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Q8BSY0

- ASPH_MOUSE

UniProt

Q8BSY0 - ASPH_MOUSE

Protein

Aspartyl/asparaginyl beta-hydroxylase

Gene

Asph

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins.

    Catalytic activityi

    Peptide L-aspartate + 2-oxoglutarate + O2 = peptide 3-hydroxy-L-aspartate + succinate + CO2.

    Cofactori

    Iron.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei608 – 60812-oxoglutarateBy similarity
    Binding sitei651 – 65112-oxoglutarateBy similarity
    Metal bindingi662 – 6621IronBy similarity
    Metal bindingi708 – 7081IronBy similarity
    Binding sitei718 – 71812-oxoglutarateBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. peptide-aspartate beta-dioxygenase activity Source: MGI
    3. protein binding Source: BHF-UCL

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity Source: Ensembl
    2. activation of store-operated calcium channel activity Source: Ensembl
    3. calcium ion transmembrane transport Source: Ensembl
    4. cellular response to calcium ion Source: Ensembl
    5. face morphogenesis Source: MGI
    6. limb morphogenesis Source: MGI
    7. negative regulation of cell proliferation Source: MGI
    8. palate development Source: MGI
    9. pattern specification process Source: MGI
    10. peptidyl-aspartic acid hydroxylation Source: MGI
    11. positive regulation of calcium ion transport into cytosol Source: Ensembl
    12. positive regulation of intracellular protein transport Source: Ensembl
    13. positive regulation of proteolysis Source: Ensembl
    14. positive regulation of transcription, DNA-templated Source: Ensembl
    15. regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Source: Ensembl
    16. regulation of protein depolymerization Source: BHF-UCL
    17. regulation of protein stability Source: BHF-UCL
    18. response to ATP Source: Ensembl

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Ligandi

    Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.16)
    Alternative name(s):
    Aspartate beta-hydroxylase
    Short name:
    ASP beta-hydroxylase
    Peptide-aspartate beta-dioxygenase
    Gene namesi
    Name:Asph
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1914186. Asph.

    Subcellular locationi

    GO - Cellular componenti

    1. cortical endoplasmic reticulum Source: Ensembl
    2. cytoplasm Source: BHF-UCL
    3. integral component of endoplasmic reticulum membrane Source: Ensembl
    4. integral component of membrane Source: MGI
    5. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 741741Aspartyl/asparaginyl beta-hydroxylasePRO_0000254161Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi453 – 4531N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi624 ↔ 631By similarity
    Glycosylationi689 – 6891N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Might be processed to the 56 kDa (AA 274-757) or 52 kDa (AA 315-757) forms in the lumen of the endoplasmic reticulum.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ8BSY0.
    PaxDbiQ8BSY0.
    PRIDEiQ8BSY0.

    PTM databases

    PhosphoSiteiQ8BSY0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8BSY0.
    BgeeiQ8BSY0.
    CleanExiMM_ASPH.
    GenevestigatoriQ8BSY0.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi211167. 2 interactions.
    IntActiQ8BSY0. 5 interactions.
    MINTiMINT-4112262.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BSY0.
    SMRiQ8BSY0. Positions 331-368, 440-528, 545-741.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 6262CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini84 – 741658LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei63 – 8321Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati324 – 35734TPR 1Add
    BLAST
    Repeati365 – 39834TPR 2Add
    BLAST
    Repeati437 – 47034TPR 3Add
    BLAST
    Repeati472 – 50433TPR 4Add
    BLAST
    Repeati508 – 54033TPR 5Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni671 – 67332-oxoglutarate bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi9 – 6153Gly-richAdd
    BLAST
    Compositional biasi14 – 3825Ser-richAdd
    BLAST
    Compositional biasi310 – 3156Poly-Lys

    Sequence similaritiesi

    Contains 5 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal-anchor, TPR repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG3555.
    GeneTreeiENSGT00530000063281.
    HOGENOMiHOG000231625.
    HOVERGENiHBG004290.
    InParanoidiQ8BSY0.
    KOiK00476.
    OMAiRNENACK.
    OrthoDBiEOG715Q44.
    PhylomeDBiQ8BSY0.
    TreeFamiTF312799.

    Family and domain databases

    Gene3Di1.25.40.10. 1 hit.
    2.60.120.330. 1 hit.
    InterProiIPR007943. Asp-B-hydro/Triadin_dom.
    IPR007803. Asp_Arg_Pro-Hydrxlase.
    IPR027443. IPNS-like.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR013105. TPR_2.
    IPR019734. TPR_repeat.
    [Graphical view]
    PfamiPF05279. Asp-B-Hydro_N. 1 hit.
    PF05118. Asp_Arg_Hydrox. 1 hit.
    PF07719. TPR_2. 1 hit.
    [Graphical view]
    PROSITEiPS50005. TPR. 2 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8BSY0-1 [UniParc]FASTAAdd to Basket

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    MAPRKNAKGG GGNSSSSGSG SGSGSGSPST GSSGSSSSPG ARREAKHGGH    50
    KNGRRGGISG GSFFTWFMVI ALLGVWTSVA VVWFDLVDYE EVLGKLGVYD 100
    ADGDGDFDVD DAKVLLGLKE RSPSERTFPP EEEAETHAEL EEQAPEGADI 150
    QNVEDEVKEQ IQSLLQESVH TDHDLEADGL AGEPQPEVED FLTVTDSDDR 200
    FEDLEPGTVH EEIEDTYHVE DTASQNHPND MEEMTNEQEN SDPSEAVTDA 250
    GVLLPHAEEV RHQDYDEPVY EPSEHEGVAI SDNTIDDSSI ISEEINVASV 300
    EEQQDTPPVK KKKPKLLNKF DKTIKAELDA AEKLRKRGKI EEAVNAFEEL 350
    VRKYPQSPRA RYGKAQCEDD LAEKQRSNEV LRRAIETYQE AADLPDAPTD 400
    LVKLSLKRRS ERQQFLGHMR GSLLTLQRLV QLFPSDTTLK NDLGVGYLLL 450
    GDNDSAKKVY EEVLNVTPND GFAKVHYGFI LKAQNKISES IPYLKEGIES 500
    GDPGTDDGRF YFHLGDAMQR VGNKEAYKWY ELGHKRGHFA SVWQRSLYNV 550
    NGLKAQPWWT PRETGYTELV KSLERNWKLI RDEGLMVMDK AKGLFLPEDE 600
    NLREKGDWSQ FTLWQQGRKN ENACKGAPKT CALLEKFSET TGCRRGQIKY 650
    SIMHPGTHVW PHTGPTNCRL RMHLGLVIPK EGCKIRCANE TRTWEEGKVL 700
    IFDDSFEHEV WQDASSFRLI FIVDVWHPEL TPQQRRSLPA I 741
    Length:741
    Mass (Da):83,042
    Last modified:March 1, 2003 - v1
    Checksum:i0660A6A5E34418C8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti131 – 1322Missing in AAG40808. (PubMed:10956665)Curated
    Sequence conflicti131 – 1322Missing in AAG40809. (PubMed:10956665)Curated
    Sequence conflicti279 – 2791A → E in AAG40808. (PubMed:10956665)Curated
    Sequence conflicti279 – 2791A → E in AAG40809. (PubMed:10956665)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF289486 mRNA. Translation: AAG40808.1.
    AF289487 mRNA. Translation: AAG40809.1.
    AK030293 mRNA. Translation: BAC26882.1.
    CCDSiCCDS38690.1.
    RefSeqiNP_001171321.1. NM_001177850.1.
    NP_001171323.1. NM_001177852.1.
    NP_001171324.1. NM_001177853.1.
    NP_001171325.1. NM_001177854.1.
    NP_001171326.1. NM_001177855.1.
    NP_001277296.1. NM_001290367.1.
    NP_075553.2. NM_023066.3.
    UniGeneiMm.222206.
    Mm.412008.

    Genome annotation databases

    EnsembliENSMUST00000078139; ENSMUSP00000077273; ENSMUSG00000028207.
    GeneIDi65973.
    KEGGimmu:65973.
    UCSCiuc008ryf.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF289486 mRNA. Translation: AAG40808.1 .
    AF289487 mRNA. Translation: AAG40809.1 .
    AK030293 mRNA. Translation: BAC26882.1 .
    CCDSi CCDS38690.1.
    RefSeqi NP_001171321.1. NM_001177850.1.
    NP_001171323.1. NM_001177852.1.
    NP_001171324.1. NM_001177853.1.
    NP_001171325.1. NM_001177854.1.
    NP_001171326.1. NM_001177855.1.
    NP_001277296.1. NM_001290367.1.
    NP_075553.2. NM_023066.3.
    UniGenei Mm.222206.
    Mm.412008.

    3D structure databases

    ProteinModelPortali Q8BSY0.
    SMRi Q8BSY0. Positions 331-368, 440-528, 545-741.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 211167. 2 interactions.
    IntActi Q8BSY0. 5 interactions.
    MINTi MINT-4112262.

    PTM databases

    PhosphoSitei Q8BSY0.

    Proteomic databases

    MaxQBi Q8BSY0.
    PaxDbi Q8BSY0.
    PRIDEi Q8BSY0.

    Protocols and materials databases

    DNASUi 65973.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000078139 ; ENSMUSP00000077273 ; ENSMUSG00000028207 .
    GeneIDi 65973.
    KEGGi mmu:65973.
    UCSCi uc008ryf.2. mouse.

    Organism-specific databases

    CTDi 444.
    MGIi MGI:1914186. Asph.

    Phylogenomic databases

    eggNOGi COG3555.
    GeneTreei ENSGT00530000063281.
    HOGENOMi HOG000231625.
    HOVERGENi HBG004290.
    InParanoidi Q8BSY0.
    KOi K00476.
    OMAi RNENACK.
    OrthoDBi EOG715Q44.
    PhylomeDBi Q8BSY0.
    TreeFami TF312799.

    Miscellaneous databases

    NextBioi 320434.
    PROi Q8BSY0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BSY0.
    Bgeei Q8BSY0.
    CleanExi MM_ASPH.
    Genevestigatori Q8BSY0.

    Family and domain databases

    Gene3Di 1.25.40.10. 1 hit.
    2.60.120.330. 1 hit.
    InterProi IPR007943. Asp-B-hydro/Triadin_dom.
    IPR007803. Asp_Arg_Pro-Hydrxlase.
    IPR027443. IPNS-like.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR013105. TPR_2.
    IPR019734. TPR_repeat.
    [Graphical view ]
    Pfami PF05279. Asp-B-Hydro_N. 1 hit.
    PF05118. Asp_Arg_Hydrox. 1 hit.
    PF07719. TPR_2. 1 hit.
    [Graphical view ]
    PROSITEi PS50005. TPR. 2 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Aspartyl beta -hydroxylase (Asph) and an evolutionarily conserved isoform of Asph missing the catalytic domain share exons with junctin."
      Dinchuk J.E., Henderson N.L., Burn T.C., Huber R., Ho S.P., Link J., O'Neil K.T., Focht R.J., Scully M.S., Hollis J.M., Hollis G.F., Friedman P.A.
      J. Biol. Chem. 275:39543-39554(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Liver.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.

    Entry informationi

    Entry nameiASPH_MOUSE
    AccessioniPrimary (citable) accession number: Q8BSY0
    Secondary accession number(s): Q9EPA6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2006
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 105 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3