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Q53Y83

- Q53Y83_HUMAN

UniProt

Q53Y83 - Q53Y83_HUMAN

Protein
Submitted name:

Galactosidase, alpha

Gene

GLA

Organism
Homo sapiens (Human)
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (24 May 2005)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. alpha-galactosidase activity Source: Ensembl
    2. galactoside binding Source: Ensembl

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. glycosylceramide catabolic process Source: Ensembl
    3. negative regulation of nitric oxide biosynthetic process Source: Ensembl
    4. negative regulation of nitric-oxide synthase activity Source: Ensembl

    Keywords - Molecular functioni

    GlycosidaseUniRule annotationSAAS annotation, Hydrolase

    Protein family/group databases

    CAZyiGH27. Glycoside Hydrolase Family 27.

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    Galactosidase, alphaImported
    Submitted name:
    Galactosidase, alpha, isoform CRA_aImported
    Submitted name:
    cDNA FLJ76285, highly similar to Homo sapiens galactosidase, alpha (GLA), mRNAImported
    Gene namesi
    Name:GLAImported
    ORF Names:hCG_20401Imported
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

    Subcellular locationi

    GO - Cellular componenti

    1. lysosome Source: Ensembl

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28707.

    Protein family/group databases

    Allergomei9621. Hom s alpha-Galactosidase.

    PTM / Processingi

    Keywords - PTMi

    Disulfide bondUniRule annotation

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Structurei

    3D structure databases

    SMRiQ53Y83. Positions 32-426.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 27 family.UniRule annotation

    Phylogenomic databases

    HOVERGENiHBG001989.
    KOiK01189.
    OMAiNDLRDIC.
    PhylomeDBiQ53Y83.

    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.

    Q53Y83-1 [UniParc]FASTAAdd to Basket

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    MQLRNPELHL GCALALRFLA LVSWDIPGAR ALDNGLARTP TMGWLHWERF    50
    MCNLDCQEEP DSCISEKLFM EMAELMVSEG WKDAGYEYLC IDDCWMAPQR 100
    DSEGRLQADP QRFPHGIRQL ANYVHSKGLK LGIYADVGNK TCAGFPGSFG 150
    YYDIDAQTFA DWGVDLLKFD GCYCDSLENL ADGYKHMSLA LNRTGRSIVY 200
    SCEWPLYMWP FQKPNYTEIR QYCNHWRNFA DIDDSWKSIK SILDWTSFNQ 250
    ERIVDVAGPG GWNDPDMLVI GNFGLSWNQQ VTQMALWAIM AAPLFMSNDL 300
    RHISPQAKAL LQDKDVIAIN QDPLGKQGYQ LRQGDNFEVW ERPLSGLAWA 350
    VAMINRQEIG GPRSYTIAVA SLGKGVACNP ACFITQLLPV KRKLGFYEWT 400
    SRLRSHINPT GTVLLQLENT MQMSLKDLL 429
    Length:429
    Mass (Da):48,767
    Last modified:May 24, 2005 - v1
    Checksum:i613F8BF21B107D7B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BT006864 mRNA. Translation: AAP35510.1.
    AK291095 mRNA. Translation: BAF83784.1.
    CH471115 Genomic DNA. Translation: EAX02862.1.
    RefSeqiNP_000160.1. NM_000169.2.
    UniGeneiHs.69089.

    Genome annotation databases

    GeneIDi2717.
    KEGGihsa:2717.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BT006864 mRNA. Translation: AAP35510.1 .
    AK291095 mRNA. Translation: BAF83784.1 .
    CH471115 Genomic DNA. Translation: EAX02862.1 .
    RefSeqi NP_000160.1. NM_000169.2.
    UniGenei Hs.69089.

    3D structure databases

    SMRi Q53Y83. Positions 32-426.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    Allergomei 9621. Hom s alpha-Galactosidase.
    CAZyi GH27. Glycoside Hydrolase Family 27.

    Protocols and materials databases

    DNASUi 2717.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2717.
    KEGGi hsa:2717.

    Organism-specific databases

    CTDi 2717.
    PharmGKBi PA28707.

    Phylogenomic databases

    HOVERGENi HBG001989.
    KOi K01189.
    OMAi NDLRDIC.
    PhylomeDBi Q53Y83.

    Miscellaneous databases

    GenomeRNAii 2717.
    NextBioi 10728.

    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. "The sequence of the human genome."
      Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.
      , Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.
      Science 291:1304-1351(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    2. "Cloning of human full-length CDSs in BD Creator(TM) System Donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
    3. Cited for: NUCLEOTIDE SEQUENCE.
    4. Cited for: NUCLEOTIDE SEQUENCE.

    Entry informationi

    Entry nameiQ53Y83_HUMAN
    AccessioniPrimary (citable) accession number: Q53Y83
    Entry historyi
    Integrated into UniProtKB/TrEMBL: May 24, 2005
    Last sequence update: May 24, 2005
    Last modified: October 1, 2014
    This is version 72 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)
    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.