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Q8BFR4

- GNS_MOUSE

UniProt

Q8BFR4 - GNS_MOUSE

Protein

N-acetylglucosamine-6-sulfatase

Gene

Gns

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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 bindingi47 – 471CalciumBy similarity
    Metal bindingi48 – 481CalciumBy similarity
    Metal bindingi83 – 831Calcium; via 3-oxoalanineBy similarity
    Metal bindingi318 – 3181CalciumBy similarity
    Metal bindingi319 – 3191CalciumBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. glycosaminoglycan metabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_198960. Keratan sulfate degradation.

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:1922862. Gns.

    Subcellular locationi

    Lysosome By similarity

    GO - Cellular componenti

    1. lysosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Lysosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3535Sequence AnalysisAdd
    BLAST
    Chaini36 – 544509N-acetylglucosamine-6-sulfatasePRO_0000273189Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei83 – 8313-oxoalanine (Cys)By similarity
    Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi175 – 1751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi190 – 1901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi202 – 2021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi271 – 2711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi379 – 3791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi397 – 3971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi414 – 4141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi441 – 4411N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi472 – 4721N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    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

    MaxQBiQ8BFR4.
    PaxDbiQ8BFR4.
    PRIDEiQ8BFR4.

    PTM databases

    PhosphoSiteiQ8BFR4.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8BFR4.
    BgeeiQ8BFR4.
    CleanExiMM_GNS.
    GenevestigatoriQ8BFR4.

    Interactioni

    Protein-protein interaction databases

    IntActiQ8BFR4. 1 interaction.
    MINTiMINT-4110937.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BFR4.
    SMRiQ8BFR4. Positions 39-418.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the sulfatase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3119.
    GeneTreeiENSGT00400000022041.
    HOGENOMiHOG000169239.
    HOVERGENiHBG005840.
    InParanoidiQ8BFR4.
    KOiK01137.
    OMAiAPQYQKA.
    OrthoDBiEOG75QR3Q.
    PhylomeDBiQ8BFR4.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    Q8BFR4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRLPSAAGPR PGRPRRLPAL LLLPLLGGCL GLVGAARRPN VLLLLTDDQD    50
    AELGGMTPLK KTKALIGEKG MTFSSAYVPS ALCCPSRASI LTGKYPHNHH 100
    VVNNTLEGNC SSKAWQKIQE PYTFPAILKS VCGYQTFFAG KYLNEYGAPD 150
    AGGLEHIPLG WSYWYALEKN SKYYNYTLSI NGKARKHGEN YSVDYLTDVL 200
    ANLSLDFLDY KSNSEPFFMM ISTPAPHSPW TAAPQYQKAF QNVIAPRNKN 250
    FNIHGTNKHW LIRQAKTPMT NSSIRFLDDA FRRRWQTLLS VDDLVEKLVK 300
    RLDSTGELDN TYIFYTSDNG YHTGQFSLPI DKRQLYEFDI KVPLLVRGPG 350
    IKPNQTSKML VSNIDLGPTI LDLAGYDLNK TQMDGMSLLP ILKGDRNLTW 400
    RSDVLVEYQG EGRNVTDPTC PSLSPGVSQC FPDCVCEDAY NNTYACVRTL 450
    SSLWNLQYCE FDDQEVFVEV YNITADPDQI TNIAKSIDPE LLGKMNYRLM 500
    MLQSCSGPTC RTPGVFDPGY RFDLRLMFNS HGSVRTRRFS KHPL 544
    Length:544
    Mass (Da):61,175
    Last modified:March 1, 2003 - v1
    Checksum:iF9E95AFA6CBEA842
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti65 – 651L → V in BAC35632. (PubMed:16141072)Curated
    Sequence conflicti138 – 1381F → L in BAE35186. (PubMed:16141072)Curated
    Sequence conflicti314 – 3141F → L in BAC38966. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK030773 mRNA. Translation: BAC27129.1.
    AK049162 mRNA. Translation: BAC33578.1.
    AK054046 mRNA. Translation: BAC35632.1.
    AK083597 mRNA. Translation: BAC38966.1.
    AK159562 mRNA. Translation: BAE35186.1.
    AK169485 mRNA. Translation: BAE41197.1.
    AK165180 mRNA. Translation: BAE38063.1.
    AK170791 mRNA. Translation: BAE42031.1.
    BC055328 mRNA. Translation: AAH55328.1.
    CCDSiCCDS24210.1.
    RefSeqiNP_083640.1. NM_029364.3.
    UniGeneiMm.207683.

    Genome annotation databases

    EnsembliENSMUST00000040344; ENSMUSP00000043167; ENSMUSG00000034707.
    GeneIDi75612.
    KEGGimmu:75612.
    UCSCiuc007hfo.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK030773 mRNA. Translation: BAC27129.1 .
    AK049162 mRNA. Translation: BAC33578.1 .
    AK054046 mRNA. Translation: BAC35632.1 .
    AK083597 mRNA. Translation: BAC38966.1 .
    AK159562 mRNA. Translation: BAE35186.1 .
    AK169485 mRNA. Translation: BAE41197.1 .
    AK165180 mRNA. Translation: BAE38063.1 .
    AK170791 mRNA. Translation: BAE42031.1 .
    BC055328 mRNA. Translation: AAH55328.1 .
    CCDSi CCDS24210.1.
    RefSeqi NP_083640.1. NM_029364.3.
    UniGenei Mm.207683.

    3D structure databases

    ProteinModelPortali Q8BFR4.
    SMRi Q8BFR4. Positions 39-418.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8BFR4. 1 interaction.
    MINTi MINT-4110937.

    PTM databases

    PhosphoSitei Q8BFR4.

    Proteomic databases

    MaxQBi Q8BFR4.
    PaxDbi Q8BFR4.
    PRIDEi Q8BFR4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000040344 ; ENSMUSP00000043167 ; ENSMUSG00000034707 .
    GeneIDi 75612.
    KEGGi mmu:75612.
    UCSCi uc007hfo.1. mouse.

    Organism-specific databases

    CTDi 2799.
    MGIi MGI:1922862. Gns.

    Phylogenomic databases

    eggNOGi COG3119.
    GeneTreei ENSGT00400000022041.
    HOGENOMi HOG000169239.
    HOVERGENi HBG005840.
    InParanoidi Q8BFR4.
    KOi K01137.
    OMAi APQYQKA.
    OrthoDBi EOG75QR3Q.
    PhylomeDBi Q8BFR4.
    TreeFami TF313545.

    Enzyme and pathway databases

    Reactomei REACT_198960. Keratan sulfate degradation.

    Miscellaneous databases

    ChiTaRSi GNS. mouse.
    NextBioi 343508.
    PROi Q8BFR4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BFR4.
    Bgeei Q8BFR4.
    CleanExi MM_GNS.
    Genevestigatori Q8BFR4.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Oviduct and Thymus.
    2. "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].
      Strain: C57BL/6.
      Tissue: Brain.

    Entry informationi

    Entry nameiGNS_MOUSE
    AccessioniPrimary (citable) accession number: Q8BFR4
    Secondary accession number(s): Q3TWT0, Q8BJJ7, Q8BK91
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 94 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3