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P17050

- NAGAB_HUMAN

UniProt

P17050 - NAGAB_HUMAN

Protein

Alpha-N-acetylgalactosaminidase

Gene

NAGA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 2 (01 Mar 1992)
      Previous versions | rss
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    Functioni

    Removes terminal alpha-N-acetylgalactosamine residues from glycolipids and glycopeptides. Required for the breakdown of glycolipids.1 Publication

    Catalytic activityi

    Cleavage of non-reducing alpha-(1->3)-N-acetylgalactosamine residues from human blood group A and AB mucin glycoproteins, Forssman hapten and blood group A lacto series glycolipids.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei154 – 1541Substrate
    Active sitei156 – 1561Nucleophile
    Binding sitei188 – 1881Substrate
    Binding sitei213 – 2131Substrate
    Active sitei217 – 2171Proton donor
    Binding sitei217 – 2171Substrate

    GO - Molecular functioni

    1. alpha-galactosidase activity Source: RefGenome
    2. alpha-N-acetylgalactosaminidase activity Source: UniProtKB
    3. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. carbohydrate catabolic process Source: UniProtKB
    2. glycolipid catabolic process Source: UniProtKB
    3. glycoside catabolic process Source: RefGenome
    4. glycosylceramide catabolic process Source: RefGenome
    5. oligosaccharide metabolic process Source: RefGenome

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01993-MONOMER.
    SABIO-RKP17050.

    Protein family/group databases

    CAZyiGH27. Glycoside Hydrolase Family 27.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-N-acetylgalactosaminidase (EC:3.2.1.49)
    Alternative name(s):
    Alpha-galactosidase B
    Gene namesi
    Name:NAGA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:7631. NAGA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: RefGenome
    2. extracellular vesicular exosome Source: UniProt
    3. lysosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Involvement in diseasei

    Schindler disease (SCHIND) [MIM:609241]: Form of NAGA deficiency characterized by early-onset neuroaxonal dystrophy and neurological signs (convulsion during fever, epilepsy, psychomotor retardation and hypotonia). NAGA deficiency is typically classified in three main phenotypes: NAGA deficiency type I (Schindler disease or Schindler disease type I) with severe manifestations; NAGA deficiency type II (Kanzazi disease or Schindler disease type II) which is mild; NAGA deficiency type III (Schindler disease type III) characterized by mild-to-moderate neurologic manifestations. NAGA deficiency results in the increased urinary excretion of glycopeptides and oligosaccharides containing alpha-N-acetylgalactosaminyl moieties. Inheritance is autosomal recessive.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti160 – 1601S → C in SCHIND; type III. 1 Publication
    Corresponds to variant rs121434532 [ dbSNP | Ensembl ].
    VAR_000496
    Natural varianti325 – 3251E → K in SCHIND; type I and type III. 2 Publications
    VAR_000497
    Kanzaki disease (KANZD) [MIM:609242]: Autosomal recessive disorder characterized by late-onset, angiokeratoma corporis diffusum and mild intellectual impairment.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti329 – 3291R → Q in KANZD. 1 Publication
    Corresponds to variant rs121434533 [ dbSNP | Ensembl ].
    VAR_022525
    Natural varianti329 – 3291R → W in KANZD; loss of activity. 1 Publication
    VAR_000498

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi201 – 2011N → Q: Loss of glycosylation site; no effect on enzyme activity and stability. 1 Publication

    Keywords - Diseasei

    Disease mutation, Epilepsy

    Organism-specific databases

    MIMi609241. phenotype.
    609242. phenotype.
    Orphaneti79279. Alpha-N-acetylgalactosaminidase deficiency type 1.
    79280. Alpha-N-acetylgalactosaminidase deficiency type 2.
    79281. Alpha-N-acetylgalactosaminidase deficiency type 3.
    PharmGKBiPA31435.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 17171 PublicationAdd
    BLAST
    Chaini18 – 411394Alpha-N-acetylgalactosaminidasePRO_0000001018Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi38 ↔ 801 Publication
    Disulfide bondi42 ↔ 491 Publication
    Glycosylationi124 – 1241N-linked (GlcNAc...)1 Publication
    Disulfide bondi127 ↔ 1581 Publication
    Glycosylationi177 – 1771N-linked (GlcNAc...)2 Publications
    Disulfide bondi187 ↔ 2091 Publication
    Glycosylationi201 – 2011N-linked (GlcNAc...)1 Publication
    Modified residuei322 – 3221Phosphoserine1 Publication
    Modified residuei332 – 3321Phosphoserine1 Publication
    Glycosylationi359 – 3591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi385 – 3851N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP17050.
    PaxDbiP17050.
    PeptideAtlasiP17050.
    PRIDEiP17050.

    PTM databases

    PhosphoSiteiP17050.
    UniCarbKBiP17050.

    Expressioni

    Gene expression databases

    BgeeiP17050.
    CleanExiHS_NAGA.
    GenevestigatoriP17050.

    Organism-specific databases

    HPAiHPA000649.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi110749. 3 interactions.
    STRINGi9606.ENSP00000379680.

    Structurei

    Secondary structure

    1
    411
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 325
    Helixi33 – 364
    Turni42 – 443
    Turni46 – 483
    Beta strandi49 – 513
    Helixi52 – 6413
    Helixi67 – 704
    Beta strandi74 – 763
    Beta strandi82 – 854
    Beta strandi91 – 933
    Turni95 – 973
    Helixi102 – 11110
    Beta strandi115 – 12511
    Helixi135 – 1373
    Helixi138 – 14710
    Beta strandi152 – 1565
    Helixi162 – 17817
    Beta strandi184 – 1874
    Helixi189 – 1924
    Turni197 – 1993
    Helixi202 – 2087
    Beta strandi210 – 2134
    Helixi222 – 23413
    Helixi236 – 2394
    Helixi240 – 2423
    Beta strandi247 – 2504
    Beta strandi258 – 2603
    Helixi263 – 27513
    Beta strandi280 – 2823
    Turni286 – 2883
    Helixi291 – 2977
    Helixi300 – 3067
    Beta strandi315 – 3195
    Beta strandi323 – 3308
    Helixi332 – 3343
    Beta strandi336 – 3427
    Beta strandi345 – 3473
    Beta strandi349 – 3546
    Helixi355 – 3584
    Beta strandi365 – 3706
    Turni371 – 3733
    Beta strandi376 – 3805
    Beta strandi385 – 3906
    Beta strandi395 – 4039

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3H53X-ray2.01A/B18-411[»]
    3H54X-ray2.20A/B18-411[»]
    3H55X-ray1.91A/B18-411[»]
    3IGUX-ray2.15A/B18-411[»]
    4DO4X-ray1.40A/B18-411[»]
    4DO5X-ray1.51A/B18-411[»]
    4DO6X-ray1.60A/B18-411[»]
    ProteinModelPortaliP17050.
    SMRiP17050. Positions 18-411.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17050.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni78 – 792Substrate binding

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 27 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG68897.
    HOGENOMiHOG000161224.
    HOVERGENiHBG001989.
    InParanoidiP17050.
    KOiK01204.
    OMAiVIYEAQD.
    OrthoDBiEOG7F24SV.
    PhylomeDBiP17050.
    TreeFamiTF312909.

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR013780. Glyco_hydro_13_b.
    IPR002241. Glyco_hydro_27.
    IPR000111. Glyco_hydro_GHD.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF02065. Melibiase. 1 hit.
    [Graphical view]
    PRINTSiPR00740. GLHYDRLASE27.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00512. ALPHA_GALACTOSIDASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P17050-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLLKTVLLLG HVAQVLMLDN GLLQTPPMGW LAWERFRCNI NCDEDPKNCI    50
    SEQLFMEMAD RMAQDGWRDM GYTYLNIDDC WIGGRDASGR LMPDPKRFPH 100
    GIPFLADYVH SLGLKLGIYA DMGNFTCMGY PGTTLDKVVQ DAQTFAEWKV 150
    DMLKLDGCFS TPEERAQGYP KMAAALNATG RPIAFSCSWP AYEGGLPPRV 200
    NYSLLADICN LWRNYDDIQD SWWSVLSILN WFVEHQDILQ PVAGPGHWND 250
    PDMLLIGNFG LSLEQSRAQM ALWTVLAAPL LMSTDLRTIS AQNMDILQNP 300
    LMIKINQDPL GIQGRRIHKE KSLIEVYMRP LSNKASALVF FSCRTDMPYR 350
    YHSSLGQLNF TGSVIYEAQD VYSGDIISGL RDETNFTVII NPSGVVMWYL 400
    YPIKNLEMSQ Q 411
    Length:411
    Mass (Da):46,565
    Last modified:March 1, 1992 - v2
    Checksum:i781A0728C0B29CD9
    GO

    Sequence cautioni

    The sequence AAA59902.1 differs from that shown. Reason: Frameshift at position 320.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 241Q → N AA sequence (PubMed:2256909)Curated
    Sequence conflicti165 – 1651R → A in AAA59902. (PubMed:1646157)Curated
    Sequence conflicti175 – 1751A → G in AAA59902. (PubMed:1646157)Curated
    Sequence conflicti205 – 2051L → Q in AAA59902. (PubMed:1646157)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti160 – 1601S → C in SCHIND; type III. 1 Publication
    Corresponds to variant rs121434532 [ dbSNP | Ensembl ].
    VAR_000496
    Natural varianti325 – 3251E → K in SCHIND; type I and type III. 2 Publications
    VAR_000497
    Natural varianti329 – 3291R → Q in KANZD. 1 Publication
    Corresponds to variant rs121434533 [ dbSNP | Ensembl ].
    VAR_022525
    Natural varianti329 – 3291R → W in KANZD; loss of activity. 1 Publication
    VAR_000498

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M62783 mRNA. Translation: AAA51677.1.
    M59199 Genomic DNA. Translation: AAB06718.1.
    M29276 mRNA. Translation: AAA59902.1. Frameshift.
    M38083 mRNA. Translation: AAA36351.1.
    CR456527 mRNA. Translation: CAG30413.1.
    Z99716 Genomic DNA. Translation: CAB41237.1.
    BC000095 mRNA. Translation: AAH00095.1.
    CCDSiCCDS14030.1.
    PIRiA33265.
    A36530. A35485.
    RefSeqiNP_000253.1. NM_000262.2.
    XP_005261672.1. XM_005261615.2.
    XP_005261673.1. XM_005261616.2.
    UniGeneiHs.75372.

    Genome annotation databases

    EnsembliENST00000396398; ENSP00000379680; ENSG00000198951.
    ENST00000402937; ENSP00000384603; ENSG00000198951.
    ENST00000403363; ENSP00000385283; ENSG00000198951.
    GeneIDi4668.
    KEGGihsa:4668.
    UCSCiuc003bbw.4. human.

    Polymorphism databases

    DMDMi127801.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M62783 mRNA. Translation: AAA51677.1 .
    M59199 Genomic DNA. Translation: AAB06718.1 .
    M29276 mRNA. Translation: AAA59902.1 . Frameshift.
    M38083 mRNA. Translation: AAA36351.1 .
    CR456527 mRNA. Translation: CAG30413.1 .
    Z99716 Genomic DNA. Translation: CAB41237.1 .
    BC000095 mRNA. Translation: AAH00095.1 .
    CCDSi CCDS14030.1.
    PIRi A33265.
    A36530. A35485.
    RefSeqi NP_000253.1. NM_000262.2.
    XP_005261672.1. XM_005261615.2.
    XP_005261673.1. XM_005261616.2.
    UniGenei Hs.75372.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3H53 X-ray 2.01 A/B 18-411 [» ]
    3H54 X-ray 2.20 A/B 18-411 [» ]
    3H55 X-ray 1.91 A/B 18-411 [» ]
    3IGU X-ray 2.15 A/B 18-411 [» ]
    4DO4 X-ray 1.40 A/B 18-411 [» ]
    4DO5 X-ray 1.51 A/B 18-411 [» ]
    4DO6 X-ray 1.60 A/B 18-411 [» ]
    ProteinModelPortali P17050.
    SMRi P17050. Positions 18-411.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110749. 3 interactions.
    STRINGi 9606.ENSP00000379680.

    Chemistry

    ChEMBLi CHEMBL3132.

    Protein family/group databases

    CAZyi GH27. Glycoside Hydrolase Family 27.

    PTM databases

    PhosphoSitei P17050.
    UniCarbKBi P17050.

    Polymorphism databases

    DMDMi 127801.

    Proteomic databases

    MaxQBi P17050.
    PaxDbi P17050.
    PeptideAtlasi P17050.
    PRIDEi P17050.

    Protocols and materials databases

    DNASUi 4668.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000396398 ; ENSP00000379680 ; ENSG00000198951 .
    ENST00000402937 ; ENSP00000384603 ; ENSG00000198951 .
    ENST00000403363 ; ENSP00000385283 ; ENSG00000198951 .
    GeneIDi 4668.
    KEGGi hsa:4668.
    UCSCi uc003bbw.4. human.

    Organism-specific databases

    CTDi 4668.
    GeneCardsi GC22M042428.
    HGNCi HGNC:7631. NAGA.
    HPAi HPA000649.
    MIMi 104170. gene.
    609241. phenotype.
    609242. phenotype.
    neXtProti NX_P17050.
    Orphaneti 79279. Alpha-N-acetylgalactosaminidase deficiency type 1.
    79280. Alpha-N-acetylgalactosaminidase deficiency type 2.
    79281. Alpha-N-acetylgalactosaminidase deficiency type 3.
    PharmGKBi PA31435.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG68897.
    HOGENOMi HOG000161224.
    HOVERGENi HBG001989.
    InParanoidi P17050.
    KOi K01204.
    OMAi VIYEAQD.
    OrthoDBi EOG7F24SV.
    PhylomeDBi P17050.
    TreeFami TF312909.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS01993-MONOMER.
    SABIO-RK P17050.

    Miscellaneous databases

    EvolutionaryTracei P17050.
    GeneWikii NAGA_(gene).
    GenomeRNAii 4668.
    NextBioi 17986.
    PROi P17050.
    SOURCEi Search...

    Gene expression databases

    Bgeei P17050.
    CleanExi HS_NAGA.
    Genevestigatori P17050.

    Family and domain databases

    Gene3Di 2.60.40.1180. 1 hit.
    3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR013780. Glyco_hydro_13_b.
    IPR002241. Glyco_hydro_27.
    IPR000111. Glyco_hydro_GHD.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF02065. Melibiase. 1 hit.
    [Graphical view ]
    PRINTSi PR00740. GLHYDRLASE27.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00512. ALPHA_GALACTOSIDASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human alpha-N-acetylgalactosaminidase-molecular cloning, nucleotide sequence, and expression of a full-length cDNA. Homology with human alpha-galactosidase A suggests evolution from a common ancestral gene."
      Wang A.M., Bishop D.F., Desnick R.J.
      J. Biol. Chem. 265:21859-21866(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Lung.
    2. "Structural organization and complete sequence of the human alpha-N-acetylgalactosaminidase gene: homology with the alpha-galactosidase A gene provides evidence for evolution from a common ancestral gene."
      Wang A.M., Desnick R.J.
      Genomics 10:133-142(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Molecular cloning of a full-length cDNA for human alpha-N-acetylgalactosaminidase (alpha-galactosidase B)."
      Tsuji S., Yamauchi T., Hiraiwa M., Isobe T., Okuyama T., Sakimura K., Takahashi Y., Nishizawa M., Uda Y., Miyatake T.
      Biochem. Biophys. Res. Commun. 163:1498-1504(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    4. "Molecular cloning of two species of cDNAs for human alpha-N-acetylgalactosaminidase and expression in mammalian cells."
      Yamauchi T., Hiraiwa M., Kobayashi H., Uda Y., Miyatake T., Tsuji S.
      Biochem. Biophys. Res. Commun. 170:231-237(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Placenta.
    8. "Photolabeling of the alpha-neuraminidase/beta-galactosidase complex from human placenta with a photoreactive neuraminidase inhibitor."
      Warner T.G., Louie A., Potier M.
      Biochem. Biophys. Res. Commun. 173:13-19(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 18-37.
      Tissue: Placenta.
    9. "Degradation of blood group A glycolipid A-6-2 by normal and mutant human skin fibroblasts."
      Asfaw B., Schindler D., Ledvinova J., Cerny B., Smid F., Conzelmann E.
      J. Lipid Res. 39:1768-1780(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
      Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
      Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322 AND SER-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    11. "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-177 AND ASN-201.
      Tissue: Liver.
    12. "The 1.9 A structure of human alpha-N-acetylgalactosaminidase: the molecular basis of Schindler and Kanzaki diseases."
      Clark N.E., Garman S.C.
      J. Mol. Biol. 393:435-447(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 18-411 IN COMPLEXES WITH N-ACETYLGALACTOSAMINE AND GALACTOSE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-124; ASN-177 AND ASN-385, SUBUNIT, CATALYTIC ACTIVITY, MUTAGENESIS OF ASN-201.
    13. "Schindler disease: the molecular lesion in the alpha-N-acetylgalactosaminidase gene that causes an infantile neuroaxonal dystrophy."
      Wang A.M., Schindler D., Desnick R.J.
      J. Clin. Invest. 86:1752-1756(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SCHIND LYS-325.
    14. "The molecular lesion in the alpha-N-acetylgalactosaminidase gene that causes angiokeratoma corporis diffusum with glycopeptiduria."
      Wang A.M., Kanzaki T., Desnick R.J.
      J. Clin. Invest. 94:839-845(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT KANZD TRP-329, CHARACTERIZATION OF VARIANT KANZD TRP-329.
    15. Cited for: VARIANTS SCHIND CYS-160 AND LYS-325.
    16. "A new case of alpha-N-acetylgalactosaminidase deficiency with angiokeratoma corporis diffusum, with Meniere's syndrome and without mental retardation."
      Kodama K., Kobayashi H., Abe R., Ohkawara A., Yoshii N., Yotsumoto S., Fukushige T., Nagatsuka Y., Hirabayashi Y., Kanzaki T.
      Br. J. Dermatol. 144:363-368(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT KANZD GLN-329.

    Entry informationi

    Entry nameiNAGAB_HUMAN
    AccessioniPrimary (citable) accession number: P17050
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: March 1, 1992
    Last modified: October 1, 2014
    This is version 156 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

    Miscellaneous

    Alpha-galactosidase B was first found to be an isoenzyme of alpha-galactosidases, but apparently it differs from alpha-galactosidase A in substrate specificity and is alpha-N-acetylgalactosaminidase.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3