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Q12797

- ASPH_HUMAN

UniProt

Q12797 - ASPH_HUMAN

Protein

Aspartyl/asparaginyl beta-hydroxylase

Gene

ASPH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 3 (17 Apr 2007)
      Previous versions | rss
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    Functioni

    Isoform 1: specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins.1 Publication
    Isoform 8: membrane-bound Ca2+-sensing protein, which is a structural component of the ER-plasma membrane junctions. Isoform 8 regulates the activity of Ca(+2) released-activated Ca(+2) (CRAC) channels in T-cells.1 Publication

    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 sitei625 – 62512-oxoglutarate
    Binding sitei668 – 66812-oxoglutarate
    Metal bindingi679 – 6791IronCurated
    Metal bindingi725 – 7251IronCurated
    Binding sitei735 – 73512-oxoglutarate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi90 – 10213CuratedAdd
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. electron carrier activity Source: UniProtKB
    3. ion channel binding Source: BHF-UCL
    4. peptide-aspartate beta-dioxygenase activity Source: ProtInc
    5. protein binding Source: UniProtKB
    6. structural constituent of muscle Source: ProtInc
    7. structural molecule activity Source: ProtInc

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity Source: BHF-UCL
    2. activation of store-operated calcium channel activity Source: UniProtKB
    3. calcium ion transmembrane transport Source: UniProtKB
    4. cellular response to calcium ion Source: UniProtKB
    5. detection of calcium ion Source: BHF-UCL
    6. face morphogenesis Source: Ensembl
    7. limb morphogenesis Source: Ensembl
    8. muscle contraction Source: ProtInc
    9. negative regulation of cell proliferation Source: Ensembl
    10. palate development Source: Ensembl
    11. pattern specification process Source: Ensembl
    12. peptidyl-aspartic acid hydroxylation Source: Ensembl
    13. positive regulation of calcium ion transport into cytosol Source: UniProtKB
    14. positive regulation of intracellular protein transport Source: UniProtKB
    15. positive regulation of proteolysis Source: BHF-UCL
    16. positive regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
    17. positive regulation of transcription, DNA-templated Source: UniProtKB
    18. regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
    19. regulation of cell communication by electrical coupling Source: BHF-UCL
    20. regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Source: UniProtKB
    21. regulation of protein depolymerization Source: Ensembl
    22. regulation of protein stability Source: Ensembl
    23. regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
    24. regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
    25. response to ATP Source: UniProtKB

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Ligandi

    Calcium, 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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:757. ASPH.

    Subcellular locationi

    GO - Cellular componenti

    1. calcium channel complex Source: BHF-UCL
    2. cortical endoplasmic reticulum Source: UniProtKB
    3. endoplasmic reticulum Source: HPA
    4. endoplasmic reticulum membrane Source: UniProtKB
    5. integral component of endoplasmic reticulum membrane Source: UniProtKB
    6. integral component of membrane Source: UniProtKB-KW
    7. junctional sarcoplasmic reticulum membrane Source: BHF-UCL
    8. plasma membrane Source: UniProtKB
    9. sarcoplasmic reticulum lumen Source: BHF-UCL
    10. sarcoplasmic reticulum membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi91 – 933DAD → AAA: Increase in cytoplasmic Ca(2+) via activation of endogenous CRAC channels. 1 Publication

    Organism-specific databases

    PharmGKBiPA25056.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 758758Aspartyl/asparaginyl beta-hydroxylasePRO_0000064706Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi452 – 4521N-linked (GlcNAc...)
    Disulfide bondi641 ↔ 6481 Publication
    Glycosylationi706 – 7061N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ12797.
    PaxDbiQ12797.
    PRIDEiQ12797.

    PTM databases

    PhosphoSiteiQ12797.

    Expressioni

    Tissue specificityi

    Isoform 1 is detected in all tissues tested. Isoform 8 is mainly expressed in pancreas, heart, brain, kidney and liver. Isoform 8 is expressed in kidney (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ12797.
    BgeeiQ12797.
    CleanExiHS_ASPH.
    GenevestigatoriQ12797.

    Organism-specific databases

    HPAiHPA055161.
    HPA057838.
    HPA059303.

    Interactioni

    Subunit structurei

    Monomer By similarity. Isoform 8 interacts with ORAI1 and STIM1.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi106936. 8 interactions.
    IntActiQ12797. 5 interactions.
    STRINGi9606.ENSP00000368767.

    Structurei

    Secondary structure

    1
    758
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi574 – 5763
    Helixi578 – 5814
    Helixi584 – 5929
    Helixi594 – 60411
    Turni607 – 6104
    Beta strandi620 – 6234
    Beta strandi625 – 6328
    Helixi638 – 6436
    Helixi645 – 6517
    Helixi655 – 6584
    Beta strandi664 – 6707
    Beta strandi674 – 6796
    Beta strandi686 – 6949
    Beta strandi697 – 7048
    Beta strandi707 – 7093
    Beta strandi716 – 7194
    Beta strandi725 – 7295
    Beta strandi731 – 7333
    Beta strandi735 – 7439
    Helixi749 – 7546

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3RCQX-ray2.05A562-758[»]
    ProteinModelPortaliQ12797.
    SMRiQ12797. Positions 348-386, 431-485, 562-758.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12797.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5353CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini75 – 758684LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei54 – 7421Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati341 – 37434TPR 1Add
    BLAST
    Repeati454 – 48734TPR 2Add
    BLAST
    Repeati489 – 52133TPR 3Add
    BLAST
    Repeati525 – 55733TPR 4Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni688 – 69032-oxoglutarate binding

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi9 – 2921Ser-richAdd
    BLAST
    Compositional biasi111 – 312202Glu-richAdd
    BLAST
    Compositional biasi323 – 33210Poly-Lys

    Sequence similaritiesi

    Contains 4 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

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

    Phylogenomic databases

    eggNOGiCOG3555.
    HOVERGENiHBG004290.
    InParanoidiQ12797.
    KOiK00476.
    OMAiRNENACK.
    OrthoDBiEOG715Q44.
    PhylomeDBiQ12797.
    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]

    Sequences (10)i

    Sequence statusi: Complete.

    This entry describes 10 isoformsi produced by alternative splicing. Align

    Note: Comment: 3 functionally distinct proteins are produced by alternative splicing: Aspartyl/asparaginyl beta-hydroxylase, Junctin and Junctate. Additional isoforms are produced by alternative splicing.1 Publication

    Isoform 1 (identifier: Q12797-1) [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

    MAQRKNAKSS GNSSSSGSGS GSTSAGSSSP GARRETKHGG HKNGRKGGLS    50
    GTSFFTWFMV IALLGVWTSV AVVWFDLVDY EEVLGKLGIY DADGDGDFDV 100
    DDAKVLLGLK ERSTSEPAVP PEEAEPHTEP EEQVPVEAEP QNIEDEAKEQ 150
    IQSLLHEMVH AEHVEGEDLQ QEDGPTGEPQ QEDDEFLMAT DVDDRFETLE 200
    PEVSHEETEH SYHVEETVSQ DCNQDMEEMM SEQENPDSSE PVVEDERLHH 250
    DTDDVTYQVY EEQAVYEPLE NEGIEITEVT APPEDNPVED SQVIVEEVSI 300
    FPVEEQQEVP PETNRKTDDP EQKAKVKKKK PKLLNKFDKT IKAELDAAEK 350
    LRKRGKIEEA VNAFKELVRK YPQSPRARYG KAQCEDDLAE KRRSNEVLRG 400
    AIETYQEVAS LPDVPADLLK LSLKRRSDRQ QFLGHMRGSL LTLQRLVQLF 450
    PNDTSLKNDL GVGYLLIGDN DNAKKVYEEV LSVTPNDGFA KVHYGFILKA 500
    QNKIAESIPY LKEGIESGDP GTDDGRFYFH LGDAMQRVGN KEAYKWYELG 550
    HKRGHFASVW QRSLYNVNGL KAQPWWTPKE TGYTELVKSL ERNWKLIRDE 600
    GLAVMDKAKG LFLPEDENLR EKGDWSQFTL WQQGRRNENA CKGAPKTCTL 650
    LEKFPETTGC RRGQIKYSIM HPGTHVWPHT GPTNCRLRMH LGLVIPKEGC 700
    KIRCANETKT WEEGKVLIFD DSFEHEVWQD ASSFRLIFIV DVWHPELTPQ 750
    QRRSLPAI 758
    Length:758
    Mass (Da):85,863
    Last modified:April 17, 2007 - v3
    Checksum:i4AE56D1D8DF0AF0C
    GO
    Isoform 2 (identifier: Q12797-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         312-313: ET → DT
         314-758: Missing.

    Show »
    Length:313
    Mass (Da):34,646
    Checksum:i7885A18B81CD6D0D
    GO
    Isoform 3 (identifier: Q12797-3) [UniParc]FASTAAdd to Basket

    Also known as: Junctin-1, Cardiac junctin

    The sequence of this isoform differs from the canonical sequence as follows:
         1-34: MAQRKNAKSSGNSSSSGSGSGSTSAGSSSPGARR → MAEDK
         84-84: L → LAKAKDFRYNLSEVLQ
         108-239: GLKERSTSEP...MSEQENPDSS → EGPSGVAKRK...TKGNTQKRNG
         240-758: Missing.

    Note: Glycosylated on Asn-64.

    Show »
    Length:225
    Mass (Da):25,560
    Checksum:i27D331DD6D88E0D3
    GO
    Isoform 4 (identifier: Q12797-4) [UniParc]FASTAAdd to Basket

    Also known as: Junctin-2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-34: MAQRKNAKSSGNSSSSGSGSGSTSAGSSSPGARR → MAEDK
         108-239: GLKERSTSEP...MSEQENPDSS → EGPSGVAKRK...TKGNTQKRNG
         240-758: Missing.

    Show »
    Length:210
    Mass (Da):23,796
    Checksum:i8E7C39D69F2B22C7
    GO
    Isoform 5 (identifier: Q12797-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-34: MAQRKNAKSSGNSSSSGSGSGSTSAGSSSPGARR → MAEDK
         84-84: L → LAKAKDFRYNLSEVLQ
         264-264: Missing.
         312-313: ET → DT
         314-758: Missing.

    Show »
    Length:298
    Mass (Da):33,744
    Checksum:iB28D921E5021348B
    GO
    Isoform 10 (identifier: Q12797-10) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-34: MAQRKNAKSSGNSSSSGSGSGSTSAGSSSPGARR → MAEDK

    Show »
    Length:729
    Mass (Da):83,268
    Checksum:iEA17281494828D62
    GO
    Isoform 6 (identifier: Q12797-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         164-206: Missing.
         312-313: ET → DT
         314-758: Missing.

    Show »
    Length:270
    Mass (Da):29,757
    Checksum:i8551773C7272202A
    GO
    Isoform 7 (identifier: Q12797-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         84-84: L → LAKAKDFRYNLSEVLQ
         110-188: KERSTSEPAV...PQQEDDEFLM → TKDGSNENID...TCVILDLHNQ
         189-758: Missing.

    Show »
    Length:203
    Mass (Da):21,963
    Checksum:i3EC728B1E417091C
    GO
    Isoform 8 (identifier: Q12797-8) [UniParc]FASTAAdd to Basket

    Also known as: Junctate

    The sequence of this isoform differs from the canonical sequence as follows:
         1-34: MAQRKNAKSSGNSSSSGSGSGSTSAGSSSPGARR → MAEDK
         84-84: L → LAKAKDFRYNLSEVLQ
         312-313: ET → DT
         314-758: Missing.

    Show »
    Length:299
    Mass (Da):33,815
    Checksum:i658F88C34EC2CA37
    GO
    Isoform 9 (identifier: Q12797-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-34: MAQRKNAKSSGNSSSSGSGSGSTSAGSSSPGARR → MAEDK
         84-84: L → LAKAKDFRYNLSEVLQ
         164-206: Missing.
         312-313: ET → DT
         314-758: Missing.

    Show »
    Length:256
    Mass (Da):28,926
    Checksum:i8C892EC3D1AE1BCC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti519 – 5191D → N in BAG65166. (PubMed:14702039)Curated
    Sequence conflicti565 – 5651Y → I in AAA82108. (PubMed:7821814)Curated
    Sequence conflicti575 – 5773WWT → CG in AAA82108. (PubMed:7821814)Curated
    Sequence conflicti585 – 5851E → Q in AAA82108. (PubMed:7821814)Curated
    Sequence conflicti599 – 5991D → Y in BAG65166. (PubMed:14702039)Curated
    Sequence conflicti709 – 7091K → R in AAB50779. (PubMed:8823296)Curated
    Sequence conflicti734 – 7341F → L in BAG65166. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti354 – 3541R → M.
    Corresponds to variant rs6995412 [ dbSNP | Ensembl ].
    VAR_053781

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3434MAQRK…PGARR → MAEDK in isoform 3, isoform 4, isoform 5, isoform 8, isoform 9 and isoform 10. 5 PublicationsVSP_039165Add
    BLAST
    Alternative sequencei84 – 841L → LAKAKDFRYNLSEVLQ in isoform 3, isoform 5, isoform 7, isoform 8 and isoform 9. 5 PublicationsVSP_039166
    Alternative sequencei108 – 239132GLKER…NPDSS → EGPSGVAKRKTKAKVKELTK EELKKEKEKPESRKESKNEE RKKGKKEDVRKDKKIADADL SRKESPKGKKDREKEKVDLE KSAKTKENRKKSTNMKDVSS KMASRDKDDRKESRSSTRYA HLTKGNTQKRNG in isoform 3 and isoform 4. 2 PublicationsVSP_039167Add
    BLAST
    Alternative sequencei110 – 18879KERST…DEFLM → TKDGSNENIDSLEEVLNILA EESSDWFYGFLSFLYDIMTP FEMLEEEEEESETADGVDGT SQNEGVQGKTCVILDLHNQ in isoform 7. 1 PublicationVSP_044235Add
    BLAST
    Alternative sequencei164 – 20643Missing in isoform 6 and isoform 9. 2 PublicationsVSP_044236Add
    BLAST
    Alternative sequencei189 – 758570Missing in isoform 7. 1 PublicationVSP_044237Add
    BLAST
    Alternative sequencei240 – 758519Missing in isoform 3 and isoform 4. 2 PublicationsVSP_039168Add
    BLAST
    Alternative sequencei264 – 2641Missing in isoform 5. 1 PublicationVSP_044238
    Alternative sequencei312 – 3132ET → DT in isoform 2, isoform 5, isoform 6, isoform 8 and isoform 9. 4 PublicationsVSP_039169
    Alternative sequencei314 – 758445Missing in isoform 2, isoform 5, isoform 6, isoform 8 and isoform 9. 4 PublicationsVSP_039170Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03109 mRNA. Translation: AAA82108.1.
    S83325 mRNA. Translation: AAB50779.1.
    AF224468 mRNA. Translation: AAF82246.1.
    AF224469 mRNA. Translation: AAF82247.1.
    AF289489 mRNA. Translation: AAG40811.1.
    AF306765 mRNA. Translation: AAG42257.1.
    AF184241 mRNA. Translation: AAG16983.1.
    AK295528 mRNA. Translation: BAG58441.1.
    AK304314 mRNA. Translation: BAG65166.1.
    AC067881 Genomic DNA. No translation available.
    AC090094 Genomic DNA. No translation available.
    CH471068 Genomic DNA. Translation: EAW86841.1.
    CH471068 Genomic DNA. Translation: EAW86840.1.
    CH471068 Genomic DNA. Translation: EAW86847.1.
    CH471068 Genomic DNA. Translation: EAW86848.1.
    CH471068 Genomic DNA. Translation: EAW86849.1.
    BC025236 mRNA. Translation: AAH25236.1.
    BC066929 mRNA. Translation: AAH66929.1.
    BC142967 mRNA. Translation: AAI42968.1.
    BC144362 mRNA. Translation: AAI44363.1.
    CCDSiCCDS34898.1. [Q12797-1]
    CCDS34899.1. [Q12797-4]
    CCDS34900.1. [Q12797-3]
    CCDS43742.1. [Q12797-2]
    CCDS47866.1. [Q12797-8]
    CCDS55234.1. [Q12797-10]
    CCDS55235.1. [Q12797-9]
    CCDS55236.1. [Q12797-5]
    CCDS55237.1. [Q12797-6]
    CCDS55238.1. [Q12797-7]
    PIRiI38423.
    RefSeqiNP_001158222.1. NM_001164750.1. [Q12797-10]
    NP_001158223.1. NM_001164751.1. [Q12797-5]
    NP_001158225.1. NM_001164753.1. [Q12797-9]
    NP_001158227.1. NM_001164755.1. [Q12797-6]
    NP_001158228.1. NM_001164756.1. [Q12797-7]
    NP_004309.2. NM_004318.3. [Q12797-1]
    NP_064549.1. NM_020164.4. [Q12797-3]
    NP_115855.1. NM_032466.3. [Q12797-2]
    NP_115856.1. NM_032467.3. [Q12797-4]
    NP_115857.1. NM_032468.4. [Q12797-8]
    UniGeneiHs.332422.

    Genome annotation databases

    EnsembliENST00000356457; ENSP00000348841; ENSG00000198363. [Q12797-2]
    ENST00000379449; ENSP00000368762; ENSG00000198363. [Q12797-7]
    ENST00000379454; ENSP00000368767; ENSG00000198363. [Q12797-1]
    ENST00000389204; ENSP00000373856; ENSG00000198363. [Q12797-3]
    ENST00000445642; ENSP00000394013; ENSG00000198363. [Q12797-8]
    ENST00000517847; ENSP00000429954; ENSG00000198363. [Q12797-8]
    ENST00000517903; ENSP00000430245; ENSG00000198363. [Q12797-5]
    ENST00000518068; ENSP00000429286; ENSG00000198363. [Q12797-6]
    ENST00000522603; ENSP00000436188; ENSG00000198363. [Q12797-4]
    ENST00000522835; ENSP00000429160; ENSG00000198363. [Q12797-9]
    ENST00000541428; ENSP00000437864; ENSG00000198363. [Q12797-10]
    GeneIDi444.
    KEGGihsa:444.
    UCSCiuc003xuj.3. human. [Q12797-1]
    uc003xul.3. human. [Q12797-8]
    uc003xum.3. human. [Q12797-2]
    uc003xun.3. human. [Q12797-6]
    uc003xur.3. human. [Q12797-7]
    uc011lei.2. human. [Q12797-5]
    uc011lej.2. human. [Q12797-9]
    uc011lel.2. human. [Q12797-3]
    uc011lem.2. human. [Q12797-4]

    Polymorphism databases

    DMDMi145559444.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03109 mRNA. Translation: AAA82108.1 .
    S83325 mRNA. Translation: AAB50779.1 .
    AF224468 mRNA. Translation: AAF82246.1 .
    AF224469 mRNA. Translation: AAF82247.1 .
    AF289489 mRNA. Translation: AAG40811.1 .
    AF306765 mRNA. Translation: AAG42257.1 .
    AF184241 mRNA. Translation: AAG16983.1 .
    AK295528 mRNA. Translation: BAG58441.1 .
    AK304314 mRNA. Translation: BAG65166.1 .
    AC067881 Genomic DNA. No translation available.
    AC090094 Genomic DNA. No translation available.
    CH471068 Genomic DNA. Translation: EAW86841.1 .
    CH471068 Genomic DNA. Translation: EAW86840.1 .
    CH471068 Genomic DNA. Translation: EAW86847.1 .
    CH471068 Genomic DNA. Translation: EAW86848.1 .
    CH471068 Genomic DNA. Translation: EAW86849.1 .
    BC025236 mRNA. Translation: AAH25236.1 .
    BC066929 mRNA. Translation: AAH66929.1 .
    BC142967 mRNA. Translation: AAI42968.1 .
    BC144362 mRNA. Translation: AAI44363.1 .
    CCDSi CCDS34898.1. [Q12797-1 ]
    CCDS34899.1. [Q12797-4 ]
    CCDS34900.1. [Q12797-3 ]
    CCDS43742.1. [Q12797-2 ]
    CCDS47866.1. [Q12797-8 ]
    CCDS55234.1. [Q12797-10 ]
    CCDS55235.1. [Q12797-9 ]
    CCDS55236.1. [Q12797-5 ]
    CCDS55237.1. [Q12797-6 ]
    CCDS55238.1. [Q12797-7 ]
    PIRi I38423.
    RefSeqi NP_001158222.1. NM_001164750.1. [Q12797-10 ]
    NP_001158223.1. NM_001164751.1. [Q12797-5 ]
    NP_001158225.1. NM_001164753.1. [Q12797-9 ]
    NP_001158227.1. NM_001164755.1. [Q12797-6 ]
    NP_001158228.1. NM_001164756.1. [Q12797-7 ]
    NP_004309.2. NM_004318.3. [Q12797-1 ]
    NP_064549.1. NM_020164.4. [Q12797-3 ]
    NP_115855.1. NM_032466.3. [Q12797-2 ]
    NP_115856.1. NM_032467.3. [Q12797-4 ]
    NP_115857.1. NM_032468.4. [Q12797-8 ]
    UniGenei Hs.332422.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3RCQ X-ray 2.05 A 562-758 [» ]
    ProteinModelPortali Q12797.
    SMRi Q12797. Positions 348-386, 431-485, 562-758.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106936. 8 interactions.
    IntActi Q12797. 5 interactions.
    STRINGi 9606.ENSP00000368767.

    Chemistry

    DrugBanki DB00128. L-Aspartic Acid.
    DB00139. Succinic acid.

    PTM databases

    PhosphoSitei Q12797.

    Polymorphism databases

    DMDMi 145559444.

    Proteomic databases

    MaxQBi Q12797.
    PaxDbi Q12797.
    PRIDEi Q12797.

    Protocols and materials databases

    DNASUi 444.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356457 ; ENSP00000348841 ; ENSG00000198363 . [Q12797-2 ]
    ENST00000379449 ; ENSP00000368762 ; ENSG00000198363 . [Q12797-7 ]
    ENST00000379454 ; ENSP00000368767 ; ENSG00000198363 . [Q12797-1 ]
    ENST00000389204 ; ENSP00000373856 ; ENSG00000198363 . [Q12797-3 ]
    ENST00000445642 ; ENSP00000394013 ; ENSG00000198363 . [Q12797-8 ]
    ENST00000517847 ; ENSP00000429954 ; ENSG00000198363 . [Q12797-8 ]
    ENST00000517903 ; ENSP00000430245 ; ENSG00000198363 . [Q12797-5 ]
    ENST00000518068 ; ENSP00000429286 ; ENSG00000198363 . [Q12797-6 ]
    ENST00000522603 ; ENSP00000436188 ; ENSG00000198363 . [Q12797-4 ]
    ENST00000522835 ; ENSP00000429160 ; ENSG00000198363 . [Q12797-9 ]
    ENST00000541428 ; ENSP00000437864 ; ENSG00000198363 . [Q12797-10 ]
    GeneIDi 444.
    KEGGi hsa:444.
    UCSCi uc003xuj.3. human. [Q12797-1 ]
    uc003xul.3. human. [Q12797-8 ]
    uc003xum.3. human. [Q12797-2 ]
    uc003xun.3. human. [Q12797-6 ]
    uc003xur.3. human. [Q12797-7 ]
    uc011lei.2. human. [Q12797-5 ]
    uc011lej.2. human. [Q12797-9 ]
    uc011lel.2. human. [Q12797-3 ]
    uc011lem.2. human. [Q12797-4 ]

    Organism-specific databases

    CTDi 444.
    GeneCardsi GC08M062465.
    HGNCi HGNC:757. ASPH.
    HPAi HPA055161.
    HPA057838.
    HPA059303.
    MIMi 600582. gene.
    neXtProti NX_Q12797.
    PharmGKBi PA25056.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3555.
    HOVERGENi HBG004290.
    InParanoidi Q12797.
    KOi K00476.
    OMAi RNENACK.
    OrthoDBi EOG715Q44.
    PhylomeDBi Q12797.
    TreeFami TF312799.

    Miscellaneous databases

    ChiTaRSi ASPH. human.
    EvolutionaryTracei Q12797.
    GeneWikii ASPH.
    GenomeRNAii 444.
    NextBioi 1859.
    PROi Q12797.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q12797.
    Bgeei Q12797.
    CleanExi HS_ASPH.
    Genevestigatori Q12797.

    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. "Cloning and characterization of the human gene encoding aspartyl beta-hydroxylase."
      Korioth F., Gieffers C., Frey J.
      Gene 150:395-399(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Overexpression of human aspartyl(asparaginyl)beta-hydroxylase in hepatocellular carcinoma and cholangiocarcinoma."
      Lavaissiere L., Jia S., Nishiyama M., de la Monte S., Stern A.M., Wands J.R., Friedman P.A.
      J. Clin. Invest. 98:1313-1323(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "cDNA cloning and characterization of human cardiac junctin."
      Lim K.Y., Hong C.-S., Kim D.H.
      Gene 255:35-42(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
      Tissue: Heart.
    4. "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] (ISOFORM 2).
      Tissue: Liver.
    5. "Molecular cloning, expression, functional characterization, chromosomal localization, and gene structure of junctate, a novel integral calcium binding protein of sarco(endo)plasmic reticulum membrane."
      Treves S., Feriotto G., Moccagatta L., Gambari R., Zorzato F.
      J. Biol. Chem. 275:39555-39568(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), CALCIUM-BINDING, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Tissue: Muscle.
    6. "Molecular cloning of junctin from human and developing rabbit heart."
      Wetzel G.T., Ding S., Chen F.
      Mol. Genet. Metab. 69:252-258(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Heart.
    7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 9 AND 10).
      Tissue: Hippocampus and Trachea.
    8. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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] (ISOFORMS 5; 6 AND 7).
      Tissue: Brain and Pancreatic carcinoma.
    11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Junctate is a Ca2+-sensing structural component of Orai1 and stromal interaction molecule 1 (STIM1)."
      Srikanth S., Jew M., Kim K.D., Yee M.K., Abramson J., Gwack Y.
      Proc. Natl. Acad. Sci. U.S.A. 109:8682-8687(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CALCIUM-BINDING DOMAIN, INTERACTION WITH ORAI1 AND STIM1 (ISOFORM 8), MUTAGENESIS OF 91-ASP--ASP-93.
    14. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-452 (ISOFORM 1), GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64 (ISOFORM 3).
      Tissue: Liver.
    15. "Crystal structure of human aspartate beta-hydroxylase isoform A."
      Structural genomics consortium (SGC)
      Submitted (MAY-2011) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 562-758 IN COMPLEX WITH N-OXALYOLGLYCINE AND ZINC IONS, DISULFIDE BOND.

    Entry informationi

    Entry nameiASPH_HUMAN
    AccessioniPrimary (citable) accession number: Q12797
    Secondary accession number(s): A6NDF4
    , A6NHI2, B4DIC9, B4E2K4, B7ZM95, E5RGP5, F5H667, Q6NXR7, Q8TB28, Q9H291, Q9H2C4, Q9NRI0, Q9NRI1, Q9Y4J0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: April 17, 2007
    Last modified: October 1, 2014
    This is version 143 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3