CCC2/YDR270W Literature Guide Help

Other names published for CCC2: Cu(2+)-transporting P-type ATPase CCC2, YDR270W

CCC2 - Protein Sequence Features (12)

ReferenceOther Genes Addressed
Kovalchuk A and Driessen AJ  (2010) Phylogenetic analysis of fungal ABC transporters. BMC Genomics 11():177
Valverde RH, et al.  (2008) Cyclic AMP-dependent protein kinase controls energy interconversion during the catalytic cycle of the yeast copper-ATPase. FEBS Lett 582(6):891-5
Banci L, et al.  (2007) Interaction of the two soluble metal-binding domains of yeast Ccc2 with copper(I)-Atx1. Biochem Biophys Res Commun 364(3):645-9
Bertini I, et al.  (2006) Mapping protein-protein interaction by (13)C'-detected heteronuclear NMR spectroscopy. J Biomol NMR 36(2):111-22
Morin I, et al.  (2005) Cd2+- or Hg2+-binding proteins can replace the Cu+-chaperone Atx1 in delivering Cu+ to the secretory pathway in yeast. FEBS Lett 579(5):1117-23
Lowe J, et al.  (2004) A mutational study in the transmembrane domain of Ccc2p, the yeast Cu(I)-ATPase, shows different roles for each Cys-Pro-Cys cysteine. J Biol Chem 279(25):25986-94
van Dongen EM, et al.  (2004) Copper-dependent protein-protein interactions studied by yeast two-hybrid analysis. Biochem Biophys Res Commun 323(3):789-95
Arnesano F, et al.  (2002) Metallochaperones and metal-transporting ATPases: a comparative analysis of sequences and structures. Genome Res 12(2):255-71
Banci L, et al.  (2002) A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118). J Mol Biol 323(5):883-97
Nakanishi Y, et al.  (2001) Mutagenic analysis of functional residues in putative substrate-binding site and acidic domains of vacuolar H+-pyrophosphatase. J Biol Chem 276(10):7654-60
Catty P, et al.  (1997) The complete inventory of the yeast Saccharomyces cerevisiae P-type transport ATPases. FEBS Lett 409(3):325-32
Fu D, et al.  (1995) Sequence, mapping and disruption of CCC2, a gene that cross-complements the Ca(2+)-sensitive phenotype of csg1 mutants and encodes a P-type ATPase belonging to the Cu(2+)-ATPase subfamily. Yeast 11(3):283-92