SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q99519

- NEUR1_HUMAN

UniProt

Q99519 - NEUR1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Sialidase-1
Gene
NEU1, NANH
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 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.1 Publication

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.3 Publications

pH dependencei

Optimum pH is 4.6.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei78 – 781Substrate By similarity
Binding sitei97 – 971Substrate By similarity
Active sitei103 – 1031Proton acceptor By similarity
Binding sitei264 – 2641Substrate By similarity
Binding sitei280 – 2801Substrate By similarity
Binding sitei341 – 3411Substrate By similarity
Active sitei370 – 3701Nucleophile By similarity
Active sitei394 – 3941 Reviewed prediction

GO - Molecular functioni

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

GO - Biological processi

  1. glycosphingolipid metabolic process Source: Reactome
  2. lipid catabolic process Source: UniProtKB-KW
  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-RKQ99519.

Protein family/group databases

CAZyiGH33. Glycoside Hydrolase Family 33.

Names & Taxonomyi

Protein namesi
Recommended name:
Sialidase-1 (EC:3.2.1.18)
Alternative name(s):
Acetylneuraminyl hydrolase
G9 sialidase
Lysosomal sialidase
N-acetyl-alpha-neuraminidase 1
Gene namesi
Name:NEU1
Synonyms:NANH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:7758. NEU1.

Subcellular locationi

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.3 Publications

GO - Cellular componenti

  1. cell junction Source: HPA
  2. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
  3. extracellular vesicular exosome Source: UniProt
  4. intracellular membrane-bounded organelle Source: HPA
  5. lysosomal lumen Source: Reactome
  6. lysosomal membrane Source: UniProtKB-SubCell
  7. lysosome Source: UniProtKB
  8. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Lysosome, Membrane

Pathology & Biotechi

Involvement in diseasei

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.8 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti54 – 541V → M in SIALIDOSIS; type 1; mild mutation as residual activity is still measurable. 1 Publication
VAR_012207
Natural varianti68 – 681G → V in SIALIDOSIS; type 2; less than 10% of activity. 3 Publications
VAR_012208
Natural varianti80 – 801P → L in SIALIDOSIS; type 2; no enzyme activity; retained in the endoplasmic reticulum / Golgi or rapidly degraded in the lysosomes. 1 Publication
VAR_017460
Natural varianti91 – 911L → R in SIALIDOSIS; type 2. 2 Publications
VAR_012209
Natural varianti182 – 1821S → G in SIALIDOSIS; type 1; normally processed. 3 Publications
VAR_012210
Natural varianti217 – 2171V → M in SIALIDOSIS; type 1; partial transport and residual transport activity. 1 Publication
Corresponds to variant rs28940583 [ dbSNP | Ensembl ].
VAR_012211
Natural varianti219 – 2191G → A in SIALIDOSIS; type 1; unable to reach the lysosomes. 1 Publication
VAR_012212
Natural varianti225 – 2251R → P in SIALIDOSIS; type 2; impaired enzyme folding. 1 Publication
Corresponds to variant rs28940584 [ dbSNP | Ensembl ].
VAR_018076
Natural varianti227 – 2271G → R in SIALIDOSIS; type 1 and juvenile type 2; catalytically inactive; retained in pre-lysosomal compartments. 3 Publications
VAR_012213
Natural varianti231 – 2311L → H in SIALIDOSIS; type 1; unable to reach the lysosomes. 1 Publication
VAR_012214
Natural varianti240 – 2401W → R in SIALIDOSIS; type 2; no enzyme activity; retained in the endoplasmic reticulum / Golgi or rapidly degraded in the lysosomes. 2 Publications
VAR_012215
Natural varianti243 – 2431G → R in SIALIDOSIS; type 1; no enzyme activity and no transport to the lysosome. 1 Publication
VAR_012216
Natural varianti260 – 2601F → Y in SIALIDOSIS; infantile type 2; catalytically inactive; rapid intralysosomal degradation. 4 Publications
VAR_012217
Natural varianti270 – 2701L → F in SIALIDOSIS; type 2; reduction in enzyme activity; rapid intralysosomal degradation. 2 Publications
VAR_012219
Natural varianti270 – 2701L → P in SIALIDOSIS. 1 Publication
VAR_012218
Natural varianti294 – 2941R → S in SIALIDOSIS; type 1; mild mutation as residual activity is still measurable. 1 Publication
VAR_012220
Natural varianti298 – 2981A → V in SIALIDOSIS; type 2; less than 10% of activity; rapid intralysosomal degradation; impaired enzyme folding. 4 Publications
VAR_012221
Natural varianti316 – 3161P → S in SIALIDOSIS; type 1; no enzyme activity; retained in the endoplasmic reticulum / Golgi or rapidly degraded in the lysosomes. 1 Publication
VAR_017461
Natural varianti328 – 3281G → S in SIALIDOSIS; type 1; reduction in enzyme activity. 3 Publications
VAR_012222
Natural varianti335 – 3351P → Q in SIALIDOSIS; type 2; unable to reach the lysosomes. 1 Publication
VAR_012223
Natural varianti341 – 3411R → G in SIALIDOSIS; type 2; affects substrate binding or catalysis. 1 Publication
VAR_018077
Natural varianti363 – 3631L → P in SIALIDOSIS; infantile type 2; unable to reach the lysosomes. 4 Publications
VAR_012224
Natural varianti370 – 3701Y → C in SIALIDOSIS; infantile type 2; catalytically inactive. 1 Publication
VAR_012225
Natural varianti400 – 4001Y → YHY in SIALIDOSIS; type 1; mild mutation as residual activity is still measurable.
VAR_012226

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi412 – 4121Y → A: Correct sorting to the plasma membrane but no endocytosis and internalization. 1 Publication
Mutagenesisi413 – 4131G → A: Correct sorting to the plasma membrane but no endocytosis and internalization. 1 Publication
Mutagenesisi415 – 4151L → A: Correct sorting to the plasma membrane but no endocytosis and internalization. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi256550. phenotype.
Orphaneti93400. Congenital sialidosis type 2.
93399. Juvenile sialidosis type 2.
812. Sialidosis type 1.
PharmGKBiPA31560.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 47471 Publication
Add
BLAST
Chaini48 – 415368Sialidase-1
PRO_0000012026Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi186 – 1861N-linked (GlcNAc...) Reviewed prediction
Glycosylationi343 – 3431N-linked (GlcNAc...) Reviewed prediction
Glycosylationi352 – 3521N-linked (GlcNAc...)1 Publication

Post-translational modificationi

N-glycosylated.2 Publications
Phosphorylation of tyrosine within the internalization signal results in inhibition of sialidase internalization and blockage on the plasma membrane.

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ99519.
PaxDbiQ99519.
PeptideAtlasiQ99519.
PRIDEiQ99519.

PTM databases

PhosphoSiteiQ99519.

Expressioni

Tissue specificityi

Highly expressed in pancreas, followed by skeletal muscle, kidney, placenta, heart, lung and liver. Weakly expressed in brain.2 Publications

Gene expression databases

ArrayExpressiQ99519.
BgeeiQ99519.
CleanExiHS_NEU1.
GenevestigatoriQ99519.

Organism-specific databases

HPAiHPA015634.
HPA021506.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi110831. 11 interactions.
IntActiQ99519. 5 interactions.
MINTiMINT-1389413.
STRINGi9606.ENSP00000399309.

Structurei

3D structure databases

ProteinModelPortaliQ99519.
SMRiQ99519. Positions 55-396.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati112 – 12312BNR 1
Add
BLAST
Repeati172 – 18312BNR 2
Add
BLAST
Repeati231 – 24212BNR 3
Add
BLAST
Repeati347 – 35812BNR 4
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi77 – 804FRIP motif
Motifi412 – 4154Internalization signal

Domaini

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

Sequence similaritiesi

Contains 4 BNR repeats.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG4409.
HOGENOMiHOG000007651.
HOVERGENiHBG057314.
InParanoidiQ99519.
KOiK01186.
OMAiGTEMFAP.
PhylomeDBiQ99519.
TreeFamiTF331063.

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
InterProiIPR026856. Sialidase_fam.
IPR011040. Sialidases.
[Graphical view]
PANTHERiPTHR10628. PTHR10628. 1 hit.
SUPFAMiSSF50939. SSF50939. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99519-1 [UniParc]FASTAAdd to Basket

« Hide

MTGERPSTAL PDRRWGPRIL GFWGGCRVWV FAAIFLLLSL AASWSKAEND    50
FGLVQPLVTM EQLLWVSGRQ IGSVDTFRIP LITATPRGTL LAFAEARKMS 100
SSDEGAKFIA LRRSMDQGST WSPTAFIVND GDVPDGLNLG AVVSDVETGV 150
VFLFYSLCAH KAGCQVASTM LVWSKDDGVS WSTPRNLSLD IGTEVFAPGP 200
GSGIQKQREP RKGRLIVCGH GTLERDGVFC LLSDDHGASW RYGSGVSGIP 250
YGQPKQENDF NPDECQPYEL PDGSVVINAR NQNNYHCHCR IVLRSYDACD 300
TLRPRDVTFD PELVDPVVAA GAVVTSSGIV FFSNPAHPEF RVNLTLRWSF 350
SNGTSWRKET VQLWPGPSGY SSLATLEGSM DGEEQAPQLY VLYEKGRNHY 400
TESISVAKIS VYGTL 415
Length:415
Mass (Da):45,467
Last modified:May 1, 1997 - v1
Checksum:i360E60A256DEA07F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti54 – 541V → M in SIALIDOSIS; type 1; mild mutation as residual activity is still measurable. 1 Publication
VAR_012207
Natural varianti68 – 681G → V in SIALIDOSIS; type 2; less than 10% of activity. 3 Publications
VAR_012208
Natural varianti80 – 801P → L in SIALIDOSIS; type 2; no enzyme activity; retained in the endoplasmic reticulum / Golgi or rapidly degraded in the lysosomes. 1 Publication
VAR_017460
Natural varianti88 – 881G → A.
Corresponds to variant rs34712643 [ dbSNP | Ensembl ].
VAR_049203
Natural varianti91 – 911L → R in SIALIDOSIS; type 2. 2 Publications
VAR_012209
Natural varianti182 – 1821S → G in SIALIDOSIS; type 1; normally processed. 3 Publications
VAR_012210
Natural varianti217 – 2171V → M in SIALIDOSIS; type 1; partial transport and residual transport activity. 1 Publication
Corresponds to variant rs28940583 [ dbSNP | Ensembl ].
VAR_012211
Natural varianti219 – 2191G → A in SIALIDOSIS; type 1; unable to reach the lysosomes. 1 Publication
VAR_012212
Natural varianti225 – 2251R → P in SIALIDOSIS; type 2; impaired enzyme folding. 1 Publication
Corresponds to variant rs28940584 [ dbSNP | Ensembl ].
VAR_018076
Natural varianti227 – 2271G → R in SIALIDOSIS; type 1 and juvenile type 2; catalytically inactive; retained in pre-lysosomal compartments. 3 Publications
VAR_012213
Natural varianti231 – 2311L → H in SIALIDOSIS; type 1; unable to reach the lysosomes. 1 Publication
VAR_012214
Natural varianti240 – 2401W → R in SIALIDOSIS; type 2; no enzyme activity; retained in the endoplasmic reticulum / Golgi or rapidly degraded in the lysosomes. 2 Publications
VAR_012215
Natural varianti243 – 2431G → R in SIALIDOSIS; type 1; no enzyme activity and no transport to the lysosome. 1 Publication
VAR_012216
Natural varianti260 – 2601F → Y in SIALIDOSIS; infantile type 2; catalytically inactive; rapid intralysosomal degradation. 4 Publications
VAR_012217
Natural varianti270 – 2701L → F in SIALIDOSIS; type 2; reduction in enzyme activity; rapid intralysosomal degradation. 2 Publications
VAR_012219
Natural varianti270 – 2701L → P in SIALIDOSIS. 1 Publication
VAR_012218
Natural varianti294 – 2941R → S in SIALIDOSIS; type 1; mild mutation as residual activity is still measurable. 1 Publication
VAR_012220
Natural varianti298 – 2981A → V in SIALIDOSIS; type 2; less than 10% of activity; rapid intralysosomal degradation; impaired enzyme folding. 4 Publications
VAR_012221
Natural varianti316 – 3161P → S in SIALIDOSIS; type 1; no enzyme activity; retained in the endoplasmic reticulum / Golgi or rapidly degraded in the lysosomes. 1 Publication
VAR_017461
Natural varianti328 – 3281G → S in SIALIDOSIS; type 1; reduction in enzyme activity. 3 Publications
VAR_012222
Natural varianti335 – 3351P → Q in SIALIDOSIS; type 2; unable to reach the lysosomes. 1 Publication
VAR_012223
Natural varianti341 – 3411R → G in SIALIDOSIS; type 2; affects substrate binding or catalysis. 1 Publication
VAR_018077
Natural varianti363 – 3631L → P in SIALIDOSIS; infantile type 2; unable to reach the lysosomes. 4 Publications
VAR_012224
Natural varianti370 – 3701Y → C in SIALIDOSIS; infantile type 2; catalytically inactive. 1 Publication
VAR_012225
Natural varianti400 – 4001Y → YHY in SIALIDOSIS; type 1; mild mutation as residual activity is still measurable.
VAR_012226

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS4723.1.
RefSeqiNP_000425.1. NM_000434.3.
UniGeneiHs.520037.

Genome annotation databases

EnsembliENST00000229725; ENSP00000229725; ENSG00000184494.
ENST00000375631; ENSP00000364782; ENSG00000204386.
ENST00000411774; ENSP00000399309; ENSG00000234846.
ENST00000422978; ENSP00000408957; ENSG00000227129.
ENST00000423382; ENSP00000401067; ENSG00000228691.
ENST00000434496; ENSP00000409489; ENSG00000234343.
ENST00000437432; ENSP00000403720; ENSG00000223957.
ENST00000439648; ENSP00000408207; ENSG00000227315.
GeneIDi4758.
KEGGihsa:4758.
UCSCiuc003nxq.4. human.

Polymorphism databases

DMDMi17368612.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Neuraminidase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS4723.1.
RefSeqi NP_000425.1. NM_000434.3.
UniGenei Hs.520037.

3D structure databases

ProteinModelPortali Q99519.
SMRi Q99519. Positions 55-396.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110831. 11 interactions.
IntActi Q99519. 5 interactions.
MINTi MINT-1389413.
STRINGi 9606.ENSP00000399309.

Chemistry

BindingDBi Q99519.
ChEMBLi CHEMBL2726.
DrugBanki DB00198. Oseltamivir.
DB00558. Zanamivir.

Protein family/group databases

CAZyi GH33. Glycoside Hydrolase Family 33.

PTM databases

PhosphoSitei Q99519.

Polymorphism databases

DMDMi 17368612.

Proteomic databases

MaxQBi Q99519.
PaxDbi Q99519.
PeptideAtlasi Q99519.
PRIDEi Q99519.

Protocols and materials databases

DNASUi 4758.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000229725 ; ENSP00000229725 ; ENSG00000184494 .
ENST00000375631 ; ENSP00000364782 ; ENSG00000204386 .
ENST00000411774 ; ENSP00000399309 ; ENSG00000234846 .
ENST00000422978 ; ENSP00000408957 ; ENSG00000227129 .
ENST00000423382 ; ENSP00000401067 ; ENSG00000228691 .
ENST00000434496 ; ENSP00000409489 ; ENSG00000234343 .
ENST00000437432 ; ENSP00000403720 ; ENSG00000223957 .
ENST00000439648 ; ENSP00000408207 ; ENSG00000227315 .
GeneIDi 4758.
KEGGi hsa:4758.
UCSCi uc003nxq.4. human.

Organism-specific databases

CTDi 4758.
GeneCardsi GC06M031825.
GC06Mi31836.
GC06Mj31813.
GC06Mk31807.
GC06Ml31865.
GC06Mm31901.
GC06Mn31815.
GC06Mo31817.
HGNCi HGNC:7758. NEU1.
HPAi HPA015634.
HPA021506.
MIMi 256550. phenotype.
608272. gene.
neXtProti NX_Q99519.
Orphaneti 93400. Congenital sialidosis type 2.
93399. Juvenile sialidosis type 2.
812. Sialidosis type 1.
PharmGKBi PA31560.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4409.
HOGENOMi HOG000007651.
HOVERGENi HBG057314.
InParanoidi Q99519.
KOi K01186.
OMAi GTEMFAP.
PhylomeDBi Q99519.
TreeFami TF331063.

Enzyme and pathway databases

BRENDAi 3.2.1.18. 2681.
Reactomei REACT_116105. Glycosphingolipid metabolism.
REACT_200874. Sialic acid metabolism.
SABIO-RK Q99519.

Miscellaneous databases

ChiTaRSi NEU1. human.
GeneWikii NEU1.
GenomeRNAii 4758.
NextBioi 18328.
PROi Q99519.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q99519.
Bgeei Q99519.
CleanExi HS_NEU1.
Genevestigatori Q99519.

Family and domain databases

Gene3Di 2.120.10.10. 1 hit.
InterProi IPR026856. Sialidase_fam.
IPR011040. Sialidases.
[Graphical view ]
PANTHERi PTHR10628. PTHR10628. 1 hit.
SUPFAMi SSF50939. SSF50939. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiNEUR1_HUMAN
AccessioniPrimary (citable) accession number: Q99519
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: May 1, 1997
Last modified: September 3, 2014
This is version 151 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, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 6
    Human chromosome 6: 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

Similar proteinsi