Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
A cDNA clone for human glucosamine-6-sulphatase reveals differences between arylsulphatases and non-arylsulphatases.
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GNS (glucosamine-6-sulphatase) is a lysosomal exo-hydrolase required for degradation of heparan sulphate and keratan sulphate; its deficiency causes MPS IIID with lysosomal storage of heparan sulphate. The full 552-aa precursor with a 36-aa leader was cloned and its catalytic activity (EC 3.1.6.14) established.
"Glucosamine-6-sulphatase is an exo-hydrolase required for the lysosomal degradation of heparan sulphate and keratan sulphate."
Purification of a 75 kDa protein from the organelle matrix of human neutrophils and identification as N-acetylglucosamine-6-sulphatase.
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A 75 kDa neutrophil granule-matrix protein was purified and identified by MS as N-acetylglucosamine-6-sulphatase (EC 3.1.6.14), with confirmed activity toward N-acetylglucosamine-6-sulphate and O-desulphation of heparan-sulphate-derived saccharides; it localizes to primary (azurophil) granules and is released on PMA stimulation.
"identified the protein to be N-acetylglucosamine-6-sulphatase (EC 3.1.6.14). The identity of the protein was confirmed by demostrating enzymatic activity towards the substrate N-acetylglucosamine 6-sulphate."
Sulphatase activities are regulated by the interaction of sulphatase-modifying factor 1 with SUMF2.
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GNS is a formylglycine-dependent sulphatase; it was among the sulphatases whose activity is enhanced by SUMF1 (formylglycine-generating enzyme) and modulated by SUMF2. Supports the broad sulfuric-ester-hydrolase annotation, which is best refined to the specific GlcNAc-6-sulfatase activity.
"we transfected Cos7 cells with several sulphatase cDNAs ( ARSA , ARSC , ARSF , IDS , SGSH , GALNS , GNS )"
Systematic identification of SH3 domain-mediated human protein-protein interactions by peptide array target screening.
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GNS appears as a peptide-array hit for SH3 domains (including NCK1) in a proteome-wide screen. This underlies the bare "protein binding" IPI, which is uninformative about GNS's molecular function.
"A group of 12 Src homology (SH) 3 domains from eight human proteins (Swiss-Prot ID: SRC, PLCG1, P85A, NCK1, GRB2, FYN, CRK) were used to screen a peptide target array"
In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.
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GNS was detected among ~900 proteins in a shotgun-proteomics survey of urinary prostatic- secretion exosomes, underlying the extracellular-exosome location annotation.
"In pooled EPS-urine exosome samples, ~900 proteins were detected."
Human liver N-acetylglucosamine-6-sulphate sulphatase. Catalytic properties.
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Human liver GNS is a highly specific exo-sulfatase for glucosamine-6-sulphate / glucose-6- sulphate residues, desulfating keratan-sulphate- and heparin-derived substrates; it shows no activity toward internal sulphate ester bonds, and sulphate/phosphate ions are potent inhibitors.
"Both forms A and B are exo-enzymes, since activity towards internal sulphate ester bonds was not observed."
GNS:Ca2+ cleaves sulfate from GlcNAc-6-sulfate units of keratan sulfate
Defective GNS does not hydrolyse 6-sulfate from GlcNAc6S
Exocytosis of azurophil granule lumen proteins
Exocytosis of ficolin-rich granule lumen proteins
UniProtKB entry P15586 (GNS_HUMAN)
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UniProt records GNS as a lysosomal N-acetylglucosamine-6-sulfatase (EC 3.1.6.14) that hydrolyzes 6-sulfate groups of N-acetyl-D-glucosaminide units of heparan and keratan sulfate, requires a catalytic formylglycine (3-oxoalanine) residue, and whose deficiency causes MPS IIID.
"Hydrolyzes 6-sulfate groups in N-acetyl-d-glucosaminide units"