Showing Protein Copper chaperone for superoxide dismutase (HMDBP08238)

• 13950

1. Superoxide dismutase copper chaperone

1. Cytoplasm

>825 bp
ATGGCTTCGGATTCGGGGAACCAGGGGACCCTCTGCACGTTGGAGTTCGCGGTGCAGATG
ACCTGTCAGAGCTGTGTGGACGCGGTGCGCAAATCCCTGCAAGGGGTGGCAGGTGTCCAG
GATGTGGAGGTGCACTTGGAGGACCAGATGGTCTTGGTACACACCACTCTACCCAGCCAG
GAGGTGCAGGCTCTCCTGGAAGGCACGGGGCGGCAGGCGGTACTCAAGGGCATGGGCAGC
GGCCAGTTGCAGAATCTGGGGGCAGCAGTGGCCATCCTGGGGGGGCCTGGCACCGTGCAG
GGGGTGGTGCGCTTCCTACAGCTGACCCCTGAGCGCTGCCTCATCGAGGGAACTATTGAC
GGCCTGGAGCCTGGGCTGCATGGACTCCACGTCCATCAGTACGGGGACCTTACAAACAAC
TGCAACAGCTGTGGGAATCACTTTAACCCTGATGGAGCATCTCATGGGGGCCCCCAGGAC
TCTGACCGGCACCGCGGAGACCTGGGCAATGTCCGTGCTGATGCTGACGGCCGCGCCATC
TTCAGAATGGAGGATGAGCAGCTGAAGGTGTGGGATGTGATTGGCCGCAGCCTGATTATT
GATGAGGGAGAAGATGACCTGGGCCGGGGAGGCCATCCCTTATCCAAGATCACAGGGAAC
TCCGGGGAGAGGTTGGCCTGTGGCATCATTGCACGCTCCGCTGGCCTTTTCCAGAACCCC
AAGCAGATCTGCTCTTGCGATGGCCTCACCATCTGGGAGGAGCGAGGCCGGCCCATCGCT
GGCAAGGGCCGAAAGGAGTCAGCGCAGCCCCCTGCCCACCTTTGA

• Sod_Cu (PF00080 )
• HMA (PF00403 )

• None

• None

>Copper chaperone for superoxide dismutase
MASDSGNQGTLCTLEFAVQMTCQSCVDAVRKSLQGVAGVQDVEVHLEDQMVLVHTTLPSQ
EVQALLEGTGRQAVLKGMGSGQLQNLGAAVAILGGPGTVQGVVRFLQLTPERCLIEGTID
GLEPGLHGLHVHQYGDLTNNCNSCGNHFNPDGASHGGPQDSDRHRGDLGNVRADADGRAI
FRMEDEQLKVWDVIGRSLIIDEGEDDLGRGGHPLSKITGNSGERLACGIIARSAGLFQNP
KQICSCDGLTIWEERGRPIAGKGRKESAQPPAHL

• 1DO5

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 ]