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Q6FH48

- Q6FH48_HUMAN

UniProt

Q6FH48 - Q6FH48_HUMAN

Protein
Submitted name:

ASPA protein

Gene

ASPA

Organism
Homo sapiens (Human)
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (10 May 2005)
      Previous versions | rss
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    Functioni

    Cofactori

    Binds 1 zinc ion per subunit.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi21 – 211ZincUniRule annotation
    Metal bindingi24 – 241ZincUniRule annotation
    Binding sitei63 – 631Substrate
    Metal bindingi116 – 1161ZincUniRule annotation
    Active sitei178 – 1781UniRule annotation
    Binding sitei178 – 1781Substrate
    Binding sitei288 – 2881Substrate

    GO - Molecular functioni

    1. hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides Source: InterPro
    2. hydrolase activity, acting on ester bonds Source: InterPro
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. central nervous system myelination Source: Ensembl
    2. positive regulation of oligodendrocyte differentiation Source: Ensembl

    Keywords - Ligandi

    Metal-bindingUniRule annotation, ZincUniRule annotation

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    ASPA proteinImported
    Submitted name:
    Aspartoacylase (Canavan disease), isoform CRA_aImported
    Submitted name:
    cDNA, FLJ93347, Homo sapiens aspartoacylase (aminoacylase 2, Canavan disease)(ASPA), mRNAImported
    Gene namesi
    Name:ASPAImported
    ORF Names:hCG_32633Imported
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleus Source: Ensembl

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25055.

    Structurei

    3D structure databases

    SMRiQ6FH48. Positions 9-310.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni70 – 712Substrate bindingUniRule annotation
    Regioni164 – 1685Substrate binding

    Phylogenomic databases

    HOVERGENiHBG004172.
    KOiK01437.
    OMAiTTRSVAK.
    PhylomeDBiQ6FH48.

    Family and domain databases

    HAMAPiMF_00704. Aspartoacylase.
    InterProiIPR016708. Aspartoacylase.
    IPR007036. Aste_AspA.
    [Graphical view]
    PfamiPF04952. AstE_AspA. 1 hit.
    [Graphical view]
    PIRSFiPIRSF018001. Aspartoacylase. 1 hit.

    Sequencei

    Sequence statusi: Fragment.

    Q6FH48-1 [UniParc]FASTAAdd to Basket

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    MTSCHIAEEH IQKVAIFGGT HGNELTGVFL VKHWLENGAE IQRTGLEVKP    50
    FITNPRAVKK CTRYIDCDLN RIFDLENLGK KMSEDLPYEV RRAQEINHLF 100
    GPKDSEDSYD IIFDLHNTTS NMGCTLILED SRNNFLIQMF HYIKTSLAPL 150
    PCYVYLIEHP SLKYATTRSI AKYPVGIEVG PQPQGVLRAD ILDQMRKMIK 200
    HALDFIHHFN EGKEFPPCAI EVYKIIEKVD YPRDENGEIA AIIHPNLQDQ 250
    DWKPLHPGDP MFLTLDGKTI PLGGDCTVYP VFVNEAAYYE KKEAFAKTTK 300
    LTLNAKSIRC CLH 313
    Length:313
    Mass (Da):35,735
    Last modified:May 10, 2005 - v1
    Checksum:i33C0B9B07839E7F5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei313 – 3131Imported

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK312901 mRNA. Translation: BAG35747.1.
    CR541908 mRNA. Translation: CAG46706.1.
    CH471108 Genomic DNA. Translation: EAW90506.1.
    RefSeqiNP_000040.1. NM_000049.2.
    NP_001121557.1. NM_001128085.1.
    XP_006721590.1. XM_006721527.1.
    UniGeneiHs.171142.

    Genome annotation databases

    GeneIDi443.
    KEGGihsa:443.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK312901 mRNA. Translation: BAG35747.1 .
    CR541908 mRNA. Translation: CAG46706.1 .
    CH471108 Genomic DNA. Translation: EAW90506.1 .
    RefSeqi NP_000040.1. NM_000049.2.
    NP_001121557.1. NM_001128085.1.
    XP_006721590.1. XM_006721527.1.
    UniGenei Hs.171142.

    3D structure databases

    SMRi Q6FH48. Positions 9-310.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    DNASUi 443.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 443.
    KEGGi hsa:443.

    Organism-specific databases

    CTDi 443.
    PharmGKBi PA25055.

    Phylogenomic databases

    HOVERGENi HBG004172.
    KOi K01437.
    OMAi TTRSVAK.
    PhylomeDBi Q6FH48.

    Miscellaneous databases

    GenomeRNAii 443.
    NextBioi 1855.

    Family and domain databases

    HAMAPi MF_00704. Aspartoacylase.
    InterProi IPR016708. Aspartoacylase.
    IPR007036. Aste_AspA.
    [Graphical view ]
    Pfami PF04952. AstE_AspA. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF018001. Aspartoacylase. 1 hit.
    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 open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
    3. Cited for: NUCLEOTIDE SEQUENCE.
    4. "NEDO functional analysis of protein and research application project."
      Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y., Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R., Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N., Isogai T.
      Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Tissue: BrainImported.

    Entry informationi

    Entry nameiQ6FH48_HUMAN
    AccessioniPrimary (citable) accession number: Q6FH48
    Entry historyi
    Integrated into UniProtKB/TrEMBL: May 10, 2005
    Last sequence update: May 10, 2005
    Last modified: October 1, 2014
    This is version 69 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.