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Q9Y3R4

- NEUR2_HUMAN

UniProt

Q9Y3R4 - NEUR2_HUMAN

Protein

Sialidase-2

Gene

NEU2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (05 May 2009)
      Previous versions | rss
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    Functioni

    Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moities from glycoproteins, oligosaccharides and gangliosides.2 Publications

    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.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei21 – 211Substrate
    Binding sitei41 – 411Substrate
    Active sitei46 – 461Proton acceptor
    Binding sitei179 – 1791Substrate
    Binding sitei181 – 1811Substrate
    Binding sitei218 – 2181Substrate
    Binding sitei237 – 2371Substrate
    Binding sitei304 – 3041Substrate
    Active sitei334 – 3341Nucleophile
    Active sitei355 – 3551Sequence Analysis

    GO - Molecular functioni

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

    GO - Biological processi

    1. ganglioside catabolic process Source: UniProtKB
    2. glycosphingolipid metabolic process Source: Reactome
    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-RKQ9Y3R4.

    Protein family/group databases

    CAZyiGH33. Glycoside Hydrolase Family 33.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sialidase-2 (EC:3.2.1.18)
    Alternative name(s):
    Cytosolic sialidase
    N-acetyl-alpha-neuraminidase 2
    Gene namesi
    Name:NEU2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:7759. NEU2.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi46 – 461D → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi218 – 2181E → A or Q: Loss of enzyme activity. 1 Publication
    Mutagenesisi270 – 2701Q → E: No effect on enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA31561.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 380380Sialidase-2PRO_0000208899Add
    BLAST

    Proteomic databases

    MaxQBiQ9Y3R4.
    PaxDbiQ9Y3R4.
    PRIDEiQ9Y3R4.

    PTM databases

    PhosphoSiteiQ9Y3R4.

    Expressioni

    Tissue specificityi

    Expressed in skeletal muscle, fetal liver and embryonic carcinoma cell line NT2-D1.1 Publication

    Gene expression databases

    BgeeiQ9Y3R4.
    CleanExiHS_NEU2.
    GenevestigatoriQ9Y3R4.

    Organism-specific databases

    HPAiCAB022336.
    HPA034704.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000233840.

    Structurei

    Secondary structure

    1
    380
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 148
    Beta strandi16 – 183
    Beta strandi20 – 289
    Turni29 – 324
    Beta strandi33 – 408
    Helixi46 – 483
    Beta strandi51 – 6010
    Turni61 – 644
    Beta strandi65 – 684
    Beta strandi75 – 773
    Beta strandi82 – 9110
    Turni93 – 953
    Beta strandi98 – 10811
    Helixi111 – 1155
    Beta strandi116 – 1183
    Beta strandi123 – 1319
    Helixi143 – 1475
    Helixi148 – 1536
    Beta strandi154 – 1596
    Beta strandi174 – 1829
    Beta strandi185 – 1884
    Beta strandi191 – 20111
    Beta strandi213 – 22513
    Beta strandi230 – 25021
    Beta strandi259 – 2657
    Turni268 – 2703
    Beta strandi275 – 2806
    Beta strandi290 – 2989
    Beta strandi301 – 31414
    Helixi318 – 3203
    Beta strandi325 – 34218
    Beta strandi346 – 35611
    Turni357 – 3604
    Beta strandi361 – 3688
    Helixi369 – 3724
    Helixi374 – 3763

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SNTX-ray1.75A1-380[»]
    1SO7X-ray1.49A1-380[»]
    1VCUX-ray2.85A/B1-380[»]
    2F0ZX-ray2.80A1-380[»]
    2F10X-ray2.90A1-380[»]
    2F11X-ray2.57A1-380[»]
    2F12X-ray2.27A1-380[»]
    2F13X-ray2.26A1-380[»]
    2F24X-ray1.76A1-380[»]
    2F25X-ray1.95A/B1-380[»]
    2F26X-ray1.58A1-380[»]
    2F27X-ray2.15A/B1-380[»]
    2F28X-ray1.67A1-380[»]
    2F29X-ray2.92A/B1-380[»]
    4NC5X-ray2.51A1-380[»]
    4NCSX-ray2.20A1-380[»]
    DisProtiDP00261.
    ProteinModelPortaliQ9Y3R4.
    SMRiQ9Y3R4. Positions 1-377.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y3R4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati127 – 13812BNR 1Add
    BLAST
    Repeati197 – 20812BNR 2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi20 – 234FRIP motif

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 33 family.Curated
    Contains 2 BNR repeats.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG84455.
    HOGENOMiHOG000233778.
    HOVERGENiHBG052608.
    InParanoidiQ9Y3R4.
    KOiK12357.
    OMAiQSMGTGP.
    OrthoDBiEOG7MSMNP.
    PhylomeDBiQ9Y3R4.
    TreeFamiTF331063.

    Family and domain databases

    Gene3Di2.120.10.10. 1 hit.
    InterProiIPR026945. Sialidase-2.
    IPR026856. Sialidase_fam.
    IPR011040. Sialidases.
    [Graphical view]
    PANTHERiPTHR10628. PTHR10628. 1 hit.
    PTHR10628:SF6. PTHR10628:SF6. 1 hit.
    SUPFAMiSSF50939. SSF50939. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9Y3R4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASLPVLQKE SVFQSGAHAY RIPALLYLPG QQSLLAFAEQ RASKKDEHAE    50
    LIVLRRGDYD APTHQVQWQA QEVVAQARLD GHRSMNPCPL YDAQTGTLFL 100
    FFIAIPGQVT EQQQLQTRAN VTRLCQVTST DHGRTWSSPR DLTDAAIGPA 150
    YREWSTFAVG PGHCLQLHDR ARSLVVPAYA YRKLHPIQRP IPSAFCFLSH 200
    DHGRTWARGH FVAQDTLECQ VAEVETGEQR VVTLNARSHL RARVQAQSTN 250
    DGLDFQESQL VKKLVEPPPQ GCQGSVISFP SPRSGPGSPA QWLLYTHPTH 300
    SWQRADLGAY LNPRPPAPEA WSEPVLLAKG SCAYSDLQSM GTGPDGSPLF 350
    GCLYEANDYE EIVFLMFTLK QAFPAEYLPQ 380
    Length:380
    Mass (Da):42,254
    Last modified:May 5, 2009 - v2
    Checksum:iAD7B08C478F4D0D9
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti11 – 111S → R.
    Corresponds to variant rs2233384 [ dbSNP | Ensembl ].
    VAR_024461
    Natural varianti41 – 411R → Q Reduced activity; increased sensitivity to inhibition by oseltamivir carboxylate.
    Corresponds to variant rs2233385 [ dbSNP | Ensembl ].
    VAR_024462
    Natural varianti145 – 1451A → T.
    Corresponds to variant rs2233390 [ dbSNP | Ensembl ].
    VAR_049204
    Natural varianti168 – 1681H → N.2 Publications
    Corresponds to variant rs2233391 [ dbSNP | Ensembl ].
    VAR_055311
    Natural varianti182 – 1821R → Q.
    Corresponds to variant rs2233393 [ dbSNP | Ensembl ].
    VAR_055312

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y16535 Genomic DNA. Translation: CAB41449.1.
    AC106876 Genomic DNA. Translation: AAY24360.1.
    CH471063 Genomic DNA. Translation: EAW71028.1.
    BC069151 mRNA. Translation: AAH69151.1.
    BC107053 mRNA. Translation: AAI07054.1.
    CCDSiCCDS2501.1.
    RefSeqiNP_005374.2. NM_005383.2.
    UniGeneiHs.532681.

    Genome annotation databases

    EnsembliENST00000233840; ENSP00000233840; ENSG00000115488.
    GeneIDi4759.
    KEGGihsa:4759.
    UCSCiuc010zmn.2. human.

    Polymorphism databases

    DMDMi229462907.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y16535 Genomic DNA. Translation: CAB41449.1 .
    AC106876 Genomic DNA. Translation: AAY24360.1 .
    CH471063 Genomic DNA. Translation: EAW71028.1 .
    BC069151 mRNA. Translation: AAH69151.1 .
    BC107053 mRNA. Translation: AAI07054.1 .
    CCDSi CCDS2501.1.
    RefSeqi NP_005374.2. NM_005383.2.
    UniGenei Hs.532681.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SNT X-ray 1.75 A 1-380 [» ]
    1SO7 X-ray 1.49 A 1-380 [» ]
    1VCU X-ray 2.85 A/B 1-380 [» ]
    2F0Z X-ray 2.80 A 1-380 [» ]
    2F10 X-ray 2.90 A 1-380 [» ]
    2F11 X-ray 2.57 A 1-380 [» ]
    2F12 X-ray 2.27 A 1-380 [» ]
    2F13 X-ray 2.26 A 1-380 [» ]
    2F24 X-ray 1.76 A 1-380 [» ]
    2F25 X-ray 1.95 A/B 1-380 [» ]
    2F26 X-ray 1.58 A 1-380 [» ]
    2F27 X-ray 2.15 A/B 1-380 [» ]
    2F28 X-ray 1.67 A 1-380 [» ]
    2F29 X-ray 2.92 A/B 1-380 [» ]
    4NC5 X-ray 2.51 A 1-380 [» ]
    4NCS X-ray 2.20 A 1-380 [» ]
    DisProti DP00261.
    ProteinModelPortali Q9Y3R4.
    SMRi Q9Y3R4. Positions 1-377.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000233840.

    Chemistry

    BindingDBi Q9Y3R4.
    ChEMBLi CHEMBL3200.

    Protein family/group databases

    CAZyi GH33. Glycoside Hydrolase Family 33.

    PTM databases

    PhosphoSitei Q9Y3R4.

    Polymorphism databases

    DMDMi 229462907.

    Proteomic databases

    MaxQBi Q9Y3R4.
    PaxDbi Q9Y3R4.
    PRIDEi Q9Y3R4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000233840 ; ENSP00000233840 ; ENSG00000115488 .
    GeneIDi 4759.
    KEGGi hsa:4759.
    UCSCi uc010zmn.2. human.

    Organism-specific databases

    CTDi 4759.
    GeneCardsi GC02P233897.
    H-InvDB HIX0029978.
    HGNCi HGNC:7759. NEU2.
    HPAi CAB022336.
    HPA034704.
    MIMi 605528. gene.
    neXtProti NX_Q9Y3R4.
    PharmGKBi PA31561.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG84455.
    HOGENOMi HOG000233778.
    HOVERGENi HBG052608.
    InParanoidi Q9Y3R4.
    KOi K12357.
    OMAi QSMGTGP.
    OrthoDBi EOG7MSMNP.
    PhylomeDBi Q9Y3R4.
    TreeFami TF331063.

    Enzyme and pathway databases

    BRENDAi 3.2.1.18. 2681.
    Reactomei REACT_116105. Glycosphingolipid metabolism.
    REACT_200874. Sialic acid metabolism.
    SABIO-RK Q9Y3R4.

    Miscellaneous databases

    EvolutionaryTracei Q9Y3R4.
    GeneWikii NEU2.
    GenomeRNAii 4759.
    NextBioi 18332.
    PROi Q9Y3R4.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Y3R4.
    CleanExi HS_NEU2.
    Genevestigatori Q9Y3R4.

    Family and domain databases

    Gene3Di 2.120.10.10. 1 hit.
    InterProi IPR026945. Sialidase-2.
    IPR026856. Sialidase_fam.
    IPR011040. Sialidases.
    [Graphical view ]
    PANTHERi PTHR10628. PTHR10628. 1 hit.
    PTHR10628:SF6. PTHR10628:SF6. 1 hit.
    SUPFAMi SSF50939. SSF50939. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of NEU2, a human gene homologous to rodent soluble sialidases."
      Monti E., Preti A., Rossi E., Ballabio A., Borsani G.
      Genomics 57:137-143(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, VARIANT ASN-168.
    2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. 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], VARIANT ASN-168.
    5. "Properties of recombinant human cytosolic sialidase HsNEU2. The enzyme hydrolyzes monomerically dispersed GM1 ganglioside molecules."
      Tringali C., Papini N., Fusi P., Croci G., Borsani G., Preti A., Tortora P., Tettamanti G., Venerando B., Monti E.
      J. Biol. Chem. 279:3169-3179(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION.
    6. "Molecular insight into substrate recognition by human cytosolic sialidase NEU2."
      Mozzi A., Mazzacuva P., Zampella G., Forcella M.E., Fusi P.A., Monti E.
      Proteins 80:1123-1132(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION, ACTIVE SITE, MUTAGENESIS OF ASP-46; GLU-218 AND GLN-270.
    7. "Crystal structure of the human cytosolic sialidase Neu2. Evidence for the dynamic nature of substrate recognition."
      Chavas L.M.G., Tringali C., Fusi P., Venerando B., Tettamanti G., Kato R., Monti E., Wakatsuki S.
      J. Biol. Chem. 280:469-475(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR 2-DEOXY-2,3-DEHYDRO-N-ACETYLNEURAMINIC ACID.
    8. "Tuning mechanism-based inactivators of neuraminidases: mechanistic and structural insights."
      Buchini S., Gallat F.X., Greig I.R., Kim J.H., Wakatsuki S., Withers S.G.
      Submitted (NOV-2013) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, ACTIVE SITE.
    9. "A nonsynonymous SNP in human cytosolic sialidase in a small Asian population results in reduced enzyme activity: potential link with severe adverse reactions to oseltamivir."
      Li C.-Y., Yu Q., Ye Z.-Q., Sun Y., He Q., Li X.-M., Zhang W., Luo J., Gu X., Zheng X., Wei L.
      Cell Res. 17:357-362(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT GLN-41.

    Entry informationi

    Entry nameiNEUR2_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y3R4
    Secondary accession number(s): Q3KNW4, Q6NTB4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2001
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 119 of the entry and version 2 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. Human chromosome 2
      Human chromosome 2: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3