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Protein

Sialidase-2

Gene

NEU2

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

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)DescriptionActionsGraphical viewLength
Binding sitei21Substrate1
Binding sitei41Substrate1
Active sitei46Proton acceptor1
Binding sitei179Substrate1
Binding sitei181Substrate1
Binding sitei218Substrate1
Binding sitei237Substrate1
Binding sitei304Substrate1
Active sitei334Nucleophile1
Active sitei355Sequence analysis1

GO - Molecular functioni

GO - Biological processi

  • ganglioside catabolic process Source: UniProtKB
  • glycosphingolipid metabolic process Source: Reactome
  • oligosaccharide catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BioCyciZFISH:HS03898-MONOMER.
BRENDAi3.2.1.18. 2681.
ReactomeiR-HSA-1660662. Glycosphingolipid metabolism.
R-HSA-4085001. Sialic acid metabolism.
SABIO-RKQ9Y3R4.

Protein family/group databases

CAZyiGH33. Glycoside Hydrolase Family 33.

Chemistry databases

SwissLipidsiSLP:000001360.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:7759. NEU2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • cytosol Source: Reactome
  • intracellular membrane-bounded organelle Source: GO_Central
  • membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi46D → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi218E → A or Q: Loss of enzyme activity. 1 Publication1
Mutagenesisi270Q → E: No effect on enzyme activity. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000115488.
PharmGKBiPA31561.

Chemistry databases

ChEMBLiCHEMBL3200.
DrugBankiDB00198. Oseltamivir.
DB00558. Zanamivir.

Polymorphism and mutation databases

BioMutaiNEU2.
DMDMi229462907.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002088991 – 380Sialidase-2Add BLAST380

Proteomic databases

PaxDbiQ9Y3R4.
PeptideAtlasiQ9Y3R4.
PRIDEiQ9Y3R4.

PTM databases

iPTMnetiQ9Y3R4.
PhosphoSitePlusiQ9Y3R4.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000115488.
CleanExiHS_NEU2.
GenevisibleiQ9Y3R4. HS.

Organism-specific databases

HPAiCAB022336.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
NOTCH2NLQ7Z3S93EBI-10327976,EBI-945833

Protein-protein interaction databases

BioGridi110832. 21 interactors.
IntActiQ9Y3R4. 1 interactor.
STRINGi9606.ENSP00000233840.

Chemistry databases

BindingDBiQ9Y3R4.

Structurei

Secondary structure

1380
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 14Combined sources8
Beta strandi16 – 18Combined sources3
Beta strandi20 – 28Combined sources9
Turni29 – 32Combined sources4
Beta strandi33 – 40Combined sources8
Helixi46 – 48Combined sources3
Beta strandi51 – 60Combined sources10
Turni61 – 64Combined sources4
Beta strandi65 – 68Combined sources4
Beta strandi75 – 77Combined sources3
Beta strandi82 – 91Combined sources10
Turni93 – 95Combined sources3
Beta strandi98 – 108Combined sources11
Helixi111 – 115Combined sources5
Beta strandi116 – 118Combined sources3
Beta strandi123 – 131Combined sources9
Helixi143 – 147Combined sources5
Helixi148 – 153Combined sources6
Beta strandi154 – 159Combined sources6
Beta strandi174 – 182Combined sources9
Beta strandi185 – 188Combined sources4
Beta strandi191 – 201Combined sources11
Beta strandi213 – 225Combined sources13
Beta strandi230 – 250Combined sources21
Beta strandi259 – 265Combined sources7
Turni268 – 270Combined sources3
Beta strandi275 – 280Combined sources6
Beta strandi290 – 298Combined sources9
Beta strandi301 – 314Combined sources14
Helixi318 – 320Combined sources3
Beta strandi325 – 342Combined sources18
Beta strandi346 – 356Combined sources11
Turni357 – 360Combined sources4
Beta strandi361 – 368Combined sources8
Helixi369 – 372Combined sources4
Helixi374 – 376Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y3R4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati127 – 138BNR 1Add BLAST12
Repeati197 – 208BNR 2Add BLAST12

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi20 – 23FRIP motif4

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IFVF. Eukaryota.
ENOG410Y74Z. LUCA.
GeneTreeiENSGT00390000011171.
HOGENOMiHOG000233778.
HOVERGENiHBG052608.
InParanoidiQ9Y3R4.
KOiK12357.
OMAiQDTLECQ.
OrthoDBiEOG091G08BI.
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.
PfamiPF13088. BNR_2. 1 hit.
[Graphical view]
SUPFAMiSSF50939. SSF50939. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9Y3R4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASLPVLQKE SVFQSGAHAY RIPALLYLPG QQSLLAFAEQ RASKKDEHAE
60 70 80 90 100
LIVLRRGDYD APTHQVQWQA QEVVAQARLD GHRSMNPCPL YDAQTGTLFL
110 120 130 140 150
FFIAIPGQVT EQQQLQTRAN VTRLCQVTST DHGRTWSSPR DLTDAAIGPA
160 170 180 190 200
YREWSTFAVG PGHCLQLHDR ARSLVVPAYA YRKLHPIQRP IPSAFCFLSH
210 220 230 240 250
DHGRTWARGH FVAQDTLECQ VAEVETGEQR VVTLNARSHL RARVQAQSTN
260 270 280 290 300
DGLDFQESQL VKKLVEPPPQ GCQGSVISFP SPRSGPGSPA QWLLYTHPTH
310 320 330 340 350
SWQRADLGAY LNPRPPAPEA WSEPVLLAKG SCAYSDLQSM GTGPDGSPLF
360 370 380
GCLYEANDYE EIVFLMFTLK QAFPAEYLPQ
Length:380
Mass (Da):42,254
Last modified:May 5, 2009 - v2
Checksum:iAD7B08C478F4D0D9
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02446111S → R.Corresponds to variant rs2233384dbSNPEnsembl.1
Natural variantiVAR_02446241R → Q Reduced activity; increased sensitivity to inhibition by oseltamivir carboxylate. 1 PublicationCorresponds to variant rs2233385dbSNPEnsembl.1
Natural variantiVAR_049204145A → T.Corresponds to variant rs2233390dbSNPEnsembl.1
Natural variantiVAR_055311168H → N.2 PublicationsCorresponds to variant rs2233391dbSNPEnsembl.1
Natural variantiVAR_055312182R → Q.Corresponds to variant rs2233393dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110832. 21 interactors.
IntActiQ9Y3R4. 1 interactor.
STRINGi9606.ENSP00000233840.

Chemistry databases

BindingDBiQ9Y3R4.
ChEMBLiCHEMBL3200.
DrugBankiDB00198. Oseltamivir.
DB00558. Zanamivir.
SwissLipidsiSLP:000001360.

Protein family/group databases

CAZyiGH33. Glycoside Hydrolase Family 33.

PTM databases

iPTMnetiQ9Y3R4.
PhosphoSitePlusiQ9Y3R4.

Polymorphism and mutation databases

BioMutaiNEU2.
DMDMi229462907.

Proteomic databases

PaxDbiQ9Y3R4.
PeptideAtlasiQ9Y3R4.
PRIDEiQ9Y3R4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4759.
GeneCardsiNEU2.
H-InvDBHIX0029978.
HGNCiHGNC:7759. NEU2.
HPAiCAB022336.
MIMi605528. gene.
neXtProtiNX_Q9Y3R4.
OpenTargetsiENSG00000115488.
PharmGKBiPA31561.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFVF. Eukaryota.
ENOG410Y74Z. LUCA.
GeneTreeiENSGT00390000011171.
HOGENOMiHOG000233778.
HOVERGENiHBG052608.
InParanoidiQ9Y3R4.
KOiK12357.
OMAiQDTLECQ.
OrthoDBiEOG091G08BI.
PhylomeDBiQ9Y3R4.
TreeFamiTF331063.

Enzyme and pathway databases

BioCyciZFISH:HS03898-MONOMER.
BRENDAi3.2.1.18. 2681.
ReactomeiR-HSA-1660662. Glycosphingolipid metabolism.
R-HSA-4085001. Sialic acid metabolism.
SABIO-RKQ9Y3R4.

Miscellaneous databases

EvolutionaryTraceiQ9Y3R4.
GeneWikiiNEU2.
GenomeRNAii4759.
PROiQ9Y3R4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000115488.
CleanExiHS_NEU2.
GenevisibleiQ9Y3R4. HS.

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.
PfamiPF13088. BNR_2. 1 hit.
[Graphical view]
SUPFAMiSSF50939. SSF50939. 1 hit.
ProtoNetiSearch...

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: November 2, 2016
This is version 138 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.