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Protein

O-acetyl-ADP-ribose deacetylase 1

Gene

OARD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins. Catalyzes the deacylation of O-acetyl-ADP-ribose, O-propionyl-ADP-ribose and O-butyryl-ADP-ribose, yielding ADP-ribose plus acetate, propionate and butyrate, respectively.

Enzyme regulationi

Subject to competitive inhibition by the product ADP-ribose.1 Publication

Kineticsi

  1. KM=182 µM for O-acetyl-ADP-ribose1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei21Substrate; via amide nitrogen1
    Active sitei125Proton acceptor1 Publication1
    Binding sitei152Substrate; via carboxylate1

    GO - Molecular functioni

    • deacetylase activity Source: UniProtKB
    • purine nucleoside binding Source: UniProtKB

    GO - Biological processi

    • purine nucleoside metabolic process Source: UniProtKB

    Keywordsi

    Molecular functionHydrolase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    O-acetyl-ADP-ribose deacetylase 1 (EC:3.5.1.-)
    Gene namesi
    Name:OARD1
    Synonyms:C6orf130
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 6

    Organism-specific databases

    EuPathDBiHostDB:ENSG00000124596.16
    HGNCiHGNC:21257 OARD1
    MIMi614393 gene
    neXtProtiNX_Q9Y530

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi32H → A: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi33C → S: No effect. 1 Publication1
    Mutagenesisi35S → A: Reduced catalytic activity. No effect on affinity towards substrate. 1 Publication1
    Mutagenesisi83T → A: Reduced catalytic activity. No effect on affinity towards substrate. 1
    Mutagenesisi123G → E: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi125D → A: Abolishes enzyme activity. 1 Publication1

    Organism-specific databases

    DisGeNETi221443
    OpenTargetsiENSG00000124596
    PharmGKBiPA134879529

    Polymorphism and mutation databases

    BioMutaiOARD1
    DMDMi38258957

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources
    ChainiPRO_00000895292 – 152O-acetyl-ADP-ribose deacetylase 1Add BLAST151

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylalanineCombined sources1
    Modified residuei4PhosphoserineCombined sources1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    EPDiQ9Y530
    MaxQBiQ9Y530
    PaxDbiQ9Y530
    PeptideAtlasiQ9Y530
    PRIDEiQ9Y530
    ProteomicsDBi86280

    PTM databases

    iPTMnetiQ9Y530
    PhosphoSitePlusiQ9Y530

    Expressioni

    Gene expression databases

    BgeeiENSG00000124596
    CleanExiHS_C6orf130
    ExpressionAtlasiQ9Y530 baseline and differential
    GenevisibleiQ9Y530 HS

    Organism-specific databases

    HPAiHPA029036

    Interactioni

    Binary interactionsi

    Show more details

    Protein-protein interaction databases

    BioGridi128727, 10 interactors
    IntActiQ9Y530, 4 interactors
    MINTiQ9Y530
    STRINGi9606.ENSP00000416829

    Structurei

    Secondary structure

    1152
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi14 – 19Combined sources6
    Helixi21 – 23Combined sources3
    Beta strandi28 – 35Combined sources8
    Beta strandi41 – 43Combined sources3
    Helixi45 – 52Combined sources8
    Helixi55 – 61Combined sources7
    Beta strandi67 – 73Combined sources7
    Beta strandi76 – 86Combined sources11
    Helixi93 – 110Combined sources18
    Beta strandi114 – 117Combined sources4
    Helixi123 – 125Combined sources3
    Helixi129 – 140Combined sources12
    Beta strandi146 – 151Combined sources6

    3D structure databases

    ProteinModelPortaliQ9Y530
    SMRiQ9Y530
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y530

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini2 – 152MacroPROSITE-ProRule annotationAdd BLAST151

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni119 – 125Substrate binding7

    Phylogenomic databases

    eggNOGiENOG410IFQM Eukaryota
    ENOG4111MFZ LUCA
    GeneTreeiENSGT00390000006988
    HOGENOMiHOG000012894
    HOVERGENiHBG050914
    InParanoidiQ9Y530
    OMAiAMKTHCL
    OrthoDBiEOG091G0MUU
    PhylomeDBiQ9Y530
    TreeFamiTF324128

    Family and domain databases

    InterProiView protein in InterPro
    IPR002589 Macro_dom
    PfamiView protein in Pfam
    PF01661 Macro, 1 hit
    SMARTiView protein in SMART
    SM00506 A1pp, 1 hit
    PROSITEiView protein in PROSITE
    PS51154 MACRO, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9Y530-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MASSLNEDPE GSRITYVKGD LFACPKTDSL AHCISEDCRM GAGIAVLFKK
    60 70 80 90 100
    KFGGVQELLN QQKKSGEVAV LKRDGRYIYY LITKKRASHK PTYENLQKSL
    110 120 130 140 150
    EAMKSHCLKN GVTDLSMPRI GCGLDRLQWE NVSAMIEEVF EATDIKITVY

    TL
    Length:152
    Mass (Da):17,025
    Last modified:November 7, 2003 - v2
    Checksum:i8CC43CBDABA73E0B
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK290939 mRNA Translation: BAF83628.1
    AK313361 mRNA Translation: BAG36161.1
    AL031778 Genomic DNA No translation available.
    CH471081 Genomic DNA Translation: EAX04011.1
    BC011709 mRNA Translation: AAH11709.1
    CCDSiCCDS34445.1
    RefSeqiNP_001316613.1, NM_001329684.1
    NP_001316614.1, NM_001329685.1
    NP_001316615.1, NM_001329686.1
    NP_001316617.1, NM_001329688.1
    NP_659500.1, NM_145063.3
    UniGeneiHs.227457

    Genome annotation databases

    EnsembliENST00000424266; ENSP00000416829; ENSG00000124596
    ENST00000463088; ENSP00000420193; ENSG00000124596
    ENST00000468811; ENSP00000420601; ENSG00000124596
    ENST00000479950; ENSP00000420484; ENSG00000124596
    GeneIDi221443
    KEGGihsa:221443
    UCSCiuc003opm.4 human

    Similar proteinsi

    Entry informationi

    Entry nameiOARD1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y530
    Secondary accession number(s): A6NEK4, A8K4H4, Q96F23
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 7, 2003
    Last modified: July 18, 2018
    This is version 134 of the entry and version 2 of the sequence. See 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 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

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