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Q9UQ49

- NEUR3_HUMAN

UniProt

Q9UQ49 - NEUR3_HUMAN

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Protein
Sialidase-3
Gene
NEU3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 251Substrate By similarity
Binding sitei45 – 451Substrate Inferred
Active sitei50 – 501Proton acceptor1 Publication
Binding sitei179 – 1791Substrate Inferred
Binding sitei181 – 1811Substrate Inferred
Binding sitei225 – 2251Substrate Inferred
Binding sitei245 – 2451Substrate Inferred
Binding sitei340 – 3401Substrate Inferred
Active sitei370 – 3701Nucleophile1 Publication
Active sitei387 – 3871 Reviewed prediction

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
Complete GO annotation...

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; Peripheral membrane protein 1 Publication

GO - Cellular componenti

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

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-3
PRO_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.

Family & Domainsi

Domains and Repeats

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

Motif

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

Sequence similaritiesi

Contains 3 BNR repeats.

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.
VSP_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.
ENST00000544263; ENSP00000445591; ENSG00000162139.
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 .
ENST00000544263 ; ENSP00000445591 ; ENSG00000162139 .
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 114 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

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