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Q99519 (NEUR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sialidase-1

EC=3.2.1.18
Alternative name(s):
Acetylneuraminyl hydrolase
G9 sialidase
Lysosomal sialidase
N-acetyl-alpha-neuraminidase 1
Gene names
Name:NEU1
Synonyms:NANH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length415 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moities from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage. Ref.1

Catalytic activity

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. Ref.1 Ref.3 Ref.17

Subunit structure

Interacts with cathepsin A (protective protein), beta-galactosidase and N-acetylgalactosamine-6-sulfate sulfatase in a multienzyme complex.

Subcellular location

Lysosome membrane; Peripheral membrane protein; Lumenal side. Lysosome lumen. Cell membrane. Cytoplasmic vesicle. Note: Localized not only on the inner side of the lysosomal membrane and in the lysosomal lumen, but also on the plasma membrane and in intracellular vesicles. Ref.1 Ref.9 Ref.17

Tissue specificity

Highly expressed in pancreas, followed by skeletal muscle, kidney, placenta, heart, lung and liver. Weakly expressed in brain. Ref.1 Ref.3

Domain

A C-terminal internalization signal (YGTL) appears to allow the targeting of plasma membrane proteins to endosomes.

Post-translational modification

N-glycosylated. Ref.1 Ref.8

Phosphorylation of tyrosine within the internalization signal results in inhibition of sialidase internalization and blockage on the plasma membrane.

Involvement in disease

Sialidosis (SIALIDOSIS) [MIM:256550]: Lysosomal storage disease occurring as two types with various manifestations. Type 1 sialidosis (cherry red spot-myoclonus syndrome or normosomatic type) is late-onset and it is characterized by the formation of cherry red macular spots in childhood, progressive debilitating myoclonus, insiduous visual loss and rarely ataxia. The diagnosis can be confirmed by the screening of the urine for sialyloligosaccharides. Type 2 sialidosis (also known as dysmorphic type) occurs as several variants of increasing severity with earlier age of onset. It is characterized by the presence of abnormal somatic features including coarse facies and dysostosis multiplex, vertebral deformities, mental retardation, cherry-red spot/myoclonus, sialuria, cytoplasmic vacuolation of peripheral lymphocytes, bone marrow cells and conjunctival epithelial cells.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.3 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17

Sequence similarities

Belongs to the glycosyl hydrolase 33 family.

Contains 4 BNR repeats.

Biophysicochemical properties

pH dependence:

Optimum pH is 4.6.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Lipid degradation
Lipid metabolism
   Cellular componentCell membrane
Cytoplasmic vesicle
Lysosome
Membrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processglycosphingolipid metabolic process

Traceable author statement. Source: Reactome

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oligosaccharide catabolic process

Inferred from mutant phenotype Ref.1. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

sphingolipid metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcell junction

Inferred from direct assay. Source: HPA

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

lysosomal lumen

Traceable author statement. Source: Reactome

lysosomal membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

lysosome

Inferred from direct assay Ref.1. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionexo-alpha-(2->3)-sialidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

exo-alpha-(2->6)-sialidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

exo-alpha-(2->8)-sialidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

exo-alpha-sialidase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4747 Ref.8
Chain48 – 415368Sialidase-1
PRO_0000012026

Regions

Repeat112 – 12312BNR 1
Repeat172 – 18312BNR 2
Repeat231 – 24212BNR 3
Repeat347 – 35812BNR 4
Motif77 – 804FRIP motif
Motif412 – 4154Internalization signal

Sites

Active site1031Proton acceptor By similarity
Active site3701Nucleophile By similarity
Active site3941 Potential
Binding site781Substrate By similarity
Binding site971Substrate By similarity
Binding site2641Substrate By similarity
Binding site2801Substrate By similarity
Binding site3411Substrate By similarity

Amino acid modifications

Glycosylation1861N-linked (GlcNAc...) Potential
Glycosylation3431N-linked (GlcNAc...) Potential
Glycosylation3521N-linked (GlcNAc...) Ref.10

Natural variations

Natural variant541V → M in SIALIDOSIS; type 1; mild mutation as residual activity is still measurable. Ref.13
VAR_012207
Natural variant681G → V in SIALIDOSIS; type 2; less than 10% of activity. Ref.12 Ref.13 Ref.15
VAR_012208
Natural variant801P → L in SIALIDOSIS; type 2; no enzyme activity; retained in the endoplasmic reticulum / Golgi or rapidly degraded in the lysosomes. Ref.16
VAR_017460
Natural variant881G → A.
Corresponds to variant rs34712643 [ dbSNP | Ensembl ].
VAR_049203
Natural variant911L → R in SIALIDOSIS; type 2. Ref.1 Ref.13
VAR_012209
Natural variant1821S → G in SIALIDOSIS; type 1; normally processed. Ref.12 Ref.13 Ref.15
VAR_012210
Natural variant2171V → M in SIALIDOSIS; type 1; partial transport and residual transport activity. Ref.14
Corresponds to variant rs28940583 [ dbSNP | Ensembl ].
VAR_012211
Natural variant2191G → A in SIALIDOSIS; type 1; unable to reach the lysosomes. Ref.13
VAR_012212
Natural variant2251R → P in SIALIDOSIS; type 2; impaired enzyme folding. Ref.17
Corresponds to variant rs28940584 [ dbSNP | Ensembl ].
VAR_018076
Natural variant2271G → R in SIALIDOSIS; type 1 and juvenile type 2; catalytically inactive; retained in pre-lysosomal compartments. Ref.12 Ref.13 Ref.15
VAR_012213
Natural variant2311L → H in SIALIDOSIS; type 1; unable to reach the lysosomes. Ref.13
VAR_012214
Natural variant2401W → R in SIALIDOSIS; type 2; no enzyme activity; retained in the endoplasmic reticulum / Golgi or rapidly degraded in the lysosomes. Ref.15 Ref.16
VAR_012215
Natural variant2431G → R in SIALIDOSIS; type 1; no enzyme activity and no transport to the lysosome. Ref.14
VAR_012216
Natural variant2601F → Y in SIALIDOSIS; infantile type 2; catalytically inactive; rapid intralysosomal degradation. Ref.3 Ref.12 Ref.13 Ref.15
VAR_012217
Natural variant2701L → F in SIALIDOSIS; type 2; reduction in enzyme activity; rapid intralysosomal degradation. Ref.12 Ref.15
VAR_012219
Natural variant2701L → P in SIALIDOSIS. Ref.13
VAR_012218
Natural variant2941R → S in SIALIDOSIS; type 1; mild mutation as residual activity is still measurable. Ref.13
VAR_012220
Natural variant2981A → V in SIALIDOSIS; type 2; less than 10% of activity; rapid intralysosomal degradation; impaired enzyme folding. Ref.12 Ref.13 Ref.15 Ref.17
VAR_012221
Natural variant3161P → S in SIALIDOSIS; type 1; no enzyme activity; retained in the endoplasmic reticulum / Golgi or rapidly degraded in the lysosomes. Ref.16
VAR_017461
Natural variant3281G → S in SIALIDOSIS; type 1; reduction in enzyme activity. Ref.12 Ref.13 Ref.15
VAR_012222
Natural variant3351P → Q in SIALIDOSIS; type 2; unable to reach the lysosomes. Ref.13
VAR_012223
Natural variant3411R → G in SIALIDOSIS; type 2; affects substrate binding or catalysis. Ref.17
VAR_018077
Natural variant3631L → P in SIALIDOSIS; infantile type 2; unable to reach the lysosomes. Ref.3 Ref.12 Ref.13 Ref.15
VAR_012224
Natural variant3701Y → C in SIALIDOSIS; infantile type 2; catalytically inactive. Ref.13
VAR_012225
Natural variant4001Y → YHY in SIALIDOSIS; type 1; mild mutation as residual activity is still measurable.
VAR_012226

Experimental info

Mutagenesis4121Y → A: Correct sorting to the plasma membrane but no endocytosis and internalization. Ref.9
Mutagenesis4131G → A: Correct sorting to the plasma membrane but no endocytosis and internalization. Ref.9
Mutagenesis4151L → A: Correct sorting to the plasma membrane but no endocytosis and internalization. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Q99519 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 360E60A256DEA07F

FASTA41545,467
        10         20         30         40         50         60 
MTGERPSTAL PDRRWGPRIL GFWGGCRVWV FAAIFLLLSL AASWSKAEND FGLVQPLVTM 

        70         80         90        100        110        120 
EQLLWVSGRQ IGSVDTFRIP LITATPRGTL LAFAEARKMS SSDEGAKFIA LRRSMDQGST 

       130        140        150        160        170        180 
WSPTAFIVND GDVPDGLNLG AVVSDVETGV VFLFYSLCAH KAGCQVASTM LVWSKDDGVS 

       190        200        210        220        230        240 
WSTPRNLSLD IGTEVFAPGP GSGIQKQREP RKGRLIVCGH GTLERDGVFC LLSDDHGASW 

       250        260        270        280        290        300 
RYGSGVSGIP YGQPKQENDF NPDECQPYEL PDGSVVINAR NQNNYHCHCR IVLRSYDACD 

       310        320        330        340        350        360 
TLRPRDVTFD PELVDPVVAA GAVVTSSGIV FFSNPAHPEF RVNLTLRWSF SNGTSWRKET 

       370        380        390        400        410 
VQLWPGPSGY SSLATLEGSM DGEEQAPQLY VLYEKGRNHY TESISVAKIS VYGTL 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of human lysosomal neuraminidase defines the molecular basis of the metabolic storage disorder sialidosis."
Bonten E.J., van der Spoel A., Fornerod M., Grosveld G., d'Azzo A.
Genes Dev. 10:3156-3169(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, VARIANT TYPE II SIALIDOSIS ARG-91.
Tissue: Fibroblast.
[2]"Identification of a sialidase encoded in the human major histocompatibility complex."
Milner C.M., Smith S.V., Carrillo M.B., Taylor G.L., Hollinshead M., Campbell R.D.
J. Biol. Chem. 272:4549-4558(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Monocyte.
[3]"Cloning, expression and chromosomal mapping of human lysosomal sialidase and characterization of mutations in sialidosis."
Pshezhetsky A.V., Richard C., Michaud L., Igdoura S.A., Wang S., Elsliger M.-A., Ou J., Leclerc D., Gravel R.A., Dallaire L., Potier M.
Nat. Genet. 15:316-320(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY, VARIANTS SIALIDOSIS TYR-260 AND PRO-363.
Tissue: Fibroblast.
[4]"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
Shiina S., Tamiya G., Oka A., Inoko H.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"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].
Tissue: Brain and Kidney.
[8]"Molecular mechanism of lysosomal sialidase deficiency in galactosialidosis involves its rapid degradation."
Vinogradova M.V., Michaud L., Mezentsev A.V., Lukong K.E., El-Alfy M., Morales C.R., Potier M., Pshezhetsky A.V.
Biochem. J. 330:641-650(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 48-55, GLYCOSYLATION.
Tissue: Placenta.
[9]"Intracellular distribution of lysosomal sialidase is controlled by the internalization signal in its cytoplasmic tail."
Lukong K.E., Seyrantepe V., Landry K., Trudel S., Ahmad A., Gahl W.A., Lefrancois S., Morales C.R., Pshezhetsky A.V.
J. Biol. Chem. 276:46172-46181(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-412; GLY-413 AND LEU-415.
[10]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-352.
Tissue: Liver.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Characterization of the sialidase molecular defects in sialidosis patients suggests the structural organization of the lysosomal multienzyme complex."
Lukong K.E., Elsliger M.-A., Chang Y., Richard C., Thomas G., Carey W., Tylki-Szymanska A., Czartoryska B., Buchholz T., Rodriguez Criado G., Palmeri S., Pshezhetsky A.V.
Hum. Mol. Genet. 9:1075-1085(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS SIALIDOSIS VAL-68; GLY-182; ARG-227; TYR-260; PHE-270; VAL-298; SER-328 AND PRO-363.
[13]"Novel mutations in lysosomal neuraminidase identify functional domains and determine clinical severity in sialidosis."
Bonten E.J., Arts W.F., Beck M., Covanis A., Donati M.A., Parini R., Zammarchi E., d'Azzo A.
Hum. Mol. Genet. 9:2715-2725(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SIALIDOSIS MET-54; VAL-68; ARG-91; GLY-182; ALA-219; ARG-227; HIS-231; TYR-260; PRO-270; SER-294; VAL-298; SER-328; GLN-335; PRO-363; CYS-370 AND HIS-TYR-400 INS.
[14]"Molecular and structural studies of Japanese patients with sialidosis type 1."
Naganawa Y., Itoh K., Shimmoto M., Takiguchi K., Doi H., Nishizawa Y., Kobayashi T., Kamei S., Lukong K.E., Pshezhetsky A.V., Sakuraba H.
J. Hum. Genet. 45:241-249(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SIALIDOSIS MET-217 AND ARG-243, CHARACTERIZATION OF VARIANTS SIALIDOSIS MET-217 AND ARG-243.
[15]"Mutations in sialidosis impair sialidase binding to the lysosomal multienzyme complex."
Lukong K.E., Landry K., Elsliger M.-A., Chang Y., Lefrancois S., Morales C.R., Pshezhetsky A.V.
J. Biol. Chem. 276:17286-17290(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SIALIDOSIS VAL-68; GLY-182; ARG-227; ARG-240; TYR-260; PHE-270; VAL-298; SER-328 AND PRO-363, CHARACTERIZATION OF VARIANTS SIALIDOSIS VAL-68; GLY-182; ARG-227; TYR-260; PHE-270; VAL-298; SER-328 AND PRO-363.
[16]"Novel missense mutations in the human lysosomal sialidase gene in sialidosis patients and prediction of structural alterations of mutant enzymes."
Itoh K., Naganawa Y., Matsuzawa F., Aikawa S., Doi H., Sasagasako N., Yamada T., Kira J., Kobayashi T., Pshezhetsky A.V., Sakuraba H.
J. Hum. Genet. 47:29-37(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SIALIDOSIS LEU-80; ARG-240 AND SER-316.
[17]"Five novel mutations in the lysosomal sialidase gene (NEU1) in type II sialidosis patients and assessment of their impact on enzyme activity and intracellular targeting using adenovirus-mediated expression."
Pattison S., Pankarican M., Rupar C.A., Graham F.L., Igdoura S.A.
Hum. Mutat. 23:32-39(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SIALIDOSIS PRO-225; VAL-298 AND GLY-341, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS SIALIDOSIS PRO-225; VAL-298 AND GLY-341.
+Additional computationally mapped references.

Web resources

GeneReviews
Wikipedia

Neuraminidase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF040958 mRNA. Translation: AAB96774.1.
X78687 mRNA. Translation: CAA55356.1.
U84246 mRNA. Translation: AAD09239.1.
AF134726 Genomic DNA. Translation: AAD21814.1.
BA000025 Genomic DNA. Translation: BAB63297.1.
BT007206 mRNA. Translation: AAP35870.1.
BC000722 mRNA. Translation: AAH00722.1.
BC011900 mRNA. Translation: AAH11900.1.
RefSeqNP_000425.1. NM_000434.3.
UniGeneHs.520037.

3D structure databases

ProteinModelPortalQ99519.
SMRQ99519. Positions 55-396.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110831. 11 interactions.
IntActQ99519. 5 interactions.
MINTMINT-1389413.
STRING9606.ENSP00000399309.

Chemistry

BindingDBQ99519.
ChEMBLCHEMBL2726.
DrugBankDB00198. Oseltamivir.
DB00558. Zanamivir.

Protein family/group databases

CAZyGH33. Glycoside Hydrolase Family 33.

PTM databases

PhosphoSiteQ99519.

Polymorphism databases

DMDM17368612.

Proteomic databases

PaxDbQ99519.
PeptideAtlasQ99519.
PRIDEQ99519.

Protocols and materials databases

DNASU4758.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000229725; ENSP00000229725; ENSG00000184494.
ENST00000375631; ENSP00000364782; ENSG00000204386.
ENST00000411774; ENSP00000399309; ENSG00000234846.
ENST00000422978; ENSP00000408957; ENSG00000227129.
ENST00000423382; ENSP00000401067; ENSG00000228691.
ENST00000434496; ENSP00000409489; ENSG00000234343.
ENST00000437432; ENSP00000403720; ENSG00000223957.
ENST00000439648; ENSP00000408207; ENSG00000227315.
GeneID4758.
KEGGhsa:4758.
UCSCuc003nxq.4. human.

Organism-specific databases

CTD4758.
GeneCardsGC06M031825.
GC06Mi31836.
GC06Mj31813.
GC06Mk31807.
GC06Ml31865.
GC06Mm31901.
GC06Mn31815.
GC06Mo31817.
HGNCHGNC:7758. NEU1.
HPAHPA015634.
HPA021506.
MIM256550. phenotype.
608272. gene.
neXtProtNX_Q99519.
Orphanet93400. Congenital sialidosis type 2.
93399. Juvenile sialidosis type 2.
812. Sialidosis type 1.
PharmGKBPA31560.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4409.
HOGENOMHOG000007651.
HOVERGENHBG057314.
InParanoidQ99519.
KOK01186.
OMAGTEMFAP.
PhylomeDBQ99519.
TreeFamTF331063.

Enzyme and pathway databases

BRENDA3.2.1.18. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKQ99519.

Gene expression databases

ArrayExpressQ99519.
BgeeQ99519.
CleanExHS_NEU1.
GenevestigatorQ99519.

Family and domain databases

Gene3D2.120.10.10. 1 hit.
InterProIPR026942. Sialidase-1.
IPR026856. Sialidase_fam.
IPR011040. Sialidases.
[Graphical view]
PANTHERPTHR10628. PTHR10628. 1 hit.
PTHR10628:SF9. PTHR10628:SF9. 1 hit.
SUPFAMSSF50939. SSF50939. 1 hit.
ProtoNetSearch...

Other

ChiTaRSNEU1. human.
GeneWikiNEU1.
GenomeRNAi4758.
NextBio18328.
PROQ99519.
SOURCESearch...

Entry information

Entry nameNEUR1_HUMAN
AccessionPrimary (citable) accession number: Q99519
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: May 1, 1997
Last modified: April 16, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries