SUMF1

Sulfatase-modifying factor 1 is an enzyme that in humans is encoded by the SUMF1 gene.^[5][6][7]

SUMF1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1Y1E, 1Y1F, 1Y1G, 1Y1H, 1Y1I, 1Y1J, 1Z70, 2AFT, 2AFY, 2AII, 2AIJ, 2AIK, 2HI8, 2HIB
Identifiers
Aliases	SUMF1, AAPA3037, FGE, UNQ3037, sulfatase modifying factor 1
External IDs	OMIM: 607939; MGI: 1889844; HomoloGene: 16268; GeneCards: SUMF1; OMA:SUMF1 - orthologs
Gene location (Human) Chr. Chromosome 3 (human)[1] Band 3p26.1 Start 3,700,814 bp[1] End 4,467,273 bp[1]
Gene location (Mouse) Chr. Chromosome 6 (mouse)[2] Band 6|6 E1 Start 108,083,989 bp[2] End 108,162,543 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in renal medulla skin of arm synovial membrane synovial joint tibia human penis skin of thigh nipple stromal cell of endometrium pylorus Top expressed in ascending aorta aortic valve stroma of bone marrow epithelium of lens Epithelium of choroid plexus conjunctival fornix iris supraoptic nucleus cumulus cell tunica media of zone of aorta More reference expression data BioGPS n/a
Gene ontology Molecular function protein homodimerization activity metal ion binding oxidoreductase activity Formylglycine-generating oxidase activity cupric ion binding Cellular component endoplasmic reticulum lumen endoplasmic reticulum Biological process post-translational protein modification glycosphingolipid metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 285362 58911 Ensembl ENSG00000144455 ENSMUSG00000030101 UniProt Q8NBK3 Q8R0F3 RefSeq (mRNA) NM_001164674 NM_001164675 NM_182760 NM_145937 RefSeq (protein) NP_001158146 NP_001158147 NP_877437 NP_666049 Location (UCSC) Chr 3: 3.7 – 4.47 Mb Chr 6: 108.08 – 108.16 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Sulfatases catalyze the hydrolysis of sulfate esters such as glycosaminoglycans, sulfolipids, and steroid sulfates. C-alpha-formylglycine (FGly), the catalytic residue in the active site of eukaryotic sulfatases, is posttranslationally generated from a cysteine by SUMF1, the human form of the aerobic Formylglycine-generating enzyme (FGE), in the endoplasmic reticulum (ER). The genetic defect of FGly formation caused by mutations in the SUMF1 gene results in inactive FGE, and subsequently multiple sulfatase deficiency (MSD; MIM 272200), a lysosomal storage disorder (Roeser et al., 2006).[supplied by OMIM]^[7]