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Alpha-N-acetylglucosaminidase (EC 3.2.1.50) (N-acetyl-alpha-glucosaminidase) (NAG) [Cleaved into: Alpha-N-acetylglucosaminidase 82 kDa form; Alpha-N-acetylglucosaminidase 77 kDa form]

 ANAG_HUMAN              Reviewed;         743 AA.
P54802;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
22-NOV-2017, entry version 171.
RecName: Full=Alpha-N-acetylglucosaminidase;
EC=3.2.1.50;
AltName: Full=N-acetyl-alpha-glucosaminidase;
Short=NAG;
Contains:
RecName: Full=Alpha-N-acetylglucosaminidase 82 kDa form;
Contains:
RecName: Full=Alpha-N-acetylglucosaminidase 77 kDa form;
Flags: Precursor;
Name=NAGLU; Synonyms=UFHSD1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT GLY-737.
TISSUE=Testis;
PubMed=8650226; DOI=10.1073/pnas.93.12.6101;
Zhao H.G., Li H.H., Bach G., Schmidtchen A., Neufeld E.F.;
"The molecular basis of Sanfilippo syndrome type B.";
Proc. Natl. Acad. Sci. U.S.A. 93:6101-6105(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE,
CHARACTERIZATION, AND VARIANT GLY-737.
PubMed=8776591; DOI=10.1093/hmg/5.6.771;
Weber B., Blanch L., Clements P.R., Scott H.S., Hopwood J.J.;
"Cloning and expression of the gene involved in Sanfilippo B syndrome
(mucopolysaccharidosis III B).";
Hum. Mol. Genet. 5:771-777(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-737.
PubMed=8703123; DOI=10.1007/s003359900206;
Zhao Z., Yazdani A., Shen Y., Sun Z.S., Bailey J., Caskey C.T.,
Lee C.C.;
"Molecular dissection of a cosmid from a gene-rich region in 17q21 and
characterization of a candidate gene for alpha-N-acetylglucosaminidase
with two cDNA isoforms.";
Mamm. Genome 7:686-690(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-737.
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-532.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[7]
X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 24-743, AND GLYCOSYLATION AT
ASN-261; ASN-272; ASN-435; ASN-503; ASN-526 AND ASN-532.
Birrane G., Meiyappan M., Dassier A.;
"Crystal structure of N-acetylglucosaminidase.";
Submitted (JAN-2015) to the PDB data bank.
[8]
INVOLVEMENT IN CMT2V, AND VARIANT CMT2V THR-403.
PubMed=25818867; DOI=10.1093/brain/awv074;
Tetreault M., Gonzalez M., Dicaire M.J., Allard P., Gehring K.,
Leblanc D., Leclerc N., Schondorf R., Mathieu J., Zuchner S.,
Brais B.;
"Adult-onset painful axonal polyneuropathy caused by a dominant NAGLU
mutation.";
Brain 138:1477-1483(2015).
[9]
VARIANTS MPS3B CYS-140; CYS-455; LEU-521; GLY-612; CYS-674 AND
HIS-674.
PubMed=9443875; DOI=10.1086/301682;
Zhao H.G., Aronovich E.L., Whitley C.B.;
"Genotype-phenotype correspondence in Sanfilippo syndrome type B.";
Am. J. Hum. Genet. 62:53-63(1998).
[10]
VARIANTS MPS3B HIS-92; SER-115; CYS-140; LYS-153; LEU-358; VAL-664 AND
ARG-682.
PubMed=9443878; DOI=10.1086/301685;
Schmidtchen A., Greenberg D., Zhao H.G., Li H.H., Huang Y., Tieu P.,
Zhao H.-Z., Cheng S., Zhao Z., Whitley C.B., di Natale P.,
Neufeld E.F.;
"NAGLU mutations underlying Sanfilippo syndrome type B.";
Am. J. Hum. Genet. 62:64-69(1998).
[11]
VARIANTS MPS3B CYS-48; CYS-140; CYS-234; ARG-268; LEU-521; TRP-565;
PRO-591 AND LYS-705.
PubMed=9832037; DOI=10.1136/jmg.35.11.910;
Beesley C.E., Young E.P., Vellodi A., Winchester B.G.;
"Identification of 12 novel mutations in the alpha-N-
acetylglucosaminidase gene in 14 patients with Sanfilippo syndrome
type B (mucopolysaccharidosis type IIIB).";
J. Med. Genet. 35:910-914(1998).
[12]
VARIANTS MPS3B CYS-79; ARG-100; CYS-140; PHE-142 DEL; LEU-243;
PHE-277; PRO-280; ARG-292; LYS-452; TRP-482; ARG-561; GLN-565; HIS-674
AND LYS-705, AND VARIANT GLY-737.
PubMed=9950362;
Bunge S., Knigge A., Steglich C., Kleijer W.J., van Diggelen O.P.,
Beck M., Gal A.;
"Mucopolysaccharidosis type IIIB (Sanfilippo B): identification of 18
novel alpha-N-acetylglucosaminidase gene mutations.";
J. Med. Genet. 36:28-31(1999).
[13]
VARIANTS MPS3B LEU-48; SER-69; PRO-227; ARG-248; ARG-292; PHE-334;
SER-410; ARG-414; LEU-521; PRO-560; PRO-565; TRP-565; PHE-617;
CYS-643; GLU-650; CYS-674 AND PRO-676, AND VARIANT GLY-737.
PubMed=10094189; DOI=10.1038/sj.ejhg.5200242;
Weber B., Guo X.-H., Kleijer W.J., van de Kamp J.J.P.,
Poorthuis B.J.H.M., Hopwood J.J.;
"Sanfilippo type B syndrome (mucopolysaccharidosis III B): allelic
heterogeneity corresponds to the wide spectrum of clinical
phenotypes.";
Eur. J. Hum. Genet. 7:34-44(1999).
[14]
VARIANT MPS3B LEU-48, AND CHARACTERIZATION OF VARIANT MPS3B LEU-48.
PubMed=11068184; DOI=10.1016/S0925-4439(00)00066-1;
Yogalingam G., Weber B., Meehan J., Rogers J., Hopwood J.J.;
"Mucopolysaccharidosis type IIIB: characterisation and expression of
wild-type and mutant recombinant alpha-N-acetylglucosaminidase and
relationship with sanfilippo phenotype in an attenuated patient.";
Biochim. Biophys. Acta 1502:415-425(2000).
[15]
VARIANTS MPS3B PHE-35; ASP-82; CYS-140; CYS-156; CYS-234; ARG-292;
GLY-501; TRP-520; TYR-534 AND CYS-649, AND CHARACTERIZATION OF
VARIANTS MPS3B PHE-35; ASP-82; CYS-156; GLY-501; TRP-520; TYR-534 AND
CYS-649.
PubMed=11153910; DOI=10.1007/s004390000429;
Tessitore A., Villani G.R.D., Di Domenico C., Filocamo M., Gatti R.,
Di Natale P.;
"Molecular defects in the alpha-N-acetylglucosaminidase gene in
Italian Sanfilippo type B patients.";
Hum. Genet. 107:568-576(2000).
[16]
VARIANTS MPS3B SER-79; CYS-234; GLY-474; TRP-565 AND PHE-658.
PubMed=11286389; DOI=10.1023/A:1005627311402;
Coll M.J., Anton C., Chabas A.;
"Allelic heterogeneity in Spanish patients with Sanfilippo disease
type B. Identification of eight new mutations.";
J. Inherit. Metab. Dis. 24:83-84(2001).
[17]
VARIANTS MPS3B LYS-153; ARG-248; ILE-437 AND ARG-682.
PubMed=11793481; DOI=10.1002/humu.9009;
Emre S., Terzioglu M., Tokatli A., Coskun T., Ozalp I., Weber B.,
Hopwood J.J.;
"Sanfilippo syndrome in Turkey: identification of novel mutations in
subtypes A and B.";
Hum. Mutat. 19:184-185(2002).
[18]
VARIANTS MPS3B MET-241; LEU-314; TRP-482; PRO-565 AND TRP-565.
PubMed=12202988; DOI=10.1007/s100380200070;
Tanaka A., Kimura M., Lan H.T.N., Takaura N., Yamano T.;
"Molecular analysis of the alpha-N-acetylglucosaminidase gene in seven
Japanese patients from six unrelated families with
mucopolysaccharidosis IIIB (Sanfilippo type B), including two novel
mutations.";
J. Hum. Genet. 47:484-487(2002).
[19]
VARIANTS MPS3B CYS-130; ARG-154; CYS-309; GLU-412 AND TRP-565, AND
CHARACTERIZATION OF VARIANTS MPS3B CYS-130; ARG-154; CYS-309; GLU-412
AND TRP-565.
PubMed=11836372; DOI=10.1136/jmg.39.2.e3;
Lee-Chen G.J., Lin S.P., Lin S.Z., Chuang C.K., Hsiao K.T.,
Huang C.F., Lien W.C.;
"Identification and characterisation of mutations underlying
Sanfilippo syndrome type B (mucopolysaccharidosis type IIIB).";
J. Med. Genet. 39:E3-E3(2002).
[20]
VARIANTS MPS3B CYS-140; PRO-242; ARG-292; ARG-414; LYS-446; LYS-452;
GLN-482 AND LEU-516, AND CHARACTERIZATION OF VARIANTS MPS3B PRO-242;
ARG-414; LYS-446; GLN-482 AND LEU-516.
PubMed=14984474; DOI=10.1111/j.0009-9163.2004.00210.x;
Beesley C., Moraitou M., Winchester B., Schulpis K., Dimitriou E.,
Michelakakis H.;
"Sanfilippo B syndrome: molecular defects in Greek patients.";
Clin. Genet. 65:143-149(2004).
[21]
VARIANT MPS3B PRO-565.
PubMed=15933803; DOI=10.1007/s10038-005-0258-4;
Chinen Y., Tohma T., Izumikawa Y., Uehara H., Ohta T.;
"Sanfilippo type B syndrome: five patients with an R565P homozygous
mutation in the alpha-N-acetylglucosaminidase gene from the Okinawa
islands in Japan.";
J. Hum. Genet. 50:357-359(2005).
[22]
VARIANTS MPS3B TRP-38; GLY-77; CYS-79; CYS-130; PRO-246; CYS-309;
CYS-335; ARG-414; LYS-452; TRP-482; TRP-520; LEU-521 AND TRP-565, AND
CHARACTERIZATION OF VARIANTS MPS3B TRP-38; GLY-77 AND CYS-335.
PubMed=16151907; DOI=10.1007/s10545-005-0093-y;
Beesley C.E., Jackson M., Young E.P., Vellodi A., Winchester B.G.;
"Molecular defects in Sanfilippo syndrome type B
(mucopolysaccharidosis IIIB).";
J. Inherit. Metab. Dis. 28:759-767(2005).
[23]
VARIANTS MPS3B 153-GLU--TRP-743 DEL AND PRO-550.
PubMed=28101780; DOI=10.1007/s12519-017-0005-x;
Ouesleti S., Coutinho M.F., Ribeiro I., Miled A., Mosbahi D.S.,
Alves S.;
"Update of the spectrum of mucopolysaccharidoses type III in Tunisia:
identification of three novel mutations and in silico structural
analysis of the missense mutations.";
World J. Pediatr. 13:374-380(2017).
-!- FUNCTION: Involved in the degradation of heparan sulfate.
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing N-acetyl-
D-glucosamine residues in N-acetyl-alpha-D-glucosaminides.
-!- SUBUNIT: Monomer and homodimer.
-!- SUBCELLULAR LOCATION: Lysosome.
-!- TISSUE SPECIFICITY: Liver, ovary, peripheral blood leukocytes,
testis, prostate, spleen, colon, lung, placenta and kidney.
-!- DISEASE: Mucopolysaccharidosis 3B (MPS3B) [MIM:252920]: A form of
mucopolysaccharidosis type 3, an autosomal recessive lysosomal
storage disease due to impaired degradation of heparan sulfate.
MPS3 is characterized by severe central nervous system
degeneration, but only mild somatic disease. Onset of clinical
features usually occurs between 2 and 6 years; severe neurologic
degeneration occurs in most patients between 6 and 10 years of
age, and death occurs typically during the second or third decade
of life. {ECO:0000269|PubMed:10094189,
ECO:0000269|PubMed:11068184, ECO:0000269|PubMed:11153910,
ECO:0000269|PubMed:11286389, ECO:0000269|PubMed:11793481,
ECO:0000269|PubMed:11836372, ECO:0000269|PubMed:12202988,
ECO:0000269|PubMed:14984474, ECO:0000269|PubMed:15933803,
ECO:0000269|PubMed:16151907, ECO:0000269|PubMed:28101780,
ECO:0000269|PubMed:9443875, ECO:0000269|PubMed:9443878,
ECO:0000269|PubMed:9832037, ECO:0000269|PubMed:9950362}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Charcot-Marie-Tooth disease 2V (CMT2V) [MIM:616491]: An
axonal form of Charcot-Marie-Tooth disease, a disorder of the
peripheral nervous system, characterized by progressive weakness
and atrophy, initially of the peroneal muscles and later of the
distal muscles of the arms. Charcot-Marie-Tooth disease is
classified in two main groups on the basis of electrophysiologic
properties and histopathology: primary peripheral demyelinating
neuropathies (designated CMT1 when they are dominantly inherited)
and primary peripheral axonal neuropathies (CMT2). Neuropathies of
the CMT2 group are characterized by signs of axonal degeneration
in the absence of obvious myelin alterations, normal or slightly
reduced nerve conduction velocities, and progressive distal muscle
weakness and atrophy. CMT2V is an autosomal dominant sensory
neuropathy with late onset. The main clinical feature is recurrent
leg pain that progresses to constant painful paraesthesias in the
feet and later the hands. As it evolves, some patients develop a
mild sensory ataxia. {ECO:0000269|PubMed:25818867}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 89 family.
{ECO:0000305}.
-!- CAUTION: A MPS3B mutation at position 100 was erroneously reported
(PubMed:9950362) as an amino acid change from Arg to His. The
right amino acid change is from His to Arg.
{ECO:0000305|PubMed:9950362}.
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EMBL; U43572; AAC50512.1; -; Genomic_DNA.
EMBL; U43573; AAC50513.1; -; mRNA.
EMBL; U40846; AAB06188.1; -; mRNA.
EMBL; L78464; AAB36604.1; -; mRNA.
EMBL; AC067852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC053991; AAH53991.1; -; mRNA.
CCDS; CCDS11427.1; -.
PIR; G02270; G02270.
RefSeq; NP_000254.2; NM_000263.3.
UniGene; Hs.50727; -.
PDB; 4XWH; X-ray; 2.32 A; A=24-743.
PDBsum; 4XWH; -.
ProteinModelPortal; P54802; -.
SMR; P54802; -.
BioGrid; 110750; 27.
STRING; 9606.ENSP00000225927; -.
DrugBank; DB00141; N-Acetyl-D-glucosamine.
CAZy; GH89; Glycoside Hydrolase Family 89.
iPTMnet; P54802; -.
PhosphoSitePlus; P54802; -.
UniCarbKB; P54802; -.
BioMuta; NAGLU; -.
DMDM; 317373322; -.
EPD; P54802; -.
MaxQB; P54802; -.
PaxDb; P54802; -.
PeptideAtlas; P54802; -.
PRIDE; P54802; -.
TopDownProteomics; P54802; -.
Ensembl; ENST00000225927; ENSP00000225927; ENSG00000108784.
GeneID; 4669; -.
KEGG; hsa:4669; -.
UCSC; uc002hzv.4; human.
CTD; 4669; -.
DisGeNET; 4669; -.
EuPathDB; HostDB:ENSG00000108784.9; -.
GeneCards; NAGLU; -.
H-InvDB; HIX0202517; -.
HGNC; HGNC:7632; NAGLU.
HPA; HPA038815; -.
MalaCards; NAGLU; -.
MIM; 252920; phenotype.
MIM; 609701; gene.
MIM; 616491; phenotype.
neXtProt; NX_P54802; -.
OpenTargets; ENSG00000108784; -.
Orphanet; 79270; Sanfilippo syndrome type B.
PharmGKB; PA31437; -.
eggNOG; KOG2233; Eukaryota.
eggNOG; ENOG410XNMK; LUCA.
GeneTree; ENSGT00390000005900; -.
HOGENOM; HOG000214539; -.
HOVERGEN; HBG004225; -.
InParanoid; P54802; -.
KO; K01205; -.
OMA; LFPNSTM; -.
OrthoDB; EOG091G02QN; -.
PhylomeDB; P54802; -.
TreeFam; TF300689; -.
BRENDA; 3.2.1.50; 2681.
Reactome; R-HSA-2024096; HS-GAG degradation.
Reactome; R-HSA-2206282; MPS IIIB - Sanfilippo syndrome B.
ChiTaRS; NAGLU; human.
GenomeRNAi; 4669; -.
PRO; PR:P54802; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108784; -.
CleanEx; HS_NAGLU; -.
ExpressionAtlas; P54802; baseline and differential.
Genevisible; P54802; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0005764; C:lysosome; TAS:ProtInc.
GO; GO:0004561; F:alpha-N-acetylglucosaminidase activity; TAS:Reactome.
GO; GO:0021680; P:cerebellar Purkinje cell layer development; IEA:Ensembl.
GO; GO:0006027; P:glycosaminoglycan catabolic process; TAS:Reactome.
GO; GO:0060119; P:inner ear receptor cell development; IEA:Ensembl.
GO; GO:0045475; P:locomotor rhythm; IEA:Ensembl.
GO; GO:0007040; P:lysosome organization; IEA:Ensembl.
GO; GO:0042474; P:middle ear morphogenesis; IEA:Ensembl.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:0046548; P:retinal rod cell development; IEA:Ensembl.
Gene3D; 3.30.379.10; -; 1.
InterPro; IPR029018; Chitobiase/Hex-like_dom2.
InterPro; IPR017853; Glycoside_hydrolase_SF.
InterPro; IPR007781; NAGLU.
InterPro; IPR024732; NAGLU_C.
InterPro; IPR024240; NAGLU_N.
InterPro; IPR024733; NAGLU_tim-barrel.
PANTHER; PTHR12872; PTHR12872; 1.
Pfam; PF05089; NAGLU; 1.
Pfam; PF12972; NAGLU_C; 1.
Pfam; PF12971; NAGLU_N; 1.
SUPFAM; SSF51445; SSF51445; 2.
1: Evidence at protein level;
3D-structure; Charcot-Marie-Tooth disease; Complete proteome;
Direct protein sequencing; Disease mutation; Glycoprotein;
Glycosidase; Hydrolase; Lysosome; Mucopolysaccharidosis;
Neurodegeneration; Neuropathy; Polymorphism; Reference proteome;
Signal.
SIGNAL 1 23
CHAIN 24 743 Alpha-N-acetylglucosaminidase 82 kDa
form.
/FTId=PRO_0000020728.
CHAIN 59 743 Alpha-N-acetylglucosaminidase 77 kDa
form.
/FTId=PRO_0000020729.
COMPBIAS 68 71 Poly-Gly.
COMPBIAS 84 87 Poly-Ala.
CARBOHYD 261 261 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4XWH,
ECO:0000269|Ref.7}.
CARBOHYD 272 272 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4XWH,
ECO:0000269|Ref.7}.
CARBOHYD 435 435 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4XWH,
ECO:0000269|Ref.7}.
CARBOHYD 503 503 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4XWH,
ECO:0000269|Ref.7}.
CARBOHYD 526 526 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4XWH,
ECO:0000269|Ref.7}.
CARBOHYD 532 532 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4XWH,
ECO:0000269|PubMed:19159218,
ECO:0000269|Ref.7}.
VARIANT 35 35 L -> F (in MPS3B; no enzyme activity;
synthesizes a polypeptide with a
molecular size similar to that of the
wild-type).
{ECO:0000269|PubMed:11153910}.
/FTId=VAR_054699.
VARIANT 38 38 R -> W (in MPS3B; decreases the enzyme
activity markedly).
{ECO:0000269|PubMed:16151907}.
/FTId=VAR_054700.
VARIANT 48 48 F -> C (in MPS3B; dbSNP:rs867910252).
{ECO:0000269|PubMed:9832037}.
/FTId=VAR_054701.
VARIANT 48 48 F -> L (in MPS3B; associated with a
partially degraded polypeptide in a 16-
hour chase experiment suggesting that L-
48 NAGLU affects the processing and
stability of the gene; some L-48 NAGLU is
being correctly sorted to the lysosomal
compartment; dbSNP:rs104894599).
{ECO:0000269|PubMed:10094189,
ECO:0000269|PubMed:11068184}.
/FTId=VAR_025489.
VARIANT 69 69 G -> S (in MPS3B).
{ECO:0000269|PubMed:10094189}.
/FTId=VAR_054702.
VARIANT 77 77 V -> G (in MPS3B; decreases the enzyme
activity markedly).
{ECO:0000269|PubMed:16151907}.
/FTId=VAR_054703.
VARIANT 79 79 G -> C (in MPS3B).
{ECO:0000269|PubMed:16151907,
ECO:0000269|PubMed:9950362}.
/FTId=VAR_008979.
VARIANT 79 79 G -> S (in MPS3B).
{ECO:0000269|PubMed:11286389}.
/FTId=VAR_054704.
VARIANT 82 82 G -> D (in MPS3B; no enzyme activity;
synthesizes a polypeptide with a
molecular size similar to that of the
wild-type).
{ECO:0000269|PubMed:11153910}.
/FTId=VAR_054705.
VARIANT 92 92 Y -> H (in MPS3B).
{ECO:0000269|PubMed:9443878}.
/FTId=VAR_005007.
VARIANT 100 100 H -> R (in MPS3B).
{ECO:0000269|PubMed:9950362}.
/FTId=VAR_008980.
VARIANT 115 115 P -> S (in MPS3B; dbSNP:rs758785463).
{ECO:0000269|PubMed:9443878}.
/FTId=VAR_005008.
VARIANT 130 130 R -> C (in MPS3B; does not yield active
enzyme). {ECO:0000269|PubMed:11836372,
ECO:0000269|PubMed:16151907}.
/FTId=VAR_054706.
VARIANT 140 140 Y -> C (in MPS3B; dbSNP:rs753520553).
{ECO:0000269|PubMed:11153910,
ECO:0000269|PubMed:14984474,
ECO:0000269|PubMed:9443875,
ECO:0000269|PubMed:9443878,
ECO:0000269|PubMed:9832037,
ECO:0000269|PubMed:9950362}.
/FTId=VAR_005009.
VARIANT 142 142 Missing (in MPS3B).
{ECO:0000269|PubMed:9950362}.
/FTId=VAR_008981.
VARIANT 153 743 Missing (in MPS3B).
{ECO:0000269|PubMed:28101780}.
/FTId=VAR_079424.
VARIANT 153 153 E -> K (in MPS3B).
{ECO:0000269|PubMed:11793481,
ECO:0000269|PubMed:9443878}.
/FTId=VAR_005010.
VARIANT 154 154 I -> R (in MPS3B; does not yield active
enzyme; dbSNP:rs770684838).
{ECO:0000269|PubMed:11836372}.
/FTId=VAR_054707.
VARIANT 156 156 W -> C (in MPS3B; no enzyme activity;
synthesizes a polypeptide with a
molecular size similar to that of the
wild-type).
{ECO:0000269|PubMed:11153910}.
/FTId=VAR_054708.
VARIANT 227 227 H -> P (in MPS3B; dbSNP:rs747155746).
{ECO:0000269|PubMed:10094189}.
/FTId=VAR_054709.
VARIANT 234 234 R -> C (in MPS3B; dbSNP:rs104894601).
{ECO:0000269|PubMed:11153910,
ECO:0000269|PubMed:11286389,
ECO:0000269|PubMed:9832037}.
/FTId=VAR_054710.
VARIANT 241 241 V -> M (in MPS3B).
{ECO:0000269|PubMed:12202988}.
/FTId=VAR_054711.
VARIANT 242 242 L -> P (in MPS3B; no enzyme activity).
{ECO:0000269|PubMed:14984474}.
/FTId=VAR_054712.
VARIANT 243 243 P -> L (in MPS3B).
{ECO:0000269|PubMed:9950362}.
/FTId=VAR_008982.
VARIANT 246 246 A -> P (in MPS3B; produces 12.7% residual
enzyme activity).
{ECO:0000269|PubMed:16151907}.
/FTId=VAR_054713.
VARIANT 248 248 H -> R (in MPS3B).
{ECO:0000269|PubMed:10094189,
ECO:0000269|PubMed:11793481}.
/FTId=VAR_054714.
VARIANT 268 268 W -> R (in MPS3B).
{ECO:0000269|PubMed:9832037}.
/FTId=VAR_054715.
VARIANT 277 277 C -> F (in MPS3B).
{ECO:0000269|PubMed:9950362}.
/FTId=VAR_008983.
VARIANT 280 280 L -> P (in MPS3B).
{ECO:0000269|PubMed:9950362}.
/FTId=VAR_008984.
VARIANT 292 292 G -> R (in MPS3B).
{ECO:0000269|PubMed:10094189,
ECO:0000269|PubMed:11153910,
ECO:0000269|PubMed:14984474,
ECO:0000269|PubMed:9950362}.
/FTId=VAR_008985.
VARIANT 309 309 Y -> C (in MPS3B; does not yield active
enzyme). {ECO:0000269|PubMed:11836372,
ECO:0000269|PubMed:16151907}.
/FTId=VAR_054716.
VARIANT 314 314 F -> L (in MPS3B; dbSNP:rs104894600).
{ECO:0000269|PubMed:12202988}.
/FTId=VAR_025490.
VARIANT 334 334 V -> F (in MPS3B; dbSNP:rs749140168).
{ECO:0000269|PubMed:10094189}.
/FTId=VAR_054717.
VARIANT 335 335 Y -> C (in MPS3B; decreases the enzyme
activity markedly; dbSNP:rs768918822).
{ECO:0000269|PubMed:16151907}.
/FTId=VAR_054718.
VARIANT 358 358 P -> L (in MPS3B; dbSNP:rs368687817).
{ECO:0000269|PubMed:9443878}.
/FTId=VAR_005011.
VARIANT 403 403 I -> T (in CMT2V; dbSNP:rs796052122).
{ECO:0000269|PubMed:25818867}.
/FTId=VAR_074607.
VARIANT 410 410 F -> S (in MPS3B; dbSNP:rs574688121).
{ECO:0000269|PubMed:10094189}.
/FTId=VAR_054719.
VARIANT 412 412 G -> E (in MPS3B; does not yield active
enzyme). {ECO:0000269|PubMed:11836372}.
/FTId=VAR_054720.
VARIANT 414 414 H -> R (in MPS3B; no enzyme activity;
dbSNP:rs768814260).
{ECO:0000269|PubMed:10094189,
ECO:0000269|PubMed:14984474,
ECO:0000269|PubMed:16151907}.
/FTId=VAR_054721.
VARIANT 437 437 T -> I (in MPS3B).
{ECO:0000269|PubMed:11793481}.
/FTId=VAR_054722.
VARIANT 446 446 E -> K (in MPS3B; no enzyme activity;
dbSNP:rs114625063).
{ECO:0000269|PubMed:14984474}.
/FTId=VAR_054723.
VARIANT 452 452 E -> K (in MPS3B).
{ECO:0000269|PubMed:14984474,
ECO:0000269|PubMed:16151907,
ECO:0000269|PubMed:9950362}.
/FTId=VAR_008986.
VARIANT 455 455 Y -> C (in MPS3B; dbSNP:rs375103824).
{ECO:0000269|PubMed:9443875}.
/FTId=VAR_054724.
VARIANT 474 474 W -> G (in MPS3B).
{ECO:0000269|PubMed:11286389}.
/FTId=VAR_054725.
VARIANT 482 482 R -> Q (in MPS3B; no enzyme activity;
dbSNP:rs200909691).
{ECO:0000269|PubMed:14984474}.
/FTId=VAR_054726.
VARIANT 482 482 R -> W (in MPS3B; dbSNP:rs104894596).
{ECO:0000269|PubMed:12202988,
ECO:0000269|PubMed:16151907,
ECO:0000269|PubMed:9950362}.
/FTId=VAR_008987.
VARIANT 501 501 V -> G (in MPS3B; no enzyme activity;
synthesizes a polypeptide with a
molecular size similar to that of the
wild-type).
{ECO:0000269|PubMed:11153910}.
/FTId=VAR_054727.
VARIANT 516 516 P -> L (in MPS3B; no enzyme activity;
dbSNP:rs773054539).
{ECO:0000269|PubMed:14984474}.
/FTId=VAR_054728.
VARIANT 520 520 R -> W (in MPS3B; no enzyme activity;
synthesizes a polypeptide with a
molecular size similar to that of the
wild-type). {ECO:0000269|PubMed:11153910,
ECO:0000269|PubMed:16151907}.
/FTId=VAR_054729.
VARIANT 521 521 P -> L (in MPS3B; accounts for
approximately 6% of mutations in
Australasian patients with MPS3B;
dbSNP:rs104894595).
{ECO:0000269|PubMed:10094189,
ECO:0000269|PubMed:16151907,
ECO:0000269|PubMed:9443875,
ECO:0000269|PubMed:9832037}.
/FTId=VAR_025491.
VARIANT 534 534 S -> Y (in MPS3B; no enzyme activity;
synthesizes a polypeptide with a
molecular size similar to that of the
wild-type).
{ECO:0000269|PubMed:11153910}.
/FTId=VAR_054730.
VARIANT 550 550 L -> P (in MPS3B; unknown pathological
significance).
{ECO:0000269|PubMed:28101780}.
/FTId=VAR_079425.
VARIANT 560 560 L -> P (in MPS3B).
{ECO:0000269|PubMed:10094189}.
/FTId=VAR_054731.
VARIANT 561 561 L -> R (in MPS3B).
{ECO:0000269|PubMed:9950362}.
/FTId=VAR_008988.
VARIANT 565 565 R -> P (in MPS3B; does not yield active
enzyme; dbSNP:rs104894598).
{ECO:0000269|PubMed:10094189,
ECO:0000269|PubMed:12202988,
ECO:0000269|PubMed:15933803}.
/FTId=VAR_025492.
VARIANT 565 565 R -> Q (in MPS3B; dbSNP:rs104894598).
{ECO:0000269|PubMed:9950362}.
/FTId=VAR_008989.
VARIANT 565 565 R -> W (in MPS3B; accounts for
approximately 6% of the mutant alleles in
Australasian patients with MPS3B;
dbSNP:rs104894597).
{ECO:0000269|PubMed:10094189,
ECO:0000269|PubMed:11286389,
ECO:0000269|PubMed:11836372,
ECO:0000269|PubMed:12202988,
ECO:0000269|PubMed:16151907,
ECO:0000269|PubMed:9832037}.
/FTId=VAR_025493.
VARIANT 591 591 L -> P (in MPS3B).
{ECO:0000269|PubMed:9832037}.
/FTId=VAR_054732.
VARIANT 612 612 S -> G (in MPS3B; dbSNP:rs148881970).
{ECO:0000269|PubMed:9443875}.
/FTId=VAR_054733.
VARIANT 617 617 L -> F (in MPS3B).
{ECO:0000269|PubMed:10094189}.
/FTId=VAR_054734.
VARIANT 643 643 R -> C (in MPS3B; accounts for
approximately 20% of MPS3B alleles in a
Dutch patient group; dbSNP:rs104894594).
{ECO:0000269|PubMed:10094189}.
/FTId=VAR_025494.
VARIANT 643 643 R -> H (in MPS3B; dbSNP:rs104894593).
/FTId=VAR_005012.
VARIANT 649 649 W -> C (in MPS3B; no enzyme activity;
synthesizes a polypeptide with a
molecular size similar to that of the
wild-type).
{ECO:0000269|PubMed:11153910}.
/FTId=VAR_054735.
VARIANT 650 650 G -> E (in MPS3B; dbSNP:rs527236037).
{ECO:0000269|PubMed:10094189}.
/FTId=VAR_054736.
VARIANT 658 658 Y -> F (in MPS3B).
{ECO:0000269|PubMed:11286389}.
/FTId=VAR_054737.
VARIANT 664 664 A -> V (in MPS3B; dbSNP:rs746006696).
{ECO:0000269|PubMed:9443878}.
/FTId=VAR_005013.
VARIANT 674 674 R -> C (in MPS3B; dbSNP:rs763299645).
{ECO:0000269|PubMed:10094189,
ECO:0000269|PubMed:9443875}.
/FTId=VAR_054738.
VARIANT 674 674 R -> H (in MPS3B; dbSNP:rs104894590).
{ECO:0000269|PubMed:9443875,
ECO:0000269|PubMed:9950362}.
/FTId=VAR_005014.
VARIANT 676 676 R -> P (in MPS3B).
{ECO:0000269|PubMed:10094189}.
/FTId=VAR_054739.
VARIANT 682 682 L -> R (in MPS3B).
{ECO:0000269|PubMed:11793481,
ECO:0000269|PubMed:9443878}.
/FTId=VAR_005015.
VARIANT 705 705 E -> K (in MPS3B).
{ECO:0000269|PubMed:9832037,
ECO:0000269|PubMed:9950362}.
/FTId=VAR_008990.
VARIANT 737 737 R -> G (in dbSNP:rs86312).
{ECO:0000269|PubMed:10094189,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8650226,
ECO:0000269|PubMed:8703123,
ECO:0000269|PubMed:8776591,
ECO:0000269|PubMed:9950362}.
/FTId=VAR_008991.
CONFLICT 551 551 A -> L (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 553 553 S -> L (in Ref. 2; AA sequence).
{ECO:0000305}.
HELIX 25 40 {ECO:0000244|PDB:4XWH}.
HELIX 42 45 {ECO:0000244|PDB:4XWH}.
STRAND 48 52 {ECO:0000244|PDB:4XWH}.
HELIX 54 56 {ECO:0000244|PDB:4XWH}.
STRAND 64 69 {ECO:0000244|PDB:4XWH}.
STRAND 75 81 {ECO:0000244|PDB:4XWH}.
HELIX 82 95 {ECO:0000244|PDB:4XWH}.
STRAND 100 102 {ECO:0000244|PDB:4XWH}.
STRAND 105 107 {ECO:0000244|PDB:4XWH}.
STRAND 121 124 {ECO:0000244|PDB:4XWH}.
STRAND 128 132 {ECO:0000244|PDB:4XWH}.
HELIX 137 140 {ECO:0000244|PDB:4XWH}.
HELIX 147 159 {ECO:0000244|PDB:4XWH}.
STRAND 164 166 {ECO:0000244|PDB:4XWH}.
HELIX 171 182 {ECO:0000244|PDB:4XWH}.
HELIX 186 192 {ECO:0000244|PDB:4XWH}.
HELIX 196 198 {ECO:0000244|PDB:4XWH}.
HELIX 199 203 {ECO:0000244|PDB:4XWH}.
HELIX 216 235 {ECO:0000244|PDB:4XWH}.
STRAND 239 243 {ECO:0000244|PDB:4XWH}.
STRAND 247 249 {ECO:0000244|PDB:4XWH}.
HELIX 253 256 {ECO:0000244|PDB:4XWH}.
STRAND 262 264 {ECO:0000244|PDB:4XWH}.
TURN 273 275 {ECO:0000244|PDB:4XWH}.
STRAND 279 281 {ECO:0000244|PDB:4XWH}.
HELIX 287 303 {ECO:0000244|PDB:4XWH}.
STRAND 307 310 {ECO:0000244|PDB:4XWH}.
HELIX 324 339 {ECO:0000244|PDB:4XWH}.
STRAND 346 350 {ECO:0000244|PDB:4XWH}.
HELIX 352 356 {ECO:0000244|PDB:4XWH}.
TURN 358 360 {ECO:0000244|PDB:4XWH}.
HELIX 363 370 {ECO:0000244|PDB:4XWH}.
STRAND 377 382 {ECO:0000244|PDB:4XWH}.
TURN 383 387 {ECO:0000244|PDB:4XWH}.
HELIX 391 393 {ECO:0000244|PDB:4XWH}.
HELIX 395 398 {ECO:0000244|PDB:4XWH}.
STRAND 402 406 {ECO:0000244|PDB:4XWH}.
HELIX 420 432 {ECO:0000244|PDB:4XWH}.
STRAND 438 443 {ECO:0000244|PDB:4XWH}.
HELIX 452 461 {ECO:0000244|PDB:4XWH}.
HELIX 471 483 {ECO:0000244|PDB:4XWH}.
HELIX 488 499 {ECO:0000244|PDB:4XWH}.
TURN 500 502 {ECO:0000244|PDB:4XWH}.
HELIX 516 518 {ECO:0000244|PDB:4XWH}.
HELIX 533 545 {ECO:0000244|PDB:4XWH}.
HELIX 547 550 {ECO:0000244|PDB:4XWH}.
HELIX 554 584 {ECO:0000244|PDB:4XWH}.
HELIX 588 600 {ECO:0000244|PDB:4XWH}.
HELIX 602 610 {ECO:0000244|PDB:4XWH}.
HELIX 614 616 {ECO:0000244|PDB:4XWH}.
HELIX 618 628 {ECO:0000244|PDB:4XWH}.
HELIX 632 646 {ECO:0000244|PDB:4XWH}.
TURN 654 659 {ECO:0000244|PDB:4XWH}.
HELIX 666 669 {ECO:0000244|PDB:4XWH}.
HELIX 671 687 {ECO:0000244|PDB:4XWH}.
HELIX 694 710 {ECO:0000244|PDB:4XWH}.
HELIX 723 740 {ECO:0000244|PDB:4XWH}.
SEQUENCE 743 AA; 82266 MW; 6D8D6A42C7BA7CF3 CRC64;
MEAVAVAAAV GVLLLAGAGG AAGDEAREAA AVRALVARLL GPGPAADFSV SVERALAAKP
GLDTYSLGGG GAARVRVRGS TGVAAAAGLH RYLRDFCGCH VAWSGSQLRL PRPLPAVPGE
LTEATPNRYR YYQNVCTQSY SFVWWDWARW EREIDWMALN GINLALAWSG QEAIWQRVYL
ALGLTQAEIN EFFTGPAFLA WGRMGNLHTW DGPLPPSWHI KQLYLQHRVL DQMRSFGMTP
VLPAFAGHVP EAVTRVFPQV NVTKMGSWGH FNCSYSCSFL LAPEDPIFPI IGSLFLRELI
KEFGTDHIYG ADTFNEMQPP SSEPSYLAAA TTAVYEAMTA VDTEAVWLLQ GWLFQHQPQF
WGPAQIRAVL GAVPRGRLLV LDLFAESQPV YTRTASFQGQ PFIWCMLHNF GGNHGLFGAL
EAVNGGPEAA RLFPNSTMVG TGMAPEGISQ NEVVYSLMAE LGWRKDPVPD LAAWVTSFAA
RRYGVSHPDA GAAWRLLLRS VYNCSGEACR GHNRSPLVRR PSLQMNTSIW YNRSDVFEAW
RLLLTSAPSL ATSPAFRYDL LDLTRQAVQE LVSLYYEEAR SAYLSKELAS LLRAGGVLAY
ELLPALDEVL ASDSRFLLGS WLEQARAAAV SEAEADFYEQ NSRYQLTLWG PEGNILDYAN
KQLAGLVANY YTPRWRLFLE ALVDSVAQGI PFQQHQFDKN VFQLEQAFVL SKQRYPSQPR
GDTVDLAKKI FLKYYPRWVA GSW


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