PMR1/YGL167C Literature Guide Help

Other names published for PMR1: BSD1, LDB1, SSC1, Ca(2+)/Mn(2+)-transporting P-type ATPase PMR1, YGL167C

PMR1 - Protein Sequence Features (11)

ReferenceOther Genes Addressed
Krauke Y and Sychrova H  (2011) Cnh1 Na(+) /H(+) antiporter and Ena1 Na(+) -ATPase play different roles in cation homeostasis and cell physiology of Candida glabrata. FEMS Yeast Res 11(1):29-41
Kovalchuk A and Driessen AJ  (2010) Phylogenetic analysis of fungal ABC transporters. BMC Genomics 11():177
Ma L, et al.  (2010) Proteins deleterious on overexpression are associated with high intrinsic disorder, specific interaction domains, and low abundance. J Proteome Res 9(3):1218-25
Li X, et al.  (2008) A Distinct Endosomal Ca2+/Mn2+ Pump Affects Root Growth through the Secretory Process. Plant Physiol 147(4):1675-89
Mandal D, et al.  (2003) Packing interactions between transmembrane helices alter ion selectivity of the yeast Golgi Ca2+/Mn2+-ATPase PMR1. J Biol Chem 278(37):35292-8
Funakoshi M, et al.  (2000) Isolation and characterisation of a mutation in the PMR1 gene encoding a Golgi membrane ATPase, which causes hypersensitivity to over-expression of Clb3 in Saccharomyces cerevisiae. Mol Gen Genet 264(1-2):29-36
Mandal D, et al.  (2000) Manganese selectivity of pmr1, the yeast secretory pathway ion pump, is defined by residue gln783 in transmembrane segment 6. Residue Asp778 is essential for cation transport. J Biol Chem 275(31):23933-8
Wei Y, et al.  (2000) Phenotypic screening of mutations in Pmr1, the yeast secretory pathway Ca2+/Mn2+-ATPase, reveals residues critical for ion selectivity and transport. J Biol Chem 275(31):23927-32
Wei Y, et al.  (1999) An N-terminal EF hand-like motif modulates ion transport by Pmr1, the yeast Golgi Ca(2+)/Mn(2+)-ATPase. Biochemistry 38(44):14534-41
Catty P, et al.  (1997) The complete inventory of the yeast Saccharomyces cerevisiae P-type transport ATPases. FEBS Lett 409(3):325-32
Rudolph HK, et al.  (1989) The yeast secretory pathway is perturbed by mutations in PMR1, a member of a Ca2+ ATPase family. Cell 58(1):133-45