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Q9Y3R4

- NEUR2_HUMAN

UniProt

Q9Y3R4 - NEUR2_HUMAN

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Protein

Sialidase-2

Gene

NEU2

Organism
Homo sapiens (Human)
Status
Reviewed - 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)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
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-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
Complete GO annotation...

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

BioGridi110832. 12 interactions.
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.
GeneTreeiENSGT00390000011171.
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

        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)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

BioGridi 110832. 12 interactions.
STRINGi 9606.ENSP00000233840.

Chemistry

BindingDBi Q9Y3R4.
ChEMBLi CHEMBL3200.
DrugBanki DB00198. Oseltamivir.
DB00558. Zanamivir.

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.
GeneTreei ENSGT00390000011171.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 120 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