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Q14697

- GANAB_HUMAN

UniProt

Q14697 - GANAB_HUMAN

Protein

Neutral alpha-glucosidase AB

Gene

GANAB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 3 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc2Man9GlcNAc2 oligosaccharide precursor of immature glycoproteins.1 Publication

    Catalytic activityi

    Hydrolysis of terminal (1->3)-alpha-D-glucosidic links in (1->3)-alpha-D-glucans.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei542 – 5421Nucleophile
    Active sitei545 – 5451By similarity
    Active sitei618 – 6181Proton donorBy similarity

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro
    2. glucan 1,3-alpha-glucosidase activity Source: UniProtKB-EC
    3. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. post-translational protein modification Source: Reactome
    3. protein folding Source: Reactome
    4. protein N-linked glycosylation via asparagine Source: Reactome

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BRENDAi3.2.1.84. 2681.
    ReactomeiREACT_23810. Calnexin/calreticulin cycle.
    REACT_23878. N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
    UniPathwayiUPA00957.

    Protein family/group databases

    CAZyiGH31. Glycoside Hydrolase Family 31.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neutral alpha-glucosidase AB (EC:3.2.1.84)
    Alternative name(s):
    Alpha-glucosidase 2
    Glucosidase II subunit alpha
    Gene namesi
    Name:GANAB
    Synonyms:G2AN, KIAA0088
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:4138. GANAB.

    Subcellular locationi

    Endoplasmic reticulum By similarity. Golgi apparatus By similarity. Melanosome 2 Publications
    Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. glucosidase II complex Source: Ensembl
    4. Golgi apparatus Source: UniProtKB-SubCell
    5. melanosome Source: UniProtKB-SubCell
    6. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi542 – 5421D → N: Loss of activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA28551.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Chaini29 – 944916Neutral alpha-glucosidase ABPRO_0000018571Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi97 – 971N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ14697.
    PaxDbiQ14697.
    PRIDEiQ14697.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00383581.

    PTM databases

    PhosphoSiteiQ14697.

    Expressioni

    Tissue specificityi

    Detected in placenta.1 Publication

    Gene expression databases

    ArrayExpressiQ14697.
    BgeeiQ14697.
    CleanExiHS_GANAB.
    GenevestigatoriQ14697.

    Organism-specific databases

    HPAiHPA026874.

    Interactioni

    Subunit structurei

    Heterodimer of a catalytic alpha subunit (GANAB) and a beta subunit (PRKCSH). Binds glycosylated PTPRC By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ELF3P785451EBI-348004,EBI-1057285
    PRRC2AP486341EBI-348004,EBI-347545
    TRAF6Q9Y4K31EBI-348004,EBI-359276

    Protein-protein interaction databases

    BioGridi116802. 65 interactions.
    IntActiQ14697. 17 interactions.
    MINTiMINT-5001279.
    STRINGi9606.ENSP00000340466.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14697.
    SMRiQ14697. Positions 249-911.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 31 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1501.
    HOVERGENiHBG051683.
    KOiK05546.
    OMAiAIDDQLY.
    OrthoDBiEOG7VQJDS.
    PhylomeDBiQ14697.
    TreeFamiTF300337.

    Family and domain databases

    InterProiIPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    IPR025887. Glyco_hydro_31_N_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF13802. Gal_mutarotas_2. 1 hit.
    PF01055. Glyco_hydro_31. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF74650. SSF74650. 2 hits.
    PROSITEiPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
    PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14697-1) [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

    MAAVAAVAAR RRRSWASLVL AFLGVCLGIT LAVDRSNFKT CEESSFCKRQ    50
    RSIRPGLSPY RALLDSLQLG PDSLTVHLIH EVTKVLLVLE LQGLQKNMTR 100
    FRIDELEPRR PRYRVPDVLV ADPPIARLSV SGRDENSVEL TMAEGPYKII 150
    LTARPFRLDL LEDRSLLLSV NARGLLEFEH QRAPRVSQGS KDPAEGDGAQ 200
    PEETPRDGDK PEETQGKAEK DEPGAWEETF KTHSDSKPYG PMSVGLDFSL 250
    PGMEHVYGIP EHADNLRLKV TEGGEPYRLY NLDVFQYELY NPMALYGSVP 300
    VLLAHNPHRD LGIFWLNAAE TWVDISSNTA GKTLFGKMMD YLQGSGETPQ 350
    TDVRWMSETG IIDVFLLLGP SISDVFRQYA SLTGTQALPP LFSLGYHQSR 400
    WNYRDEADVL EVDQGFDDHN LPCDVIWLDI EHADGKRYFT WDPSRFPQPR 450
    TMLERLASKR RKLVAIVDPH IKVDSGYRVH EELRNLGLYV KTRDGSDYEG 500
    WCWPGSAGYP DFTNPTMRAW WANMFSYDNY EGSAPNLFVW NDMNEPSVFN 550
    GPEVTMLKDA QHYGGWEHRD VHNIYGLYVH MATADGLRQR SGGMERPFVL 600
    ARAFFAGSQR FGAVWTGDNT AEWDHLKISI PMCLSLGLVG LSFCGADVGG 650
    FFKNPEPELL VRWYQMGAYQ PFFRAHAHLD TGRREPWLLP SQHNDIIRDA 700
    LGQRYSLLPF WYTLLYQAHR EGIPVMRPLW VQYPQDVTTF NIDDQYLLGD 750
    ALLVHPVSDS GAHGVQVYLP GQGEVWYDIQ SYQKHHGPQT LYLPVTLSSI 800
    PVFQRGGTIV PRWMRVRRSS ECMKDDPITL FVALSPQGTA QGELFLDDGH 850
    TFNYQTRQEF LLRRFSFSGN TLVSSSADPE GHFETPIWIE RVVIIGAGKP 900
    AAVVLQTKGS PESRLSFQHD PETSVLVLRK PGINVASDWS IHLR 944
    Length:944
    Mass (Da):106,874
    Last modified:July 5, 2004 - v3
    Checksum:i9E3426FE9A016BF1
    GO
    Isoform 2 (identifier: Q14697-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         187-187: S → SFSDKVNLTLGSIWDKIKNLFSR

    Show »
    Length:966
    Mass (Da):109,438
    Checksum:iD0CD9E47C8E88FB5
    GO
    Isoform 3 (identifier: Q14697-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         49-52: RQRS → CCWC
         53-944: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:52
    Mass (Da):5,673
    Checksum:i012B4BAD808BCD74
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti400 – 4001R → C in AAH65266. (PubMed:15489334)Curated
    Sequence conflicti461 – 4611R → W in AAH65266. (PubMed:15489334)Curated
    Sequence conflicti850 – 8501H → Y in CAA04006. 1 PublicationCurated
    Sequence conflicti850 – 8501H → Y in BAA07642. (PubMed:7788527)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti154 – 1541R → W.
    Corresponds to variant rs2276296 [ dbSNP | Ensembl ].
    VAR_024529
    Natural varianti173 – 1731R → Q.
    Corresponds to variant rs2276295 [ dbSNP | Ensembl ].
    VAR_022086
    Natural varianti309 – 3091R → C.
    Corresponds to variant rs1063445 [ dbSNP | Ensembl ].
    VAR_050272

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei49 – 524RQRS → CCWC in isoform 3. 1 PublicationVSP_039976
    Alternative sequencei53 – 944892Missing in isoform 3. 1 PublicationVSP_039977Add
    BLAST
    Alternative sequencei187 – 1871S → SFSDKVNLTLGSIWDKIKNL FSR in isoform 2. 1 PublicationVSP_010674

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ000332 mRNA. Translation: CAA04006.1.
    AF144074 mRNA. Translation: AAF66685.1.
    AP001458 Genomic DNA. No translation available.
    D42041 mRNA. Translation: BAA07642.1.
    BC017433 mRNA. Translation: AAH17433.2.
    BC017435 mRNA. Translation: AAH17435.2.
    BC065266 mRNA. Translation: AAH65266.1. Sequence problems.
    CCDSiCCDS41656.1. [Q14697-2]
    CCDS8026.1. [Q14697-1]
    RefSeqiNP_001265121.1. NM_001278192.1.
    NP_001265122.1. NM_001278193.1.
    NP_001265123.1. NM_001278194.1.
    NP_938148.1. NM_198334.2. [Q14697-1]
    NP_938149.2. NM_198335.3. [Q14697-2]
    UniGeneiHs.595071.

    Genome annotation databases

    EnsembliENST00000346178; ENSP00000340466; ENSG00000089597. [Q14697-2]
    ENST00000356638; ENSP00000349053; ENSG00000089597. [Q14697-1]
    ENST00000526210; ENSP00000433799; ENSG00000089597. [Q14697-3]
    ENST00000532402; ENSP00000432181; ENSG00000089597. [Q14697-3]
    ENST00000534613; ENSP00000434921; ENSG00000089597. [Q14697-3]
    GeneIDi23193.
    KEGGihsa:23193.
    UCSCiuc001nua.4. human. [Q14697-2]
    uc001nub.4. human. [Q14697-1]

    Polymorphism databases

    DMDMi54037162.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ000332 mRNA. Translation: CAA04006.1 .
    AF144074 mRNA. Translation: AAF66685.1 .
    AP001458 Genomic DNA. No translation available.
    D42041 mRNA. Translation: BAA07642.1 .
    BC017433 mRNA. Translation: AAH17433.2 .
    BC017435 mRNA. Translation: AAH17435.2 .
    BC065266 mRNA. Translation: AAH65266.1 . Sequence problems.
    CCDSi CCDS41656.1. [Q14697-2 ]
    CCDS8026.1. [Q14697-1 ]
    RefSeqi NP_001265121.1. NM_001278192.1.
    NP_001265122.1. NM_001278193.1.
    NP_001265123.1. NM_001278194.1.
    NP_938148.1. NM_198334.2. [Q14697-1 ]
    NP_938149.2. NM_198335.3. [Q14697-2 ]
    UniGenei Hs.595071.

    3D structure databases

    ProteinModelPortali Q14697.
    SMRi Q14697. Positions 249-911.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116802. 65 interactions.
    IntActi Q14697. 17 interactions.
    MINTi MINT-5001279.
    STRINGi 9606.ENSP00000340466.

    Chemistry

    BindingDBi Q14697.
    ChEMBLi CHEMBL2519.

    Protein family/group databases

    CAZyi GH31. Glycoside Hydrolase Family 31.

    PTM databases

    PhosphoSitei Q14697.

    Polymorphism databases

    DMDMi 54037162.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00383581.

    Proteomic databases

    MaxQBi Q14697.
    PaxDbi Q14697.
    PRIDEi Q14697.

    Protocols and materials databases

    DNASUi 23193.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000346178 ; ENSP00000340466 ; ENSG00000089597 . [Q14697-2 ]
    ENST00000356638 ; ENSP00000349053 ; ENSG00000089597 . [Q14697-1 ]
    ENST00000526210 ; ENSP00000433799 ; ENSG00000089597 . [Q14697-3 ]
    ENST00000532402 ; ENSP00000432181 ; ENSG00000089597 . [Q14697-3 ]
    ENST00000534613 ; ENSP00000434921 ; ENSG00000089597 . [Q14697-3 ]
    GeneIDi 23193.
    KEGGi hsa:23193.
    UCSCi uc001nua.4. human. [Q14697-2 ]
    uc001nub.4. human. [Q14697-1 ]

    Organism-specific databases

    CTDi 23193.
    GeneCardsi GC11M062430.
    HGNCi HGNC:4138. GANAB.
    HPAi HPA026874.
    MIMi 104160. gene.
    neXtProti NX_Q14697.
    PharmGKBi PA28551.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1501.
    HOVERGENi HBG051683.
    KOi K05546.
    OMAi AIDDQLY.
    OrthoDBi EOG7VQJDS.
    PhylomeDBi Q14697.
    TreeFami TF300337.

    Enzyme and pathway databases

    UniPathwayi UPA00957 .
    BRENDAi 3.2.1.84. 2681.
    Reactomei REACT_23810. Calnexin/calreticulin cycle.
    REACT_23878. N-glycan trimming in the ER and Calnexin/Calreticulin cycle.

    Miscellaneous databases

    ChiTaRSi GANAB. human.
    GeneWikii GANAB.
    GenomeRNAii 23193.
    NextBioi 44685.
    PROi Q14697.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14697.
    Bgeei Q14697.
    CleanExi HS_GANAB.
    Genevestigatori Q14697.

    Family and domain databases

    InterProi IPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    IPR025887. Glyco_hydro_31_N_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF13802. Gal_mutarotas_2. 1 hit.
    PF01055. Glyco_hydro_31. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    SSF74650. SSF74650. 2 hits.
    PROSITEi PS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
    PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and analysis of the endoplasmic reticulum protein glucosidase II."
      Stuerzenhofecker B., Nguyenvan P., Soeling H.D.
      Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo."
      Pelletier M.F., Marcil A., Sevigny G., Jakob C.A., Tessier D.C., Chevet E., Menard R., Bergeron J.J.M., Thomas D.Y.
      Glycobiology 10:815-827(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, MUTAGENESIS OF ASP-542, INTERACTION WITH PRKCSH, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
      DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-944 (ISOFORM 1).
      Tissue: Bone marrow.
    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] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 457-944 (ISOFORMS 1/2).
      Tissue: Lymph and Uterus.
    6. Lubec G., Afjehi-Sadat L.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 915-929, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    7. "Identity of neutral alpha-glucosidase AB and the glycoprotein processing enzyme glucosidase II. Biochemical and genetic studies."
      Martiniuk F., Ellenbogen A., Hirschhorn R.
      J. Biol. Chem. 260:1238-1242(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION, TISSUE SPECIFICITY.
    8. "Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit."
      Trombetta E.S., Simons J.F., Helenius A.
      J. Biol. Chem. 271:27509-27516(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRKCSH.
    9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiGANAB_HUMAN
    AccessioniPrimary (citable) accession number: Q14697
    Secondary accession number(s): A6NC20, Q8WTS9, Q9P0X0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2004
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 130 of the entry and version 3 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. Human chromosome 11
      Human chromosome 11: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3