UniProtKB - Q8NBK3 (SUMF1_HUMAN)
Protein
Formylglycine-generating enzyme
Gene
SUMF1
Organism
Homo sapiens (Human)
Status
Functioni
Oxidase that catalyzes the conversion of cysteine to 3-oxoalanine on target proteins, using molecular oxygen and an unidentified reducing agent (PubMed:12757706, PubMed:15657036, PubMed:15907468, PubMed:25931126, PubMed:16368756, PubMed:21224894). 3-oxoalanine modification, which is also named formylglycine (fGly), occurs in the maturation of arylsulfatases and some alkaline phosphatases that use the hydrated form of 3-oxoalanine as a catalytic nucleophile (PubMed:12757706, PubMed:15657036, PubMed:15907468, PubMed:25931126, PubMed:16368756). Known substrates include GALNS, ARSA, STS and ARSE (PubMed:12757706, PubMed:15907468, PubMed:15657036).6 Publications
Miscellaneous
The resulting 3-oxoalanine in the substrate protein is called C(alpha)-formylglycine by many authors. It should not be confused with N-formylglycine.
Caution
The disulfide bond observed in the structure does not exist in vivo (PubMed:15907468). The enzyme reaction was initially thought to act via a redox-active disulfide bond mechanism; however the disulfide bond only takes place with inactive enzyme that lacks the copper cofactor (PubMed:25931126). The catalytic copper is required to activate oxygen and catalyze oxidative C-H activation (PubMed:25931126).2 Publications
Catalytic activityi
- 2 a thiol + L-cysteinyl-[sulfatase] + O2 = 3-oxo-L-alanyl-[sulfatase] + an organic disulfide + H+ + H2O + hydrogen sulfide2 PublicationsEC:1.8.3.72 Publications
Cofactori
Cu2+1 PublicationNote: The catalytic copper is required to activate oxygen and catalyze oxidative C-H activation.1 Publication
Kineticsi
Kcat is 6.06 min(-1) with [sulfatase]-L-cysteine as substrate.1 Publication
- KM=0.34 µM for [sulfatase]-L-cysteine1 Publication
: sulfatase oxidation Pathwayi
This protein is involved in the pathway sulfatase oxidation, which is part of Protein modification.4 PublicationsView 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 |
---|---|---|---|---|
Metal bindingi | 130 | Calcium 21 Publication | 1 | |
Metal bindingi | 259 | Calcium 11 Publication | 1 | |
Metal bindingi | 260 | Calcium 1; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 273 | Calcium 11 Publication | 1 | |
Metal bindingi | 275 | Calcium 1; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 293 | Calcium 2; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 296 | Calcium 2; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 298 | Calcium 2; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 300 | Calcium 21 Publication | 1 | |
Metal bindingi | 336 | Copper(2+); catalytic1 Publication | 1 | |
Metal bindingi | 341 | Copper(2+); catalytic1 Publication | 1 |
GO - Molecular functioni
- cupric ion binding Source: UniProtKB
- Formylglycine-generating oxidase activity Source: UniProtKB
- oxidoreductase activity Source: Reactome
- protein homodimerization activity Source: Ensembl
GO - Biological processi
- glycosphingolipid metabolic process Source: Reactome
- post-translational protein modification Source: UniProtKB
- protein oxidation Source: UniProtKB
Keywordsi
Molecular function | Oxidoreductase |
Ligand | Calcium, Copper, Metal-binding |
Enzyme and pathway databases
BioCyci | MetaCyc:ENSG00000144455-MONOMER |
Reactomei | R-HSA-1660662 Glycosphingolipid metabolism R-HSA-1663150 The activation of arylsulfatases |
UniPathwayi | UPA00910 |
Names & Taxonomyi
Protein namesi | Recommended name: Formylglycine-generating enzyme1 Publication (EC:1.8.3.72 Publications)Short name: FGE1 Publication Alternative name(s): C-alpha-formylglycine-generating enzyme 11 Publication Sulfatase-modifying factor 11 Publication |
Gene namesi | ORF Names:PSEC01521 Publication, UNQ3037/PRO98521 Publication |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:20376 SUMF1 |
MIMi | 607939 gene |
neXtProti | NX_Q8NBK3 |
Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum lumen 4 Publications
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB
- endoplasmic reticulum lumen Source: Reactome
Keywords - Cellular componenti
Endoplasmic reticulumPathology & Biotechi
Involvement in diseasei
Multiple sulfatase deficiency (MSD)5 Publications
The disease is caused by mutations affecting the gene represented in this entry. SUMF1 mutations result in defective post-translational modification of sulfatases.1 Publication
Disease descriptionA clinically and biochemically heterogeneous disorder caused by the simultaneous impairment of all sulfatases, due to defective post-translational modification and activation. It combines features of individual sulfatase deficiencies such as metachromatic leukodystrophy, mucopolysaccharidosis, chondrodysplasia punctata, hydrocephalus, ichthyosis, neurologic deterioration and developmental delay.
Related information in OMIMFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_019050 | 20 | L → F in MSD; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs200142963EnsemblClinVar. | 1 | |
Natural variantiVAR_016053 | 155 | S → P in MSD; loss of enzyme activity. 3 PublicationsCorresponds to variant dbSNP:rs137852850EnsemblClinVar. | 1 | |
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 | 1 | |
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 PublicationCorresponds to variant dbSNP:rs757323641Ensembl. | 1 | |
Natural variantiVAR_016054 | 218 | C → Y in MSD; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs137852854EnsemblClinVar. | 1 | |
Natural variantiVAR_019052 | 224 | R → W in MSD; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs759888604Ensembl. | 1 | |
Natural variantiVAR_080468 | 247 | G → R in MSD. 1 PublicationCorresponds to variant dbSNP:rs1057517363EnsemblClinVar. | 1 | |
Natural variantiVAR_019053 | 259 | N → I in MSD; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs764215221Ensembl. | 1 | |
Natural variantiVAR_080469 | 263 | G → V in MSD; mild phenotype; reduced but not abolished activity. 1 PublicationCorresponds to variant dbSNP:rs387906976EnsemblClinVar. | 1 | |
Natural variantiVAR_019054 | 266 | P → L in MSD; retains some activity. 1 PublicationCorresponds to variant dbSNP:rs763243827Ensembl. | 1 | |
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 PublicationsCorresponds to variant dbSNP:rs137852849EnsemblClinVar. | 1 | |
Natural variantiVAR_080470 | 327 – 374 | Missing in MSD; almost abolished enzyme activity. 1 PublicationAdd BLAST | 48 | |
Natural variantiVAR_016056 | 336 | C → R in MSD; loss of activity. 3 PublicationsCorresponds to variant dbSNP:rs137852848EnsemblClinVar. | 1 | |
Natural variantiVAR_016057 | 345 | R → C in MSD; reduced but not abolished activity. 3 PublicationsCorresponds to variant dbSNP:rs137852852EnsemblClinVar. | 1 | |
Natural variantiVAR_016058 | 348 | A → P in MSD; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs137852853EnsemblClinVar. | 1 | |
Natural variantiVAR_016059 | 349 | R → Q in MSD; loss of activity. 3 PublicationsCorresponds to variant dbSNP:rs137852847EnsemblClinVar. | 1 | |
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 PublicationsCorresponds to variant dbSNP:rs137852846EnsemblClinVar. | 1 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 333 | S → A: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 333 | S → T: Reduces activity by 99%. 1 Publication | 1 | |
Mutagenesisi | 336 | C → S: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 337 | H → A: Reduces activity 5-fold. 1 Publication | 1 | |
Mutagenesisi | 340 | Y → F: No effect. 1 Publication | 1 | |
Mutagenesisi | 341 | C → S: Loss of activity. 1 Publication | 1 |
Keywords - Diseasei
Disease mutation, Ichthyosis, Leukodystrophy, Metachromatic leukodystrophy, MucopolysaccharidosisOrganism-specific databases
DisGeNETi | 285362 |
MalaCardsi | SUMF1 |
MIMi | 272200 phenotype |
OpenTargetsi | ENSG00000144455 |
Orphaneti | 585 Multiple sulfatase deficiency |
PharmGKBi | PA134977552 |
Miscellaneous databases
Pharosi | Q8NBK3 |
Polymorphism and mutation databases
BioMutai | SUMF1 |
DMDMi | 62298562 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 33 | 1 PublicationAdd BLAST | 33 | |
ChainiPRO_0000033456 | 34 – 374 | Formylglycine-generating enzymeAdd BLAST | 341 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 50 ↔ 52 | 2 Publications | ||
Glycosylationi | 141 | N-linked (GlcNAc...) asparagine3 Publications | 1 | |
Disulfide bondi | 218 ↔ 365 | 2 Publications | ||
Disulfide bondi | 235 ↔ 346 | 2 Publications |
Post-translational modificationi
N-glycosylated. Contains high-mannose-type oligosaccharides.3 Publications
Keywords - PTMi
Disulfide bond, GlycoproteinProteomic databases
EPDi | Q8NBK3 |
jPOSTi | Q8NBK3 |
MassIVEi | Q8NBK3 |
MaxQBi | Q8NBK3 |
PaxDbi | Q8NBK3 |
PeptideAtlasi | Q8NBK3 |
PRIDEi | Q8NBK3 |
ProteomicsDBi | 20338 33885 72786 [Q8NBK3-1] 72787 [Q8NBK3-2] 72788 [Q8NBK3-3] |
PTM databases
GlyConnecti | 1772 |
iPTMneti | Q8NBK3 |
PhosphoSitePlusi | Q8NBK3 |
Expressioni
Tissue specificityi
Ubiquitous. Highly expressed in kidney, pancreas and liver. Detected at lower levels in leukocytes, lung, placenta, small intestine, skeletal muscle and heart.1 Publication
Gene expression databases
Bgeei | ENSG00000144455 Expressed in 209 organ(s), highest expression level in metanephros |
ExpressionAtlasi | Q8NBK3 baseline and differential |
Genevisiblei | Q8NBK3 HS |
Organism-specific databases
HPAi | HPA038025 |
Interactioni
Subunit structurei
Monomer, homodimer and heterodimer with SUMF2.
3 PublicationsGO - Molecular functioni
- protein homodimerization activity Source: Ensembl
Protein-protein interaction databases
BioGridi | 130091, 19 interactors |
IntActi | Q8NBK3, 17 interactors |
MINTi | Q8NBK3 |
STRINGi | 9606.ENSP00000272902 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q8NBK3 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q8NBK3 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 341 – 360 | Interaction with sulfatases1 PublicationAdd BLAST | 20 |
Sequence similaritiesi
Belongs to the sulfatase-modifying factor family.Curated
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | ENOG410IEYZ Eukaryota COG1262 LUCA |
GeneTreei | ENSGT00390000008983 |
HOGENOMi | HOG000135466 |
InParanoidi | Q8NBK3 |
KOi | K13444 |
OMAi | WTADLWD |
OrthoDBi | 835112at2759 |
PhylomeDBi | Q8NBK3 |
TreeFami | TF324027 |
Family and domain databases
Gene3Di | 3.90.1580.10, 1 hit |
InterProi | View protein in InterPro IPR016187 CTDL_fold IPR005532 SUMF_dom IPR042095 SUMF_sf |
Pfami | View protein in Pfam PF03781 FGE-sulfatase, 1 hit |
SUPFAMi | SSF56436 SSF56436, 1 hit |
s (5+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 5 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 5 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All
Isoform 1 (identifier: Q8NBK3-1) [UniParc]FASTAAdd to basket
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketE9PF05 | E9PF05_HUMAN | Formylglycine-generating enzyme | SUMF1 | 242 | Annotation score: | ||
F5GXA0 | F5GXA0_HUMAN | Formylglycine-generating enzyme | SUMF1 | 426 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 112 | G → E in BAG63417 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 119 | V → A in AAI21124 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 124 | F → L in BAC11634 (PubMed:16303743).Curated | 1 | |
Sequence conflicti | 264 | E → D in BAC11634 (PubMed:16303743).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_019050 | 20 | L → F in MSD; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs200142963EnsemblClinVar. | 1 | |
Natural variantiVAR_016052 | 63 | S → N2 PublicationsCorresponds to variant dbSNP:rs2819590EnsemblClinVar. | 1 | |
Natural variantiVAR_016053 | 155 | S → P in MSD; loss of enzyme activity. 3 PublicationsCorresponds to variant dbSNP:rs137852850EnsemblClinVar. | 1 | |
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 | 1 | |
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 PublicationCorresponds to variant dbSNP:rs757323641Ensembl. | 1 | |
Natural variantiVAR_016054 | 218 | C → Y in MSD; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs137852854EnsemblClinVar. | 1 | |
Natural variantiVAR_019052 | 224 | R → W in MSD; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs759888604Ensembl. | 1 | |
Natural variantiVAR_080468 | 247 | G → R in MSD. 1 PublicationCorresponds to variant dbSNP:rs1057517363EnsemblClinVar. | 1 | |
Natural variantiVAR_019053 | 259 | N → I in MSD; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs764215221Ensembl. | 1 | |
Natural variantiVAR_080469 | 263 | G → V in MSD; mild phenotype; reduced but not abolished activity. 1 PublicationCorresponds to variant dbSNP:rs387906976EnsemblClinVar. | 1 | |
Natural variantiVAR_019054 | 266 | P → L in MSD; retains some activity. 1 PublicationCorresponds to variant dbSNP:rs763243827Ensembl. | 1 | |
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 PublicationsCorresponds to variant dbSNP:rs137852849EnsemblClinVar. | 1 | |
Natural variantiVAR_080470 | 327 – 374 | Missing in MSD; almost abolished enzyme activity. 1 PublicationAdd BLAST | 48 | |
Natural variantiVAR_016056 | 336 | C → R in MSD; loss of activity. 3 PublicationsCorresponds to variant dbSNP:rs137852848EnsemblClinVar. | 1 | |
Natural variantiVAR_016057 | 345 | R → C in MSD; reduced but not abolished activity. 3 PublicationsCorresponds to variant dbSNP:rs137852852EnsemblClinVar. | 1 | |
Natural variantiVAR_016058 | 348 | A → P in MSD; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs137852853EnsemblClinVar. | 1 | |
Natural variantiVAR_016059 | 349 | R → Q in MSD; loss of activity. 3 PublicationsCorresponds to variant dbSNP:rs137852847EnsemblClinVar. | 1 | |
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 PublicationsCorresponds to variant dbSNP:rs137852846EnsemblClinVar. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_007877 | 1 – 90 | Missing in isoform 2. 1 PublicationAdd BLAST | 90 | |
Alternative sequenceiVSP_045414 | 149 – 173 | Missing in isoform 4. 1 PublicationAdd BLAST | 25 | |
Alternative sequenceiVSP_045415 | 319 – 338 | Missing in isoform 5. 1 PublicationAdd BLAST | 20 | |
Alternative sequenceiVSP_013185 | 340 – 374 | YCYRY…LPTMD → QEYYDPYFQDVASEMLRRHT ASRWKAFSSLEPCCSIRRHQ QYAAIERLTCGKFELRCASL RKIDCLNTNIACSYSMRQHG PRLHCVD in isoform 3. 1 PublicationAdd BLAST | 35 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links 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 |
CCDSi | CCDS2564.1 [Q8NBK3-1] CCDS54548.1 [Q8NBK3-4] CCDS54549.1 [Q8NBK3-5] |
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] |
Genome annotation databases
Ensembli | ENST00000272902; ENSP00000272902; ENSG00000144455 [Q8NBK3-1] ENST00000383843; ENSP00000373355; ENSG00000144455 [Q8NBK3-4] ENST00000405420; ENSP00000384977; ENSG00000144455 [Q8NBK3-5] |
GeneIDi | 285362 |
KEGGi | hsa:285362 |
UCSCi | uc003bpz.3 human [Q8NBK3-1] |
Keywords - Coding sequence diversityi
Alternative splicing, PolymorphismSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links 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 |
CCDSi | CCDS2564.1 [Q8NBK3-1] CCDS54548.1 [Q8NBK3-4] CCDS54549.1 [Q8NBK3-5] |
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] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links 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 | [»] | |
SMRi | Q8NBK3 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGridi | 130091, 19 interactors |
IntActi | Q8NBK3, 17 interactors |
MINTi | Q8NBK3 |
STRINGi | 9606.ENSP00000272902 |
PTM databases
GlyConnecti | 1772 |
iPTMneti | Q8NBK3 |
PhosphoSitePlusi | Q8NBK3 |
Polymorphism and mutation databases
BioMutai | SUMF1 |
DMDMi | 62298562 |
Proteomic databases
EPDi | Q8NBK3 |
jPOSTi | Q8NBK3 |
MassIVEi | Q8NBK3 |
MaxQBi | Q8NBK3 |
PaxDbi | Q8NBK3 |
PeptideAtlasi | Q8NBK3 |
PRIDEi | Q8NBK3 |
ProteomicsDBi | 20338 33885 72786 [Q8NBK3-1] 72787 [Q8NBK3-2] 72788 [Q8NBK3-3] |
Genome annotation databases
Ensembli | ENST00000272902; ENSP00000272902; ENSG00000144455 [Q8NBK3-1] ENST00000383843; ENSP00000373355; ENSG00000144455 [Q8NBK3-4] ENST00000405420; ENSP00000384977; ENSG00000144455 [Q8NBK3-5] |
GeneIDi | 285362 |
KEGGi | hsa:285362 |
UCSCi | uc003bpz.3 human [Q8NBK3-1] |
Organism-specific databases
CTDi | 285362 |
DisGeNETi | 285362 |
GeneCardsi | SUMF1 |
HGNCi | HGNC:20376 SUMF1 |
HPAi | HPA038025 |
MalaCardsi | SUMF1 |
MIMi | 272200 phenotype 607939 gene |
neXtProti | NX_Q8NBK3 |
OpenTargetsi | ENSG00000144455 |
Orphaneti | 585 Multiple sulfatase deficiency |
PharmGKBi | PA134977552 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | ENOG410IEYZ Eukaryota COG1262 LUCA |
GeneTreei | ENSGT00390000008983 |
HOGENOMi | HOG000135466 |
InParanoidi | Q8NBK3 |
KOi | K13444 |
OMAi | WTADLWD |
OrthoDBi | 835112at2759 |
PhylomeDBi | Q8NBK3 |
TreeFami | TF324027 |
Enzyme and pathway databases
UniPathwayi | UPA00910 |
BioCyci | MetaCyc:ENSG00000144455-MONOMER |
Reactomei | R-HSA-1660662 Glycosphingolipid metabolism R-HSA-1663150 The activation of arylsulfatases |
Miscellaneous databases
ChiTaRSi | SUMF1 human |
EvolutionaryTracei | Q8NBK3 |
GeneWikii | SUMF1 |
GenomeRNAii | 285362 |
Pharosi | Q8NBK3 |
PROi | PR:Q8NBK3 |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000144455 Expressed in 209 organ(s), highest expression level in metanephros |
ExpressionAtlasi | Q8NBK3 baseline and differential |
Genevisiblei | Q8NBK3 HS |
Family and domain databases
Gene3Di | 3.90.1580.10, 1 hit |
InterProi | View protein in InterPro IPR016187 CTDL_fold IPR005532 SUMF_dom IPR042095 SUMF_sf |
Pfami | View protein in Pfam PF03781 FGE-sulfatase, 1 hit |
SUPFAMi | SSF56436 SSF56436, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | SUMF1_HUMAN | |
Accessioni | Q8NBK3Primary (citable) accession number: Q8NBK3 Secondary accession number(s): B4DXK5 Q96DK8 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 25, 2003 |
Last sequence update: | March 29, 2005 | |
Last modified: | November 13, 2019 | |
This is version 162 of the entry and version 3 of the sequence. See complete history. | ||
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. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - SIMILARITY comments
Index of protein domains and families - Human chromosome 3
Human chromosome 3: entries, gene names and cross-references to MIM - 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