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Protein

Sulfatase-modifying factor 1

Gene

SUMF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Using molecular oxygen and an unidentified reducing agent, oxidizes a cysteine residue in the substrate sulfatase to an active site 3-oxoalanine residue, which is also called C(alpha)-formylglycine. Known substrates include GALNS, ARSA, STS and ARSE.2 Publications

Catalytic activityi

[sulfatase]-cysteine + acceptor = [sulfatase]-3-oxoalanine + reduced acceptor.

Pathwayi: sulfatase oxidation

This protein is involved in the pathway sulfatase oxidation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway sulfatase oxidation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi130Calcium 21 Publication1
Metal bindingi259Calcium 11 Publication1
Metal bindingi260Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi273Calcium 11 Publication1
Metal bindingi275Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi293Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi296Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi298Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi300Calcium 21 Publication1
Active sitei333Proton acceptorCurated1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-1660662. Glycosphingolipid metabolism.
R-HSA-1663150. The activation of arylsulfatases.
UniPathwayiUPA00910.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfatase-modifying factor 1 (EC:1.8.99.-)
Alternative name(s):
C-alpha-formylglycine-generating enzyme 1
Gene namesi
Name:SUMF1
Synonyms:FGE
ORF Names:PSEC0152, UNQ3037/PRO9852
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:20376. SUMF1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Multiple sulfatase deficiency (MSD)3 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.
See also OMIM:272200
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01905020L → F in MSD; loss of activity. 1 PublicationCorresponds to variant rs200142963dbSNPEnsembl.1
Natural variantiVAR_016053155S → P in MSD; loss of activity. 2 PublicationsCorresponds to variant rs137852850dbSNPEnsembl.1
Natural variantiVAR_019051177A → 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 Publications1
Natural variantiVAR_042602179W → 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 rs757323641dbSNPEnsembl.1
Natural variantiVAR_016054218C → Y in MSD; loss of activity. 2 PublicationsCorresponds to variant rs137852854dbSNPEnsembl.1
Natural variantiVAR_019052224R → W in MSD; loss of activity. 1 PublicationCorresponds to variant rs759888604dbSNPEnsembl.1
Natural variantiVAR_019053259N → I in MSD; loss of activity. 1 PublicationCorresponds to variant rs764215221dbSNPEnsembl.1
Natural variantiVAR_019054266P → L in MSD; retains some activity. 1 PublicationCorresponds to variant rs763243827dbSNPEnsembl.1
Natural variantiVAR_016055279A → 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 rs137852849dbSNPEnsembl.1
Natural variantiVAR_016056336C → R in MSD; loss of activity. 3 PublicationsCorresponds to variant rs137852848dbSNPEnsembl.1
Natural variantiVAR_016057345R → C in MSD; retains some activity. 2 PublicationsCorresponds to variant rs137852852dbSNPEnsembl.1
Natural variantiVAR_016058348A → P in MSD; loss of activity. 2 PublicationsCorresponds to variant rs137852853dbSNPEnsembl.1
Natural variantiVAR_016059349R → Q in MSD; loss of activity. 3 PublicationsCorresponds to variant rs137852847dbSNPEnsembl.1
Natural variantiVAR_016060349R → 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 rs137852846dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi333S → A: Loss of activity. 1 Publication1
Mutagenesisi333S → T: Reduces activity by 99%. 1 Publication1
Mutagenesisi336C → S: Loss of activity. 1 Publication1
Mutagenesisi337H → A: Reduces activity 5-fold. 1 Publication1
Mutagenesisi340Y → F: No effect. 1 Publication1
Mutagenesisi341C → S: Loss of activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Ichthyosis, Leukodystrophy, Metachromatic leukodystrophy, Mucopolysaccharidosis

Organism-specific databases

DisGeNETi285362.
MalaCardsiSUMF1.
MIMi272200. phenotype.
OpenTargetsiENSG00000144455.
Orphaneti585. Multiple sulfatase deficiency.
PharmGKBiPA134977552.

Polymorphism and mutation databases

BioMutaiSUMF1.
DMDMi62298562.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 331 PublicationAdd BLAST33
ChainiPRO_000003345634 – 374Sulfatase-modifying factor 1Add BLAST341

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi50 ↔ 52
Glycosylationi141N-linked (GlcNAc...)3 Publications1
Disulfide bondi218 ↔ 365
Disulfide bondi235 ↔ 346
Disulfide bondi336 ↔ 341Redox-active

Post-translational modificationi

N-glycosylated. Contains high-mannose-type oligosaccharides.3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ8NBK3.
MaxQBiQ8NBK3.
PaxDbiQ8NBK3.
PeptideAtlasiQ8NBK3.
PRIDEiQ8NBK3.

PTM databases

iPTMnetiQ8NBK3.
PhosphoSitePlusiQ8NBK3.

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

BgeeiENSG00000144455.
CleanExiHS_SUMF1.
ExpressionAtlasiQ8NBK3. baseline and differential.
GenevisibleiQ8NBK3. HS.

Organism-specific databases

HPAiHPA038025.

Interactioni

Subunit structurei

Monomer, homodimer and heterodimer with SUMF2.3 Publications

Protein-protein interaction databases

BioGridi130091. 14 interactors.
IntActiQ8NBK3. 4 interactors.
MINTiMINT-4534860.
STRINGi9606.ENSP00000272902.

Structurei

Secondary structure

1374
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi91 – 94Combined sources4
Beta strandi97 – 102Combined sources6
Helixi109 – 111Combined sources3
Beta strandi117 – 121Combined sources5
Beta strandi124 – 129Combined sources6
Helixi133 – 143Combined sources11
Helixi148 – 152Combined sources5
Beta strandi154 – 158Combined sources5
Helixi159 – 161Combined sources3
Beta strandi180 – 184Combined sources5
Helixi211 – 220Combined sources10
Helixi228 – 236Combined sources9
Helixi252 – 254Combined sources3
Turni265 – 267Combined sources3
Beta strandi293 – 305Combined sources13
Beta strandi315 – 317Combined sources3
Beta strandi325 – 331Combined sources7
Turni338 – 340Combined sources3
Beta strandi350 – 352Combined sources3
Beta strandi366 – 369Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y1EX-ray1.73X73-374[»]
1Y1FX-ray1.80X73-374[»]
1Y1GX-ray1.67X73-374[»]
1Y1HX-ray1.67X73-374[»]
1Y1IX-ray2.61X73-374[»]
1Y1JX-ray1.55X73-374[»]
1Z70X-ray1.15X73-374[»]
2AFTX-ray1.66X86-371[»]
2AFYX-ray1.49X86-371[»]
2AIIX-ray1.54X86-371[»]
2AIJX-ray1.55X86-371[»]
2AIKX-ray1.73X86-371[»]
2HI8X-ray1.64X86-371[»]
2HIBX-ray2.00X86-371[»]
ProteinModelPortaliQ8NBK3.
SMRiQ8NBK3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8NBK3.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni341 – 360Interaction with sulfatasesAdd BLAST20

Sequence similaritiesi

Belongs to the sulfatase-modifying factor family.Curated

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

eggNOGiENOG410IEYZ. Eukaryota.
COG1262. LUCA.
GeneTreeiENSGT00390000008983.
HOGENOMiHOG000135466.
HOVERGENiHBG054193.
InParanoidiQ8NBK3.
KOiK13444.
OMAiDTYEVSN.
OrthoDBiEOG091G0DD2.
PhylomeDBiQ8NBK3.
TreeFamiTF324027.

Family and domain databases

Gene3Di3.90.1580.10. 1 hit.
InterProiIPR016187. CTDL_fold.
IPR005532. SUMF_dom.
[Graphical view]
PfamiPF03781. FGE-sulfatase. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8NBK3-1) [UniParc]FASTAAdd 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.

« Hide

        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
Length:374
Mass (Da):40,556
Last modified:March 29, 2005 - v3
Checksum:iE64F2DF004C8CEA3
GO
Isoform 2 (identifier: Q8NBK3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-90: Missing.

Note: No experimental confirmation available.
Show »
Length:284
Mass (Da):31,900
Checksum:iE616A28A77F81996
GO
Isoform 3 (identifier: Q8NBK3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     340-374: YCYRYRCAARSQNTPDSSASNLGFRCAADRLPTMD → QEYYDPYFQD...QHGPRLHCVD

Show »
Length:426
Mass (Da):46,857
Checksum:i957E7E1E13D034A6
GO
Isoform 4 (identifier: Q8NBK3-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     149-173: Missing.

Note: No experimental confirmation available.
Show »
Length:349
Mass (Da):37,770
Checksum:i4C5192677FABF9CC
GO
Isoform 5 (identifier: Q8NBK3-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     319-338: Missing.

Note: No experimental confirmation available.
Show »
Length:354
Mass (Da):38,386
Checksum:iAB2E4103EAC0E027
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti112G → E in BAG63417 (PubMed:14702039).Curated1
Sequence conflicti119V → A in AAI21124 (PubMed:15489334).Curated1
Sequence conflicti124F → L in BAC11634 (PubMed:16303743).Curated1
Sequence conflicti264E → D in BAC11634 (PubMed:16303743).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01905020L → F in MSD; loss of activity. 1 PublicationCorresponds to variant rs200142963dbSNPEnsembl.1
Natural variantiVAR_01605263S → N.2 PublicationsCorresponds to variant rs2819590dbSNPEnsembl.1
Natural variantiVAR_016053155S → P in MSD; loss of activity. 2 PublicationsCorresponds to variant rs137852850dbSNPEnsembl.1
Natural variantiVAR_019051177A → 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 Publications1
Natural variantiVAR_042602179W → 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 rs757323641dbSNPEnsembl.1
Natural variantiVAR_016054218C → Y in MSD; loss of activity. 2 PublicationsCorresponds to variant rs137852854dbSNPEnsembl.1
Natural variantiVAR_019052224R → W in MSD; loss of activity. 1 PublicationCorresponds to variant rs759888604dbSNPEnsembl.1
Natural variantiVAR_019053259N → I in MSD; loss of activity. 1 PublicationCorresponds to variant rs764215221dbSNPEnsembl.1
Natural variantiVAR_019054266P → L in MSD; retains some activity. 1 PublicationCorresponds to variant rs763243827dbSNPEnsembl.1
Natural variantiVAR_016055279A → 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 rs137852849dbSNPEnsembl.1
Natural variantiVAR_016056336C → R in MSD; loss of activity. 3 PublicationsCorresponds to variant rs137852848dbSNPEnsembl.1
Natural variantiVAR_016057345R → C in MSD; retains some activity. 2 PublicationsCorresponds to variant rs137852852dbSNPEnsembl.1
Natural variantiVAR_016058348A → P in MSD; loss of activity. 2 PublicationsCorresponds to variant rs137852853dbSNPEnsembl.1
Natural variantiVAR_016059349R → Q in MSD; loss of activity. 3 PublicationsCorresponds to variant rs137852847dbSNPEnsembl.1
Natural variantiVAR_016060349R → 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 rs137852846dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0078771 – 90Missing in isoform 2. 1 PublicationAdd BLAST90
Alternative sequenceiVSP_045414149 – 173Missing in isoform 4. 1 PublicationAdd BLAST25
Alternative sequenceiVSP_045415319 – 338Missing in isoform 5. 1 PublicationAdd BLAST20
Alternative sequenceiVSP_013185340 – 374YCYRY…LPTMD → QEYYDPYFQDVASEMLRRHT ASRWKAFSSLEPCCSIRRHQ QYAAIERLTCGKFELRCASL RKIDCLNTNIACSYSMRQHG PRLHCVD in isoform 3. 1 PublicationAdd BLAST35

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.
CCDSiCCDS2564.1. [Q8NBK3-1]
CCDS54548.1. [Q8NBK3-4]
CCDS54549.1. [Q8NBK3-5]
RefSeqiNP_001158146.1. NM_001164674.1. [Q8NBK3-4]
NP_001158147.1. NM_001164675.1. [Q8NBK3-5]
NP_877437.2. NM_182760.3. [Q8NBK3-1]
UniGeneiHs.350475.

Genome annotation databases

EnsembliENST00000272902; ENSP00000272902; ENSG00000144455. [Q8NBK3-1]
ENST00000383843; ENSP00000373355; ENSG00000144455. [Q8NBK3-4]
ENST00000405420; ENSP00000384977; ENSG00000144455. [Q8NBK3-5]
GeneIDi285362.
KEGGihsa:285362.
UCSCiuc003bpz.3. human. [Q8NBK3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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.
CCDSiCCDS2564.1. [Q8NBK3-1]
CCDS54548.1. [Q8NBK3-4]
CCDS54549.1. [Q8NBK3-5]
RefSeqiNP_001158146.1. NM_001164674.1. [Q8NBK3-4]
NP_001158147.1. NM_001164675.1. [Q8NBK3-5]
NP_877437.2. NM_182760.3. [Q8NBK3-1]
UniGeneiHs.350475.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y1EX-ray1.73X73-374[»]
1Y1FX-ray1.80X73-374[»]
1Y1GX-ray1.67X73-374[»]
1Y1HX-ray1.67X73-374[»]
1Y1IX-ray2.61X73-374[»]
1Y1JX-ray1.55X73-374[»]
1Z70X-ray1.15X73-374[»]
2AFTX-ray1.66X86-371[»]
2AFYX-ray1.49X86-371[»]
2AIIX-ray1.54X86-371[»]
2AIJX-ray1.55X86-371[»]
2AIKX-ray1.73X86-371[»]
2HI8X-ray1.64X86-371[»]
2HIBX-ray2.00X86-371[»]
ProteinModelPortaliQ8NBK3.
SMRiQ8NBK3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi130091. 14 interactors.
IntActiQ8NBK3. 4 interactors.
MINTiMINT-4534860.
STRINGi9606.ENSP00000272902.

PTM databases

iPTMnetiQ8NBK3.
PhosphoSitePlusiQ8NBK3.

Polymorphism and mutation databases

BioMutaiSUMF1.
DMDMi62298562.

Proteomic databases

EPDiQ8NBK3.
MaxQBiQ8NBK3.
PaxDbiQ8NBK3.
PeptideAtlasiQ8NBK3.
PRIDEiQ8NBK3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000272902; ENSP00000272902; ENSG00000144455. [Q8NBK3-1]
ENST00000383843; ENSP00000373355; ENSG00000144455. [Q8NBK3-4]
ENST00000405420; ENSP00000384977; ENSG00000144455. [Q8NBK3-5]
GeneIDi285362.
KEGGihsa:285362.
UCSCiuc003bpz.3. human. [Q8NBK3-1]

Organism-specific databases

CTDi285362.
DisGeNETi285362.
GeneCardsiSUMF1.
HGNCiHGNC:20376. SUMF1.
HPAiHPA038025.
MalaCardsiSUMF1.
MIMi272200. phenotype.
607939. gene.
neXtProtiNX_Q8NBK3.
OpenTargetsiENSG00000144455.
Orphaneti585. Multiple sulfatase deficiency.
PharmGKBiPA134977552.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEYZ. Eukaryota.
COG1262. LUCA.
GeneTreeiENSGT00390000008983.
HOGENOMiHOG000135466.
HOVERGENiHBG054193.
InParanoidiQ8NBK3.
KOiK13444.
OMAiDTYEVSN.
OrthoDBiEOG091G0DD2.
PhylomeDBiQ8NBK3.
TreeFamiTF324027.

Enzyme and pathway databases

UniPathwayiUPA00910.
ReactomeiR-HSA-1660662. Glycosphingolipid metabolism.
R-HSA-1663150. The activation of arylsulfatases.

Miscellaneous databases

ChiTaRSiSUMF1. human.
EvolutionaryTraceiQ8NBK3.
GeneWikiiSUMF1.
GenomeRNAii285362.
PROiQ8NBK3.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000144455.
CleanExiHS_SUMF1.
ExpressionAtlasiQ8NBK3. baseline and differential.
GenevisibleiQ8NBK3. HS.

Family and domain databases

Gene3Di3.90.1580.10. 1 hit.
InterProiIPR016187. CTDL_fold.
IPR005532. SUMF_dom.
[Graphical view]
PfamiPF03781. FGE-sulfatase. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSUMF1_HUMAN
AccessioniPrimary (citable) accession number: Q8NBK3
Secondary accession number(s): B4DXK5
, B7XD05, E9PGL0, G5E9B0, Q0VAC6, Q0VAC7, Q2NL78, Q53ZE4, Q6UY39, Q96AK5, Q96DK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: March 29, 2005
Last modified: November 30, 2016
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.