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P17050

- NAGAB_HUMAN

UniProt

P17050 - NAGAB_HUMAN

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Protein

Alpha-N-acetylgalactosaminidase

Gene

NAGA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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: UniProtKB
  3. lysosome Source: UniProtKB-KW
Complete GO annotation...

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. 4 interactions.
STRINGi9606.ENSP00000379680.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000008751.
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

        10         20         30         40         50
MLLKTVLLLG HVAQVLMLDN GLLQTPPMGW LAWERFRCNI NCDEDPKNCI
60 70 80 90 100
SEQLFMEMAD RMAQDGWRDM GYTYLNIDDC WIGGRDASGR LMPDPKRFPH
110 120 130 140 150
GIPFLADYVH SLGLKLGIYA DMGNFTCMGY PGTTLDKVVQ DAQTFAEWKV
160 170 180 190 200
DMLKLDGCFS TPEERAQGYP KMAAALNATG RPIAFSCSWP AYEGGLPPRV
210 220 230 240 250
NYSLLADICN LWRNYDDIQD SWWSVLSILN WFVEHQDILQ PVAGPGHWND
260 270 280 290 300
PDMLLIGNFG LSLEQSRAQM ALWTVLAAPL LMSTDLRTIS AQNMDILQNP
310 320 330 340 350
LMIKINQDPL GIQGRRIHKE KSLIEVYMRP LSNKASALVF FSCRTDMPYR
360 370 380 390 400
YHSSLGQLNF TGSVIYEAQD VYSGDIISGL RDETNFTVII NPSGVVMWYL
410
YPIKNLEMSQ Q
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 4 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.
GeneTreei ENSGT00390000008751.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 158 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

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