P54802 (ANAG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-N-acetylglucosaminidase
EC=3.2.1.50

Alternative name(s):
N-acetyl-alpha-glucosaminidase
Short name=NAG

Cleaved into the following 2 chains:

1. Alpha-N-acetylglucosaminidase 82 kDa form
2. Alpha-N-acetylglucosaminidase 77 kDa form

Gene names

Name:	NAGLU
Synonyms:	UFHSD1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	743 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Lysosome
Coding sequence diversity	Polymorphism
Disease	Disease mutation Mucopolysaccharidosis
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Traceable author statement. Source: Reactome cerebellar Purkinje cell layer development Inferred from electronic annotation. Source: Compara glycosaminoglycan catabolic process Traceable author statement. Source: Reactome inner ear receptor cell development Inferred from electronic annotation. Source: Compara locomotor rhythm Inferred from electronic annotation. Source: Compara lysosome organization Inferred from electronic annotation. Source: Compara middle ear morphogenesis Inferred from electronic annotation. Source: Compara nervous system development Traceable author statement Ref.1. Source: ProtInc retinal rod cell development Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	lysosomal lumen Traceable author statement. Source: Reactome
Molecular_function	alpha-N-acetylglucosaminidase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23
	Chain	24 – 743	720	Alpha-N-acetylglucosaminidase 82 kDa form		PRO_0000020728
	Chain	59 – 743	685	Alpha-N-acetylglucosaminidase 77 kDa form		PRO_0000020729
Regions
	Compositional bias	68 – 71	4	Poly-Gly
	Compositional bias	84 – 87	4	Poly-Ala
Amino acid modifications
	Glycosylation	261	1	N-linked (GlcNAc...) Potential
	Glycosylation	272	1	N-linked (GlcNAc...) Potential
	Glycosylation	435	1	N-linked (GlcNAc...) Potential
	Glycosylation	503	1	N-linked (GlcNAc...) Potential
	Glycosylation	526	1	N-linked (GlcNAc...) Potential
	Glycosylation	532	1	N-linked (GlcNAc...) Ref.6
Natural variations
	Natural variant	35	1	L → 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 variant	38	1	R → W in MPS3B; decreases the enzyme activity markedly. Ref.20		VAR_054700
	Natural variant	48	1	F → C in MPS3B. Ref.9		VAR_054701
	Natural variant	48	1	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. Ref.11 Ref.12		VAR_025489
	Natural variant	69	1	G → S in MPS3B. Ref.11		VAR_054702
	Natural variant	77	1	V → G in MPS3B; decreases the enzyme activity markedly. Ref.20		VAR_054703
	Natural variant	79	1	G → C in MPS3B. Ref.10 Ref.20		VAR_008979
	Natural variant	79	1	G → S in MPS3B. Ref.14		VAR_054704
	Natural variant	82	1	G → 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 variant	92	1	Y → H in MPS3B. Ref.8		VAR_005007
	Natural variant	100	1	H → R in MPS3B. Ref.10		VAR_008980
	Natural variant	115	1	P → S in MPS3B. Ref.8		VAR_005008
	Natural variant	130	1	R → C in MPS3B; does not yield active enzyme. Ref.17 Ref.20		VAR_054706
	Natural variant	140	1	Y → C in MPS3B. Ref.7 Ref.8 Ref.9 Ref.10 Ref.13 Ref.18		VAR_005009
	Natural variant	142	1	Missing in MPS3B. Ref.10		VAR_008981
	Natural variant	153	1	E → K in MPS3B. Ref.8 Ref.15		VAR_005010
	Natural variant	154	1	I → R in MPS3B; does not yield active enzyme. Ref.17		VAR_054707
	Natural variant	156	1	W → 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 variant	227	1	H → P in MPS3B. Ref.11		VAR_054709
	Natural variant	234	1	R → C in MPS3B. Ref.9 Ref.13 Ref.14		VAR_054710
	Natural variant	241	1	V → M in MPS3B. Ref.16		VAR_054711
	Natural variant	242	1	L → P in MPS3B; no enzyme activity. Ref.18		VAR_054712
	Natural variant	243	1	P → L in MPS3B. Ref.10		VAR_008982
	Natural variant	246	1	A → P in MPS3B; produces 12.7% residual enzyme activity. Ref.20		VAR_054713
	Natural variant	248	1	H → R in MPS3B. Ref.11 Ref.15		VAR_054714
	Natural variant	268	1	W → R in MPS3B. Ref.9		VAR_054715
	Natural variant	277	1	C → F in MPS3B. Ref.10		VAR_008983
	Natural variant	280	1	L → P in MPS3B. Ref.10		VAR_008984
	Natural variant	292	1	G → R in MPS3B. Ref.10 Ref.11 Ref.13 Ref.18		VAR_008985
	Natural variant	309	1	Y → C in MPS3B; does not yield active enzyme. Ref.17 Ref.20		VAR_054716
	Natural variant	314	1	F → L in MPS3B. Ref.16		VAR_025490
	Natural variant	334	1	V → F in MPS3B. Ref.11		VAR_054717
	Natural variant	335	1	Y → C in MPS3B; decreases the enzyme activity markedly. Ref.20		VAR_054718
	Natural variant	358	1	P → L in MPS3B. Ref.8		VAR_005011
	Natural variant	410	1	F → S in MPS3B. Ref.11		VAR_054719
	Natural variant	412	1	G → E in MPS3B; does not yield active enzyme. Ref.17		VAR_054720
	Natural variant	414	1	H → R in MPS3B; no enzyme activity. Ref.11 Ref.18 Ref.20		VAR_054721
	Natural variant	437	1	T → I in MPS3B. Ref.15		VAR_054722
	Natural variant	446	1	E → K in MPS3B; no enzyme activity. Ref.18		VAR_054723
	Natural variant	452	1	E → K in MPS3B. Ref.10 Ref.18 Ref.20		VAR_008986
	Natural variant	455	1	Y → C in MPS3B. Ref.7		VAR_054724
	Natural variant	474	1	W → G in MPS3B. Ref.14		VAR_054725
	Natural variant	482	1	R → Q in MPS3B; no enzyme activity. Ref.18		VAR_054726
	Natural variant	482	1	R → W in MPS3B. Ref.10 Ref.16 Ref.20		VAR_008987
	Natural variant	501	1	V → 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 variant	516	1	P → L in MPS3B; no enzyme activity. Ref.18		VAR_054728
	Natural variant	520	1	R → 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 variant	521	1	P → 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 variant	534	1	S → 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 variant	560	1	L → P in MPS3B. Ref.11		VAR_054731
	Natural variant	561	1	L → R in MPS3B. Ref.10		VAR_008988
	Natural variant	565	1	R → P in MPS3B; does not yield active enzyme. Ref.11 Ref.16 Ref.19		VAR_025492
	Natural variant	565	1	R → Q in MPS3B. Ref.10		VAR_008989
	Natural variant	565	1	R → 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 variant	591	1	L → P in MPS3B. Ref.9		VAR_054732
	Natural variant	612	1	S → G in MPS3B. Ref.7		VAR_054733
	Natural variant	617	1	L → F in MPS3B. Ref.11		VAR_054734
	Natural variant	643	1	R → C in MPS3B; accounts for approximately 20% of MPS3B alleles in a Dutch patient group. Ref.11		VAR_025494
	Natural variant	643	1	R → H in MPS3B.		VAR_005012
	Natural variant	649	1	W → 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 variant	650	1	G → E in MPS3B. Ref.11		VAR_054736
	Natural variant	658	1	Y → F in MPS3B. Ref.14		VAR_054737
	Natural variant	664	1	A → V in MPS3B. Ref.8		VAR_005013
	Natural variant	674	1	R → C in MPS3B. Ref.7 Ref.11		VAR_054738
	Natural variant	674	1	R → H in MPS3B. Ref.7 Ref.10		VAR_005014
	Natural variant	676	1	R → P in MPS3B. Ref.11		VAR_054739
	Natural variant	682	1	L → R in MPS3B. Ref.8 Ref.15		VAR_005015
	Natural variant	705	1	E → K in MPS3B. Ref.9 Ref.10		VAR_008990
	Natural variant	737	1	R → G. Ref.1 Ref.2 Ref.3 Ref.5 Ref.10 Ref.11 Corresponds to variant rs86312 [ dbSNP | Ensembl ].		VAR_008991
Experimental info
	Sequence conflict	551	1	A → L AA sequence Ref.2
	Sequence conflict	553	1	S → L AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P54802 [UniParc]. Last modified January 11, 2011. Version 2. Checksum: 6D8D6A42C7BA7CF3	FASTA	743	82,266
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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

GeneReviews

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.
IPI	IPI00008787.
PIR	G02270.
RefSeq	NP_000254.2. NM_000263.3.
UniGene	Hs.50727.
3D structure databases
ProteinModelPortal	P54802.
SMR	P54802. Positions 32-735.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000225927.
Protein family/group databases
CAZy	GH89. Glycoside Hydrolase Family 89.
PTM databases
PhosphoSite	P54802.
Polymorphism databases
DMDM	1703303.
Proteomic databases
PaxDb	P54802.
PRIDE	P54802.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000225927; ENSP00000225927; ENSG00000108784.
GeneID	4669.
KEGG	hsa:4669.
UCSC	uc002hzv.3. human.
Organism-specific databases
CTD	4669.
GeneCards	GC17P040687.
H-InvDB	HIX0202517.
HGNC	HGNC:7632. NAGLU.
HPA	HPA038815.
MIM	252920. phenotype. 609701. gene.
neXtProt	NX_P54802.
Orphanet	79270. Sanfilippo syndrome type B.
PharmGKB	PA31437.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG86381.
HOGENOM	HOG000214539.
HOVERGEN	HBG004225.
InParanoid	P54802.
KO	K01205.
OMA	LFPNSTM.
OrthoDB	EOG4Q84X0.
PhylomeDB	P54802.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism. REACT_116125. Disease.
Gene expression databases
Bgee	P54802.
CleanEx	HS_NAGLU.
Genevestigator	P54802.
GermOnline	ENSG00000108784. Homo sapiens.
Family and domain databases
InterPro	IPR007781. NAGLU. IPR024732. NAGLU_C. IPR024240. NAGLU_N. IPR024733. NAGLU_tim-barrel. [Graphical view]
PANTHER	PTHR12872. PTHR12872. 1 hit.
Pfam	PF05089. NAGLU. 1 hit. PF12972. NAGLU_C. 1 hit. PF12971. NAGLU_N. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	NAGLU. human.
DrugBank	DB00141. N-Acetyl-D-glucosamine.
GenomeRNAi	4669.
NextBio	17990.
SOURCE	Search...

Entry information

Entry name

ANAG_HUMAN

Accession

Primary (citable) accession number: P54802

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 11, 2011
Last modified:	May 1, 2013
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.