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Q9H227

- GBA3_HUMAN

UniProt

Q9H227 - GBA3_HUMAN

Protein

Cytosolic beta-glucosidase

Gene

GBA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (11 Oct 2005)
      Previous versions | rss
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    Functioni

    Glycosidase probably involved in the intestinal absorption and metabolism of dietary flavonoid glycosides. Able to hydrolyze a broad variety of glycosides including phytoestrogens, flavonols, flavones, flavanones and cyanogens. Possesses beta-glycosylceramidase activity and may be involved in a nonlysosomal catabolic pathway of glycosylceramide.3 Publications

    Catalytic activityi

    Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.

    Enzyme regulationi

    Inhibited by 2,4-dinitrophenyl-2-fluoro-2-deoxy-beta-D-glucopyranoside and sodium taurocholate.2 Publications

    Kineticsi

    1. KM=40 µM for 4-methylumbelliferyl-beta-D-glucopyranoside2 Publications
    2. KM=50 µM for 4-methylumbelliferyl-beta-D-galactopyranoside2 Publications
    3. KM=370 µM for 4-nitrophenyl-beta-D-fucopyranoside2 Publications
    4. KM=570 µM for 4-nitrophenyl-alpha-D-arabinopyranoside2 Publications
    5. KM=1.76 mM for 4-nitrophenyl-beta-D-glucopyranoside2 Publications
    6. KM=3.14 mM for 4-nitrophenyl-beta-D-galactopyranoside2 Publications
    7. KM=1.58 mM for 4-nitrophenyl-beta-D-xylopyranoside2 Publications
    8. KM=52.6 mM for 4-nitrophenyl-beta-L-arabinopyranoside2 Publications
    9. KM=35 µM for genistein-7-glucoside2 Publications
    10. KM=118 µM for daidzein-7-glucoside2 Publications
    11. KM=31.8 µM for quercetin-4'-glucoside2 Publications
    12. KM=42.2 µM for quercetin-7-glucoside2 Publications
    13. KM=21.5 µM for apigenin-7-glucoside2 Publications
    14. KM=10 µM for luteolin-4'-glucoside2 Publications
    15. KM=50 µM for luteolin-7-glucoside2 Publications
    16. KM=432 µM for naringenin-7-glucoside2 Publications
    17. KM=253 µM for eriodictyol-7-glucoside2 Publications

    Vmax=10 µmol/min/mg enzyme toward 4-nitrophenyl-beta-D-glucopyranoside2 Publications

    Vmax=1.73 µmol/min/mg enzyme toward genistein-7-glucoside2 Publications

    Vmax=2.75 µmol/min/mg enzyme toward daidzein-7-glucoside2 Publications

    Vmax=1.19 µmol/min/mg enzyme toward quercetin-4'-glucoside2 Publications

    Vmax=0.77 µmol/min/mg enzyme toward quercetin-7-glucoside2 Publications

    Vmax=1.30 µmol/min/mg enzyme toward apigenin-7-glucoside2 Publications

    Vmax=1.30 µmol/min/mg enzyme toward luteolin-4'-glucoside2 Publications

    Vmax=2.85 µmol/min/mg enzyme toward luteolin-7-glucoside2 Publications

    Vmax=0.93 µmol/min/mg enzyme toward naringenin-7-glucoside2 Publications

    Vmax=0.90 µmol/min/mg enzyme toward eriodictyol-7-glucoside2 Publications

    pH dependencei

    Optimum pH is 6.5. Active from pH 5 to 7.5. Activity decreases sharply with increasing acidity and is less than 4% at pH 4.2 Publications

    Temperature dependencei

    Optimum temperature is 50 degrees Celsius. Stable more than 24 hours at 37 degrees Celsius. Loses activity at 58 degrees Celsius.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei17 – 171Substrate
    Binding sitei120 – 1201Substrate
    Binding sitei164 – 1641Substrate
    Active sitei165 – 1651Proton donorSequence Analysis
    Binding sitei309 – 3091Substrate
    Active sitei373 – 3731NucleophileSequence Analysis
    Binding sitei417 – 4171Substrate

    GO - Molecular functioni

    1. beta-galactosidase activity Source: UniProtKB
    2. beta-glucosidase activity Source: UniProtKB
    3. glycosylceramidase activity Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. glycoside catabolic process Source: UniProtKB
    3. glycosphingolipid metabolic process Source: Reactome
    4. glycosylceramide catabolic process Source: UniProtKB
    5. small molecule metabolic process Source: Reactome
    6. sphingolipid metabolic process Source: Reactome

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    ReactomeiREACT_116105. Glycosphingolipid metabolism.
    SABIO-RKQ9H227.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytosolic beta-glucosidase (EC:3.2.1.21)
    Alternative name(s):
    Cytosolic beta-glucosidase-like protein 1
    Gene namesi
    Name:GBA3
    Synonyms:CBG, CBGL1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Organism-specific databases

    HGNCiHGNC:19069. GBA3.

    Subcellular locationi

    Cytoplasmcytosol 2 Publications

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi165 – 1651E → D: Reduces catalytic activity 2-fold. 2 Publications
    Mutagenesisi165 – 1651E → Q: Loss of catalytic activity. 2 Publications
    Mutagenesisi168 – 1681V → Y: No change in temperature or pH dependence. Decrease in specific activity. 1 Publication
    Mutagenesisi225 – 2251F → S: Decrease in specific activity. 1 Publication
    Mutagenesisi308 – 3081Y → F or A: Decrease in specific activity. 1 Publication
    Mutagenesisi373 – 3731E → D: Reduces catalytic activity 2-fold. 1 Publication
    Mutagenesisi373 – 3731E → Q: Loss of catalytic activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA134861643.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 469469Cytosolic beta-glucosidasePRO_0000063908Add
    BLAST

    Post-translational modificationi

    The N-terminus is blocked.

    Proteomic databases

    PRIDEiQ9H227.

    PTM databases

    PhosphoSiteiQ9H227.

    Expressioni

    Tissue specificityi

    Present in small intestine (at protein level). Expressed in liver, small intestine, colon, spleen and kidney. Down-regulated in renal cell carcinomas and hepatocellular carcinomas.2 Publications

    Gene expression databases

    CleanExiHS_GBA3.
    GenevestigatoriQ9H227.

    Interactioni

    Protein-protein interaction databases

    BioGridi121753. 2 interactions.
    IntActiQ9H227. 1 interaction.

    Structurei

    Secondary structure

    1
    469
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 125
    Helixi15 – 184
    Helixi24 – 263
    Helixi31 – 388
    Beta strandi40 – 434
    Helixi44 – 463
    Beta strandi49 – 513
    Turni55 – 573
    Helixi59 – 6911
    Beta strandi72 – 776
    Helixi80 – 834
    Helixi94 – 10916
    Beta strandi113 – 1219
    Helixi125 – 1295
    Helixi132 – 1343
    Helixi138 – 15316
    Turni154 – 1563
    Beta strandi159 – 1646
    Helixi166 – 1749
    Turni186 – 1883
    Helixi189 – 21123
    Helixi213 – 2164
    Beta strandi219 – 2213
    Beta strandi223 – 23311
    Helixi237 – 25014
    Helixi252 – 2598
    Helixi266 – 27813
    Helixi291 – 2977
    Beta strandi302 – 31615
    Helixi326 – 3305
    Beta strandi332 – 3354
    Helixi351 – 36313
    Beta strandi369 – 3746
    Beta strandi378 – 3814
    Helixi387 – 40519
    Beta strandi411 – 4177
    Helixi425 – 4306
    Beta strandi435 – 4384
    Beta strandi442 – 4443
    Beta strandi447 – 4493
    Helixi451 – 46212

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E9LX-ray1.60A1-469[»]
    2E9MX-ray1.80A1-469[»]
    2JFEX-ray2.70X1-469[»]
    2ZOXX-ray1.90A1-469[»]
    3VKKX-ray2.00A1-469[»]
    ProteinModelPortaliQ9H227.
    SMRiQ9H227. Positions 1-466.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H227.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni424 – 4252Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    HOVERGENiHBG053101.
    InParanoidiQ9H227.
    KOiK05350.
    PhylomeDBiQ9H227.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10353. PTHR10353. 1 hit.
    PfamiPF00232. Glyco_hydro_1. 1 hit.
    [Graphical view]
    PRINTSiPR00131. GLHYDRLASE1.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H227-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAFPAGFGWA AATAAYQVEG GWDADGKGPC VWDTFTHQGG ERVFKNQTGD    50
    VACGSYTLWE EDLKCIKQLG LTHYRFSLSW SRLLPDGTTG FINQKGIDYY 100
    NKIIDDLLKN GVTPIVTLYH FDLPQTLEDQ GGWLSEAIIE SFDKYAQFCF 150
    STFGDRVKQW ITINEANVLS VMSYDLGMFP PGIPHFGTGG YQAAHNLIKA 200
    HARSWHSYDS LFRKKQKGMV SLSLFAVWLE PADPNSVSDQ EAAKRAITFH 250
    LDLFAKPIFI DGDYPEVVKS QIASMSQKQG YPSSRLPEFT EEEKKMIKGT 300
    ADFFAVQYYT TRLIKYQENK KGELGILQDA EIEFFPDPSW KNVDWIYVVP 350
    WGVCKLLKYI KDTYNNPVIY ITENGFPQSD PAPLDDTQRW EYFRQTFQEL 400
    FKAIQLDKVN LQVYCAWSLL DNFEWNQGYS SRFGLFHVDF EDPARPRVPY 450
    TSAKEYAKII RNNGLEAHL 469
    Length:469
    Mass (Da):53,696
    Last modified:October 11, 2005 - v2
    Checksum:i9036455485CE2E2F
    GO
    Isoform 2 (identifier: Q9H227-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         95-401: Missing.

    Show »
    Length:162
    Mass (Da):18,265
    Checksum:iAC2A05DB957E6997
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti29 – 291P → L in AAH70188. (PubMed:15489334)Curated
    Sequence conflicti134 – 1341L → W in AAG39217. (PubMed:11784319)Curated
    Sequence conflicti309 – 3091Y → C in BAD96683. 1 PublicationCurated
    Sequence conflicti321 – 3211K → R in BAD96683. 1 PublicationCurated
    Sequence conflicti326 – 3261I → T in CAC08178. (PubMed:11389701)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti106 – 1061D → N Rare polymorphism. 1 Publication
    VAR_023587
    Natural varianti172 – 1721M → I.
    Corresponds to variant rs36090352 [ dbSNP | Ensembl ].
    VAR_049298
    Natural varianti213 – 2131R → P.
    Corresponds to variant rs17612341 [ dbSNP | Ensembl ].
    VAR_023588
    Natural varianti354 – 3541C → R.
    Corresponds to variant rs16873108 [ dbSNP | Ensembl ].
    VAR_023589

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei95 – 401307Missing in isoform 2. 1 PublicationVSP_015835Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB017913 mRNA. Translation: BAB18741.1.
    AJ278964 mRNA. Translation: CAC08178.1.
    AF317840 mRNA. Translation: AAG39217.1.
    AF323990 mRNA. Translation: AAL37305.1.
    AK222963 mRNA. Translation: BAD96683.1.
    BC029362 mRNA. Translation: AAH29362.1.
    BC070188 mRNA. Translation: AAH70188.1.
    BC101829 mRNA. Translation: AAI01830.1.
    BC109377 mRNA. Translation: AAI09378.1.
    RefSeqiNP_001121904.1. NM_001128432.2. [Q9H227-2]
    NP_001264154.1. NM_001277225.1.
    NP_066024.1. NM_020973.4. [Q9H227-1]
    UniGeneiHs.653107.

    Genome annotation databases

    GeneIDi57733.
    KEGGihsa:57733.
    UCSCiuc031sdv.1. human. [Q9H227-1]
    uc031sdw.1. human. [Q9H227-2]

    Polymorphism databases

    DMDMi77416427.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB017913 mRNA. Translation: BAB18741.1 .
    AJ278964 mRNA. Translation: CAC08178.1 .
    AF317840 mRNA. Translation: AAG39217.1 .
    AF323990 mRNA. Translation: AAL37305.1 .
    AK222963 mRNA. Translation: BAD96683.1 .
    BC029362 mRNA. Translation: AAH29362.1 .
    BC070188 mRNA. Translation: AAH70188.1 .
    BC101829 mRNA. Translation: AAI01830.1 .
    BC109377 mRNA. Translation: AAI09378.1 .
    RefSeqi NP_001121904.1. NM_001128432.2. [Q9H227-2 ]
    NP_001264154.1. NM_001277225.1.
    NP_066024.1. NM_020973.4. [Q9H227-1 ]
    UniGenei Hs.653107.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2E9L X-ray 1.60 A 1-469 [» ]
    2E9M X-ray 1.80 A 1-469 [» ]
    2JFE X-ray 2.70 X 1-469 [» ]
    2ZOX X-ray 1.90 A 1-469 [» ]
    3VKK X-ray 2.00 A 1-469 [» ]
    ProteinModelPortali Q9H227.
    SMRi Q9H227. Positions 1-466.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121753. 2 interactions.
    IntActi Q9H227. 1 interaction.

    Chemistry

    BindingDBi Q9H227.
    ChEMBLi CHEMBL3865.

    Protein family/group databases

    CAZyi GH1. Glycoside Hydrolase Family 1.

    PTM databases

    PhosphoSitei Q9H227.

    Polymorphism databases

    DMDMi 77416427.

    Proteomic databases

    PRIDEi Q9H227.

    Protocols and materials databases

    DNASUi 57733.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 57733.
    KEGGi hsa:57733.
    UCSCi uc031sdv.1. human. [Q9H227-1 ]
    uc031sdw.1. human. [Q9H227-2 ]

    Organism-specific databases

    CTDi 57733.
    GeneCardsi GC04P022694.
    HGNCi HGNC:19069. GBA3.
    MIMi 606619. gene.
    neXtProti NX_Q9H227.
    PharmGKBi PA134861643.
    GenAtlasi Search...

    Phylogenomic databases

    HOVERGENi HBG053101.
    InParanoidi Q9H227.
    KOi K05350.
    PhylomeDBi Q9H227.

    Enzyme and pathway databases

    Reactomei REACT_116105. Glycosphingolipid metabolism.
    SABIO-RK Q9H227.

    Miscellaneous databases

    EvolutionaryTracei Q9H227.
    GeneWikii GBA3.
    GenomeRNAii 57733.
    NextBioi 64698.
    PROi Q9H227.
    SOURCEi Search...

    Gene expression databases

    CleanExi HS_GBA3.
    Genevestigatori Q9H227.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR10353. PTHR10353. 1 hit.
    Pfami PF00232. Glyco_hydro_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00131. GLHYDRLASE1.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Fetal liver.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
      Tissue: Liver.
    3. "Functional expression of human liver cytosolic beta-glucosidase in Pichia pastoris. Insights into its role in the metabolism of dietary glucosides."
      Berrin J.-G., McLauchlan W.R., Needs P., Williamson G., Puigserver A., Kroon P.A., Juge N.
      Eur. J. Biochem. 269:249-258(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BLOCKAGE OF N-TERMINUS, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
      Tissue: Liver.
    4. Hays W.S., VanderJagt D.J., Glew R.H., Johnston D.E.
      Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Small intestine.
    6. "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] (ISOFORMS 1 AND 2).
      Tissue: Kidney and Liver.
    7. "Substrate (aglycone) specificity of human cytosolic beta-glucosidase."
      Berrin J.-G., Czjzek M., Kroon P.A., McLauchlan W.R., Puigserver A., Williamson G., Juge N.
      Biochem. J. 373:41-48(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF VAL-168; PHE-225 AND TYR-308.
    8. "Deglycosylation by small intestinal epithelial cell beta-glucosidases is a critical step in the absorption and metabolism of dietary flavonoid glycosides in humans."
      Nemeth K., Plumb G.W., Berrin J.-G., Juge N., Jacob R., Naim H.Y., Williamson G., Swallow D.M., Kroon P.A.
      Eur. J. Nutr. 42:29-42(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    9. "Klotho-related protein is a novel cytosolic neutral beta-glycosylceramidase."
      Hayashi Y., Okino N., Kakuta Y., Shikanai T., Tani M., Narimatsu H., Ito M.
      J. Biol. Chem. 282:30889-30900(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH GLUCOSE AND GALACTOSE, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-165 AND GLU-373.
    10. "The crystal structure of human cytosolic beta-glucosidase unravels the substrate aglycone specificity of a family 1 glycoside hydrolase."
      Tribolo S., Berrin J.G., Kroon P.A., Czjzek M., Juge N.
      J. Mol. Biol. 370:964-975(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
    11. "Crystal structure of the covalent intermediate of human cytosolic beta-glucosidase."
      Noguchi J., Hayashi Y., Baba Y., Okino N., Kimura M., Ito M., Kakuta Y.
      Biochem. Biophys. Res. Commun. 374:549-552(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLUCOSE, MUTAGENESIS OF GLU-165.
    12. "Mutations in the gene encoding cytosolic beta-glucosidase in Gaucher disease."
      Beutler E., Beutler L., West C.
      J. Lab. Clin. Med. 144:65-68(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ASN-106.

    Entry informationi

    Entry nameiGBA3_HUMAN
    AccessioniPrimary (citable) accession number: Q9H227
    Secondary accession number(s): Q32LY7
    , Q3MIH4, Q53GG8, Q6NSF4, Q8NHT8, Q9H3T4, Q9H4C6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2005
    Last sequence update: October 11, 2005
    Last modified: October 1, 2014
    This is version 120 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. Human chromosome 4
      Human chromosome 4: 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