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Q8NBK3

- SUMF1_HUMAN

UniProt

Q8NBK3 - SUMF1_HUMAN

Protein

Sulfatase-modifying factor 1

Gene

SUMF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 3 (29 Mar 2005)
      Previous versions | rss
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    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

    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

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Involvement in diseasei

    Multiple sulfatase deficiency (MSD) [MIM:272200]: A 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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry. SUMF1 mutations result in defective post-translational modification of sulfatases.
    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. 1 Publication
    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. 1 Publication
    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.
    VAR_042602
    Natural varianti218 – 2181C → Y in MSD; loss of activity. 1 Publication
    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. 1 Publication
    VAR_016055
    Natural varianti336 – 3361C → R in MSD; loss of activity. 2 Publications
    VAR_016056
    Natural varianti345 – 3451R → C in MSD; retains some activity. 1 Publication
    VAR_016057
    Natural varianti348 – 3481A → P in MSD; loss of activity. 1 Publication
    VAR_016058
    Natural varianti349 – 3491R → Q in MSD; loss of activity. 2 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. 2 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

    ArrayExpressiQ8NBK3.
    BgeeiQ8NBK3.
    CleanExiHS_SUMF1.
    GenevestigatoriQ8NBK3.

    Organism-specific databases

    HPAiHPA038025.

    Interactioni

    Subunit structurei

    Monomer, homodimer and heterodimer with SUMF2.3 Publications

    Protein-protein interaction databases

    BioGridi130091. 1 interaction.
    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 – 944
    Beta strandi97 – 1026
    Helixi109 – 1113
    Beta strandi117 – 1215
    Beta strandi124 – 1296
    Helixi133 – 14311
    Helixi148 – 1525
    Beta strandi154 – 1585
    Helixi159 – 1613
    Beta strandi180 – 1845
    Helixi211 – 22010
    Helixi228 – 2369
    Helixi252 – 2543
    Turni265 – 2673
    Beta strandi293 – 30513
    Beta strandi315 – 3173
    Beta strandi325 – 3317
    Turni338 – 3403
    Beta strandi350 – 3523
    Beta strandi366 – 3694

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000135466.
    HOVERGENiHBG054193.
    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

    MAAPALGLVC GRCPELGLVL LLLLLSLLCG AAGSQEAGTG AGAGSLAGSC    50
    GCGTPQRPGA HGSSAAAHRY SREANAPGPV PGERQLAHSK MVPIPAGVFT 100
    MGTDDPQIKQ DGEAPARRVT IDAFYMDAYE VSNTEFEKFV NSTGYLTEAE 150
    KFGDSFVFEG MLSEQVKTNI QQAVAAAPWW LPVKGANWRH PEGPDSTILH 200
    RPDHPVLHVS WNDAVAYCTW AGKRLPTEAE WEYSCRGGLH NRLFPWGNKL 250
    QPKGQHYANI WQGEFPVTNT GEDGFQGTAP VDAFPPNGYG LYNIVGNAWE 300
    WTSDWWTVHH SVEETLNPKG PPSGKDRVKK GGSYMCHRSY CYRYRCAARS 350
    QNTPDSSASN LGFRCAADRL PTMD 374
    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. 1 Publication
    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. 1 Publication
    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.
    VAR_042602
    Natural varianti218 – 2181C → Y in MSD; loss of activity. 1 Publication
    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. 1 Publication
    VAR_016055
    Natural varianti336 – 3361C → R in MSD; loss of activity. 2 Publications
    VAR_016056
    Natural varianti345 – 3451R → C in MSD; retains some activity. 1 Publication
    VAR_016057
    Natural varianti348 – 3481A → P in MSD; loss of activity. 1 Publication
    VAR_016058
    Natural varianti349 – 3491R → Q in MSD; loss of activity. 2 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. 2 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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 ]
    UniGenei Hs.350475.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali Q8NBK3.
    SMRi Q8NBK3. Positions 86-371.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 130091. 1 interaction.
    IntActi Q8NBK3. 4 interactions.
    MINTi MINT-4534860.
    STRINGi 9606.ENSP00000272902.

    PTM databases

    PhosphoSitei Q8NBK3.

    Polymorphism databases

    DMDMi 62298562.

    Proteomic databases

    MaxQBi Q8NBK3.
    PaxDbi Q8NBK3.
    PRIDEi Q8NBK3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

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

    Organism-specific databases

    CTDi 285362.
    GeneCardsi GC03M003742.
    HGNCi HGNC:20376. SUMF1.
    HPAi HPA038025.
    MIMi 272200. phenotype.
    607939. gene.
    neXtProti NX_Q8NBK3.
    Orphaneti 585. Multiple sulfatase deficiency.
    PharmGKBi PA134977552.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1262.
    HOGENOMi HOG000135466.
    HOVERGENi HBG054193.
    KOi K13444.
    OMAi YMCHKXG.
    OrthoDBi EOG7VX8WN.
    PhylomeDBi Q8NBK3.
    TreeFami TF324027.

    Enzyme and pathway databases

    UniPathwayi UPA00910 .
    Reactomei REACT_116105. Glycosphingolipid metabolism.
    REACT_121036. The activation of arylsulfatases.

    Miscellaneous databases

    ChiTaRSi SUMF1. human.
    EvolutionaryTracei Q8NBK3.
    GeneWikii SUMF1.
    GenomeRNAii 285362.
    NextBioi 95470.
    PROi Q8NBK3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8NBK3.
    Bgeei Q8NBK3.
    CleanExi HS_SUMF1.
    Genevestigatori Q8NBK3.

    Family and domain databases

    Gene3Di 3.90.1580.10. 1 hit.
    InterProi IPR016187. C-type_lectin_fold.
    IPR005532. FGE_dom.
    [Graphical view ]
    Pfami PF03781. FGE-sulfatase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56436. SSF56436. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 123 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