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Sulfatase modifying factor 2

pFGE, SUMF2, sulfatase modifying factor 2
The catalytic sites of sulfatases are only active if they contain a unique amino acid, C-alpha-formylglycine (FGly). The FGly residue is posttranslationally generated from a cysteine by enzymes with FGly-generating activity. The gene described in this record is a member of the sulfatase-modifying factor family and encodes a protein with a DUF323 domain that localizes to the lumen of the endoplasmic reticulum. This protein has low levels of FGly-generating activity but can heterodimerize with another family member - a protein with high levels of FGly-generating activity. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: sulfatase, IL-13, cct6, phosphoserine phosphatase, GBAS
Papers on pFGE
Integrative genomics identifies 7p11.2 as a novel locus for fever and clinical stress response in humans.
Reilly et al., Philadelphia, United States. In Hum Mol Genet, Apr 2015
The top GWAS SNPs are not located within protein-coding genes, but have significant cis-expression quantitative trait loci (eQTL) associations with expression of a cluster of genes ∼400 kb upstream, several of which (SUMF2, CCT6A, GBAS) are regulated by LPS in vivo in blood cells.
De novo 393 kb microdeletion of 7p11.2 characterized by aCGH in a boy with psychomotor retardation and dysmorphic features.
Manolakos et al., Athens, Greece. In Meta Gene, 2014
Additionally, we studied the expression of two other genes deleted in the patient, CCT6A and SUMF2, for which there is scarce data in the literature.
Downregulation of SUMF2 gene in ovalbumin-induced rat model of allergic inflammation.
Jiang et al., Harbin, China. In Int J Clin Exp Pathol, 2014
Sulfate-modifying factor 2 (SUMF2), a member of the formylglycine-generating enzyme family, was earlier found to play a role in the regulation of interleukin (IL)-13 expression and secretion in airway smooth muscle cells.
Sos recruitment system for the analysis of the interaction between sulfatase-modifying factor 2 subtypes and interleukin-13.
Jiang et al., Harbin, China. In Genet Mol Res, 2012
Our previous results have indicated that sulfatase-modifying factor 2 (SUMF2) interacts with IL-13 and inhibits its secretion.
Variants in ZNF365 isoform D are associated with Crohn's disease.
Taylor et al., Los Angeles, United States. In Gut, 2011
A whole-genome microarray expression study further suggested that the Ala62Thr change in ZNF365 isoform D is related to differential expression of the genes ARL4A, MKKS, RRAGD, SUMF2, TDR1 and ZNF148 in CD.
Genetic loci for blood lipid levels identified by linkage and association analyses in Caribbean Hispanics.
Sacco et al., Miami, United States. In J Lipid Res, 2011
In the association analysis of the linkage peaks, we found that seven SNPs near FLJ45974 were associated with LDL-C/HDL-C with a nominal P < 3.5 × 10(-5), in addition to associations (P < 0.0001) for other lipid traits with SNPs in or near CDH13, SUMF2, TLE3, FAH, ARNT2, TSHZ3, ZNF343, RPL7AL2, and TMC3.
SUMF2 interacts with interleukin-13 and inhibits interleukin-13 secretion in bronchial smooth muscle cells.
Liu et al., Harbin, China. In J Cell Biochem, 2010
SUMF2 interacted with IL-13 and inhibited IL-13 secretion in bronchial smooth muscle cells and lymphocytes, which was independent of IL-13 glycosylation
The non-catalytic N-terminal extension of formylglycine-generating enzyme is required for its biological activity and retention in the endoplasmic reticulum.
von Figura et al., Göttingen, Germany. In J Biol Chem, 2008
Moreover, when fused to the paralog of FGE (pFGE), which itself lacks FGly-generating activity, the FGE extension (residues 34-88) of this hybrid construct led to partial restoration of the biological activity of co-expressed N-terminally truncated FGE.
Paralog of the formylglycine-generating enzyme--retention in the endoplasmic reticulum by canonical and noncanonical signals.
Dierks et al., Göttingen, Germany. In Febs J, 2008
pFGE is retained in the ER through its C-terminal tetrapeptide PGEL, a noncanonical variant of the classic KDEL ER-retention signal.
De novo calcium/sulfur SAD phasing of the human formylglycine-generating enzyme using in-house data.
Rudolph et al., Göttingen, Germany. In Acta Crystallogr D Biol Crystallogr, 2005
The minimal data requirements for successful phasing and the relative contributions of the Ca and S atoms are discussed and compared with the related FGE paralogue, pFGE.
Sulphatase activities are regulated by the interaction of sulphatase-modifying factor 1 with SUMF2.
Cosma et al., Napoli, Italy. In Embo Rep, 2005
SUMF2 interacts with sulphatase-modifying factor 1 to regulate sulphatase activities.
Crystal structure of human pFGE, the paralog of the Calpha-formylglycine-generating enzyme.
Ficner et al., Göttingen, Germany. In J Biol Chem, 2005
structural analysis of human pFGE by X-ray crystallography [pFGE]
Expression, localization, structural, and functional characterization of pFGE, the paralog of the Calpha-formylglycine-generating enzyme.
von Figura et al., Göttingen, Germany. In J Biol Chem, 2005
pFGE (SUMF2) is the paralog of the Calpha-formylglycine-generating enzyme
The human SUMF1 gene, required for posttranslational sulfatase modification, defines a new gene family which is conserved from pro- to eukaryotes.
von Figura et al., Göttingen, Germany. In Gene, 2003
The genomes of vertebrates including mouse, man and pufferfish contain a sulfatase modifying factor 2 (SUMF2) gene encoding an FGE paralog of unknown function.
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