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P54802

- ANAG_HUMAN

UniProt

P54802 - ANAG_HUMAN

Protein

Alpha-N-acetylglucosaminidase

Gene

NAGLU

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Involved in the degradation of heparan sulfate.

    Catalytic activityi

    Hydrolysis of terminal non-reducing N-acetyl-D-glucosamine residues in N-acetyl-alpha-D-glucosaminides.

    GO - Molecular functioni

    1. alpha-N-acetylglucosaminidase activity Source: ProtInc

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. cerebellar Purkinje cell layer development Source: Ensembl
    3. glycosaminoglycan catabolic process Source: Reactome
    4. glycosaminoglycan metabolic process Source: Reactome
    5. inner ear receptor cell development Source: Ensembl
    6. locomotor rhythm Source: Ensembl
    7. lysosome organization Source: Ensembl
    8. middle ear morphogenesis Source: Ensembl
    9. nervous system development Source: ProtInc
    10. retinal rod cell development Source: Ensembl
    11. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    ReactomeiREACT_120752. HS-GAG degradation.

    Protein family/group databases

    CAZyiGH89. Glycoside Hydrolase Family 89.

    Names & Taxonomyi

    Protein namesi
    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:
    Gene namesi
    Name:NAGLU
    Synonyms:UFHSD1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:7632. NAGLU.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProtKB
    2. lysosomal lumen Source: Reactome
    3. lysosome Source: ProtInc

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Involvement in diseasei

    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.14 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti35 – 351L → F in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
    VAR_054699
    Natural varianti38 – 381R → W in MPS3B; decreases the enzyme activity markedly. 1 Publication
    VAR_054700
    Natural varianti48 – 481F → C in MPS3B. 1 Publication
    VAR_054701
    Natural varianti48 – 481F → 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. 2 Publications
    VAR_025489
    Natural varianti69 – 691G → S in MPS3B. 1 Publication
    VAR_054702
    Natural varianti77 – 771V → G in MPS3B; decreases the enzyme activity markedly. 1 Publication
    VAR_054703
    Natural varianti79 – 791G → C in MPS3B. 2 Publications
    VAR_008979
    Natural varianti79 – 791G → S in MPS3B. 1 Publication
    VAR_054704
    Natural varianti82 – 821G → D in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
    VAR_054705
    Natural varianti92 – 921Y → H in MPS3B. 1 Publication
    VAR_005007
    Natural varianti100 – 1001H → R in MPS3B. 1 Publication
    VAR_008980
    Natural varianti115 – 1151P → S in MPS3B. 1 Publication
    VAR_005008
    Natural varianti130 – 1301R → C in MPS3B; does not yield active enzyme. 2 Publications
    VAR_054706
    Natural varianti140 – 1401Y → C in MPS3B. 6 Publications
    VAR_005009
    Natural varianti142 – 1421Missing in MPS3B. 1 Publication
    VAR_008981
    Natural varianti153 – 1531E → K in MPS3B. 2 Publications
    VAR_005010
    Natural varianti154 – 1541I → R in MPS3B; does not yield active enzyme. 1 Publication
    VAR_054707
    Natural varianti156 – 1561W → C in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
    VAR_054708
    Natural varianti227 – 2271H → P in MPS3B. 1 Publication
    VAR_054709
    Natural varianti234 – 2341R → C in MPS3B. 3 Publications
    VAR_054710
    Natural varianti241 – 2411V → M in MPS3B. 1 Publication
    VAR_054711
    Natural varianti242 – 2421L → P in MPS3B; no enzyme activity. 1 Publication
    VAR_054712
    Natural varianti243 – 2431P → L in MPS3B. 1 Publication
    VAR_008982
    Natural varianti246 – 2461A → P in MPS3B; produces 12.7% residual enzyme activity. 1 Publication
    VAR_054713
    Natural varianti248 – 2481H → R in MPS3B. 2 Publications
    VAR_054714
    Natural varianti268 – 2681W → R in MPS3B. 1 Publication
    VAR_054715
    Natural varianti277 – 2771C → F in MPS3B. 1 Publication
    VAR_008983
    Natural varianti280 – 2801L → P in MPS3B. 1 Publication
    VAR_008984
    Natural varianti292 – 2921G → R in MPS3B. 4 Publications
    VAR_008985
    Natural varianti309 – 3091Y → C in MPS3B; does not yield active enzyme. 2 Publications
    VAR_054716
    Natural varianti314 – 3141F → L in MPS3B. 1 Publication
    VAR_025490
    Natural varianti334 – 3341V → F in MPS3B. 1 Publication
    VAR_054717
    Natural varianti335 – 3351Y → C in MPS3B; decreases the enzyme activity markedly. 1 Publication
    VAR_054718
    Natural varianti358 – 3581P → L in MPS3B. 1 Publication
    VAR_005011
    Natural varianti410 – 4101F → S in MPS3B. 1 Publication
    VAR_054719
    Natural varianti412 – 4121G → E in MPS3B; does not yield active enzyme. 1 Publication
    VAR_054720
    Natural varianti414 – 4141H → R in MPS3B; no enzyme activity. 3 Publications
    VAR_054721
    Natural varianti437 – 4371T → I in MPS3B. 1 Publication
    VAR_054722
    Natural varianti446 – 4461E → K in MPS3B; no enzyme activity. 1 Publication
    VAR_054723
    Natural varianti452 – 4521E → K in MPS3B. 3 Publications
    VAR_008986
    Natural varianti455 – 4551Y → C in MPS3B. 1 Publication
    VAR_054724
    Natural varianti474 – 4741W → G in MPS3B. 1 Publication
    VAR_054725
    Natural varianti482 – 4821R → Q in MPS3B; no enzyme activity. 1 Publication
    Corresponds to variant rs200909691 [ dbSNP | Ensembl ].
    VAR_054726
    Natural varianti482 – 4821R → W in MPS3B. 3 Publications
    VAR_008987
    Natural varianti501 – 5011V → G in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
    VAR_054727
    Natural varianti516 – 5161P → L in MPS3B; no enzyme activity. 1 Publication
    VAR_054728
    Natural varianti520 – 5201R → W in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 2 Publications
    VAR_054729
    Natural varianti521 – 5211P → L in MPS3B; accounts for approximately 6% of mutations in Australasian patients with MPS3B. 4 Publications
    VAR_025491
    Natural varianti534 – 5341S → Y in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
    VAR_054730
    Natural varianti560 – 5601L → P in MPS3B. 1 Publication
    VAR_054731
    Natural varianti561 – 5611L → R in MPS3B. 1 Publication
    VAR_008988
    Natural varianti565 – 5651R → P in MPS3B; does not yield active enzyme. 3 Publications
    VAR_025492
    Natural varianti565 – 5651R → Q in MPS3B. 1 Publication
    VAR_008989
    Natural varianti565 – 5651R → W in MPS3B; accounts for approximately 6% of the mutant alleles in Australasian patients with MPS3B. 6 Publications
    VAR_025493
    Natural varianti591 – 5911L → P in MPS3B. 1 Publication
    VAR_054732
    Natural varianti612 – 6121S → G in MPS3B. 1 Publication
    VAR_054733
    Natural varianti617 – 6171L → F in MPS3B. 1 Publication
    VAR_054734
    Natural varianti643 – 6431R → C in MPS3B; accounts for approximately 20% of MPS3B alleles in a Dutch patient group. 1 Publication
    VAR_025494
    Natural varianti643 – 6431R → H in MPS3B.
    VAR_005012
    Natural varianti649 – 6491W → C in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
    VAR_054735
    Natural varianti650 – 6501G → E in MPS3B. 1 Publication
    VAR_054736
    Natural varianti658 – 6581Y → F in MPS3B. 1 Publication
    VAR_054737
    Natural varianti664 – 6641A → V in MPS3B. 1 Publication
    VAR_005013
    Natural varianti674 – 6741R → C in MPS3B. 2 Publications
    VAR_054738
    Natural varianti674 – 6741R → H in MPS3B. 2 Publications
    VAR_005014
    Natural varianti676 – 6761R → P in MPS3B. 1 Publication
    VAR_054739
    Natural varianti682 – 6821L → R in MPS3B. 2 Publications
    VAR_005015
    Natural varianti705 – 7051E → K in MPS3B. 2 Publications
    VAR_008990

    Keywords - Diseasei

    Disease mutation, Mucopolysaccharidosis

    Organism-specific databases

    MIMi252920. phenotype.
    Orphaneti79270. Sanfilippo syndrome type B.
    PharmGKBiPA31437.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Add
    BLAST
    Chaini24 – 743720Alpha-N-acetylglucosaminidase 82 kDa formPRO_0000020728Add
    BLAST
    Chaini59 – 743685Alpha-N-acetylglucosaminidase 77 kDa formPRO_0000020729Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi261 – 2611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi272 – 2721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi435 – 4351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi503 – 5031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi526 – 5261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi532 – 5321N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiP54802.
    PaxDbiP54802.
    PRIDEiP54802.

    PTM databases

    PhosphoSiteiP54802.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP54802.
    BgeeiP54802.
    CleanExiHS_NAGLU.
    GenevestigatoriP54802.

    Organism-specific databases

    HPAiHPA038815.

    Interactioni

    Subunit structurei

    Monomer and homodimer.

    Protein-protein interaction databases

    BioGridi110750. 2 interactions.
    STRINGi9606.ENSP00000225927.

    Structurei

    3D structure databases

    ProteinModelPortaliP54802.
    SMRiP54802. Positions 32-735.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi68 – 714Poly-Gly
    Compositional biasi84 – 874Poly-Ala

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG86381.
    HOGENOMiHOG000214539.
    HOVERGENiHBG004225.
    InParanoidiP54802.
    KOiK01205.
    OMAiLFPNSTM.
    OrthoDBiEOG751NF0.
    PhylomeDBiP54802.
    TreeFamiTF300689.

    Family and domain databases

    InterProiIPR017853. Glycoside_hydrolase_SF.
    IPR007781. NAGLU.
    IPR024732. NAGLU_C.
    IPR024240. NAGLU_N.
    IPR024733. NAGLU_tim-barrel.
    [Graphical view]
    PANTHERiPTHR12872. PTHR12872. 1 hit.
    PfamiPF05089. NAGLU. 1 hit.
    PF12972. NAGLU_C. 1 hit.
    PF12971. NAGLU_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 2 hits.

    Sequencei

    Sequence statusi: Complete.

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

    P54802-1 [UniParc]FASTAAdd to Basket

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    MEAVAVAAAV GVLLLAGAGG AAGDEAREAA AVRALVARLL GPGPAADFSV    50
    SVERALAAKP GLDTYSLGGG GAARVRVRGS TGVAAAAGLH RYLRDFCGCH 100
    VAWSGSQLRL PRPLPAVPGE LTEATPNRYR YYQNVCTQSY SFVWWDWARW 150
    EREIDWMALN GINLALAWSG QEAIWQRVYL ALGLTQAEIN EFFTGPAFLA 200
    WGRMGNLHTW DGPLPPSWHI KQLYLQHRVL DQMRSFGMTP VLPAFAGHVP 250
    EAVTRVFPQV NVTKMGSWGH FNCSYSCSFL LAPEDPIFPI IGSLFLRELI 300
    KEFGTDHIYG ADTFNEMQPP SSEPSYLAAA TTAVYEAMTA VDTEAVWLLQ 350
    GWLFQHQPQF WGPAQIRAVL GAVPRGRLLV LDLFAESQPV YTRTASFQGQ 400
    PFIWCMLHNF GGNHGLFGAL EAVNGGPEAA RLFPNSTMVG TGMAPEGISQ 450
    NEVVYSLMAE LGWRKDPVPD LAAWVTSFAA RRYGVSHPDA GAAWRLLLRS 500
    VYNCSGEACR GHNRSPLVRR PSLQMNTSIW YNRSDVFEAW RLLLTSAPSL 550
    ATSPAFRYDL LDLTRQAVQE LVSLYYEEAR SAYLSKELAS LLRAGGVLAY 600
    ELLPALDEVL ASDSRFLLGS WLEQARAAAV SEAEADFYEQ NSRYQLTLWG 650
    PEGNILDYAN KQLAGLVANY YTPRWRLFLE ALVDSVAQGI PFQQHQFDKN 700
    VFQLEQAFVL SKQRYPSQPR GDTVDLAKKI FLKYYPRWVA GSW 743
    Length:743
    Mass (Da):82,266
    Last modified:January 11, 2011 - v2
    Checksum:i6D8D6A42C7BA7CF3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti551 – 5511A → L AA sequence (PubMed:8776591)Curated
    Sequence conflicti553 – 5531S → L AA sequence (PubMed:8776591)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti35 – 351L → F in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
    VAR_054699
    Natural varianti38 – 381R → W in MPS3B; decreases the enzyme activity markedly. 1 Publication
    VAR_054700
    Natural varianti48 – 481F → C in MPS3B. 1 Publication
    VAR_054701
    Natural varianti48 – 481F → 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. 2 Publications
    VAR_025489
    Natural varianti69 – 691G → S in MPS3B. 1 Publication
    VAR_054702
    Natural varianti77 – 771V → G in MPS3B; decreases the enzyme activity markedly. 1 Publication
    VAR_054703
    Natural varianti79 – 791G → C in MPS3B. 2 Publications
    VAR_008979
    Natural varianti79 – 791G → S in MPS3B. 1 Publication
    VAR_054704
    Natural varianti82 – 821G → D in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
    VAR_054705
    Natural varianti92 – 921Y → H in MPS3B. 1 Publication
    VAR_005007
    Natural varianti100 – 1001H → R in MPS3B. 1 Publication
    VAR_008980
    Natural varianti115 – 1151P → S in MPS3B. 1 Publication
    VAR_005008
    Natural varianti130 – 1301R → C in MPS3B; does not yield active enzyme. 2 Publications
    VAR_054706
    Natural varianti140 – 1401Y → C in MPS3B. 6 Publications
    VAR_005009
    Natural varianti142 – 1421Missing in MPS3B. 1 Publication
    VAR_008981
    Natural varianti153 – 1531E → K in MPS3B. 2 Publications
    VAR_005010
    Natural varianti154 – 1541I → R in MPS3B; does not yield active enzyme. 1 Publication
    VAR_054707
    Natural varianti156 – 1561W → C in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
    VAR_054708
    Natural varianti227 – 2271H → P in MPS3B. 1 Publication
    VAR_054709
    Natural varianti234 – 2341R → C in MPS3B. 3 Publications
    VAR_054710
    Natural varianti241 – 2411V → M in MPS3B. 1 Publication
    VAR_054711
    Natural varianti242 – 2421L → P in MPS3B; no enzyme activity. 1 Publication
    VAR_054712
    Natural varianti243 – 2431P → L in MPS3B. 1 Publication
    VAR_008982
    Natural varianti246 – 2461A → P in MPS3B; produces 12.7% residual enzyme activity. 1 Publication
    VAR_054713
    Natural varianti248 – 2481H → R in MPS3B. 2 Publications
    VAR_054714
    Natural varianti268 – 2681W → R in MPS3B. 1 Publication
    VAR_054715
    Natural varianti277 – 2771C → F in MPS3B. 1 Publication
    VAR_008983
    Natural varianti280 – 2801L → P in MPS3B. 1 Publication
    VAR_008984
    Natural varianti292 – 2921G → R in MPS3B. 4 Publications
    VAR_008985
    Natural varianti309 – 3091Y → C in MPS3B; does not yield active enzyme. 2 Publications
    VAR_054716
    Natural varianti314 – 3141F → L in MPS3B. 1 Publication
    VAR_025490
    Natural varianti334 – 3341V → F in MPS3B. 1 Publication
    VAR_054717
    Natural varianti335 – 3351Y → C in MPS3B; decreases the enzyme activity markedly. 1 Publication
    VAR_054718
    Natural varianti358 – 3581P → L in MPS3B. 1 Publication
    VAR_005011
    Natural varianti410 – 4101F → S in MPS3B. 1 Publication
    VAR_054719
    Natural varianti412 – 4121G → E in MPS3B; does not yield active enzyme. 1 Publication
    VAR_054720
    Natural varianti414 – 4141H → R in MPS3B; no enzyme activity. 3 Publications
    VAR_054721
    Natural varianti437 – 4371T → I in MPS3B. 1 Publication
    VAR_054722
    Natural varianti446 – 4461E → K in MPS3B; no enzyme activity. 1 Publication
    VAR_054723
    Natural varianti452 – 4521E → K in MPS3B. 3 Publications
    VAR_008986
    Natural varianti455 – 4551Y → C in MPS3B. 1 Publication
    VAR_054724
    Natural varianti474 – 4741W → G in MPS3B. 1 Publication
    VAR_054725
    Natural varianti482 – 4821R → Q in MPS3B; no enzyme activity. 1 Publication
    Corresponds to variant rs200909691 [ dbSNP | Ensembl ].
    VAR_054726
    Natural varianti482 – 4821R → W in MPS3B. 3 Publications
    VAR_008987
    Natural varianti501 – 5011V → G in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
    VAR_054727
    Natural varianti516 – 5161P → L in MPS3B; no enzyme activity. 1 Publication
    VAR_054728
    Natural varianti520 – 5201R → W in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 2 Publications
    VAR_054729
    Natural varianti521 – 5211P → L in MPS3B; accounts for approximately 6% of mutations in Australasian patients with MPS3B. 4 Publications
    VAR_025491
    Natural varianti534 – 5341S → Y in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
    VAR_054730
    Natural varianti560 – 5601L → P in MPS3B. 1 Publication
    VAR_054731
    Natural varianti561 – 5611L → R in MPS3B. 1 Publication
    VAR_008988
    Natural varianti565 – 5651R → P in MPS3B; does not yield active enzyme. 3 Publications
    VAR_025492
    Natural varianti565 – 5651R → Q in MPS3B. 1 Publication
    VAR_008989
    Natural varianti565 – 5651R → W in MPS3B; accounts for approximately 6% of the mutant alleles in Australasian patients with MPS3B. 6 Publications
    VAR_025493
    Natural varianti591 – 5911L → P in MPS3B. 1 Publication
    VAR_054732
    Natural varianti612 – 6121S → G in MPS3B. 1 Publication
    VAR_054733
    Natural varianti617 – 6171L → F in MPS3B. 1 Publication
    VAR_054734
    Natural varianti643 – 6431R → C in MPS3B; accounts for approximately 20% of MPS3B alleles in a Dutch patient group. 1 Publication
    VAR_025494
    Natural varianti643 – 6431R → H in MPS3B.
    VAR_005012
    Natural varianti649 – 6491W → C in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
    VAR_054735
    Natural varianti650 – 6501G → E in MPS3B. 1 Publication
    VAR_054736
    Natural varianti658 – 6581Y → F in MPS3B. 1 Publication
    VAR_054737
    Natural varianti664 – 6641A → V in MPS3B. 1 Publication
    VAR_005013
    Natural varianti674 – 6741R → C in MPS3B. 2 Publications
    VAR_054738
    Natural varianti674 – 6741R → H in MPS3B. 2 Publications
    VAR_005014
    Natural varianti676 – 6761R → P in MPS3B. 1 Publication
    VAR_054739
    Natural varianti682 – 6821L → R in MPS3B. 2 Publications
    VAR_005015
    Natural varianti705 – 7051E → K in MPS3B. 2 Publications
    VAR_008990
    Natural varianti737 – 7371R → G.6 Publications
    Corresponds to variant rs86312 [ dbSNP | Ensembl ].
    VAR_008991

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS11427.1.
    PIRiG02270.
    RefSeqiNP_000254.2. NM_000263.3.
    UniGeneiHs.50727.

    Genome annotation databases

    EnsembliENST00000225927; ENSP00000225927; ENSG00000108784.
    GeneIDi4669.
    KEGGihsa:4669.
    UCSCiuc002hzv.3. human.

    Polymorphism databases

    DMDMi317373322.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS11427.1.
    PIRi G02270.
    RefSeqi NP_000254.2. NM_000263.3.
    UniGenei Hs.50727.

    3D structure databases

    ProteinModelPortali P54802.
    SMRi P54802. Positions 32-735.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110750. 2 interactions.
    STRINGi 9606.ENSP00000225927.

    Chemistry

    DrugBanki DB00141. N-Acetyl-D-glucosamine.

    Protein family/group databases

    CAZyi GH89. Glycoside Hydrolase Family 89.

    PTM databases

    PhosphoSitei P54802.

    Polymorphism databases

    DMDMi 317373322.

    Proteomic databases

    MaxQBi P54802.
    PaxDbi P54802.
    PRIDEi P54802.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000225927 ; ENSP00000225927 ; ENSG00000108784 .
    GeneIDi 4669.
    KEGGi hsa:4669.
    UCSCi uc002hzv.3. human.

    Organism-specific databases

    CTDi 4669.
    GeneCardsi GC17P040687.
    H-InvDB HIX0202517.
    HGNCi HGNC:7632. NAGLU.
    HPAi HPA038815.
    MIMi 252920. phenotype.
    609701. gene.
    neXtProti NX_P54802.
    Orphaneti 79270. Sanfilippo syndrome type B.
    PharmGKBi PA31437.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG86381.
    HOGENOMi HOG000214539.
    HOVERGENi HBG004225.
    InParanoidi P54802.
    KOi K01205.
    OMAi LFPNSTM.
    OrthoDBi EOG751NF0.
    PhylomeDBi P54802.
    TreeFami TF300689.

    Enzyme and pathway databases

    Reactomei REACT_120752. HS-GAG degradation.

    Miscellaneous databases

    ChiTaRSi NAGLU. human.
    GenomeRNAii 4669.
    NextBioi 17990.
    PROi P54802.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54802.
    Bgeei P54802.
    CleanExi HS_NAGLU.
    Genevestigatori P54802.

    Family and domain databases

    InterProi IPR017853. Glycoside_hydrolase_SF.
    IPR007781. NAGLU.
    IPR024732. NAGLU_C.
    IPR024240. NAGLU_N.
    IPR024733. NAGLU_tim-barrel.
    [Graphical view ]
    PANTHERi PTHR12872. PTHR12872. 1 hit.
    Pfami PF05089. NAGLU. 1 hit.
    PF12972. NAGLU_C. 1 hit.
    PF12971. NAGLU_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. 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.
      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. 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. 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.

    Entry informationi

    Entry nameiANAG_HUMAN
    AccessioniPrimary (citable) accession number: P54802
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 140 of the entry and version 2 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

    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.1 Publication

    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 17
      Human chromosome 17: 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

    External Data

    Dasty 3