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.[6]
Referencesedit
^ abcGRCh38: Ensembl release 89: ENSG00000129103 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000025538 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Cosma MP, Pepe S, Annunziata I, Newbold RF, Grompe M, Parenti G, Ballabio A (May 2003). "The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases". Cell. 113 (4): 445–56. doi:10.1016/S0092-8674(03)00348-9. PMID 12757706. S2CID 15095377.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC139241. PMID 12477932.
Dierks T, Schmidt B, Borissenko LV, et al. (2003). "Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C(alpha)-formylglycine generating enzyme". Cell. 113 (4): 435–44. doi:10.1016/S0092-8674(03)00347-7. PMID 12757705. S2CID 11571659.
Hillier LW, Fulton RS, Fulton LA, et al. (2003). "The DNA sequence of human chromosome 7". Nature. 424 (6945): 157–64. Bibcode:2003Natur.424..157H. doi:10.1038/nature01782. PMID 12853948.
Clark HF, Gurney AL, Abaya E, et al. (2003). "The Secreted Protein Discovery Initiative (SPDI), a Large-Scale Effort to Identify Novel Human Secreted and Transmembrane Proteins: A Bioinformatics Assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC403697. PMID 12975309.
Landgrebe J, Dierks T, Schmidt B, von Figura K (2004). "The human SUMF1 gene, required for posttranslational sulfatase modification, defines a new gene family which is conserved from pro- to eukaryotes". Gene. 316: 47–56. doi:10.1016/S0378-1119(03)00746-7. PMID 14563551.
Colland F, Jacq X, Trouplin V, et al. (2004). "Functional Proteomics Mapping of a Human Signaling Pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC442148. PMID 15231748.
Suzuki Y, Yamashita R, Shirota M, et al. (2004). "Sequence Comparison of Human and Mouse Genes Reveals a Homologous Block Structure in the Promoter Regions". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC515316. PMID 15342556.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC528928. PMID 15489334.
Dickmanns A, Schmidt B, Rudolph MG, et al. (2005). "Crystal structure of human pFGE, the paralog of the Calpha-formylglycine-generating enzyme". J. Biol. Chem. 280 (15): 15180–7. doi:10.1074/jbc.M414317200. PMID 15687489.
Mariappan M, Preusser-Kunze A, Balleininger M, et al. (2005). "Expression, localization, structural, and functional characterization of pFGE, the paralog of the Calpha-formylglycine-generating enzyme". J. Biol. Chem. 280 (15): 15173–9. doi:10.1074/jbc.M413698200. PMID 15708861.
Zito E, Fraldi A, Pepe S, et al. (2005). "Sulphatase activities are regulated by the interaction of sulphatase-modifying factor 1 with SUMF2". EMBO Rep. 6 (7): 655–60. doi:10.1038/sj.embor.7400454. PMC1369113. PMID 15962010.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Otsuki T, Ota T, Nishikawa T, et al. (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries". DNA Res. 12 (2): 117–26. doi:10.1093/dnares/12.2.117. PMID 16303743.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC1356129. PMID 16344560.
This article on a gene on human chromosome 7 is a stub. You can help Wikipedia by expanding it.
sumf2, sulfatase, modifying, factor, enzyme, that, humans, encoded, gene, available, structurespdbortholog, search, pdbe, rcsblist, codes1y4jidentifiersaliases, pfge, sulfatase, modifying, factor, 2external, idsomim, 607940, 1915152, homologene, 41037, genecar. Sulfatase modifying factor 2 is an enzyme that in humans is encoded by the SUMF2 gene 5 6 SUMF2Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes1Y4JIdentifiersAliasesSUMF2 pFGE sulfatase modifying factor 2External IDsOMIM 607940 MGI 1915152 HomoloGene 41037 GeneCards SUMF2Gene location Human Chr Chromosome 7 human 1 Band7p11 2Start56 064 002 bp 1 End56 080 670 bp 1 Gene location Mouse Chr Chromosome 5 mouse 2 Band5 5 G1 3Start129 846 986 bp 2 End129 864 050 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inright uterine tubestromal cell of endometriumbody of pancreasgallbladdercanal of the cervixislet of Langerhanspancreatic ductal cellgastric mucosarectumright lobe of thyroid glandTop expressed inhandyolk sacexternal carotid arteryinternal carotid arteryrenal corpusclecumulus cellproximal tubuleneural tubemedullary collecting ductcondyleMore reference expression dataBioGPSn aGene ontologyMolecular functionmetal ion bindingCellular componentendoplasmic reticulum lumen endoplasmic reticulumBiological processpost translational protein modification glycosphingolipid metabolic processSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez2587067902EnsemblENSG00000129103ENSMUSG00000025538UniProtQ8NBJ7Q8BPG6RefSeq mRNA NM 001042468NM 001042469NM 001042470NM 001130069NM 001130070NM 001146333NM 015411NM 001366647NM 001366648NM 001366649NM 026445RefSeq protein NP 001035934NP 001035935NP 001123541NP 001139805NP 056226NP 001035933NP 001353576NP 001353577NP 001353578NP 080721Location UCSC Chr 7 56 06 56 08 MbChr 5 129 85 129 86 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse 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 6 References edit a b c GRCh38 Ensembl release 89 ENSG00000129103 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000025538 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Cosma MP Pepe S Annunziata I Newbold RF Grompe M Parenti G Ballabio A May 2003 The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases Cell 113 4 445 56 doi 10 1016 S0092 8674 03 00348 9 PMID 12757706 S2CID 15095377 a b Entrez Gene SUMF2 sulfatase modifying factor 2 Further reading editBonaldo MF Lennon G Soares MB 1997 Normalization and subtraction two approaches to facilitate gene discovery Genome Res 6 9 791 806 doi 10 1101 gr 6 9 791 PMID 8889548 Strausberg RL Feingold EA Grouse LH et al 2003 Generation and initial analysis of more than 15 000 full length human and mouse cDNA sequences Proc Natl Acad Sci U S A 99 26 16899 903 Bibcode 2002PNAS 9916899M doi 10 1073 pnas 242603899 PMC 139241 PMID 12477932 Dierks T Schmidt B Borissenko LV et al 2003 Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C alpha formylglycine generating enzyme Cell 113 4 435 44 doi 10 1016 S0092 8674 03 00347 7 PMID 12757705 S2CID 11571659 Hillier LW Fulton RS Fulton LA et al 2003 The DNA sequence of human chromosome 7 Nature 424 6945 157 64 Bibcode 2003Natur 424 157H doi 10 1038 nature01782 PMID 12853948 Clark HF Gurney AL Abaya E et al 2003 The Secreted Protein Discovery Initiative SPDI a Large Scale Effort to Identify Novel Human Secreted and Transmembrane Proteins A Bioinformatics Assessment Genome Res 13 10 2265 70 doi 10 1101 gr 1293003 PMC 403697 PMID 12975309 Landgrebe J Dierks T Schmidt B von Figura K 2004 The human SUMF1 gene required for posttranslational sulfatase modification defines a new gene family which is conserved from pro to eukaryotes Gene 316 47 56 doi 10 1016 S0378 1119 03 00746 7 PMID 14563551 Colland F Jacq X Trouplin V et al 2004 Functional Proteomics Mapping of a Human Signaling Pathway Genome Res 14 7 1324 32 doi 10 1101 gr 2334104 PMC 442148 PMID 15231748 Suzuki Y Yamashita R Shirota M et al 2004 Sequence Comparison of Human and Mouse Genes Reveals a Homologous Block Structure in the Promoter Regions Genome Res 14 9 1711 8 doi 10 1101 gr 2435604 PMC 515316 PMID 15342556 Gerhard DS Wagner L Feingold EA et al 2004 The Status Quality and Expansion of the NIH Full Length cDNA Project The Mammalian Gene Collection MGC Genome Res 14 10B 2121 7 doi 10 1101 gr 2596504 PMC 528928 PMID 15489334 Dickmanns A Schmidt B Rudolph MG et al 2005 Crystal structure of human pFGE the paralog of the Calpha formylglycine generating enzyme J Biol Chem 280 15 15180 7 doi 10 1074 jbc M414317200 PMID 15687489 Mariappan M Preusser Kunze A Balleininger M et al 2005 Expression localization structural and functional characterization of pFGE the paralog of the Calpha formylglycine generating enzyme J Biol Chem 280 15 15173 9 doi 10 1074 jbc M413698200 PMID 15708861 Zito E Fraldi A Pepe S et al 2005 Sulphatase activities are regulated by the interaction of sulphatase modifying factor 1 with SUMF2 EMBO Rep 6 7 655 60 doi 10 1038 sj embor 7400454 PMC 1369113 PMID 15962010 Rual JF Venkatesan K Hao T et al 2005 Towards a proteome scale map of the human protein protein interaction network Nature 437 7062 1173 8 Bibcode 2005Natur 437 1173R doi 10 1038 nature04209 PMID 16189514 S2CID 4427026 Otsuki T Ota T Nishikawa T et al 2007 Signal sequence and keyword trap in silico for selection of full length human cDNAs encoding secretion or membrane proteins from oligo capped cDNA libraries DNA Res 12 2 117 26 doi 10 1093 dnares 12 2 117 PMID 16303743 Kimura K Wakamatsu A Suzuki Y et al 2006 Diversification of transcriptional modulation Large scale identification and characterization of putative alternative promoters of human genes Genome Res 16 1 55 65 doi 10 1101 gr 4039406 PMC 1356129 PMID 16344560 nbsp This article on a gene on human chromosome 7 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title SUMF2 amp oldid 1142712986, wikipedia, wiki, book, books, library,
