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P15586

- GNS_HUMAN

UniProt

P15586 - GNS_HUMAN

Protein

N-acetylglucosamine-6-sulfatase

Gene

GNS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 3 (01 Apr 1993)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 1 calcium ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi55 – 551CalciumBy similarity
    Metal bindingi56 – 561CalciumBy similarity
    Metal bindingi91 – 911Calcium; via 3-oxoalanineBy similarity
    Metal bindingi326 – 3261CalciumBy similarity
    Metal bindingi327 – 3271CalciumBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. N-acetylglucosamine-6-sulfatase activity Source: ProtInc
    3. protein binding Source: IntAct
    4. sulfuric ester hydrolase activity Source: MGI

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. glycosaminoglycan catabolic process Source: ProtInc
    3. glycosaminoglycan metabolic process Source: Reactome
    4. keratan sulfate catabolic process Source: Reactome
    5. keratan sulfate metabolic process Source: Reactome
    6. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06046-MONOMER.
    BRENDAi3.1.6.14. 2681.
    ReactomeiREACT_121313. Keratan sulfate degradation.
    REACT_19287. Lysosome Vesicle Biogenesis.
    SABIO-RKP15586.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-acetylglucosamine-6-sulfatase (EC:3.1.6.14)
    Alternative name(s):
    Glucosamine-6-sulfatase
    Short name:
    G6S
    Gene namesi
    Name:GNS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:4422. GNS.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. lysosomal lumen Source: Reactome

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Involvement in diseasei

    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti94 – 941S → I in MPS3D. 1 Publication
    VAR_064070
    Natural varianti304 – 3063Missing in MPS3D.
    VAR_064071
    Natural varianti340 – 3401K → R in MPS3D. 1 Publication
    VAR_064072
    Natural varianti418 – 4181G → E in MPS3D. 1 Publication
    VAR_064073

    Keywords - Diseasei

    Disease mutation, Mucopolysaccharidosis

    Organism-specific databases

    MIMi252940. phenotype.
    Orphaneti79272. Sanfilippo syndrome type D.
    PharmGKBiPA28802.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3636Add
    BLAST
    Chaini37 – 552516N-acetylglucosamine-6-sulfatasePRO_0000033413Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei91 – 9113-oxoalanine (Cys)By similarity
    Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi183 – 1831N-linked (GlcNAc...)2 Publications
    Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi210 – 2101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi279 – 2791N-linked (GlcNAc...)1 Publication
    Glycosylationi317 – 3171N-linked (GlcNAc...)1 Publication
    Glycosylationi362 – 3621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi387 – 3871N-linked (GlcNAc...)1 Publication
    Glycosylationi405 – 4051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi422 – 4221N-linked (GlcNAc...)2 Publications
    Glycosylationi449 – 4491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi480 – 4801N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    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

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiP15586.
    PaxDbiP15586.
    PeptideAtlasiP15586.
    PRIDEiP15586.

    PTM databases

    PhosphoSiteiP15586.

    Expressioni

    Gene expression databases

    ArrayExpressiP15586.
    BgeeiP15586.
    CleanExiHS_GNS.
    GenevestigatoriP15586.

    Organism-specific databases

    HPAiCAB026011.
    HPA013695.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCK1P163332EBI-1752200,EBI-389883

    Protein-protein interaction databases

    BioGridi109061. 21 interactions.
    IntActiP15586. 7 interactions.
    STRINGi9606.ENSP00000258145.

    Structurei

    3D structure databases

    ProteinModelPortaliP15586.
    SMRiP15586. Positions 46-492.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the sulfatase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3119.
    HOGENOMiHOG000169239.
    HOVERGENiHBG005840.
    InParanoidiP15586.
    KOiK01137.
    OrthoDBiEOG75QR3Q.
    PhylomeDBiP15586.
    TreeFamiTF313545.

    Family and domain databases

    Gene3Di3.40.720.10. 3 hits.
    InterProiIPR017849. 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]
    PANTHERiPTHR10342:SF212. PTHR10342:SF212. 1 hit.
    PfamiPF00884. Sulfatase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036666. G6S. 1 hit.
    SUPFAMiSSF53649. SSF53649. 2 hits.
    PROSITEiPS00523. SULFATASE_1. 1 hit.
    PS00149. SULFATASE_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P15586-1) [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

    MRLLPLAPGR LRRGSPRHLP SCSPALLLLV LGGCLGVFGV AAGTRRPNVV    50
    LLLTDDQDEV LGGMTPLKKT KALIGEMGMT FSSAYVPSAL CCPSRASILT 100
    GKYPHNHHVV NNTLEGNCSS KSWQKIQEPN TFPAILRSMC GYQTFFAGKY 150
    LNEYGAPDAG GLEHVPLGWS YWYALEKNSK YYNYTLSING KARKHGENYS 200
    VDYLTDVLAN VSLDFLDYKS NFEPFFMMIA TPAPHSPWTA APQYQKAFQN 250
    VFAPRNKNFN IHGTNKHWLI RQAKTPMTNS SIQFLDNAFR KRWQTLLSVD 300
    DLVEKLVKRL EFTGELNNTY IFYTSDNGYH TGQFSLPIDK RQLYEFDIKV 350
    PLLVRGPGIK PNQTSKMLVA NIDLGPTILD IAGYDLNKTQ MDGMSLLPIL 400
    RGASNLTWRS DVLVEYQGEG RNVTDPTCPS LSPGVSQCFP DCVCEDAYNN 450
    TYACVRTMSA LWNLQYCEFD DQEVFVEVYN LTADPDQITN IAKTIDPELL 500
    GKMNYRLMML QSCSGPTCRT PGVFDPGYRF DPRLMFSNRG SVRTRRFSKH 550
    LL 552
    Length:552
    Mass (Da):62,082
    Last modified:April 1, 1993 - v3
    Checksum:i85094043F6E64468
    GO
    Isoform 2 (identifier: P15586-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         65-84: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:532
    Mass (Da):59,989
    Checksum:i8D6E2305AB5BBF85
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti252 – 2521F → C in BAD97204. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti94 – 941S → I in MPS3D. 1 Publication
    VAR_064070
    Natural varianti304 – 3063Missing in MPS3D.
    VAR_064071
    Natural varianti340 – 3401K → R in MPS3D. 1 Publication
    VAR_064072
    Natural varianti418 – 4181G → E in MPS3D. 1 Publication
    VAR_064073
    Natural varianti550 – 5501H → Q.
    Corresponds to variant rs2230292 [ dbSNP | Ensembl ].
    VAR_064074

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei65 – 8420Missing in isoform 2. 1 PublicationVSP_056486Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z12173 mRNA. Translation: CAA78164.1.
    AK302443 mRNA. Translation: BAG63740.1.
    AK223484 mRNA. Translation: BAD97204.1.
    AC025262 Genomic DNA. No translation available.
    BC012482 mRNA. Translation: AAH12482.1.
    CCDSiCCDS8970.1.
    PIRiS27164. KJHUGU.
    RefSeqiNP_002067.1. NM_002076.3.
    UniGeneiHs.334534.

    Genome annotation databases

    EnsembliENST00000258145; ENSP00000258145; ENSG00000135677.
    ENST00000542058; ENSP00000444819; ENSG00000135677.
    GeneIDi2799.
    KEGGihsa:2799.
    UCSCiuc001ssg.4. human.

    Polymorphism databases

    DMDMi232126.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z12173 mRNA. Translation: CAA78164.1 .
    AK302443 mRNA. Translation: BAG63740.1 .
    AK223484 mRNA. Translation: BAD97204.1 .
    AC025262 Genomic DNA. No translation available.
    BC012482 mRNA. Translation: AAH12482.1 .
    CCDSi CCDS8970.1.
    PIRi S27164. KJHUGU.
    RefSeqi NP_002067.1. NM_002076.3.
    UniGenei Hs.334534.

    3D structure databases

    ProteinModelPortali P15586.
    SMRi P15586. Positions 46-492.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109061. 21 interactions.
    IntActi P15586. 7 interactions.
    STRINGi 9606.ENSP00000258145.

    PTM databases

    PhosphoSitei P15586.

    Polymorphism databases

    DMDMi 232126.

    Proteomic databases

    MaxQBi P15586.
    PaxDbi P15586.
    PeptideAtlasi P15586.
    PRIDEi P15586.

    Protocols and materials databases

    DNASUi 2799.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000258145 ; ENSP00000258145 ; ENSG00000135677 .
    ENST00000542058 ; ENSP00000444819 ; ENSG00000135677 .
    GeneIDi 2799.
    KEGGi hsa:2799.
    UCSCi uc001ssg.4. human.

    Organism-specific databases

    CTDi 2799.
    GeneCardsi GC12M065107.
    H-InvDB HIX0010785.
    HGNCi HGNC:4422. GNS.
    HPAi CAB026011.
    HPA013695.
    MIMi 252940. phenotype.
    607664. gene.
    neXtProti NX_P15586.
    Orphaneti 79272. Sanfilippo syndrome type D.
    PharmGKBi PA28802.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3119.
    HOGENOMi HOG000169239.
    HOVERGENi HBG005840.
    InParanoidi P15586.
    KOi K01137.
    OrthoDBi EOG75QR3Q.
    PhylomeDBi P15586.
    TreeFami TF313545.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS06046-MONOMER.
    BRENDAi 3.1.6.14. 2681.
    Reactomei REACT_121313. Keratan sulfate degradation.
    REACT_19287. Lysosome Vesicle Biogenesis.
    SABIO-RK P15586.

    Miscellaneous databases

    ChiTaRSi GNS. human.
    GenomeRNAii 2799.
    NextBioi 11033.
    PROi P15586.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15586.
    Bgeei P15586.
    CleanExi HS_GNS.
    Genevestigatori P15586.

    Family and domain databases

    Gene3Di 3.40.720.10. 3 hits.
    InterProi IPR017849. 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 ]
    PANTHERi PTHR10342:SF212. PTHR10342:SF212. 1 hit.
    Pfami PF00884. Sulfatase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036666. G6S. 1 hit.
    SUPFAMi SSF53649. SSF53649. 2 hits.
    PROSITEi PS00523. SULFATASE_1. 1 hit.
    PS00149. SULFATASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-422.
      Tissue: Endothelial cell.
    2. "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] (ISOFORM 2).
      Tissue: Testis.
    3. 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] (ISOFORM 1).
    4. "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.
      , 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].
    5. "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] (ISOFORM 1).
      Tissue: Urinary bladder.
    6. "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 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    7. "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.
    8. "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.
    9. "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.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: VARIANTS MPS3D ILE-94; 304-GLU--LEU-306 DEL; ARG-340 AND GLU-418.

    Entry informationi

    Entry nameiGNS_HUMAN
    AccessioniPrimary (citable) accession number: P15586
    Secondary accession number(s): B4DYH8, Q53F05
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 138 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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3