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Q8NBK3 (SUMF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sulfatase-modifying factor 1

EC=1.8.99.-
Alternative name(s):
C-alpha-formylglycine-generating enzyme 1
Gene names
Name:SUMF1
Synonyms:FGE
ORF Names:PSEC0152, UNQ3037/PRO9852
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.11

Catalytic activity

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

Pathway

Protein modification; sulfatase oxidation.

Subunit structure

Monomer, homodimer and heterodimer with SUMF2. Ref.10

Subcellular location

Endoplasmic reticulum lumen Ref.10 Ref.11.

Tissue specificity

Ubiquitous. Highly expressed in kidney, pancreas and liver. Detected at lower levels in leukocytes, lung, placenta, small intestine, skeletal muscle and heart. Ref.10

Post-translational modification

N-glycosylated. Contains high-mannose-type oligosaccharides. Ref.11 Ref.12

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. SUMF1 mutations result in defective post-translational modification of sulfatases. Ref.1 Ref.2 Ref.15 Ref.16

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.

Sequence similarities

Belongs to the sulfatase-modifying factor family.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8NBK3-1)

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.
Isoform 2 (identifier: Q8NBK3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-90: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8NBK3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     340-374: YCYRYRCAARSQNTPDSSASNLGFRCAADRLPTMD → QEYYDPYFQD...QHGPRLHCVD
Isoform 4 (identifier: Q8NBK3-4)

The sequence of this isoform differs from the canonical sequence as follows:
     149-173: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q8NBK3-5)

The sequence of this isoform differs from the canonical sequence as follows:
     319-338: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Ref.11
Chain34 – 374341Sulfatase-modifying factor 1
PRO_0000033456

Regions

Region341 – 36020Interaction with sulfatases

Sites

Active site3331Proton acceptor Probable
Metal binding1301Calcium 2
Metal binding2591Calcium 1
Metal binding2601Calcium 1; via carbonyl oxygen
Metal binding2731Calcium 1
Metal binding2751Calcium 1; via carbonyl oxygen
Metal binding2931Calcium 2; via carbonyl oxygen
Metal binding2961Calcium 2; via carbonyl oxygen
Metal binding2981Calcium 2; via carbonyl oxygen
Metal binding3001Calcium 2

Amino acid modifications

Glycosylation1411N-linked (GlcNAc...) Ref.11 Ref.12 Ref.13
Disulfide bond50 ↔ 52 Ref.11 Ref.12
Disulfide bond218 ↔ 365 Ref.11 Ref.12
Disulfide bond235 ↔ 346 Ref.11 Ref.12
Disulfide bond336 ↔ 341Redox-active Ref.11 Ref.12

Natural variations

Alternative sequence1 – 9090Missing in isoform 2.
VSP_007877
Alternative sequence149 – 17325Missing in isoform 4.
VSP_045414
Alternative sequence319 – 33820Missing in isoform 5.
VSP_045415
Alternative sequence340 – 37435YCYRY…LPTMD → QEYYDPYFQDVASEMLRRHT ASRWKAFSSLEPCCSIRRHQ QYAAIERLTCGKFELRCASL RKIDCLNTNIACSYSMRQHG PRLHCVD in isoform 3.
VSP_013185
Natural variant201L → F in MSD; loss of activity. Ref.15
VAR_019050
Natural variant631S → N. Ref.1 Ref.4
Corresponds to variant rs2819590 [ dbSNP | Ensembl ].
VAR_016052
Natural variant1551S → P in MSD; loss of activity. Ref.2 Ref.15
VAR_016053
Natural variant1771A → 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. Ref.15 Ref.16
VAR_019051
Natural variant1791W → 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. Ref.16
VAR_042602
Natural variant2181C → Y in MSD; loss of activity. Ref.2 Ref.15
VAR_016054
Natural variant2241R → W in MSD; loss of activity. Ref.15
VAR_019052
Natural variant2591N → I in MSD; loss of activity. Ref.15
VAR_019053
Natural variant2661P → L in MSD; retains some activity. Ref.15
VAR_019054
Natural variant2791A → 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. Ref.1 Ref.15 Ref.16
VAR_016055
Natural variant3361C → R in MSD; loss of activity. Ref.1 Ref.2 Ref.15
VAR_016056
Natural variant3451R → C in MSD; retains some activity. Ref.2 Ref.15
VAR_016057
Natural variant3481A → P in MSD; loss of activity. Ref.2 Ref.15
VAR_016058
Natural variant3491R → Q in MSD; loss of activity. Ref.1 Ref.2 Ref.15
VAR_016059
Natural variant3491R → 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. Ref.1 Ref.2 Ref.15 Ref.16
VAR_016060

Experimental info

Mutagenesis3331S → A: Loss of activity. Ref.12
Mutagenesis3331S → T: Reduces activity by 99%. Ref.12
Mutagenesis3361C → S: Loss of activity. Ref.12
Mutagenesis3371H → A: Reduces activity 5-fold. Ref.12
Mutagenesis3401Y → F: No effect. Ref.12
Mutagenesis3411C → S: Loss of activity. Ref.12
Sequence conflict1121G → E in BAG63417. Ref.5
Sequence conflict1191V → A in AAI21124. Ref.9
Sequence conflict1241F → L in BAC11634. Ref.6
Sequence conflict2641E → D in BAC11634. Ref.6

Secondary structure

........................................ 374
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 29, 2005. Version 3.
Checksum: E64F2DF004C8CEA3

FASTA37440,556
        10         20         30         40         50         60 
MAAPALGLVC GRCPELGLVL LLLLLSLLCG AAGSQEAGTG AGAGSLAGSC GCGTPQRPGA 

        70         80         90        100        110        120 
HGSSAAAHRY SREANAPGPV PGERQLAHSK MVPIPAGVFT MGTDDPQIKQ DGEAPARRVT 

       130        140        150        160        170        180 
IDAFYMDAYE VSNTEFEKFV NSTGYLTEAE KFGDSFVFEG MLSEQVKTNI QQAVAAAPWW 

       190        200        210        220        230        240 
LPVKGANWRH PEGPDSTILH RPDHPVLHVS WNDAVAYCTW AGKRLPTEAE WEYSCRGGLH 

       250        260        270        280        290        300 
NRLFPWGNKL QPKGQHYANI WQGEFPVTNT GEDGFQGTAP VDAFPPNGYG LYNIVGNAWE 

       310        320        330        340        350        360 
WTSDWWTVHH SVEETLNPKG PPSGKDRVKK GGSYMCHRSY CYRYRCAARS QNTPDSSASN 

       370 
LGFRCAADRL PTMD 

« Hide

Isoform 2 [UniParc].

Checksum: E616A28A77F81996
Show »

FASTA28431,900
Isoform 3 [UniParc].

Checksum: 957E7E1E13D034A6
Show »

FASTA42646,857
Isoform 4 [UniParc].

Checksum: 4C5192677FABF9CC
Show »

FASTA34937,770
Isoform 5 [UniParc].

Checksum: AB2E4103EAC0E027
Show »

FASTA35438,386

References

« Hide 'large scale' references
[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]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Molecular and functional analysis of SUMF1 mutations in multiple sulfatase deficiency."
Cosma M.P., Pepe S., Parenti G., Settembre C., Annunziata I., Wade-Martins R., Domenico C.D., Natale P.D., Mankad A., Cox B., Uziel G., Mancini G.M., Zammarchi E., Donati M.A., Kleijer W.J., Filocamo M., Carrozzo R., Carella M., Ballabio A.
Hum. Mutat. 23:576-581(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MSD PHE-20; PRO-177; TRP-224; ILE-259 AND LEU-266, CHARACTERIZATION OF VARIANTS MSD PHE-20; PRO-155; PRO-177; TYR-218; TRP-224; ILE-259; LEU-266; VAL-279; ARG-336; CYS-345; PRO-348; TRP-349 AND GLN-349.
[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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001158146.1. NM_001164674.1.
NP_001158147.1. NM_001164675.1.
NP_877437.2. NM_182760.3.
UniGeneHs.350475.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ8NBK3.
SMRQ8NBK3. Positions 86-371.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid130091. 1 interaction.
IntActQ8NBK3. 4 interactions.
MINTMINT-4534860.
STRING9606.ENSP00000272902.

PTM databases

PhosphoSiteQ8NBK3.

Polymorphism databases

DMDM62298562.

Proteomic databases

PaxDbQ8NBK3.
PRIDEQ8NBK3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000272902; ENSP00000272902; ENSG00000144455. [Q8NBK3-1]
ENST00000383843; ENSP00000373355; ENSG00000144455. [Q8NBK3-4]
ENST00000405420; ENSP00000384977; ENSG00000144455. [Q8NBK3-5]
GeneID285362.
KEGGhsa:285362.
UCSCuc003bpz.2. human. [Q8NBK3-1]
uc011ass.2. human.

Organism-specific databases

CTD285362.
GeneCardsGC03M003742.
HGNCHGNC:20376. SUMF1.
HPAHPA038025.
MIM272200. phenotype.
607939. gene.
neXtProtNX_Q8NBK3.
Orphanet585. Multiple sulfatase deficiency.
PharmGKBPA134977552.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1262.
HOGENOMHOG000135466.
HOVERGENHBG054193.
KOK13444.
OMAYMCHKXG.
OrthoDBEOG7VX8WN.
PhylomeDBQ8NBK3.
TreeFamTF324027.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_17015. Metabolism of proteins.
UniPathwayUPA00910.

Gene expression databases

ArrayExpressQ8NBK3.
BgeeQ8NBK3.
CleanExHS_SUMF1.
GenevestigatorQ8NBK3.

Family and domain databases

Gene3D3.90.1580.10. 1 hit.
InterProIPR016187. C-type_lectin_fold.
IPR005532. FGE_dom.
[Graphical view]
PfamPF03781. FGE-sulfatase. 1 hit.
[Graphical view]
SUPFAMSSF56436. SSF56436. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSUMF1. human.
EvolutionaryTraceQ8NBK3.
GeneWikiSUMF1.
GenomeRNAi285362.
NextBio95470.
PROQ8NBK3.
SOURCESearch...

Entry information

Entry nameSUMF1_HUMAN
AccessionPrimary (citable) accession number: Q8NBK3
Secondary accession number(s): B4DXK5 expand/collapse secondary AC list , B7XD05, E9PGL0, G5E9B0, Q0VAC6, Q0VAC7, Q2NL78, Q53ZE4, Q6UY39, Q96AK5, Q96DK8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: March 29, 2005
Last modified: April 16, 2014
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM