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Q99519

- NEUR1_HUMAN

UniProt

Q99519 - NEUR1_HUMAN

Protein

Sialidase-1

Gene

NEU1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moities from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage.1 Publication

    Catalytic activityi

    Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.3 Publications

    pH dependencei

    Optimum pH is 4.6.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei78 – 781SubstrateBy similarity
    Binding sitei97 – 971SubstrateBy similarity
    Active sitei103 – 1031Proton acceptorBy similarity
    Binding sitei264 – 2641SubstrateBy similarity
    Binding sitei280 – 2801SubstrateBy similarity
    Binding sitei341 – 3411SubstrateBy similarity
    Active sitei370 – 3701NucleophileBy similarity
    Active sitei394 – 3941Sequence Analysis

    GO - Molecular functioni

    1. exo-alpha-(2->3)-sialidase activity Source: UniProtKB-EC
    2. exo-alpha-(2->6)-sialidase activity Source: UniProtKB-EC
    3. exo-alpha-(2->8)-sialidase activity Source: UniProtKB-EC
    4. exo-alpha-sialidase activity Source: UniProtKB

    GO - Biological processi

    1. glycosphingolipid metabolic process Source: Reactome
    2. lipid catabolic process Source: UniProtKB-KW
    3. oligosaccharide catabolic process Source: UniProtKB
    4. small molecule metabolic process Source: Reactome
    5. sphingolipid metabolic process Source: Reactome

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Lipid degradation, Lipid metabolism

    Enzyme and pathway databases

    BRENDAi3.2.1.18. 2681.
    ReactomeiREACT_116105. Glycosphingolipid metabolism.
    REACT_200874. Sialic acid metabolism.
    SABIO-RKQ99519.

    Protein family/group databases

    CAZyiGH33. Glycoside Hydrolase Family 33.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sialidase-1 (EC:3.2.1.18)
    Alternative name(s):
    Acetylneuraminyl hydrolase
    G9 sialidase
    Lysosomal sialidase
    N-acetyl-alpha-neuraminidase 1
    Gene namesi
    Name:NEU1
    Synonyms:NANH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:7758. NEU1.

    Subcellular locationi

    Lysosome membrane; Peripheral membrane protein; Lumenal side. Lysosome lumen. Cell membrane. Cytoplasmic vesicle
    Note: Localized not only on the inner side of the lysosomal membrane and in the lysosomal lumen, but also on the plasma membrane and in intracellular vesicles.

    GO - Cellular componenti

    1. cell junction Source: HPA
    2. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
    3. extracellular vesicular exosome Source: UniProt
    4. intracellular membrane-bounded organelle Source: HPA
    5. lysosomal lumen Source: Reactome
    6. lysosomal membrane Source: UniProtKB-SubCell
    7. lysosome Source: UniProtKB
    8. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasmic vesicle, Lysosome, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Sialidosis (SIALIDOSIS) [MIM:256550]: Lysosomal storage disease occurring as two types with various manifestations. Type 1 sialidosis (cherry red spot-myoclonus syndrome or normosomatic type) is late-onset and it is characterized by the formation of cherry red macular spots in childhood, progressive debilitating myoclonus, insiduous visual loss and rarely ataxia. The diagnosis can be confirmed by the screening of the urine for sialyloligosaccharides. Type 2 sialidosis (also known as dysmorphic type) occurs as several variants of increasing severity with earlier age of onset. It is characterized by the presence of abnormal somatic features including coarse facies and dysostosis multiplex, vertebral deformities, mental retardation, cherry-red spot/myoclonus, sialuria, cytoplasmic vacuolation of peripheral lymphocytes, bone marrow cells and conjunctival epithelial cells.7 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti54 – 541V → M in SIALIDOSIS; type 1; mild mutation as residual activity is still measurable. 1 Publication
    VAR_012207
    Natural varianti68 – 681G → V in SIALIDOSIS; type 2; less than 10% of activity. 2 Publications
    VAR_012208
    Natural varianti80 – 801P → L in SIALIDOSIS; type 2; no enzyme activity; retained in the endoplasmic reticulum / Golgi or rapidly degraded in the lysosomes. 1 Publication
    VAR_017460
    Natural varianti91 – 911L → R in SIALIDOSIS; type 2. 2 Publications
    VAR_012209
    Natural varianti182 – 1821S → G in SIALIDOSIS; type 1; normally processed. 2 Publications
    VAR_012210
    Natural varianti217 – 2171V → M in SIALIDOSIS; type 1; partial transport and residual transport activity. 1 Publication
    Corresponds to variant rs28940583 [ dbSNP | Ensembl ].
    VAR_012211
    Natural varianti219 – 2191G → A in SIALIDOSIS; type 1; unable to reach the lysosomes. 1 Publication
    VAR_012212
    Natural varianti225 – 2251R → P in SIALIDOSIS; type 2; impaired enzyme folding. 1 Publication
    Corresponds to variant rs28940584 [ dbSNP | Ensembl ].
    VAR_018076
    Natural varianti227 – 2271G → R in SIALIDOSIS; type 1 and juvenile type 2; catalytically inactive; retained in pre-lysosomal compartments. 2 Publications
    VAR_012213
    Natural varianti231 – 2311L → H in SIALIDOSIS; type 1; unable to reach the lysosomes. 1 Publication
    VAR_012214
    Natural varianti240 – 2401W → R in SIALIDOSIS; type 2; no enzyme activity; retained in the endoplasmic reticulum / Golgi or rapidly degraded in the lysosomes. 2 Publications
    VAR_012215
    Natural varianti243 – 2431G → R in SIALIDOSIS; type 1; no enzyme activity and no transport to the lysosome. 1 Publication
    VAR_012216
    Natural varianti260 – 2601F → Y in SIALIDOSIS; infantile type 2; catalytically inactive; rapid intralysosomal degradation. 3 Publications
    VAR_012217
    Natural varianti270 – 2701L → F in SIALIDOSIS; type 2; reduction in enzyme activity; rapid intralysosomal degradation. 1 Publication
    VAR_012219
    Natural varianti270 – 2701L → P in SIALIDOSIS. 1 Publication
    VAR_012218
    Natural varianti294 – 2941R → S in SIALIDOSIS; type 1; mild mutation as residual activity is still measurable. 1 Publication
    VAR_012220
    Natural varianti298 – 2981A → V in SIALIDOSIS; type 2; less than 10% of activity; rapid intralysosomal degradation; impaired enzyme folding. 3 Publications
    VAR_012221
    Natural varianti316 – 3161P → S in SIALIDOSIS; type 1; no enzyme activity; retained in the endoplasmic reticulum / Golgi or rapidly degraded in the lysosomes. 1 Publication
    VAR_017461
    Natural varianti328 – 3281G → S in SIALIDOSIS; type 1; reduction in enzyme activity. 2 Publications
    VAR_012222
    Natural varianti335 – 3351P → Q in SIALIDOSIS; type 2; unable to reach the lysosomes. 1 Publication
    VAR_012223
    Natural varianti341 – 3411R → G in SIALIDOSIS; type 2; affects substrate binding or catalysis. 1 Publication
    VAR_018077
    Natural varianti363 – 3631L → P in SIALIDOSIS; infantile type 2; unable to reach the lysosomes. 3 Publications
    VAR_012224
    Natural varianti370 – 3701Y → C in SIALIDOSIS; infantile type 2; catalytically inactive. 1 Publication
    VAR_012225
    Natural varianti400 – 4001Y → YHY in SIALIDOSIS; type 1; mild mutation as residual activity is still measurable.
    VAR_012226

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi412 – 4121Y → A: Correct sorting to the plasma membrane but no endocytosis and internalization. 1 Publication
    Mutagenesisi413 – 4131G → A: Correct sorting to the plasma membrane but no endocytosis and internalization. 1 Publication
    Mutagenesisi415 – 4151L → A: Correct sorting to the plasma membrane but no endocytosis and internalization. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi256550. phenotype.
    Orphaneti93400. Congenital sialidosis type 2.
    93399. Juvenile sialidosis type 2.
    812. Sialidosis type 1.
    PharmGKBiPA31560.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 47471 PublicationAdd
    BLAST
    Chaini48 – 415368Sialidase-1PRO_0000012026Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi343 – 3431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi352 – 3521N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

    N-glycosylated.3 Publications
    Phosphorylation of tyrosine within the internalization signal results in inhibition of sialidase internalization and blockage on the plasma membrane.

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ99519.
    PaxDbiQ99519.
    PeptideAtlasiQ99519.
    PRIDEiQ99519.

    PTM databases

    PhosphoSiteiQ99519.

    Expressioni

    Tissue specificityi

    Highly expressed in pancreas, followed by skeletal muscle, kidney, placenta, heart, lung and liver. Weakly expressed in brain.2 Publications

    Gene expression databases

    ArrayExpressiQ99519.
    BgeeiQ99519.
    CleanExiHS_NEU1.
    GenevestigatoriQ99519.

    Organism-specific databases

    HPAiHPA015634.
    HPA021506.

    Interactioni

    Subunit structurei

    Interacts with cathepsin A (protective protein), beta-galactosidase and N-acetylgalactosamine-6-sulfate sulfatase in a multienzyme complex.

    Protein-protein interaction databases

    BioGridi110831. 11 interactions.
    IntActiQ99519. 5 interactions.
    MINTiMINT-1389413.
    STRINGi9606.ENSP00000399309.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99519.
    SMRiQ99519. Positions 55-396.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati112 – 12312BNR 1Add
    BLAST
    Repeati172 – 18312BNR 2Add
    BLAST
    Repeati231 – 24212BNR 3Add
    BLAST
    Repeati347 – 35812BNR 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi77 – 804FRIP motif
    Motifi412 – 4154Internalization signal

    Domaini

    A C-terminal internalization signal (YGTL) appears to allow the targeting of plasma membrane proteins to endosomes.

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 33 family.Curated
    Contains 4 BNR repeats.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG4409.
    HOGENOMiHOG000007651.
    HOVERGENiHBG057314.
    InParanoidiQ99519.
    KOiK01186.
    OMAiGTEMFAP.
    PhylomeDBiQ99519.
    TreeFamiTF331063.

    Family and domain databases

    Gene3Di2.120.10.10. 1 hit.
    InterProiIPR026856. Sialidase_fam.
    IPR011040. Sialidases.
    [Graphical view]
    PANTHERiPTHR10628. PTHR10628. 1 hit.
    SUPFAMiSSF50939. SSF50939. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q99519-1 [UniParc]FASTAAdd to Basket

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    MTGERPSTAL PDRRWGPRIL GFWGGCRVWV FAAIFLLLSL AASWSKAEND    50
    FGLVQPLVTM EQLLWVSGRQ IGSVDTFRIP LITATPRGTL LAFAEARKMS 100
    SSDEGAKFIA LRRSMDQGST WSPTAFIVND GDVPDGLNLG AVVSDVETGV 150
    VFLFYSLCAH KAGCQVASTM LVWSKDDGVS WSTPRNLSLD IGTEVFAPGP 200
    GSGIQKQREP RKGRLIVCGH GTLERDGVFC LLSDDHGASW RYGSGVSGIP 250
    YGQPKQENDF NPDECQPYEL PDGSVVINAR NQNNYHCHCR IVLRSYDACD 300
    TLRPRDVTFD PELVDPVVAA GAVVTSSGIV FFSNPAHPEF RVNLTLRWSF 350
    SNGTSWRKET VQLWPGPSGY SSLATLEGSM DGEEQAPQLY VLYEKGRNHY 400
    TESISVAKIS VYGTL 415
    Length:415
    Mass (Da):45,467
    Last modified:May 1, 1997 - v1
    Checksum:i360E60A256DEA07F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti54 – 541V → M in SIALIDOSIS; type 1; mild mutation as residual activity is still measurable. 1 Publication
    VAR_012207
    Natural varianti68 – 681G → V in SIALIDOSIS; type 2; less than 10% of activity. 2 Publications
    VAR_012208
    Natural varianti80 – 801P → L in SIALIDOSIS; type 2; no enzyme activity; retained in the endoplasmic reticulum / Golgi or rapidly degraded in the lysosomes. 1 Publication
    VAR_017460
    Natural varianti88 – 881G → A.
    Corresponds to variant rs34712643 [ dbSNP | Ensembl ].
    VAR_049203
    Natural varianti91 – 911L → R in SIALIDOSIS; type 2. 2 Publications
    VAR_012209
    Natural varianti182 – 1821S → G in SIALIDOSIS; type 1; normally processed. 2 Publications
    VAR_012210
    Natural varianti217 – 2171V → M in SIALIDOSIS; type 1; partial transport and residual transport activity. 1 Publication
    Corresponds to variant rs28940583 [ dbSNP | Ensembl ].
    VAR_012211
    Natural varianti219 – 2191G → A in SIALIDOSIS; type 1; unable to reach the lysosomes. 1 Publication
    VAR_012212
    Natural varianti225 – 2251R → P in SIALIDOSIS; type 2; impaired enzyme folding. 1 Publication
    Corresponds to variant rs28940584 [ dbSNP | Ensembl ].
    VAR_018076
    Natural varianti227 – 2271G → R in SIALIDOSIS; type 1 and juvenile type 2; catalytically inactive; retained in pre-lysosomal compartments. 2 Publications
    VAR_012213
    Natural varianti231 – 2311L → H in SIALIDOSIS; type 1; unable to reach the lysosomes. 1 Publication
    VAR_012214
    Natural varianti240 – 2401W → R in SIALIDOSIS; type 2; no enzyme activity; retained in the endoplasmic reticulum / Golgi or rapidly degraded in the lysosomes. 2 Publications
    VAR_012215
    Natural varianti243 – 2431G → R in SIALIDOSIS; type 1; no enzyme activity and no transport to the lysosome. 1 Publication
    VAR_012216
    Natural varianti260 – 2601F → Y in SIALIDOSIS; infantile type 2; catalytically inactive; rapid intralysosomal degradation. 3 Publications
    VAR_012217
    Natural varianti270 – 2701L → F in SIALIDOSIS; type 2; reduction in enzyme activity; rapid intralysosomal degradation. 1 Publication
    VAR_012219
    Natural varianti270 – 2701L → P in SIALIDOSIS. 1 Publication
    VAR_012218
    Natural varianti294 – 2941R → S in SIALIDOSIS; type 1; mild mutation as residual activity is still measurable. 1 Publication
    VAR_012220
    Natural varianti298 – 2981A → V in SIALIDOSIS; type 2; less than 10% of activity; rapid intralysosomal degradation; impaired enzyme folding. 3 Publications
    VAR_012221
    Natural varianti316 – 3161P → S in SIALIDOSIS; type 1; no enzyme activity; retained in the endoplasmic reticulum / Golgi or rapidly degraded in the lysosomes. 1 Publication
    VAR_017461
    Natural varianti328 – 3281G → S in SIALIDOSIS; type 1; reduction in enzyme activity. 2 Publications
    VAR_012222
    Natural varianti335 – 3351P → Q in SIALIDOSIS; type 2; unable to reach the lysosomes. 1 Publication
    VAR_012223
    Natural varianti341 – 3411R → G in SIALIDOSIS; type 2; affects substrate binding or catalysis. 1 Publication
    VAR_018077
    Natural varianti363 – 3631L → P in SIALIDOSIS; infantile type 2; unable to reach the lysosomes. 3 Publications
    VAR_012224
    Natural varianti370 – 3701Y → C in SIALIDOSIS; infantile type 2; catalytically inactive. 1 Publication
    VAR_012225
    Natural varianti400 – 4001Y → YHY in SIALIDOSIS; type 1; mild mutation as residual activity is still measurable.
    VAR_012226

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF040958 mRNA. Translation: AAB96774.1.
    X78687 mRNA. Translation: CAA55356.1.
    U84246 mRNA. Translation: AAD09239.1.
    AF134726 Genomic DNA. Translation: AAD21814.1.
    BA000025 Genomic DNA. Translation: BAB63297.1.
    BT007206 mRNA. Translation: AAP35870.1.
    BC000722 mRNA. Translation: AAH00722.1.
    BC011900 mRNA. Translation: AAH11900.1.
    CCDSiCCDS4723.1.
    RefSeqiNP_000425.1. NM_000434.3.
    UniGeneiHs.520037.

    Genome annotation databases

    EnsembliENST00000229725; ENSP00000229725; ENSG00000184494.
    ENST00000375631; ENSP00000364782; ENSG00000204386.
    ENST00000411774; ENSP00000399309; ENSG00000234846.
    ENST00000422978; ENSP00000408957; ENSG00000227129.
    ENST00000423382; ENSP00000401067; ENSG00000228691.
    ENST00000434496; ENSP00000409489; ENSG00000234343.
    ENST00000437432; ENSP00000403720; ENSG00000223957.
    ENST00000439648; ENSP00000408207; ENSG00000227315.
    GeneIDi4758.
    KEGGihsa:4758.
    UCSCiuc003nxq.4. human.

    Polymorphism databases

    DMDMi17368612.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Neuraminidase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF040958 mRNA. Translation: AAB96774.1 .
    X78687 mRNA. Translation: CAA55356.1 .
    U84246 mRNA. Translation: AAD09239.1 .
    AF134726 Genomic DNA. Translation: AAD21814.1 .
    BA000025 Genomic DNA. Translation: BAB63297.1 .
    BT007206 mRNA. Translation: AAP35870.1 .
    BC000722 mRNA. Translation: AAH00722.1 .
    BC011900 mRNA. Translation: AAH11900.1 .
    CCDSi CCDS4723.1.
    RefSeqi NP_000425.1. NM_000434.3.
    UniGenei Hs.520037.

    3D structure databases

    ProteinModelPortali Q99519.
    SMRi Q99519. Positions 55-396.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110831. 11 interactions.
    IntActi Q99519. 5 interactions.
    MINTi MINT-1389413.
    STRINGi 9606.ENSP00000399309.

    Chemistry

    BindingDBi Q99519.
    ChEMBLi CHEMBL2726.
    DrugBanki DB00198. Oseltamivir.
    DB00558. Zanamivir.

    Protein family/group databases

    CAZyi GH33. Glycoside Hydrolase Family 33.

    PTM databases

    PhosphoSitei Q99519.

    Polymorphism databases

    DMDMi 17368612.

    Proteomic databases

    MaxQBi Q99519.
    PaxDbi Q99519.
    PeptideAtlasi Q99519.
    PRIDEi Q99519.

    Protocols and materials databases

    DNASUi 4758.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000229725 ; ENSP00000229725 ; ENSG00000184494 .
    ENST00000375631 ; ENSP00000364782 ; ENSG00000204386 .
    ENST00000411774 ; ENSP00000399309 ; ENSG00000234846 .
    ENST00000422978 ; ENSP00000408957 ; ENSG00000227129 .
    ENST00000423382 ; ENSP00000401067 ; ENSG00000228691 .
    ENST00000434496 ; ENSP00000409489 ; ENSG00000234343 .
    ENST00000437432 ; ENSP00000403720 ; ENSG00000223957 .
    ENST00000439648 ; ENSP00000408207 ; ENSG00000227315 .
    GeneIDi 4758.
    KEGGi hsa:4758.
    UCSCi uc003nxq.4. human.

    Organism-specific databases

    CTDi 4758.
    GeneCardsi GC06M031825.
    GC06Mi31836.
    GC06Mj31813.
    GC06Mk31807.
    GC06Ml31865.
    GC06Mm31901.
    GC06Mn31815.
    GC06Mo31817.
    HGNCi HGNC:7758. NEU1.
    HPAi HPA015634.
    HPA021506.
    MIMi 256550. phenotype.
    608272. gene.
    neXtProti NX_Q99519.
    Orphaneti 93400. Congenital sialidosis type 2.
    93399. Juvenile sialidosis type 2.
    812. Sialidosis type 1.
    PharmGKBi PA31560.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4409.
    HOGENOMi HOG000007651.
    HOVERGENi HBG057314.
    InParanoidi Q99519.
    KOi K01186.
    OMAi GTEMFAP.
    PhylomeDBi Q99519.
    TreeFami TF331063.

    Enzyme and pathway databases

    BRENDAi 3.2.1.18. 2681.
    Reactomei REACT_116105. Glycosphingolipid metabolism.
    REACT_200874. Sialic acid metabolism.
    SABIO-RK Q99519.

    Miscellaneous databases

    ChiTaRSi NEU1. human.
    GeneWikii NEU1.
    GenomeRNAii 4758.
    NextBioi 18328.
    PROi Q99519.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99519.
    Bgeei Q99519.
    CleanExi HS_NEU1.
    Genevestigatori Q99519.

    Family and domain databases

    Gene3Di 2.120.10.10. 1 hit.
    InterProi IPR026856. Sialidase_fam.
    IPR011040. Sialidases.
    [Graphical view ]
    PANTHERi PTHR10628. PTHR10628. 1 hit.
    SUPFAMi SSF50939. SSF50939. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of human lysosomal neuraminidase defines the molecular basis of the metabolic storage disorder sialidosis."
      Bonten E.J., van der Spoel A., Fornerod M., Grosveld G., d'Azzo A.
      Genes Dev. 10:3156-3169(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, VARIANT TYPE II SIALIDOSIS ARG-91.
      Tissue: Fibroblast.
    2. "Identification of a sialidase encoded in the human major histocompatibility complex."
      Milner C.M., Smith S.V., Carrillo M.B., Taylor G.L., Hollinshead M., Campbell R.D.
      J. Biol. Chem. 272:4549-4558(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Monocyte.
    3. "Cloning, expression and chromosomal mapping of human lysosomal sialidase and characterization of mutations in sialidosis."
      Pshezhetsky A.V., Richard C., Michaud L., Igdoura S.A., Wang S., Elsliger M.-A., Ou J., Leclerc D., Gravel R.A., Dallaire L., Potier M.
      Nat. Genet. 15:316-320(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY, VARIANTS SIALIDOSIS TYR-260 AND PRO-363.
      Tissue: Fibroblast.
    4. "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
      Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
      Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
      Shiina S., Tamiya G., Oka A., Inoko H.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "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: Brain and Kidney.
    8. "Molecular mechanism of lysosomal sialidase deficiency in galactosialidosis involves its rapid degradation."
      Vinogradova M.V., Michaud L., Mezentsev A.V., Lukong K.E., El-Alfy M., Morales C.R., Potier M., Pshezhetsky A.V.
      Biochem. J. 330:641-650(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 48-55, GLYCOSYLATION.
      Tissue: Placenta.
    9. "Intracellular distribution of lysosomal sialidase is controlled by the internalization signal in its cytoplasmic tail."
      Lukong K.E., Seyrantepe V., Landry K., Trudel S., Ahmad A., Gahl W.A., Lefrancois S., Morales C.R., Pshezhetsky A.V.
      J. Biol. Chem. 276:46172-46181(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-412; GLY-413 AND LEU-415.
    10. "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-352.
      Tissue: Liver.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Characterization of the sialidase molecular defects in sialidosis patients suggests the structural organization of the lysosomal multienzyme complex."
      Lukong K.E., Elsliger M.-A., Chang Y., Richard C., Thomas G., Carey W., Tylki-Szymanska A., Czartoryska B., Buchholz T., Rodriguez Criado G., Palmeri S., Pshezhetsky A.V.
      Hum. Mol. Genet. 9:1075-1085(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS SIALIDOSIS VAL-68; GLY-182; ARG-227; TYR-260; PHE-270; VAL-298; SER-328 AND PRO-363.
    13. "Novel mutations in lysosomal neuraminidase identify functional domains and determine clinical severity in sialidosis."
      Bonten E.J., Arts W.F., Beck M., Covanis A., Donati M.A., Parini R., Zammarchi E., d'Azzo A.
      Hum. Mol. Genet. 9:2715-2725(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SIALIDOSIS MET-54; VAL-68; ARG-91; GLY-182; ALA-219; ARG-227; HIS-231; TYR-260; PRO-270; SER-294; VAL-298; SER-328; GLN-335; PRO-363; CYS-370 AND HIS-TYR-400 INS.
    14. Cited for: VARIANTS SIALIDOSIS MET-217 AND ARG-243, CHARACTERIZATION OF VARIANTS SIALIDOSIS MET-217 AND ARG-243.
    15. "Mutations in sialidosis impair sialidase binding to the lysosomal multienzyme complex."
      Lukong K.E., Landry K., Elsliger M.-A., Chang Y., Lefrancois S., Morales C.R., Pshezhetsky A.V.
      J. Biol. Chem. 276:17286-17290(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SIALIDOSIS VAL-68; GLY-182; ARG-227; ARG-240; TYR-260; PHE-270; VAL-298; SER-328 AND PRO-363, CHARACTERIZATION OF VARIANTS SIALIDOSIS VAL-68; GLY-182; ARG-227; TYR-260; PHE-270; VAL-298; SER-328 AND PRO-363.
    16. "Novel missense mutations in the human lysosomal sialidase gene in sialidosis patients and prediction of structural alterations of mutant enzymes."
      Itoh K., Naganawa Y., Matsuzawa F., Aikawa S., Doi H., Sasagasako N., Yamada T., Kira J., Kobayashi T., Pshezhetsky A.V., Sakuraba H.
      J. Hum. Genet. 47:29-37(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SIALIDOSIS LEU-80; ARG-240 AND SER-316.
    17. "Five novel mutations in the lysosomal sialidase gene (NEU1) in type II sialidosis patients and assessment of their impact on enzyme activity and intracellular targeting using adenovirus-mediated expression."
      Pattison S., Pankarican M., Rupar C.A., Graham F.L., Igdoura S.A.
      Hum. Mutat. 23:32-39(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SIALIDOSIS PRO-225; VAL-298 AND GLY-341, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS SIALIDOSIS PRO-225; VAL-298 AND GLY-341.

    Entry informationi

    Entry nameiNEUR1_HUMAN
    AccessioniPrimary (citable) accession number: Q99519
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2001
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 152 of the entry and version 1 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. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

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