UniProtKB - Q8NBK3 (SUMF1_HUMAN)
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- BLAST>sp|Q8NBK3|SUMF1_HUMAN Formylglycine-generating enzyme OS=Homo sapiens OX=9606 GN=SUMF1 PE=1 SV=3 MAAPALGLVCGRCPELGLVLLLLLLSLLCGAAGSQEAGTGAGAGSLAGSCGCGTPQRPGA HGSSAAAHRYSREANAPGPVPGERQLAHSKMVPIPAGVFTMGTDDPQIKQDGEAPARRVT IDAFYMDAYEVSNTEFEKFVNSTGYLTEAEKFGDSFVFEGMLSEQVKTNIQQAVAAAPWW LPVKGANWRHPEGPDSTILHRPDHPVLHVSWNDAVAYCTWAGKRLPTEAEWEYSCRGGLH NRLFPWGNKLQPKGQHYANIWQGEFPVTNTGEDGFQGTAPVDAFPPNGYGLYNIVGNAWE WTSDWWTVHHSVEETLNPKGPPSGKDRVKKGGSYMCHRSYCYRYRCAARSQNTPDSSASN LGFRCAADRLPTMD
- Align
Formylglycine-generating enzyme
SUMF1
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.2"The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases."
Cosma M.P., Pepe S., Annunziata I., Newbold R.F., Grompe M., Parenti G., Ballabio A.
Cell 113:445-456(2003) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS MSD PRO-155; TYR-218; ARG-336; CYS-345; PRO-348; GLN-349 AND TRP-349, FUNCTION. - Ref.11"Molecular characterization of the human Calpha-formylglycine-generating enzyme."
Preusser-Kunze A., Mariappan M., Schmidt B., Gande S.L., Mutenda K., Wenzel D., von Figura K., Dierks T.
J. Biol. Chem. 280:14900-14910(2005) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, CALCIUM-BINDING, GLYCOSYLATION AT ASN-141, SUBCELLULAR LOCATION, DISULFIDE BONDS. - Ref.12"Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme."
Dierks T., Dickmanns A., Preusser-Kunze A., Schmidt B., Mariappan M., von Figura K., Ficner R., Rudolph M.G.
Cell 121:541-552(2005) [PubMed] [Europe PMC] [Abstract]Cited for: PARTIAL PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 73-374 IN COMPLEX WITH CALCIUM, FUNCTION, GLYCOSYLATION AT ASN-141, MUTAGENESIS OF SER-333; CYS-336; HIS-337; TYR-340 AND CYS-341, DISULFIDE BONDS. - Ref.16"Reconstitution of formylglycine-generating enzyme with copper(II) for aldehyde tag conversion."
Holder P.G., Jones L.C., Drake P.M., Barfield R.M., Banas S., de Hart G.W., Baker J., Rabuka D.
J. Biol. Chem. 290:15730-15745(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, COFACTOR. - Ref.17"A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme."
Roeser D., Preusser-Kunze A., Schmidt B., Gasow K., Wittmann J.G., Dierks T., von Figura K., Rudolph M.G.
Proc. Natl. Acad. Sci. U.S.A. 103:81-86(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF MUTANTS SER-336 AND SER-341 IN COMPLEX WITH SULFATASE PEPTIDE, FUNCTION. - Ref.20"SUMF1 mutations affecting stability and activity of formylglycine generating enzyme predict clinical outcome in multiple sulfatase deficiency."
Schlotawa L., Ennemann E.C., Radhakrishnan K., Schmidt B., Chakrapani A., Christen H.J., Moser H., Steinmann B., Dierks T., Gaertner J.
Eur. J. Hum. Genet. 19:253-261(2011) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS MSD PRO-155; ARG-247; VAL-263; 327-ARG--ASP-374 DEL AND CYS-345, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS MSD PRO-155; VAL-263; 327-ARG--ASP-374 DEL AND CYS-345.
Miscellaneous
Caution
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.12"Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme."
Dierks T., Dickmanns A., Preusser-Kunze A., Schmidt B., Mariappan M., von Figura K., Ficner R., Rudolph M.G.
Cell 121:541-552(2005) [PubMed] [Europe PMC] [Abstract]Cited for: PARTIAL PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 73-374 IN COMPLEX WITH CALCIUM, FUNCTION, GLYCOSYLATION AT ASN-141, MUTAGENESIS OF SER-333; CYS-336; HIS-337; TYR-340 AND CYS-341, DISULFIDE BONDS. - Ref.16"Reconstitution of formylglycine-generating enzyme with copper(II) for aldehyde tag conversion."
Holder P.G., Jones L.C., Drake P.M., Barfield R.M., Banas S., de Hart G.W., Baker J., Rabuka D.
J. Biol. Chem. 290:15730-15745(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, COFACTOR.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"Molecular characterization of the human Calpha-formylglycine-generating enzyme."
Preusser-Kunze A., Mariappan M., Schmidt B., Gande S.L., Mutenda K., Wenzel D., von Figura K., Dierks T.
J. Biol. Chem. 280:14900-14910(2005) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, CALCIUM-BINDING, GLYCOSYLATION AT ASN-141, SUBCELLULAR LOCATION, DISULFIDE BONDS. - Ref.16"Reconstitution of formylglycine-generating enzyme with copper(II) for aldehyde tag conversion."
Holder P.G., Jones L.C., Drake P.M., Barfield R.M., Banas S., de Hart G.W., Baker J., Rabuka D.
J. Biol. Chem. 290:15730-15745(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, COFACTOR.
<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.16"Reconstitution of formylglycine-generating enzyme with copper(II) for aldehyde tag conversion."
Holder P.G., Jones L.C., Drake P.M., Barfield R.M., Banas S., de Hart G.W., Baker J., Rabuka D.
J. Biol. Chem. 290:15730-15745(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, COFACTOR.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.16"Reconstitution of formylglycine-generating enzyme with copper(II) for aldehyde tag conversion."
Holder P.G., Jones L.C., Drake P.M., Barfield R.M., Banas S., de Hart G.W., Baker J., Rabuka D.
J. Biol. Chem. 290:15730-15745(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, COFACTOR.
<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.16"Reconstitution of formylglycine-generating enzyme with copper(II) for aldehyde tag conversion."
Holder P.G., Jones L.C., Drake P.M., Barfield R.M., Banas S., de Hart G.W., Baker J., Rabuka D.
J. Biol. Chem. 290:15730-15745(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, COFACTOR.
- KM=0.34 µM for [sulfatase]-L-cysteine1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.16"Reconstitution of formylglycine-generating enzyme with copper(II) for aldehyde tag conversion."
Holder P.G., Jones L.C., Drake P.M., Barfield R.M., Banas S., de Hart G.W., Baker J., Rabuka D.
J. Biol. Chem. 290:15730-15745(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, COFACTOR.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: sulfatase oxidation
This protein is involved in the pathway sulfatase oxidation, which is part of Protein modification.4 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.2"The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases."
Cosma M.P., Pepe S., Annunziata I., Newbold R.F., Grompe M., Parenti G., Ballabio A.
Cell 113:445-456(2003) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS MSD PRO-155; TYR-218; ARG-336; CYS-345; PRO-348; GLN-349 AND TRP-349, FUNCTION. - Ref.11"Molecular characterization of the human Calpha-formylglycine-generating enzyme."
Preusser-Kunze A., Mariappan M., Schmidt B., Gande S.L., Mutenda K., Wenzel D., von Figura K., Dierks T.
J. Biol. Chem. 280:14900-14910(2005) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, CALCIUM-BINDING, GLYCOSYLATION AT ASN-141, SUBCELLULAR LOCATION, DISULFIDE BONDS. - Ref.12"Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme."
Dierks T., Dickmanns A., Preusser-Kunze A., Schmidt B., Mariappan M., von Figura K., Ficner R., Rudolph M.G.
Cell 121:541-552(2005) [PubMed] [Europe PMC] [Abstract]Cited for: PARTIAL PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 73-374 IN COMPLEX WITH CALCIUM, FUNCTION, GLYCOSYLATION AT ASN-141, MUTAGENESIS OF SER-333; CYS-336; HIS-337; TYR-340 AND CYS-341, DISULFIDE BONDS. - Ref.16"Reconstitution of formylglycine-generating enzyme with copper(II) for aldehyde tag conversion."
Holder P.G., Jones L.C., Drake P.M., Barfield R.M., Banas S., de Hart G.W., Baker J., Rabuka D.
J. Biol. Chem. 290:15730-15745(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, COFACTOR.
View all proteins of this organism that are known to be involved in the pathway sulfatase oxidation and in Protein modification.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 130 | Calcium 21 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 259 | Calcium 11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 260 | Calcium 1; via carbonyl oxygen1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 273 | Calcium 11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 275 | Calcium 1; via carbonyl oxygen1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 293 | Calcium 2; via carbonyl oxygen1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 296 | Calcium 2; via carbonyl oxygen1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 298 | Calcium 2; via carbonyl oxygen1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 300 | Calcium 21 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 336 | Copper(2+); catalytic1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 341 | Copper(2+); catalytic1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- cupric ion binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- Formylglycine-generating oxidase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- oxidoreductase activity Source: Reactome
- protein homodimerization activity Source: Ensembl
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- glycosphingolipid metabolic process Source: Reactome
- post-translational protein modification Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein oxidation Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Oxidoreductase |
| Ligand | Calcium, Copper, Metal-binding |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:ENSG00000144455-MONOMER |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1660662 Glycosphingolipid metabolism R-HSA-1663150 The activation of arylsulfatases |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00910 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Formylglycine-generating enzyme1 Publication<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Short name: FGE1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Alternative name(s): C-alpha-formylglycine-generating enzyme 11 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Sulfatase-modifying factor 11 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
|
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:SUMF11 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
<p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi ORF Names:PSEC01521 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
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| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
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Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000144455.13 |
Human Gene Nomenclature Database More...HGNCi | HGNC:20376 SUMF1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 607939 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q8NBK3 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum lumen 4 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"Sulphatase activities are regulated by the interaction of sulphatase-modifying factor 1 with SUMF2."
Zito E., Fraldi A., Pepe S., Annunziata I., Kobinger G., Di Natale P., Ballabio A., Cosma M.P.
EMBO Rep. 6:655-660(2005) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, INTERACTION WITH SUMF2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.11"Molecular characterization of the human Calpha-formylglycine-generating enzyme."
Preusser-Kunze A., Mariappan M., Schmidt B., Gande S.L., Mutenda K., Wenzel D., von Figura K., Dierks T.
J. Biol. Chem. 280:14900-14910(2005) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, CALCIUM-BINDING, GLYCOSYLATION AT ASN-141, SUBCELLULAR LOCATION, DISULFIDE BONDS. - Ref.13"Paralog of the formylglycine-generating enzyme--retention in the endoplasmic reticulum by canonical and noncanonical signals."
Gande S.L., Mariappan M., Schmidt B., Pringle T.H., von Figura K., Dierks T.
FEBS J. 275:1118-1130(2008) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.20"SUMF1 mutations affecting stability and activity of formylglycine generating enzyme predict clinical outcome in multiple sulfatase deficiency."
Schlotawa L., Ennemann E.C., Radhakrishnan K., Schmidt B., Chakrapani A., Christen H.J., Moser H., Steinmann B., Dierks T., Gaertner J.
Eur. J. Hum. Genet. 19:253-261(2011) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS MSD PRO-155; ARG-247; VAL-263; 327-ARG--ASP-374 DEL AND CYS-345, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS MSD PRO-155; VAL-263; 327-ARG--ASP-374 DEL AND CYS-345.
- Endoplasmic reticulum lumen 4 Publications
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- endoplasmic reticulum lumen Source: Reactome
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Endoplasmic reticulum<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Multiple sulfatase deficiency (MSD)5 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.1"Multiple sulfatase deficiency is caused by mutations in the gene encoding the Homo sapiens C-alpha-formyglycine-generating enzyme."
Dierks T., Schmidt B., Borissenko L.V., Peng J., Preusser A., Mariappan M., von Figura K.
Cell 113:435-444(2003) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS MSD VAL-279; ARG-336; GLN-349 AND TRP-349, VARIANT ASN-63. - Ref.2"The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases."
Cosma M.P., Pepe S., Annunziata I., Newbold R.F., Grompe M., Parenti G., Ballabio A.
Cell 113:445-456(2003) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS MSD PRO-155; TYR-218; ARG-336; CYS-345; PRO-348; GLN-349 AND TRP-349, FUNCTION. - Ref.18"Molecular and functional analysis of SUMF1 mutations in multiple sulfatase deficiency."
Cosma M.P., Pepe S., Parenti G., Settembre C., Annunziata I., Wade-Martins R., Domenico C.D., Natale P.D., Mankad A., Cox B., Uziel G., Mancini G.M., Zammarchi E., Donati M.A., Kleijer W.J., Filocamo M., Carrozzo R., Carella M., Ballabio A.
Hum. Mutat. 23:576-581(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS MSD PHE-20; PRO-177; TRP-224; ILE-259 AND LEU-266, CHARACTERIZATION OF VARIANTS MSD PHE-20; PRO-155; PRO-177; TYR-218; TRP-224; ILE-259; LEU-266; VAL-279; ARG-336; CYS-345; PRO-348; TRP-349 AND GLN-349. - Ref.19"Molecular analysis of SUMF1 mutations: stability and residual activity of mutant formylglycine-generating enzyme determine disease severity in multiple sulfatase deficiency."
Schlotawa L., Steinfeld R., von Figura K., Dierks T., Gaertner J.
Hum. Mutat. 29:205-205(2008) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS MSD PRO-177; SER-179; VAL-279 AND TRP-349. - Ref.20"SUMF1 mutations affecting stability and activity of formylglycine generating enzyme predict clinical outcome in multiple sulfatase deficiency."
Schlotawa L., Ennemann E.C., Radhakrishnan K., Schmidt B., Chakrapani A., Christen H.J., Moser H., Steinmann B., Dierks T., Gaertner J.
Eur. J. Hum. Genet. 19:253-261(2011) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS MSD PRO-155; ARG-247; VAL-263; 327-ARG--ASP-374 DEL AND CYS-345, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS MSD PRO-155; VAL-263; 327-ARG--ASP-374 DEL AND CYS-345.
Dierks T., Schmidt B., Borissenko L.V., Peng J., Preusser A., Mariappan M., von Figura K.
Cell 113:435-444(2003) [PubMed] [Europe PMC] [Abstract]
Cosma M.P., Pepe S., Annunziata I., Newbold R.F., Grompe M., Parenti G., Ballabio A.
Cell 113:445-456(2003) [PubMed] [Europe PMC] [Abstract]
Cosma M.P., Pepe S., Parenti G., Settembre C., Annunziata I., Wade-Martins R., Domenico C.D., Natale P.D., Mankad A., Cox B., Uziel G., Mancini G.M., Zammarchi E., Donati M.A., Kleijer W.J., Filocamo M., Carrozzo R., Carella M., Ballabio A.
Hum. Mutat. 23:576-581(2004) [PubMed] [Europe PMC] [Abstract]
Schlotawa L., Steinfeld R., von Figura K., Dierks T., Gaertner J.
Hum. Mutat. 29:205-205(2008) [PubMed] [Europe PMC] [Abstract]
Schlotawa L., Ennemann E.C., Radhakrishnan K., Schmidt B., Chakrapani A., Christen H.J., Moser H., Steinmann B., Dierks T., Gaertner J.
Eur. J. Hum. Genet. 19:253-261(2011) [PubMed] [Europe PMC] [Abstract]
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.2"The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases."
Cosma M.P., Pepe S., Annunziata I., Newbold R.F., Grompe M., Parenti G., Ballabio A.
Cell 113:445-456(2003) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS MSD PRO-155; TYR-218; ARG-336; CYS-345; PRO-348; GLN-349 AND TRP-349, FUNCTION.
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_019050 | 20 | L → F in MSD; loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_016053 | 155 | S → P in MSD; loss of enzyme activity. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_019051 | 177 | A → P in MSD; loss of activity; decreases its specific enzyme activity to less than 1%; does not affect localization of the protein in the endoplasmic reticulum of MSD fibroblasts; protein stability is almost comparable to wild-type. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_042602 | 179 | W → S in MSD; decreases its specific enzyme activity to less than 3%; does not affect localization of the protein in the endoplasmic reticulum of MSD fibroblasts; protein stability is almost comparable to wild-type. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_016054 | 218 | C → Y in MSD; loss of activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_019052 | 224 | R → W in MSD; loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_080468 | 247 | G → R in MSD. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_019053 | 259 | N → I in MSD; loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_080469 | 263 | G → V in MSD; mild phenotype; reduced but not abolished activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_019054 | 266 | P → L in MSD; retains some activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_016055 | 279 | A → V in MSD; loss of activity; decreases its specific enzyme activity to about 23%; does not affect localization of the protein in the endoplasmic reticulum of MSD fibroblasts; protein stability is decreased. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_080470 | 327 – 374 | Missing in MSD; almost abolished enzyme activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 48 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_016056 | 336 | C → R in MSD; loss of activity. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_016057 | 345 | R → C in MSD; reduced but not abolished activity. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_016058 | 348 | A → P in MSD; loss of activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_016059 | 349 | R → Q in MSD; loss of activity. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_016060 | 349 | R → W in MSD; loss of activity; decreases its specific enzyme activity to less than 1%; does not affect localization of the protein in the endoplasmic reticulum of MSD fibroblasts; protein stability is severely decreased. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 333 | S → A: Loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 333 | S → T: Reduces activity by 99%. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 336 | C → S: Loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 337 | H → A: Reduces activity 5-fold. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 340 | Y → F: No effect. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 341 | C → S: Loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Diseasei
Disease mutation, Ichthyosis, Leukodystrophy, Metachromatic leukodystrophy, MucopolysaccharidosisOrganism-specific databases
DisGeNET More...DisGeNETi | 285362 |
MalaCards human disease database More...MalaCardsi | SUMF1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 272200 phenotype |
Open Targets More...OpenTargetsi | ENSG00000144455 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 585 Multiple sulfatase deficiency |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA134977552 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | SUMF1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 62298562 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 33 | 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 33 | |
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000033456 | 34 – 374 | Formylglycine-generating enzymeAdd BLAST | 341 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 50 ↔ 52 | 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 141 | N-linked (GlcNAc...) asparagine3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 218 ↔ 365 | 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 235 ↔ 346 | 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
|
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"Molecular characterization of the human Calpha-formylglycine-generating enzyme."
Preusser-Kunze A., Mariappan M., Schmidt B., Gande S.L., Mutenda K., Wenzel D., von Figura K., Dierks T.
J. Biol. Chem. 280:14900-14910(2005) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, CALCIUM-BINDING, GLYCOSYLATION AT ASN-141, SUBCELLULAR LOCATION, DISULFIDE BONDS. - Ref.12"Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme."
Dierks T., Dickmanns A., Preusser-Kunze A., Schmidt B., Mariappan M., von Figura K., Ficner R., Rudolph M.G.
Cell 121:541-552(2005) [PubMed] [Europe PMC] [Abstract]Cited for: PARTIAL PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 73-374 IN COMPLEX WITH CALCIUM, FUNCTION, GLYCOSYLATION AT ASN-141, MUTAGENESIS OF SER-333; CYS-336; HIS-337; TYR-340 AND CYS-341, DISULFIDE BONDS. - Ref.14"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-141.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Disulfide bond, GlycoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q8NBK3 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q8NBK3 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q8NBK3 |
PeptideAtlas More...PeptideAtlasi | Q8NBK3 |
PRoteomics IDEntifications database More...PRIDEi | Q8NBK3 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 72786 72787 [Q8NBK3-2] 72788 [Q8NBK3-3] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q8NBK3 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q8NBK3 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"Sulphatase activities are regulated by the interaction of sulphatase-modifying factor 1 with SUMF2."
Zito E., Fraldi A., Pepe S., Annunziata I., Kobinger G., Di Natale P., Ballabio A., Cosma M.P.
EMBO Rep. 6:655-660(2005) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, INTERACTION WITH SUMF2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000144455 |
CleanEx database of gene expression profiles More...CleanExi | HS_SUMF1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q8NBK3 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q8NBK3 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA038025 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"Sulphatase activities are regulated by the interaction of sulphatase-modifying factor 1 with SUMF2."
Zito E., Fraldi A., Pepe S., Annunziata I., Kobinger G., Di Natale P., Ballabio A., Cosma M.P.
EMBO Rep. 6:655-660(2005) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, INTERACTION WITH SUMF2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.12"Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme."
Dierks T., Dickmanns A., Preusser-Kunze A., Schmidt B., Mariappan M., von Figura K., Ficner R., Rudolph M.G.
Cell 121:541-552(2005) [PubMed] [Europe PMC] [Abstract]Cited for: PARTIAL PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 73-374 IN COMPLEX WITH CALCIUM, FUNCTION, GLYCOSYLATION AT ASN-141, MUTAGENESIS OF SER-333; CYS-336; HIS-337; TYR-340 AND CYS-341, DISULFIDE BONDS. - Ref.17"A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme."
Roeser D., Preusser-Kunze A., Schmidt B., Gasow K., Wittmann J.G., Dierks T., von Figura K., Rudolph M.G.
Proc. Natl. Acad. Sci. U.S.A. 103:81-86(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF MUTANTS SER-336 AND SER-341 IN COMPLEX WITH SULFATASE PEPTIDE, FUNCTION.
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- protein homodimerization activity Source: Ensembl
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 130091, 19 interactors |
Protein interaction database and analysis system More...IntActi | Q8NBK3, 4 interactors |
Molecular INTeraction database More...MINTi | Q8NBK3 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000272902 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 91 – 94 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 97 – 102 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 109 – 111 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 117 – 121 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 124 – 129 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 133 – 143 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 148 – 152 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 154 – 158 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 159 – 161 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 180 – 184 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 211 – 220 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 228 – 236 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 252 – 254 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 265 – 267 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 293 – 305 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 315 – 317 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 325 – 331 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 338 – 340 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 350 – 352 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 366 – 369 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q8NBK3 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q8NBK3 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q8NBK3 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 341 – 360 | Interaction with sulfatases1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 20 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
SignalPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IEYZ Eukaryota COG1262 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000008983 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000135466 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG054193 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q8NBK3 |
KEGG Orthology (KO) More...KOi | K13444 |
Identification of Orthologs from Complete Genome Data More...OMAi | KLFPWGN |
Database of Orthologous Groups More...OrthoDBi | EOG091G0DD2 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q8NBK3 |
TreeFam database of animal gene trees More...TreeFami | TF324027 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR016187 CTDL_fold IPR005532 SUMF_dom |
Pfam protein domain database More...Pfami | View protein in Pfam PF03781 FGE-sulfatase, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF56436 SSF56436, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (5)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 5 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MAAPALGLVC GRCPELGLVL LLLLLSLLCG AAGSQEAGTG AGAGSLAGSC
60 70 80 90 100
GCGTPQRPGA HGSSAAAHRY SREANAPGPV PGERQLAHSK MVPIPAGVFT
110 120 130 140 150
MGTDDPQIKQ DGEAPARRVT IDAFYMDAYE VSNTEFEKFV NSTGYLTEAE
160 170 180 190 200
KFGDSFVFEG MLSEQVKTNI QQAVAAAPWW LPVKGANWRH PEGPDSTILH
210 220 230 240 250
RPDHPVLHVS WNDAVAYCTW AGKRLPTEAE WEYSCRGGLH NRLFPWGNKL
260 270 280 290 300
QPKGQHYANI WQGEFPVTNT GEDGFQGTAP VDAFPPNGYG LYNIVGNAWE
310 320 330 340 350
WTSDWWTVHH SVEETLNPKG PPSGKDRVKK GGSYMCHRSY CYRYRCAARS
360 370
QNTPDSSASN LGFRCAADRL PTMD
The sequence of this isoform differs from the canonical sequence as follows:
1-90: Missing.
10 20 30 40 50
MVPIPAGVFT MGTDDPQIKQ DGEAPARRVT IDAFYMDAYE VSNTEFEKFV
60 70 80 90 100
NSTGYLTEAE KFGDSFVFEG MLSEQVKTNI QQAVAAAPWW LPVKGANWRH
110 120 130 140 150
PEGPDSTILH RPDHPVLHVS WNDAVAYCTW AGKRLPTEAE WEYSCRGGLH
160 170 180 190 200
NRLFPWGNKL QPKGQHYANI WQGEFPVTNT GEDGFQGTAP VDAFPPNGYG
210 220 230 240 250
LYNIVGNAWE WTSDWWTVHH SVEETLNPKG PPSGKDRVKK GGSYMCHRSY
260 270 280
CYRYRCAARS QNTPDSSASN LGFRCAADRL PTMD
The sequence of this isoform differs from the canonical sequence as follows:
340-374: YCYRYRCAARSQNTPDSSASNLGFRCAADRLPTMD → QEYYDPYFQD...QHGPRLHCVD
10 20 30 40 50
MAAPALGLVC GRCPELGLVL LLLLLSLLCG AAGSQEAGTG AGAGSLAGSC
60 70 80 90 100
GCGTPQRPGA HGSSAAAHRY SREANAPGPV PGERQLAHSK MVPIPAGVFT
110 120 130 140 150
MGTDDPQIKQ DGEAPARRVT IDAFYMDAYE VSNTEFEKFV NSTGYLTEAE
160 170 180 190 200
KFGDSFVFEG MLSEQVKTNI QQAVAAAPWW LPVKGANWRH PEGPDSTILH
210 220 230 240 250
RPDHPVLHVS WNDAVAYCTW AGKRLPTEAE WEYSCRGGLH NRLFPWGNKL
260 270 280 290 300
QPKGQHYANI WQGEFPVTNT GEDGFQGTAP VDAFPPNGYG LYNIVGNAWE
310 320 330 340 350
WTSDWWTVHH SVEETLNPKG PPSGKDRVKK GGSYMCHRSQ EYYDPYFQDV
360 370 380 390 400
ASEMLRRHTA SRWKAFSSLE PCCSIRRHQQ YAAIERLTCG KFELRCASLR
410 420
KIDCLNTNIA CSYSMRQHGP RLHCVD
The sequence of this isoform differs from the canonical sequence as follows:
149-173: Missing.
10 20 30 40 50
MAAPALGLVC GRCPELGLVL LLLLLSLLCG AAGSQEAGTG AGAGSLAGSC
60 70 80 90 100
GCGTPQRPGA HGSSAAAHRY SREANAPGPV PGERQLAHSK MVPIPAGVFT
110 120 130 140 150
MGTDDPQIKQ DGEAPARRVT IDAFYMDAYE VSNTEFEKFV NSTGYLTEVA
160 170 180 190 200
AAPWWLPVKG ANWRHPEGPD STILHRPDHP VLHVSWNDAV AYCTWAGKRL
210 220 230 240 250
PTEAEWEYSC RGGLHNRLFP WGNKLQPKGQ HYANIWQGEF PVTNTGEDGF
260 270 280 290 300
QGTAPVDAFP PNGYGLYNIV GNAWEWTSDW WTVHHSVEET LNPKGPPSGK
310 320 330 340
DRVKKGGSYM CHRSYCYRYR CAARSQNTPD SSASNLGFRC AADRLPTMD
The sequence of this isoform differs from the canonical sequence as follows:
319-338: Missing.
10 20 30 40 50
MAAPALGLVC GRCPELGLVL LLLLLSLLCG AAGSQEAGTG AGAGSLAGSC
60 70 80 90 100
GCGTPQRPGA HGSSAAAHRY SREANAPGPV PGERQLAHSK MVPIPAGVFT
110 120 130 140 150
MGTDDPQIKQ DGEAPARRVT IDAFYMDAYE VSNTEFEKFV NSTGYLTEAE
160 170 180 190 200
KFGDSFVFEG MLSEQVKTNI QQAVAAAPWW LPVKGANWRH PEGPDSTILH
210 220 230 240 250
RPDHPVLHVS WNDAVAYCTW AGKRLPTEAE WEYSCRGGLH NRLFPWGNKL
260 270 280 290 300
QPKGQHYANI WQGEFPVTNT GEDGFQGTAP VDAFPPNGYG LYNIVGNAWE
310 320 330 340 350
WTSDWWTVHH SVEETLNPSY CYRYRCAARS QNTPDSSASN LGFRCAADRL
PTMD
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 112 | G → E in BAG63417 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 119 | V → A in AAI21124 (PubMed:15489334).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 124 | F → L in BAC11634 (PubMed:16303743).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 264 | E → D in BAC11634 (PubMed:16303743).Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_019050 | 20 | L → F in MSD; loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_016052 | 63 | S → N2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_016053 | 155 | S → P in MSD; loss of enzyme activity. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_019051 | 177 | A → P in MSD; loss of activity; decreases its specific enzyme activity to less than 1%; does not affect localization of the protein in the endoplasmic reticulum of MSD fibroblasts; protein stability is almost comparable to wild-type. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_042602 | 179 | W → S in MSD; decreases its specific enzyme activity to less than 3%; does not affect localization of the protein in the endoplasmic reticulum of MSD fibroblasts; protein stability is almost comparable to wild-type. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_016054 | 218 | C → Y in MSD; loss of activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_019052 | 224 | R → W in MSD; loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_080468 | 247 | G → R in MSD. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_019053 | 259 | N → I in MSD; loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_080469 | 263 | G → V in MSD; mild phenotype; reduced but not abolished activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_019054 | 266 | P → L in MSD; retains some activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_016055 | 279 | A → V in MSD; loss of activity; decreases its specific enzyme activity to about 23%; does not affect localization of the protein in the endoplasmic reticulum of MSD fibroblasts; protein stability is decreased. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_080470 | 327 – 374 | Missing in MSD; almost abolished enzyme activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 48 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_016056 | 336 | C → R in MSD; loss of activity. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_016057 | 345 | R → C in MSD; reduced but not abolished activity. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_016058 | 348 | A → P in MSD; loss of activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_016059 | 349 | R → Q in MSD; loss of activity. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_016060 | 349 | R → W in MSD; loss of activity; decreases its specific enzyme activity to less than 1%; does not affect localization of the protein in the endoplasmic reticulum of MSD fibroblasts; protein stability is severely decreased. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_007877 | 1 – 90 | Missing in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 90 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_045414 | 149 – 173 | Missing in isoform 4. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 25 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_045415 | 319 – 338 | Missing in isoform 5. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 20 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_013185 | 340 – 374 | YCYRY…LPTMD → QEYYDPYFQDVASEMLRRHT ASRWKAFSSLEPCCSIRRHQ QYAAIERLTCGKFELRCASL RKIDCLNTNIACSYSMRQHG PRLHCVD in isoform 3. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 35 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AY208752 mRNA Translation: AAO34683.1 AY323910 mRNA Translation: AAP86217.1 AB448737 mRNA Translation: BAH11168.1 AY358092 mRNA Translation: AAQ88459.1 AK057983 mRNA Translation: BAB71625.1 AK302018 mRNA Translation: BAG63417.1 AK075459 mRNA Translation: BAC11634.1 AC018822 Genomic DNA No translation available. AC023480 Genomic DNA No translation available. AC023483 Genomic DNA No translation available. AC023484 Genomic DNA No translation available. AC024167 Genomic DNA No translation available. AC024168 Genomic DNA No translation available. AC034191 Genomic DNA No translation available. CH471055 Genomic DNA Translation: EAW63906.1 CH471055 Genomic DNA Translation: EAW63907.1 BC017005 mRNA Translation: AAH17005.2 BC110862 mRNA Translation: AAI10863.1 BC121122 mRNA Translation: AAI21123.1 BC121123 mRNA Translation: AAI21124.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS2564.1 [Q8NBK3-1] CCDS54548.1 [Q8NBK3-4] CCDS54549.1 [Q8NBK3-5] |
NCBI Reference Sequences More...RefSeqi | NP_001158146.1, NM_001164674.1 [Q8NBK3-4] NP_001158147.1, NM_001164675.1 [Q8NBK3-5] NP_877437.2, NM_182760.3 [Q8NBK3-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.350475 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000272902; ENSP00000272902; ENSG00000144455 [Q8NBK3-1] ENST00000383843; ENSP00000373355; ENSG00000144455 [Q8NBK3-4] ENST00000405420; ENSP00000384977; ENSG00000144455 [Q8NBK3-5] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 285362 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:285362 |
UCSC genome browser More...UCSCi | uc003bpz.3 human [Q8NBK3-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q8NBK3 | UPI00006687B1 | 286 | |||
| Q8NBK3-2 | 284 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q8NBK3 | UPI00006687B1 | 286 | |||
| SUMF1 isoform 5 | 426 | ||||
| SUMF1 isoform 2 | 426 | ||||
| UPI0005F4E943 | 410 | ||||
| Sulfatase modifying factor 1 | 374 | ||||
| +11 | |||||
| Q8NBK3-4 | UPI0007DC7820 | 423 | |||
| SUMF1 isoform 6 | 349 | ||||
| Sulfatase modifying factor 1 | 349 | ||||
| Q8NBK3-5 | UPI0007DC74FC | 428 | |||
| SUMF1 isoform 2 | 354 | ||||
| Sulfatase modifying factor 1 | 354 | ||||
| SUMF1 isoform 8 | 354 | ||||
| UPI0007DC747F | 351 | ||||
| +2 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q8NBK3 | UPI00006687B1 | 286 | |||
| SUMF1 isoform 5 | 426 | ||||
| SUMF1 isoform 2 | 426 | ||||
| UPI0005F4E943 | 410 | ||||
| Sulfatase modifying factor 1 | 374 | ||||
| +27 | |||||
| Q8NBK3-4 | UPI0007DC7820 | 423 | |||
| Sulfatase modifying factor 1 | 349 | ||||
| SUMF1 isoform 6 | 349 | ||||
| UPI00051AEFAE | 282 | ||||
| UPI0008F4A96C | 349 | ||||
| +59 | |||||
| Q8NBK3-5 | UPI0007DC74FC | 428 | |||
| SUMF1 isoform 2 | 354 | ||||
| Sulfatase modifying factor 1 | 354 | ||||
| SUMF1 isoform 8 | 354 | ||||
| UPI000809B934 | 387 | ||||
| +80 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AY208752 mRNA Translation: AAO34683.1 AY323910 mRNA Translation: AAP86217.1 AB448737 mRNA Translation: BAH11168.1 AY358092 mRNA Translation: AAQ88459.1 AK057983 mRNA Translation: BAB71625.1 AK302018 mRNA Translation: BAG63417.1 AK075459 mRNA Translation: BAC11634.1 AC018822 Genomic DNA No translation available. AC023480 Genomic DNA No translation available. AC023483 Genomic DNA No translation available. AC023484 Genomic DNA No translation available. AC024167 Genomic DNA No translation available. AC024168 Genomic DNA No translation available. AC034191 Genomic DNA No translation available. CH471055 Genomic DNA Translation: EAW63906.1 CH471055 Genomic DNA Translation: EAW63907.1 BC017005 mRNA Translation: AAH17005.2 BC110862 mRNA Translation: AAI10863.1 BC121122 mRNA Translation: AAI21123.1 BC121123 mRNA Translation: AAI21124.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS2564.1 [Q8NBK3-1] CCDS54548.1 [Q8NBK3-4] CCDS54549.1 [Q8NBK3-5] |
NCBI Reference Sequences More...RefSeqi | NP_001158146.1, NM_001164674.1 [Q8NBK3-4] NP_001158147.1, NM_001164675.1 [Q8NBK3-5] NP_877437.2, NM_182760.3 [Q8NBK3-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.350475 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1Y1E | X-ray | 1.73 | X | 73-374 | [»] | |
| 1Y1F | X-ray | 1.80 | X | 73-374 | [»] | |
| 1Y1G | X-ray | 1.67 | X | 73-374 | [»] | |
| 1Y1H | X-ray | 1.67 | X | 73-374 | [»] | |
| 1Y1I | X-ray | 2.61 | X | 73-374 | [»] | |
| 1Y1J | X-ray | 1.55 | X | 73-374 | [»] | |
| 1Z70 | X-ray | 1.15 | X | 73-374 | [»] | |
| 2AFT | X-ray | 1.66 | X | 86-371 | [»] | |
| 2AFY | X-ray | 1.49 | X | 86-371 | [»] | |
| 2AII | X-ray | 1.54 | X | 86-371 | [»] | |
| 2AIJ | X-ray | 1.55 | X | 86-371 | [»] | |
| 2AIK | X-ray | 1.73 | X | 86-371 | [»] | |
| 2HI8 | X-ray | 1.64 | X | 86-371 | [»] | |
| 2HIB | X-ray | 2.00 | X | 86-371 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q8NBK3 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q8NBK3 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 130091, 19 interactors |
Protein interaction database and analysis system More...IntActi | Q8NBK3, 4 interactors |
Molecular INTeraction database More...MINTi | Q8NBK3 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000272902 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q8NBK3 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q8NBK3 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | SUMF1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 62298562 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q8NBK3 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q8NBK3 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q8NBK3 |
PeptideAtlas More...PeptideAtlasi | Q8NBK3 |
PRoteomics IDEntifications database More...PRIDEi | Q8NBK3 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 72786 72787 [Q8NBK3-2] 72788 [Q8NBK3-3] |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000272902; ENSP00000272902; ENSG00000144455 [Q8NBK3-1] ENST00000383843; ENSP00000373355; ENSG00000144455 [Q8NBK3-4] ENST00000405420; ENSP00000384977; ENSG00000144455 [Q8NBK3-5] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 285362 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:285362 |
UCSC genome browser More...UCSCi | uc003bpz.3 human [Q8NBK3-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 285362 |
DisGeNET More...DisGeNETi | 285362 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000144455.13 |
GeneCards: human genes, protein and diseases More...GeneCardsi | SUMF1 |
Human Gene Nomenclature Database More...HGNCi | HGNC:20376 SUMF1 |
Human Protein Atlas More...HPAi | HPA038025 |
MalaCards human disease database More...MalaCardsi | SUMF1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 272200 phenotype 607939 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q8NBK3 |
Open Targets More...OpenTargetsi | ENSG00000144455 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 585 Multiple sulfatase deficiency |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA134977552 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IEYZ Eukaryota COG1262 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000008983 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000135466 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG054193 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q8NBK3 |
KEGG Orthology (KO) More...KOi | K13444 |
Identification of Orthologs from Complete Genome Data More...OMAi | KLFPWGN |
Database of Orthologous Groups More...OrthoDBi | EOG091G0DD2 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q8NBK3 |
TreeFam database of animal gene trees More...TreeFami | TF324027 |
Enzyme and pathway databases
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00910 |
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:ENSG00000144455-MONOMER |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1660662 Glycosphingolipid metabolism R-HSA-1663150 The activation of arylsulfatases |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | SUMF1 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q8NBK3 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | SUMF1 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 285362 |
Protein Ontology More...PROi | PR:Q8NBK3 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000144455 |
CleanEx database of gene expression profiles More...CleanExi | HS_SUMF1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q8NBK3 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q8NBK3 HS |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR016187 CTDL_fold IPR005532 SUMF_dom |
Pfam protein domain database More...Pfami | View protein in Pfam PF03781 FGE-sulfatase, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF56436 SSF56436, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | SUMF1_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q8NBK3Primary (citable) accession number: Q8NBK3 Secondary accession number(s): B4DXK5 , B7XD05, E9PGL0, G5E9B0, Q0VAC6, Q0VAC7, Q2NL78, Q53ZE4, Q6UY39, Q96AK5, Q96DK8 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 25, 2003 |
| Last sequence update: | March 29, 2005 | |
| Last modified: | July 18, 2018 | |
| This is version 152 of the entry and version 3 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 3
Human chromosome 3: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
