Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P15586 (GNS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-acetylglucosamine-6-sulfatase

EC=3.1.6.14
Alternative name(s):
Glucosamine-6-sulfatase
Short name=G6S
Gene names
Name:GNS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length552 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolysis of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subcellular location

Lysosome.

Post-translational modification

The form A (78 kDa) is processed by internal peptidase cleavage to a 32 kDa N-terminal species (form B) and a 48 kDa C-terminal species.

The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity By similarity.

Involvement in disease

Mucopolysaccharidosis 3D (MPS3D) [MIM:252940]: A form of mucopolysaccharidosis type 3, an autosomal recessive lysosomal storage disease due to impaired degradation of heparan sulfate. MPS3 is characterized by severe central nervous system degeneration, but only mild somatic disease. Onset of clinical features usually occurs between 2 and 6 years; severe neurologic degeneration occurs in most patients between 6 and 10 years of age, and death occurs typically during the second or third decade of life.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.10

Sequence similarities

Belongs to the sulfatase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCK1P163332EBI-1752200,EBI-389883

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3636
Chain37 – 552516N-acetylglucosamine-6-sulfatase
PRO_0000033413

Sites

Metal binding551Calcium By similarity
Metal binding561Calcium By similarity
Metal binding911Calcium; via 3-oxoalanine By similarity
Metal binding3261Calcium By similarity
Metal binding3271Calcium By similarity

Amino acid modifications

Modified residue9113-oxoalanine (Cys) By similarity
Glycosylation1111N-linked (GlcNAc...) Potential
Glycosylation1171N-linked (GlcNAc...) Potential
Glycosylation1831N-linked (GlcNAc...) Ref.6 Ref.7
Glycosylation1981N-linked (GlcNAc...) Potential
Glycosylation2101N-linked (GlcNAc...) Potential
Glycosylation2791N-linked (GlcNAc...) Ref.6
Glycosylation3171N-linked (GlcNAc...) Ref.7
Glycosylation3621N-linked (GlcNAc...) Potential
Glycosylation3871N-linked (GlcNAc...) Ref.7
Glycosylation4051N-linked (GlcNAc...) Potential
Glycosylation4221N-linked (GlcNAc...) Ref.1 Ref.7
Glycosylation4491N-linked (GlcNAc...) Potential
Glycosylation4801N-linked (GlcNAc...) Potential

Natural variations

Natural variant941S → I in MPS3D. Ref.10
VAR_064070
Natural variant304 – 3063Missing in MPS3D.
VAR_064071
Natural variant3401K → R in MPS3D. Ref.10
VAR_064072
Natural variant4181G → E in MPS3D. Ref.10
VAR_064073
Natural variant5501H → Q.
Corresponds to variant rs2230292 [ dbSNP | Ensembl ].
VAR_064074

Experimental info

Sequence conflict2521F → C in BAD97204. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P15586 [UniParc].

Last modified April 1, 1993. Version 3.
Checksum: 85094043F6E64468

FASTA55262,082
        10         20         30         40         50         60 
MRLLPLAPGR LRRGSPRHLP SCSPALLLLV LGGCLGVFGV AAGTRRPNVV LLLTDDQDEV 

        70         80         90        100        110        120 
LGGMTPLKKT KALIGEMGMT FSSAYVPSAL CCPSRASILT GKYPHNHHVV NNTLEGNCSS 

       130        140        150        160        170        180 
KSWQKIQEPN TFPAILRSMC GYQTFFAGKY LNEYGAPDAG GLEHVPLGWS YWYALEKNSK 

       190        200        210        220        230        240 
YYNYTLSING KARKHGENYS VDYLTDVLAN VSLDFLDYKS NFEPFFMMIA TPAPHSPWTA 

       250        260        270        280        290        300 
APQYQKAFQN VFAPRNKNFN IHGTNKHWLI RQAKTPMTNS SIQFLDNAFR KRWQTLLSVD 

       310        320        330        340        350        360 
DLVEKLVKRL EFTGELNNTY IFYTSDNGYH TGQFSLPIDK RQLYEFDIKV PLLVRGPGIK 

       370        380        390        400        410        420 
PNQTSKMLVA NIDLGPTILD IAGYDLNKTQ MDGMSLLPIL RGASNLTWRS DVLVEYQGEG 

       430        440        450        460        470        480 
RNVTDPTCPS LSPGVSQCFP DCVCEDAYNN TYACVRTMSA LWNLQYCEFD DQEVFVEVYN 

       490        500        510        520        530        540 
LTADPDQITN IAKTIDPELL GKMNYRLMML QSCSGPTCRT PGVFDPGYRF DPRLMFSNRG 

       550 
SVRTRRFSKH LL 

« Hide

References

« Hide 'large scale' references
[1]"A cDNA clone for human glucosamine-6-sulphatase reveals differences between arylsulphatases and non-arylsulphatases."
Robertson D.A., Freeman C., Morris C.P., Hopwood J.J.
Biochem. J. 288:539-544(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-422.
Tissue: Endothelial cell.
[2]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., 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. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
Tissue: Urinary bladder.
[5]"Human glucosamine-6-sulfatase cDNA reveals homology with steroid sulfatase."
Robertson D.A., Freeman C., Nelson P.V., Morris C.P., Hopwood J.J.
Biochem. Biophys. Res. Commun. 157:218-224(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 178-552, PARTIAL PROTEIN SEQUENCE.
[6]"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Zhang H., Li X.-J., Martin D.B., Aebersold R.
Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-183 AND ASN-279.
[7]"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-183; ASN-317; ASN-387 AND ASN-422.
Tissue: Liver.
[8]"Genomic basis of mucopolysaccharidosis type IIID (MIM 252940) revealed by sequencing of GNS encoding N-acetylglucosamine-6-sulfatase."
Mok A., Cao H., Hegele R.A.
Genomics 81:1-5(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MPS3D.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Mucopolysaccharidosis type IIID: 12 new patients and 15 novel mutations."
Valstar M.J., Bertoli-Avella A.M., Wessels M.W., Ruijter G.J.G., de Graaf B., Olmer R., Elfferich P., Neijs S., Kariminejad R., Suheyl Ezgue F., Tokatli A., Czartoryska B., Bosschaart A.N., van den Bos-Terpstra F., Puissant H., Buerger F., Omran H., Eckert D. expand/collapse author list , Filocamo M., Simeonov E., Willems P.J., Wevers R.A., Niermeijer M.F., Halley D.J.J., Poorthuis B.J.H.M., van Diggelen O.P.
Hum. Mutat. 31:E1348-E1360(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MPS3D ILE-94; 304-GLU--LEU-306 DEL; ARG-340 AND GLU-418.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z12173 mRNA. Translation: CAA78164.1.
AK223484 mRNA. Translation: BAD97204.1.
AC025262 Genomic DNA. No translation available.
BC012482 mRNA. Translation: AAH12482.1.
CCDSCCDS8970.1.
PIRKJHUGU. S27164.
RefSeqNP_002067.1. NM_002076.3.
UniGeneHs.334534.

3D structure databases

ProteinModelPortalP15586.
SMRP15586. Positions 46-492.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109061. 21 interactions.
IntActP15586. 7 interactions.
STRING9606.ENSP00000258145.

PTM databases

PhosphoSiteP15586.

Polymorphism databases

DMDM232126.

Proteomic databases

MaxQBP15586.
PaxDbP15586.
PeptideAtlasP15586.
PRIDEP15586.

Protocols and materials databases

DNASU2799.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000258145; ENSP00000258145; ENSG00000135677.
GeneID2799.
KEGGhsa:2799.
UCSCuc001ssg.4. human.

Organism-specific databases

CTD2799.
GeneCardsGC12M065107.
H-InvDBHIX0010785.
HGNCHGNC:4422. GNS.
HPACAB026011.
HPA013695.
MIM252940. phenotype.
607664. gene.
neXtProtNX_P15586.
Orphanet79272. Sanfilippo syndrome type D.
PharmGKBPA28802.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3119.
HOGENOMHOG000169239.
HOVERGENHBG005840.
InParanoidP15586.
KOK01137.
OrthoDBEOG75QR3Q.
PhylomeDBP15586.
TreeFamTF313545.

Enzyme and pathway databases

BioCycMetaCyc:HS06046-MONOMER.
BRENDA3.1.6.14. 2681.
ReactomeREACT_111217. Metabolism.
REACT_11123. Membrane Trafficking.
REACT_116125. Disease.
SABIO-RKP15586.

Gene expression databases

ArrayExpressP15586.
BgeeP15586.
CleanExHS_GNS.
GenevestigatorP15586.

Family and domain databases

Gene3D3.40.720.10. 3 hits.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR012251. GlcNAc_6-SO4ase.
IPR015981. GlcNAc_6-SO4ase_euk.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]
PANTHERPTHR10342:SF212. PTHR10342:SF212. 1 hit.
PfamPF00884. Sulfatase. 1 hit.
[Graphical view]
PIRSFPIRSF036666. G6S. 1 hit.
SUPFAMSSF53649. SSF53649. 2 hits.
PROSITEPS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGNS. human.
GenomeRNAi2799.
NextBio11033.
PROP15586.
SOURCESearch...

Entry information

Entry nameGNS_HUMAN
AccessionPrimary (citable) accession number: P15586
Secondary accession number(s): Q53F05
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1993
Last modified: July 9, 2014
This is version 136 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

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 12

Human chromosome 12: entries, gene names and cross-references to MIM