAATGGAGGATGAGCAGCTGAAGGTGTGGGATGTGATTGGCCGCAGCCTGATTATT
GATGAGGGAGAAGATGACCTGGGCCGGGGAGGCCATCCCTTATCCAAGATCACAGGGAAC
TCCGGGGAGAGGTTGGCCTGTGGCATCATTGCACGCTCCGCTGGCCTTTTCCAGAACCCC
AAGCAGATCTGCTCTTGCGATGGCCTCACCATCTGGGAGGAGCGAGGCCGGCCCATCGCT
GGCAAGGGCCGAAAGGAGTCAGCGCAGCCCCCTGCCCACCTTTGA
Protein Properties
Number of Residues 274
Molecular Weight 29040.4
Theoretical pI 5.31
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Copper chaperone for superoxide dismutase
MASDSGNQGTLCTLEFAVQMTCQSCVDAVRKSLQGVAGVQDVEVHLEDQMVLVHTTLPSQ
EVQALLEGTGRQAVLKGMGSGQLQNLGAAVAILGGPGTVQGVVRFLQLTPERCLIEGTID
GLEPGLHGLHVHQYGDLTNNCNSCGNHFNPDGASHGGPQDSDRHRGDLGNVRADADGRAI
FRMEDEQLKVWDVIGRSLIIDEGEDDLGRGGHPLSKITGNSGERLACGIIARSAGLFQNP
KQICSCDGLTIWEERGRPIAGKGRKESAQPPAHL
GenBank ID Protein 2431868
UniProtKB/Swiss-Prot ID O14618
UniProtKB/Swiss-Prot Entry Name CCS_HUMAN
PDB IDs
GenBank Gene ID AF002210
GeneCard ID CCS
GenAtlas ID CCS
HGNC ID HGNC:1613
References
General References
  1. 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. [PubMed:15489334 ]
  2. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed:17287340 ]
  3. 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. [PubMed:9295278 ]
  4. 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. [PubMed:9726962 ]
  5. 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. [PubMed:15736924 ]
  6. 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. [PubMed:10677207 ]