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Q28056

- ASPH_BOVIN

UniProt

Q28056 - ASPH_BOVIN

Protein

Aspartyl/asparaginyl beta-hydroxylase

Gene

ASPH

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      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.1 Publication

    Catalytic activityi

    Peptide L-aspartate + 2-oxoglutarate + O2 = peptide 3-hydroxy-L-aspartate + succinate + CO2.1 Publication

    Cofactori

    Iron.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei621 – 62112-oxoglutarateBy similarity
    Binding sitei664 – 66412-oxoglutarateBy similarity
    Metal bindingi675 – 6751IronBy similarity
    Metal bindingi721 – 7211IronBy similarity
    Binding sitei731 – 73112-oxoglutarateBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. peptide-aspartate beta-dioxygenase activity Source: UniProtKB

    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: Ensembl
    6. limb morphogenesis Source: Ensembl
    7. negative regulation of cell proliferation Source: Ensembl
    8. palate development Source: Ensembl
    9. pattern specification process Source: Ensembl
    10. peptidyl-aspartic acid hydroxylation Source: UniProtKB
    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: Ensembl
    17. regulation of protein stability Source: Ensembl
    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
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 14

    Subcellular locationi

    GO - Cellular componenti

    1. cortical endoplasmic reticulum Source: Ensembl
    2. integral component of endoplasmic reticulum membrane Source: Ensembl
    3. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 754754Aspartyl/asparaginyl beta-hydroxylasePRO_0000064705Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi96 – 961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi466 – 4661N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi637 ↔ 644By similarity
    Glycosylationi702 – 7021N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Might be processed to the 56 kDa (AA 289-754) or 52 kDa (AA 311-754) forms in the lumen of the endoplasmic reticulum.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ28056.
    PRIDEiQ28056.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000021267.

    Structurei

    3D structure databases

    ProteinModelPortaliQ28056.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5656CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini78 – 754677LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei57 – 7721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati337 – 37034TPR 1Add
    BLAST
    Repeati378 – 41134TPR 2Add
    BLAST
    Repeati450 – 48334TPR 3Add
    BLAST
    Repeati485 – 51733TPR 4Add
    BLAST
    Repeati521 – 55333TPR 5Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni684 – 68632-oxoglutarate bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi9 – 124Poly-Gly
    Compositional biasi14 – 218Poly-Ser
    Compositional biasi311 – 35242Lys-richAdd
    BLAST

    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.
    InParanoidiQ28056.
    KOiK00476.
    OMAiRNENACK.
    OrthoDBiEOG715Q44.
    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.
    IPR019734. TPR_repeat.
    [Graphical view]
    PfamiPF05279. Asp-B-Hydro_N. 1 hit.
    PF05118. Asp_Arg_Hydrox. 1 hit.
    [Graphical view]
    PROSITEiPS50005. TPR. 2 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q28056-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPRKNAKGG GGNSSSSSSG SPTGCTSGGS SSPGARRETK QGGLKNGRKG    50
    GLSGSSFFTW FMVIALLGVW TSVAVVWFDL VDYEEVLAKA KDFRYNLSEV 100
    LQGKLGIYDA DGDGDFDVDD AKVLLGLKEK PAPKPTVPPE EADMYPWLED 150
    QVLESPGRQN IEDEVYEQVQ SLDETVYSEP GENLPQEPEG PAEELQPDDH 200
    VFVGSDADDR YEPMGTGAVH EETEDSYHIE ETASPAYSQD MEDMMYEQEN 250
    PDSSEPVVVD DAERTYQETD DVTYRDYDEQ DHAVDNSNTI LEEPHMPPAE 300
    EQQEVPPETN KKADEPGKKG KVKKKKPKLL NKFDKTIKAE LDAAEKLRKR 350
    GKIEEAVNAF EELVRKYPQS PGARYGKAQC EDDLAEKRRS NEILRRAIET 400
    YQEAASLPDA PTDLVKLSLK RRSDRQQFLG HMRGSLLTLQ KLVQLFPDDT 450
    ALKNDLGVGY LLIGDNDSAK KVYEEVLSVT PNDGFAKVHY GFILKAQNKI 500
    AESIPYLKEG IESGDPGTDD GRFYFHLGDA MQRVGNKEAY RWYELGHQRG 550
    HFASVWQRSL YNVQGLKAQP WWTPKETGYT ELVKSLERNW KLIRDEGLAA 600
    MDRTHGLFLP EDENLREKGD WSQFTLWQQG RKNENACKGA PKTCSLLDKF 650
    PETTGCRRGQ IKYSIMHPGT HVWPHTGPTN CRLRMHLGLV IPKEGCKIRC 700
    ANETRTWEEG KVLIFDDSFE HEVWQDAASF RLIFIVDVWH PELTPHQRRS 750
    LPAI 754
    Length:754
    Mass (Da):84,999
    Last modified:November 1, 1997 - v1
    Checksum:i369593A1F0B558C8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M91213 mRNA. Translation: AAA03563.1.
    PIRiA42969. BABOH.
    RefSeqiNP_777182.1. NM_174757.2.
    UniGeneiBt.46037.

    Genome annotation databases

    EnsembliENSBTAT00000021267; ENSBTAP00000021267; ENSBTAG00000026283.
    GeneIDi286771.
    KEGGibta:286771.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M91213 mRNA. Translation: AAA03563.1 .
    PIRi A42969. BABOH.
    RefSeqi NP_777182.1. NM_174757.2.
    UniGenei Bt.46037.

    3D structure databases

    ProteinModelPortali Q28056.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000021267.

    Proteomic databases

    PaxDbi Q28056.
    PRIDEi Q28056.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000021267 ; ENSBTAP00000021267 ; ENSBTAG00000026283 .
    GeneIDi 286771.
    KEGGi bta:286771.

    Organism-specific databases

    CTDi 444.

    Phylogenomic databases

    eggNOGi COG3555.
    GeneTreei ENSGT00530000063281.
    HOGENOMi HOG000231625.
    HOVERGENi HBG004290.
    InParanoidi Q28056.
    KOi K00476.
    OMAi RNENACK.
    OrthoDBi EOG715Q44.
    TreeFami TF312799.

    Miscellaneous databases

    NextBioi 20806432.

    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.
    IPR019734. TPR_repeat.
    [Graphical view ]
    Pfami PF05279. Asp-B-Hydro_N. 1 hit.
    PF05118. Asp_Arg_Hydrox. 1 hit.
    [Graphical view ]
    PROSITEi PS50005. TPR. 2 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning and expression of bovine aspartyl (asparaginyl) beta-hydroxylase."
      Jia S., Vandusen W.J., Diehl R.E., Kohl N.E., Dixon R.A.F., Elliston K.O., Stern A.M., Friedman P.A.
      J. Biol. Chem. 267:14322-14327(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain and Liver.
    2. "Bovine liver aspartyl beta-hydroxylase. Purification and characterization."
      Wang Q., Vandusen W.J., Petroski C.J., Garsky V.M., Stern A.M., Friedman P.A.
      J. Biol. Chem. 266:14004-14010(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 289-385 AND 615-641, CATALYTIC ACTIVITY, FUNCTION, COFACTOR.
      Tissue: Liver.

    Entry informationi

    Entry nameiASPH_BOVIN
    AccessioniPrimary (citable) accession number: Q28056
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    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, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3