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Q9UQ49

- NEUR3_HUMAN

UniProt

Q9UQ49 - NEUR3_HUMAN

Protein

Sialidase-3

Gene

NEU3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Plays a role in modulating the ganglioside content of the lipid bilayer at the level of membrane-bound sialyl glycoconjugates.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

    pH dependencei

    Optimum pH is 3.8.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei25 – 251SubstrateBy similarity
    Binding sitei45 – 451SubstrateCurated
    Active sitei50 – 501Proton acceptor1 Publication
    Binding sitei179 – 1791SubstrateCurated
    Binding sitei181 – 1811SubstrateCurated
    Binding sitei225 – 2251SubstrateCurated
    Binding sitei245 – 2451SubstrateCurated
    Binding sitei340 – 3401SubstrateCurated
    Active sitei370 – 3701Nucleophile1 Publication
    Active sitei387 – 3871Sequence Analysis

    GO - Molecular functioni

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

    GO - Biological processi

    1. carbohydrate metabolic process Source: MGI
    2. ganglioside catabolic process Source: UniProtKB
    3. glycosphingolipid metabolic process Source: Reactome
    4. oligosaccharide catabolic process Source: UniProtKB
    5. small molecule metabolic process Source: Reactome
    6. 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-RKQ9UQ49.

    Protein family/group databases

    CAZyiGH33. Glycoside Hydrolase Family 33.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sialidase-3 (EC:3.2.1.18)
    Alternative name(s):
    Ganglioside sialidase
    Membrane sialidase
    N-acetyl-alpha-neuraminidase 3
    Gene namesi
    Name:NEU3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:7760. NEU3.

    Subcellular locationi

    Cell membrane 1 Publication; Peripheral membrane protein 1 Publication

    GO - Cellular componenti

    1. integral component of plasma membrane Source: ProtInc
    2. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi45 – 451R → V: Loss of enzyme activity. 1 Publication
    Mutagenesisi50 – 501D → S: Nearly abolishes enzyme activity. 1 Publication
    Mutagenesisi179 – 1791Y → F: Loss of enzyme activity. 1 Publication
    Mutagenesisi181 – 1811Y → F: Nearly abolishes enzyme activity. 1 Publication
    Mutagenesisi225 – 2251E → S: Loss of enzyme activity. 1 Publication
    Mutagenesisi245 – 2451R → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi340 – 3401R → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi370 – 3701Y → F: Loss of enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 428428Sialidase-3PRO_0000208903Add
    BLAST

    Proteomic databases

    MaxQBiQ9UQ49.
    PaxDbiQ9UQ49.
    PRIDEiQ9UQ49.

    PTM databases

    PhosphoSiteiQ9UQ49.

    Expressioni

    Tissue specificityi

    Highly expressed in skeletal muscle, testis, adrenal gland and thymus, followed by pancreas, liver, heart and thymus. Weakly expressed in kidney, placenta, brain and lung.1 Publication

    Gene expression databases

    ArrayExpressiQ9UQ49.
    BgeeiQ9UQ49.
    CleanExiHS_NEU3.
    GenevestigatoriQ9UQ49.

    Organism-specific databases

    HPAiHPA038729.
    HPA038730.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000294064.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UQ49.
    SMRiQ9UQ49. Positions 24-406.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati129 – 14012BNR 1Add
    BLAST
    Repeati203 – 21412BNR 2Add
    BLAST
    Repeati254 – 26512BNR 3Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi24 – 274FRIP motif

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 33 family.Curated
    Contains 3 BNR repeats.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG84455.
    HOVERGENiHBG052608.
    InParanoidiQ9UQ49.
    KOiK12357.
    OMAiVYLFFIC.
    OrthoDBiEOG7MSMNP.
    PhylomeDBiQ9UQ49.

    Family and domain databases

    Gene3Di2.120.10.10. 1 hit.
    InterProiIPR026944. Sialidase-3.
    IPR026856. Sialidase_fam.
    IPR011040. Sialidases.
    [Graphical view]
    PANTHERiPTHR10628. PTHR10628. 1 hit.
    PTHR10628:SF7. PTHR10628:SF7. 1 hit.
    SUPFAMiSSF50939. SSF50939. 2 hits.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UQ49-1) [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

    MEEVTTCSFN SPLFRQEDDR GITYRIPALL YIPPTHTFLA FAEKRSTRRD    50
    EDALHLVLRR GLRIGQLVQW GPLKPLMEAT LPGHRTMNPC PVWEQKSGCV 100
    FLFFICVRGH VTERQQIVSG RNAARLCFIY SQDAGCSWSE VRDLTEEVIG 150
    SELKHWATFA VGPGHGIQLQ SGRLVIPAYT YYIPSWFFCF QLPCKTRPHS 200
    LMIYSDDLGV TWHHGRLIRP MVTVECEVAE VTGRAGHPVL YCSARTPNRC 250
    RAEALSTDHG EGFQRLALSR QLCEPPHGCQ GSVVSFRPLE IPHRCQDSSS 300
    KDAPTIQQSS PGSSLRLEEE AGTPSESWLL YSHPTSRKQR VDLGIYLNQT 350
    PLEAACWSRP WILHCGPCGY SDLAALEEEG LFGCLFECGT KQECEQIAFR 400
    LFTHREILSH LQGDCTSPGR NPSQFKSN 428
    Length:428
    Mass (Da):48,252
    Last modified:May 1, 2000 - v1
    Checksum:i35D1DD9359A78C98
    GO
    Isoform 2 (identifier: Q9UQ49-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MRPADLPPRPMEESPASSSAPTETEEPGSSAEVM

    Show »
    Length:461
    Mass (Da):51,675
    Checksum:i37D6EBA8FD7458AD
    GO

    Sequence cautioni

    The sequence CAB96131.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151R → Q.
    Corresponds to variant rs7115499 [ dbSNP | Ensembl ].
    VAR_055839

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MRPADLPPRPMEESPASSSA PTETEEPGSSAEVM in isoform 2. 2 PublicationsVSP_054145

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB008185 mRNA. Translation: BAA82611.1.
    Y18563 mRNA. Translation: CAB96131.1. Different initiation.
    AK022450 mRNA. Translation: BAG51074.1.
    AK290442 mRNA. Translation: BAF83131.1.
    AP001992 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW74953.1.
    BC136397 mRNA. Translation: AAI36398.1.
    BC144059 mRNA. Translation: AAI44060.1.
    CCDSiCCDS44682.1. [Q9UQ49-2]
    RefSeqiNP_006647.3. NM_006656.5. [Q9UQ49-2]
    UniGeneiHs.191074.

    Genome annotation databases

    EnsembliENST00000294064; ENSP00000294064; ENSG00000162139. [Q9UQ49-2]
    ENST00000531509; ENSP00000432097; ENSG00000162139. [Q9UQ49-2]
    GeneIDi10825.
    KEGGihsa:10825.
    UCSCiuc001ovv.3. human.
    uc010rrl.2. human. [Q9UQ49-1]

    Polymorphism databases

    DMDMi17369720.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB008185 mRNA. Translation: BAA82611.1 .
    Y18563 mRNA. Translation: CAB96131.1 . Different initiation.
    AK022450 mRNA. Translation: BAG51074.1 .
    AK290442 mRNA. Translation: BAF83131.1 .
    AP001992 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW74953.1 .
    BC136397 mRNA. Translation: AAI36398.1 .
    BC144059 mRNA. Translation: AAI44060.1 .
    CCDSi CCDS44682.1. [Q9UQ49-2 ]
    RefSeqi NP_006647.3. NM_006656.5. [Q9UQ49-2 ]
    UniGenei Hs.191074.

    3D structure databases

    ProteinModelPortali Q9UQ49.
    SMRi Q9UQ49. Positions 24-406.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000294064.

    Chemistry

    BindingDBi Q9UQ49.
    ChEMBLi CHEMBL3046.

    Protein family/group databases

    CAZyi GH33. Glycoside Hydrolase Family 33.

    PTM databases

    PhosphoSitei Q9UQ49.

    Polymorphism databases

    DMDMi 17369720.

    Proteomic databases

    MaxQBi Q9UQ49.
    PaxDbi Q9UQ49.
    PRIDEi Q9UQ49.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000294064 ; ENSP00000294064 ; ENSG00000162139 . [Q9UQ49-2 ]
    ENST00000531509 ; ENSP00000432097 ; ENSG00000162139 . [Q9UQ49-2 ]
    GeneIDi 10825.
    KEGGi hsa:10825.
    UCSCi uc001ovv.3. human.
    uc010rrl.2. human. [Q9UQ49-1 ]

    Organism-specific databases

    CTDi 10825.
    GeneCardsi GC11P074699.
    HGNCi HGNC:7760. NEU3.
    HPAi HPA038729.
    HPA038730.
    MIMi 604617. gene.
    neXtProti NX_Q9UQ49.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG84455.
    HOVERGENi HBG052608.
    InParanoidi Q9UQ49.
    KOi K12357.
    OMAi VYLFFIC.
    OrthoDBi EOG7MSMNP.
    PhylomeDBi Q9UQ49.

    Enzyme and pathway databases

    BRENDAi 3.2.1.18. 2681.
    Reactomei REACT_116105. Glycosphingolipid metabolism.
    REACT_200874. Sialic acid metabolism.
    SABIO-RK Q9UQ49.

    Miscellaneous databases

    GeneWikii NEU3.
    NextBioi 41116.
    PROi Q9UQ49.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UQ49.
    Bgeei Q9UQ49.
    CleanExi HS_NEU3.
    Genevestigatori Q9UQ49.

    Family and domain databases

    Gene3Di 2.120.10.10. 1 hit.
    InterProi IPR026944. Sialidase-3.
    IPR026856. Sialidase_fam.
    IPR011040. Sialidases.
    [Graphical view ]
    PANTHERi PTHR10628. PTHR10628. 1 hit.
    PTHR10628:SF7. PTHR10628:SF7. 1 hit.
    SUPFAMi SSF50939. SSF50939. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression, and chromosomal mapping of a human ganglioside sialidase."
      Wada T., Yoshikawa Y., Tokuyama S., Kuwabara M., Akita H., Miyagi T.
      Biochem. Biophys. Res. Commun. 261:21-27(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Identification and expression of NEU3, a novel human sialidase associated to the plasma membrane."
      Monti E., Bassi M.T., Papini N., Riboni M., Manzoni M., Venerando B., Croci G., Preti A., Ballabio A., Tettamanti G., Borsani G.
      Biochem. J. 349:343-351(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Tissue: Skeletal muscle.
    3. "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: Mammary gland.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 2).
      Tissue: Testis.
    7. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Insight into substrate recognition and catalysis by the human neuraminidase 3 (NEU3) through molecular modeling and site-directed mutagenesis."
      Albohy A., Li M.D., Zheng R.B., Zou C., Cairo C.W.
      Glycobiology 20:1127-1138(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, BINDING SITES, MUTAGENESIS OF ARG-45; ASP-50; TYR-179; TYR-181; GLU-225; ARG-245; ARG-340 AND TYR-370.

    Entry informationi

    Entry nameiNEUR3_HUMAN
    AccessioniPrimary (citable) accession number: Q9UQ49
    Secondary accession number(s): A8K327, Q9NQE1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 115 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, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. Human chromosome 11
      Human chromosome 11: 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

    Dasty 3