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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi130 – 1301Calcium 21 Publication
Metal bindingi259 – 2591Calcium 11 Publication
Metal bindingi260 – 2601Calcium 1; via carbonyl oxygen1 Publication
Metal bindingi273 – 2731Calcium 11 Publication
Metal bindingi275 – 2751Calcium 1; via carbonyl oxygen1 Publication
Metal bindingi293 – 2931Calcium 2; via carbonyl oxygen1 Publication
Metal bindingi296 – 2961Calcium 2; via carbonyl oxygen1 Publication
Metal bindingi298 – 2981Calcium 2; via carbonyl oxygen1 Publication
Metal bindingi300 – 3001Calcium 21 Publication
Active sitei333 – 3331Proton acceptorCurated

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. oxidoreductase activity Source: UniProtKB-KW

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. glycosphingolipid metabolic process Source: Reactome
  3. post-translational protein modification Source: Reactome
  4. small molecule metabolic process Source: Reactome
  5. sphingolipid metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_116105. Glycosphingolipid metabolism.
REACT_121036. 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
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:20376. SUMF1.

Subcellular locationi

Endoplasmic reticulum lumen 2 Publications

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Multiple sulfatase deficiency3 Publications

The disease is caused by mutations affecting the gene represented in this entry. SUMF1 mutations result in defective post-translational modification of sulfatases.

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201L → F in MSD; loss of activity. 1 Publication
VAR_019050
Natural varianti155 – 1551S → P in MSD; loss of activity. 2 Publications
VAR_016053
Natural varianti177 – 1771A → 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
VAR_019051
Natural varianti179 – 1791W → 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
VAR_042602
Natural varianti218 – 2181C → Y in MSD; loss of activity. 2 Publications
VAR_016054
Natural varianti224 – 2241R → W in MSD; loss of activity. 1 Publication
VAR_019052
Natural varianti259 – 2591N → I in MSD; loss of activity. 1 Publication
VAR_019053
Natural varianti266 – 2661P → L in MSD; retains some activity. 1 Publication
VAR_019054
Natural varianti279 – 2791A → 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
VAR_016055
Natural varianti336 – 3361C → R in MSD; loss of activity. 3 Publications
VAR_016056
Natural varianti345 – 3451R → C in MSD; retains some activity. 2 Publications
VAR_016057
Natural varianti348 – 3481A → P in MSD; loss of activity. 2 Publications
VAR_016058
Natural varianti349 – 3491R → Q in MSD; loss of activity. 3 Publications
VAR_016059
Natural varianti349 – 3491R → 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
VAR_016060

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi333 – 3331S → A: Loss of activity. 1 Publication
Mutagenesisi333 – 3331S → T: Reduces activity by 99%. 1 Publication
Mutagenesisi336 – 3361C → S: Loss of activity. 1 Publication
Mutagenesisi337 – 3371H → A: Reduces activity 5-fold. 1 Publication
Mutagenesisi340 – 3401Y → F: No effect. 1 Publication
Mutagenesisi341 – 3411C → S: Loss of activity. 1 Publication

Keywords - Diseasei

Disease mutation, Ichthyosis, Leukodystrophy, Metachromatic leukodystrophy, Mucopolysaccharidosis

Organism-specific databases

MIMi272200. phenotype.
Orphaneti585. Multiple sulfatase deficiency.
PharmGKBiPA134977552.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 33331 PublicationAdd
BLAST
Chaini34 – 374341Sulfatase-modifying factor 1PRO_0000033456Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi50 ↔ 52
Glycosylationi141 – 1411N-linked (GlcNAc...)3 Publications
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

MaxQBiQ8NBK3.
PaxDbiQ8NBK3.
PRIDEiQ8NBK3.

PTM databases

PhosphoSiteiQ8NBK3.

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

BgeeiQ8NBK3.
CleanExiHS_SUMF1.
ExpressionAtlasiQ8NBK3. baseline and differential.
GenevestigatoriQ8NBK3.

Organism-specific databases

HPAiHPA038025.

Interactioni

Subunit structurei

Monomer, homodimer and heterodimer with SUMF2.3 Publications

Protein-protein interaction databases

BioGridi130091. 5 interactions.
IntActiQ8NBK3. 4 interactions.
MINTiMINT-4534860.
STRINGi9606.ENSP00000272902.

Structurei

Secondary structure

1
374
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi91 – 944Combined sources
Beta strandi97 – 1026Combined sources
Helixi109 – 1113Combined sources
Beta strandi117 – 1215Combined sources
Beta strandi124 – 1296Combined sources
Helixi133 – 14311Combined sources
Helixi148 – 1525Combined sources
Beta strandi154 – 1585Combined sources
Helixi159 – 1613Combined sources
Beta strandi180 – 1845Combined sources
Helixi211 – 22010Combined sources
Helixi228 – 2369Combined sources
Helixi252 – 2543Combined sources
Turni265 – 2673Combined sources
Beta strandi293 – 30513Combined sources
Beta strandi315 – 3173Combined sources
Beta strandi325 – 3317Combined sources
Turni338 – 3403Combined sources
Beta strandi350 – 3523Combined sources
Beta strandi366 – 3694Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 86-371.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8NBK3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni341 – 36020Interaction with sulfatasesAdd
BLAST

Sequence similaritiesi

Belongs to the sulfatase-modifying factor family.Curated

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

eggNOGiCOG1262.
GeneTreeiENSGT00390000008983.
HOGENOMiHOG000135466.
HOVERGENiHBG054193.
InParanoidiQ8NBK3.
KOiK13444.
OMAiYMCHKXG.
OrthoDBiEOG7VX8WN.
PhylomeDBiQ8NBK3.
TreeFamiTF324027.

Family and domain databases

Gene3Di3.90.1580.10. 1 hit.
InterProiIPR016187. C-type_lectin_fold.
IPR005532. FGE_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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti112 – 1121G → E in BAG63417. (PubMed:14702039)Curated
Sequence conflicti119 – 1191V → A in AAI21124. (PubMed:15489334)Curated
Sequence conflicti124 – 1241F → L in BAC11634. (PubMed:16303743)Curated
Sequence conflicti264 – 2641E → D in BAC11634. (PubMed:16303743)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201L → F in MSD; loss of activity. 1 Publication
VAR_019050
Natural varianti63 – 631S → N.2 Publications
Corresponds to variant rs2819590 [ dbSNP | Ensembl ].
VAR_016052
Natural varianti155 – 1551S → P in MSD; loss of activity. 2 Publications
VAR_016053
Natural varianti177 – 1771A → 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
VAR_019051
Natural varianti179 – 1791W → 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
VAR_042602
Natural varianti218 – 2181C → Y in MSD; loss of activity. 2 Publications
VAR_016054
Natural varianti224 – 2241R → W in MSD; loss of activity. 1 Publication
VAR_019052
Natural varianti259 – 2591N → I in MSD; loss of activity. 1 Publication
VAR_019053
Natural varianti266 – 2661P → L in MSD; retains some activity. 1 Publication
VAR_019054
Natural varianti279 – 2791A → 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
VAR_016055
Natural varianti336 – 3361C → R in MSD; loss of activity. 3 Publications
VAR_016056
Natural varianti345 – 3451R → C in MSD; retains some activity. 2 Publications
VAR_016057
Natural varianti348 – 3481A → P in MSD; loss of activity. 2 Publications
VAR_016058
Natural varianti349 – 3491R → Q in MSD; loss of activity. 3 Publications
VAR_016059
Natural varianti349 – 3491R → 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
VAR_016060

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9090Missing in isoform 2. 1 PublicationVSP_007877Add
BLAST
Alternative sequencei149 – 17325Missing in isoform 4. 1 PublicationVSP_045414Add
BLAST
Alternative sequencei319 – 33820Missing in isoform 5. 1 PublicationVSP_045415Add
BLAST
Alternative sequencei340 – 37435YCYRY…LPTMD → QEYYDPYFQDVASEMLRRHT ASRWKAFSSLEPCCSIRRHQ QYAAIERLTCGKFELRCASL RKIDCLNTNIACSYSMRQHG PRLHCVD in isoform 3. 1 PublicationVSP_013185Add
BLAST

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.2. human. [Q8NBK3-1]
uc011ass.2. human.

Polymorphism databases

DMDMi62298562.

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
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. Positions 86-371.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi130091. 5 interactions.
IntActiQ8NBK3. 4 interactions.
MINTiMINT-4534860.
STRINGi9606.ENSP00000272902.

PTM databases

PhosphoSiteiQ8NBK3.

Polymorphism databases

DMDMi62298562.

Proteomic databases

MaxQBiQ8NBK3.
PaxDbiQ8NBK3.
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.2. human. [Q8NBK3-1]
uc011ass.2. human.

Organism-specific databases

CTDi285362.
GeneCardsiGC03M003742.
HGNCiHGNC:20376. SUMF1.
HPAiHPA038025.
MIMi272200. phenotype.
607939. gene.
neXtProtiNX_Q8NBK3.
Orphaneti585. Multiple sulfatase deficiency.
PharmGKBiPA134977552.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1262.
GeneTreeiENSGT00390000008983.
HOGENOMiHOG000135466.
HOVERGENiHBG054193.
InParanoidiQ8NBK3.
KOiK13444.
OMAiYMCHKXG.
OrthoDBiEOG7VX8WN.
PhylomeDBiQ8NBK3.
TreeFamiTF324027.

Enzyme and pathway databases

UniPathwayiUPA00910.
ReactomeiREACT_116105. Glycosphingolipid metabolism.
REACT_121036. The activation of arylsulfatases.

Miscellaneous databases

ChiTaRSiSUMF1. human.
EvolutionaryTraceiQ8NBK3.
GeneWikiiSUMF1.
GenomeRNAii285362.
NextBioi95470.
PROiQ8NBK3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NBK3.
CleanExiHS_SUMF1.
ExpressionAtlasiQ8NBK3. baseline and differential.
GenevestigatoriQ8NBK3.

Family and domain databases

Gene3Di3.90.1580.10. 1 hit.
InterProiIPR016187. C-type_lectin_fold.
IPR005532. FGE_dom.
[Graphical view]
PfamiPF03781. FGE-sulfatase. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
  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.
  3. "Characterization of the arylsulfatase I (ARSI) gene preferentially expressed in the human retinal pigment epithelium cell line ARPE-19."
    Oshikawa M., Usami R., Kato S.
    Mol. Vis. 15:482-494(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT ASN-63.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
    Tissue: Gastric mucosa and Testis.
  6. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta.
  7. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
    Tissue: Colon and Prostate.
  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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  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, IDENTIFICATION BY MASS SPECTROMETRY, CALCIUM-BINDING, GLYCOSYLATION AT ASN-141, SUBCELLULAR LOCATION, DISULFIDE BONDS.
  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, GLYCOSYLATION AT ASN-141, MUTAGENESIS OF SER-333; CYS-336; HIS-337; TYR-340 AND CYS-341, DISULFIDE BONDS.
  13. "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.
    Tissue: Liver.
  14. "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.
  15. 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.
  16. "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.

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: February 4, 2015
This is version 127 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

External Data

Dasty 3

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 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.