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P54802 (ANAG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Alpha-N-acetylglucosaminidase

EC=3.2.1.50
Alternative name(s):
N-acetyl-alpha-glucosaminidase
Short name=NAG
Gene names
Name:NAGLU
Synonyms:UFHSD1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length743 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 structure

Monomer and homodimer.

Subcellular location

Lysosome.

Tissue specificity

Liver, ovary, peripheral blood leukocytes, testis, prostate, spleen, colon, lung, placenta and kidney.

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20

Caution

A MPS3B mutation at position 100 was erroneously reported (Ref.10) as an amino acid change from Arg to His. The right amino acid change is from His to Arg.

Ontologies

Keywords
   Cellular componentLysosome
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Mucopolysaccharidosis
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

cerebellar Purkinje cell layer development

Inferred from electronic annotation. Source: Ensembl

glycosaminoglycan catabolic process

Traceable author statement. Source: Reactome

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

inner ear receptor cell development

Inferred from electronic annotation. Source: Ensembl

locomotor rhythm

Inferred from electronic annotation. Source: Ensembl

lysosome organization

Inferred from electronic annotation. Source: Ensembl

middle ear morphogenesis

Inferred from electronic annotation. Source: Ensembl

nervous system development

Traceable author statement Ref.1. Source: ProtInc

retinal rod cell development

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentextracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

lysosomal lumen

Traceable author statement. Source: Reactome

lysosome

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionalpha-N-acetylglucosaminidase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323
Chain24 – 743720Alpha-N-acetylglucosaminidase 82 kDa form
PRO_0000020728
Chain59 – 743685Alpha-N-acetylglucosaminidase 77 kDa form
PRO_0000020729

Regions

Compositional bias68 – 714Poly-Gly
Compositional bias84 – 874Poly-Ala

Amino acid modifications

Glycosylation2611N-linked (GlcNAc...) Potential
Glycosylation2721N-linked (GlcNAc...) Potential
Glycosylation4351N-linked (GlcNAc...) Potential
Glycosylation5031N-linked (GlcNAc...) Potential
Glycosylation5261N-linked (GlcNAc...) Potential
Glycosylation5321N-linked (GlcNAc...) Ref.6

Natural variations

Natural variant351L → F in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. Ref.13
VAR_054699
Natural variant381R → W in MPS3B; decreases the enzyme activity markedly. Ref.20
VAR_054700
Natural variant481F → C in MPS3B. Ref.9
VAR_054701
Natural variant481F → 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. Ref.11 Ref.12
VAR_025489
Natural variant691G → S in MPS3B. Ref.11
VAR_054702
Natural variant771V → G in MPS3B; decreases the enzyme activity markedly. Ref.20
VAR_054703
Natural variant791G → C in MPS3B. Ref.10 Ref.20
VAR_008979
Natural variant791G → S in MPS3B. Ref.14
VAR_054704
Natural variant821G → D in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. Ref.13
VAR_054705
Natural variant921Y → H in MPS3B. Ref.8
VAR_005007
Natural variant1001H → R in MPS3B. Ref.10
VAR_008980
Natural variant1151P → S in MPS3B. Ref.8
VAR_005008
Natural variant1301R → C in MPS3B; does not yield active enzyme. Ref.17 Ref.20
VAR_054706
Natural variant1401Y → C in MPS3B. Ref.7 Ref.8 Ref.9 Ref.10 Ref.13 Ref.18
VAR_005009
Natural variant1421Missing in MPS3B. Ref.10
VAR_008981
Natural variant1531E → K in MPS3B. Ref.8 Ref.15
VAR_005010
Natural variant1541I → R in MPS3B; does not yield active enzyme. Ref.17
VAR_054707
Natural variant1561W → C in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. Ref.13
VAR_054708
Natural variant2271H → P in MPS3B. Ref.11
VAR_054709
Natural variant2341R → C in MPS3B. Ref.9 Ref.13 Ref.14
VAR_054710
Natural variant2411V → M in MPS3B. Ref.16
VAR_054711
Natural variant2421L → P in MPS3B; no enzyme activity. Ref.18
VAR_054712
Natural variant2431P → L in MPS3B. Ref.10
VAR_008982
Natural variant2461A → P in MPS3B; produces 12.7% residual enzyme activity. Ref.20
VAR_054713
Natural variant2481H → R in MPS3B. Ref.11 Ref.15
VAR_054714
Natural variant2681W → R in MPS3B. Ref.9
VAR_054715
Natural variant2771C → F in MPS3B. Ref.10
VAR_008983
Natural variant2801L → P in MPS3B. Ref.10
VAR_008984
Natural variant2921G → R in MPS3B. Ref.10 Ref.11 Ref.13 Ref.18
VAR_008985
Natural variant3091Y → C in MPS3B; does not yield active enzyme. Ref.17 Ref.20
VAR_054716
Natural variant3141F → L in MPS3B. Ref.16
VAR_025490
Natural variant3341V → F in MPS3B. Ref.11
VAR_054717
Natural variant3351Y → C in MPS3B; decreases the enzyme activity markedly. Ref.20
VAR_054718
Natural variant3581P → L in MPS3B. Ref.8
VAR_005011
Natural variant4101F → S in MPS3B. Ref.11
VAR_054719
Natural variant4121G → E in MPS3B; does not yield active enzyme. Ref.17
VAR_054720
Natural variant4141H → R in MPS3B; no enzyme activity. Ref.11 Ref.18 Ref.20
VAR_054721
Natural variant4371T → I in MPS3B. Ref.15
VAR_054722
Natural variant4461E → K in MPS3B; no enzyme activity. Ref.18
VAR_054723
Natural variant4521E → K in MPS3B. Ref.10 Ref.18 Ref.20
VAR_008986
Natural variant4551Y → C in MPS3B. Ref.7
VAR_054724
Natural variant4741W → G in MPS3B. Ref.14
VAR_054725
Natural variant4821R → Q in MPS3B; no enzyme activity. Ref.18
Corresponds to variant rs200909691 [ dbSNP | Ensembl ].
VAR_054726
Natural variant4821R → W in MPS3B. Ref.10 Ref.16 Ref.20
VAR_008987
Natural variant5011V → G in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. Ref.13
VAR_054727
Natural variant5161P → L in MPS3B; no enzyme activity. Ref.18
VAR_054728
Natural variant5201R → W in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. Ref.13 Ref.20
VAR_054729
Natural variant5211P → L in MPS3B; accounts for approximately 6% of mutations in Australasian patients with MPS3B. Ref.7 Ref.9 Ref.11 Ref.20
VAR_025491
Natural variant5341S → Y in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. Ref.13
VAR_054730
Natural variant5601L → P in MPS3B. Ref.11
VAR_054731
Natural variant5611L → R in MPS3B. Ref.10
VAR_008988
Natural variant5651R → P in MPS3B; does not yield active enzyme. Ref.11 Ref.16 Ref.19
VAR_025492
Natural variant5651R → Q in MPS3B. Ref.10
VAR_008989
Natural variant5651R → W in MPS3B; accounts for approximately 6% of the mutant alleles in Australasian patients with MPS3B. Ref.9 Ref.11 Ref.14 Ref.16 Ref.17 Ref.20
VAR_025493
Natural variant5911L → P in MPS3B. Ref.9
VAR_054732
Natural variant6121S → G in MPS3B. Ref.7
VAR_054733
Natural variant6171L → F in MPS3B. Ref.11
VAR_054734
Natural variant6431R → C in MPS3B; accounts for approximately 20% of MPS3B alleles in a Dutch patient group. Ref.11
VAR_025494
Natural variant6431R → H in MPS3B.
VAR_005012
Natural variant6491W → C in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. Ref.13
VAR_054735
Natural variant6501G → E in MPS3B. Ref.11
VAR_054736
Natural variant6581Y → F in MPS3B. Ref.14
VAR_054737
Natural variant6641A → V in MPS3B. Ref.8
VAR_005013
Natural variant6741R → C in MPS3B. Ref.7 Ref.11
VAR_054738
Natural variant6741R → H in MPS3B. Ref.7 Ref.10
VAR_005014
Natural variant6761R → P in MPS3B. Ref.11
VAR_054739
Natural variant6821L → R in MPS3B. Ref.8 Ref.15
VAR_005015
Natural variant7051E → K in MPS3B. Ref.9 Ref.10
VAR_008990
Natural variant7371R → G. Ref.1 Ref.2 Ref.3 Ref.5 Ref.10 Ref.11
Corresponds to variant rs86312 [ dbSNP | Ensembl ].
VAR_008991

Experimental info

Sequence conflict5511A → L AA sequence Ref.2
Sequence conflict5531S → L AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P54802 [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: 6D8D6A42C7BA7CF3

FASTA74382,266
        10         20         30         40         50         60 
MEAVAVAAAV GVLLLAGAGG AAGDEAREAA AVRALVARLL GPGPAADFSV SVERALAAKP 

        70         80         90        100        110        120 
GLDTYSLGGG GAARVRVRGS TGVAAAAGLH RYLRDFCGCH VAWSGSQLRL PRPLPAVPGE 

       130        140        150        160        170        180 
LTEATPNRYR YYQNVCTQSY SFVWWDWARW EREIDWMALN GINLALAWSG QEAIWQRVYL 

       190        200        210        220        230        240 
ALGLTQAEIN EFFTGPAFLA WGRMGNLHTW DGPLPPSWHI KQLYLQHRVL DQMRSFGMTP 

       250        260        270        280        290        300 
VLPAFAGHVP EAVTRVFPQV NVTKMGSWGH FNCSYSCSFL LAPEDPIFPI IGSLFLRELI 

       310        320        330        340        350        360 
KEFGTDHIYG ADTFNEMQPP SSEPSYLAAA TTAVYEAMTA VDTEAVWLLQ GWLFQHQPQF 

       370        380        390        400        410        420 
WGPAQIRAVL GAVPRGRLLV LDLFAESQPV YTRTASFQGQ PFIWCMLHNF GGNHGLFGAL 

       430        440        450        460        470        480 
EAVNGGPEAA RLFPNSTMVG TGMAPEGISQ NEVVYSLMAE LGWRKDPVPD LAAWVTSFAA 

       490        500        510        520        530        540 
RRYGVSHPDA GAAWRLLLRS VYNCSGEACR GHNRSPLVRR PSLQMNTSIW YNRSDVFEAW 

       550        560        570        580        590        600 
RLLLTSAPSL ATSPAFRYDL LDLTRQAVQE LVSLYYEEAR SAYLSKELAS LLRAGGVLAY 

       610        620        630        640        650        660 
ELLPALDEVL ASDSRFLLGS WLEQARAAAV SEAEADFYEQ NSRYQLTLWG PEGNILDYAN 

       670        680        690        700        710        720 
KQLAGLVANY YTPRWRLFLE ALVDSVAQGI PFQQHQFDKN VFQLEQAFVL SKQRYPSQPR 

       730        740 
GDTVDLAKKI FLKYYPRWVA GSW 

« Hide

References

« Hide 'large scale' references
[1]"The molecular basis of Sanfilippo syndrome type B."
Zhao H.G., Li H.H., Bach G., Schmidtchen A., Neufeld E.F.
Proc. Natl. Acad. Sci. U.S.A. 93:6101-6105(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT GLY-737.
Tissue: Testis.
[2]"Cloning and expression of the gene involved in Sanfilippo B syndrome (mucopolysaccharidosis III B)."
Weber B., Blanch L., Clements P.R., Scott H.S., Hopwood J.J.
Hum. Mol. Genet. 5:771-777(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION, VARIANT GLY-737.
[3]"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."
Zhao Z., Yazdani A., Shen Y., Sun Z.S., Bailey J., Caskey C.T., Lee C.C.
Mamm. Genome 7:686-690(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-737.
[4]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
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. expand/collapse author list , 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.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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 GLY-737.
Tissue: Skin.
[6]"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-532.
Tissue: Liver.
[7]"Genotype-phenotype correspondence in Sanfilippo syndrome type B."
Zhao H.G., Aronovich E.L., Whitley C.B.
Am. J. Hum. Genet. 62:53-63(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MPS3B CYS-140; CYS-455; LEU-521; GLY-612; CYS-674 AND HIS-674.
[8]"NAGLU mutations underlying Sanfilippo syndrome type B."
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.
Am. J. Hum. Genet. 62:64-69(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MPS3B HIS-92; SER-115; CYS-140; LYS-153; LEU-358; VAL-664 AND ARG-682.
[9]"Identification of 12 novel mutations in the alpha-N-acetylglucosaminidase gene in 14 patients with Sanfilippo syndrome type B (mucopolysaccharidosis type IIIB)."
Beesley C.E., Young E.P., Vellodi A., Winchester B.G.
J. Med. Genet. 35:910-914(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MPS3B CYS-48; CYS-140; CYS-234; ARG-268; LEU-521; TRP-565; PRO-591 AND LYS-705.
[10]"Mucopolysaccharidosis type IIIB (Sanfilippo B): identification of 18 novel alpha-N-acetylglucosaminidase gene mutations."
Bunge S., Knigge A., Steglich C., Kleijer W.J., van Diggelen O.P., Beck M., Gal A.
J. Med. Genet. 36:28-31(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, VARIANT GLY-737.
[11]"Sanfilippo type B syndrome (mucopolysaccharidosis III B): allelic heterogeneity corresponds to the wide spectrum of clinical phenotypes."
Weber B., Guo X.-H., Kleijer W.J., van de Kamp J.J.P., Poorthuis B.J.H.M., Hopwood J.J.
Eur. J. Hum. Genet. 7:34-44(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, VARIANT GLY-737.
[12]"Mucopolysaccharidosis type IIIB: characterisation and expression of wild-type and mutant recombinant alpha-N-acetylglucosaminidase and relationship with sanfilippo phenotype in an attenuated patient."
Yogalingam G., Weber B., Meehan J., Rogers J., Hopwood J.J.
Biochim. Biophys. Acta 1502:415-425(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MPS3B LEU-48, CHARACTERIZATION OF VARIANT MPS3B LEU-48.
[13]"Molecular defects in the alpha-N-acetylglucosaminidase gene in Italian Sanfilippo type B patients."
Tessitore A., Villani G.R.D., Di Domenico C., Filocamo M., Gatti R., Di Natale P.
Hum. Genet. 107:568-576(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MPS3B PHE-35; ASP-82; CYS-140; CYS-156; CYS-234; ARG-292; GLY-501; TRP-520; TYR-534 AND CYS-649, CHARACTERIZATION OF VARIANTS MPS3B PHE-35; ASP-82; CYS-156; GLY-501; TRP-520; TYR-534 AND CYS-649.
[14]"Allelic heterogeneity in Spanish patients with Sanfilippo disease type B. Identification of eight new mutations."
Coll M.J., Anton C., Chabas A.
J. Inherit. Metab. Dis. 24:83-84(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MPS3B SER-79; CYS-234; GLY-474; TRP-565 AND PHE-658.
[15]"Sanfilippo syndrome in Turkey: identification of novel mutations in subtypes A and B."
Emre S., Terzioglu M., Tokatli A., Coskun T., Ozalp I., Weber B., Hopwood J.J.
Hum. Mutat. 19:184-185(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MPS3B LYS-153; ARG-248; ILE-437 AND ARG-682.
[16]"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."
Tanaka A., Kimura M., Lan H.T.N., Takaura N., Yamano T.
J. Hum. Genet. 47:484-487(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MPS3B MET-241; LEU-314; TRP-482; PRO-565 AND TRP-565.
[17]"Identification and characterisation of mutations underlying Sanfilippo syndrome type B (mucopolysaccharidosis type IIIB)."
Lee-Chen G.J., Lin S.P., Lin S.Z., Chuang C.K., Hsiao K.T., Huang C.F., Lien W.C.
J. Med. Genet. 39:E3-E3(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MPS3B CYS-130; ARG-154; CYS-309; GLU-412 AND TRP-565, CHARACTERIZATION OF VARIANTS MPS3B CYS-130; ARG-154; CYS-309; GLU-412 AND TRP-565.
[18]"Sanfilippo B syndrome: molecular defects in Greek patients."
Beesley C., Moraitou M., Winchester B., Schulpis K., Dimitriou E., Michelakakis H.
Clin. Genet. 65:143-149(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MPS3B CYS-140; PRO-242; ARG-292; ARG-414; LYS-446; LYS-452; GLN-482 AND LEU-516, CHARACTERIZATION OF VARIANTS MPS3B PRO-242; ARG-414; LYS-446; GLN-482 AND LEU-516.
[19]"Sanfilippo type B syndrome: five patients with an R565P homozygous mutation in the alpha-N-acetylglucosaminidase gene from the Okinawa islands in Japan."
Chinen Y., Tohma T., Izumikawa Y., Uehara H., Ohta T.
J. Hum. Genet. 50:357-359(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MPS3B PRO-565.
[20]"Molecular defects in Sanfilippo syndrome type B (mucopolysaccharidosis IIIB)."
Beesley C.E., Jackson M., Young E.P., Vellodi A., Winchester B.G.
J. Inherit. Metab. Dis. 28:759-767(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, CHARACTERIZATION OF VARIANTS MPS3B TRP-38; GLY-77 AND CYS-335.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U43572 Genomic DNA. Translation: AAC50512.1.
U43573 mRNA. Translation: AAC50513.1.
U40846 mRNA. Translation: AAB06188.1.
L78464 mRNA. Translation: AAB36604.1.
AC067852 Genomic DNA. No translation available.
BC053991 mRNA. Translation: AAH53991.1.
PIRG02270.
RefSeqNP_000254.2. NM_000263.3.
UniGeneHs.50727.

3D structure databases

ProteinModelPortalP54802.
SMRP54802. Positions 32-735.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110750. 2 interactions.
STRING9606.ENSP00000225927.

Chemistry

DrugBankDB00141. N-Acetyl-D-glucosamine.

Protein family/group databases

CAZyGH89. Glycoside Hydrolase Family 89.

PTM databases

PhosphoSiteP54802.

Polymorphism databases

DMDM317373322.

Proteomic databases

PaxDbP54802.
PRIDEP54802.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000225927; ENSP00000225927; ENSG00000108784.
GeneID4669.
KEGGhsa:4669.
UCSCuc002hzv.3. human.

Organism-specific databases

CTD4669.
GeneCardsGC17P040687.
H-InvDBHIX0202517.
HGNCHGNC:7632. NAGLU.
HPAHPA038815.
MIM252920. phenotype.
609701. gene.
neXtProtNX_P54802.
Orphanet79270. Sanfilippo syndrome type B.
PharmGKBPA31437.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG86381.
HOGENOMHOG000214539.
HOVERGENHBG004225.
InParanoidP54802.
KOK01205.
OMALFPNSTM.
OrthoDBEOG751NF0.
PhylomeDBP54802.
TreeFamTF300689.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

ArrayExpressP54802.
BgeeP54802.
CleanExHS_NAGLU.
GenevestigatorP54802.

Family and domain databases

InterProIPR017853. Glycoside_hydrolase_SF.
IPR007781. NAGLU.
IPR024732. NAGLU_C.
IPR024240. NAGLU_N.
IPR024733. NAGLU_tim-barrel.
[Graphical view]
PANTHERPTHR12872. PTHR12872. 1 hit.
PfamPF05089. NAGLU. 1 hit.
PF12972. NAGLU_C. 1 hit.
PF12971. NAGLU_N. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 2 hits.
ProtoNetSearch...

Other

ChiTaRSNAGLU. human.
GenomeRNAi4669.
NextBio17990.
PROP54802.
SOURCESearch...

Entry information

Entry nameANAG_HUMAN
AccessionPrimary (citable) accession number: P54802
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 136 of the entry and version 2 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

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 17

Human chromosome 17: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries