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Q9Y530

- OARD1_HUMAN

UniProt

Q9Y530 - OARD1_HUMAN

Protein

O-acetyl-ADP-ribose deacetylase 1

Gene

OARD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei21 – 211Substrate; via amide nitrogen
    Active sitei125 – 1251Proton acceptor1 Publication
    Binding sitei152 – 1521Substrate; via carbonyl oxygen

    GO - Molecular functioni

    1. deacetylase activity Source: UniProtKB
    2. protein binding Source: IntAct
    3. purine nucleoside binding Source: UniProtKB

    GO - Biological processi

    1. purine nucleoside metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    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
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:21257. OARD1.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi32 – 321H → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi33 – 331C → S: No effect. 1 Publication
    Mutagenesisi35 – 351S → A: Reduced catalytic activity. No effect on affinity towards substrate. 1 Publication
    Mutagenesisi83 – 831T → A: Reduced catalytic activity. No effect on affinity towards substrate.
    Mutagenesisi123 – 1231G → E: Abolishes enzyme activity. 1 Publication
    Mutagenesisi125 – 1251D → A: Abolishes enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA134879529.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 152151O-acetyl-ADP-ribose deacetylase 1PRO_0000089529Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei4 – 41Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y530.
    PaxDbiQ9Y530.
    PRIDEiQ9Y530.

    PTM databases

    PhosphoSiteiQ9Y530.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y530.
    BgeeiQ9Y530.
    CleanExiHS_C6orf130.
    GenevestigatoriQ9Y530.

    Organism-specific databases

    HPAiHPA029036.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PARP1P098745EBI-8502288,EBI-355676
    PARP10Q53GL73EBI-8502288,EBI-2857573

    Protein-protein interaction databases

    BioGridi128727. 5 interactions.
    IntActiQ9Y530. 2 interactions.
    STRINGi9606.ENSP00000416829.

    Structurei

    Secondary structure

    1
    152
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 196
    Helixi21 – 233
    Beta strandi28 – 358
    Beta strandi41 – 433
    Helixi45 – 528
    Helixi55 – 617
    Beta strandi67 – 737
    Beta strandi76 – 8611
    Helixi93 – 11018
    Beta strandi114 – 1174
    Helixi123 – 1253
    Helixi129 – 14012
    Beta strandi146 – 1516

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EEENMR-A11-152[»]
    2L8RNMR-A3-152[»]
    2LGRNMR-A2-152[»]
    4J5QX-ray1.35A7-152[»]
    4J5RX-ray1.25A/B11-152[»]
    4J5SX-ray1.55A/B/C/D11-152[»]
    ProteinModelPortaliQ9Y530.
    SMRiQ9Y530. Positions 12-152.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y530.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 152151MacroPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni119 – 1257Substrate binding

    Sequence similaritiesi

    Contains 1 Macro domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG72109.
    HOGENOMiHOG000012894.
    HOVERGENiHBG050914.
    InParanoidiQ9Y530.
    OMAiWENVSAI.
    PhylomeDBiQ9Y530.
    TreeFamiTF324128.

    Family and domain databases

    InterProiIPR002589. Macro_dom.
    [Graphical view]
    PfamiPF01661. Macro. 1 hit.
    [Graphical view]
    PROSITEiPS51154. MACRO. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9Y530-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASSLNEDPE GSRITYVKGD LFACPKTDSL AHCISEDCRM GAGIAVLFKK    50
    KFGGVQELLN QQKKSGEVAV LKRDGRYIYY LITKKRASHK PTYENLQKSL 100
    EAMKSHCLKN GVTDLSMPRI GCGLDRLQWE NVSAMIEEVF EATDIKITVY 150
    TL 152
    Length:152
    Mass (Da):17,025
    Last modified:November 7, 2003 - v2
    Checksum:i8CC43CBDABA73E0B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK290939 mRNA. Translation: BAF83628.1.
    AK313361 mRNA. Translation: BAG36161.1.
    AL031778 Genomic DNA. Translation: CAI20285.1.
    CH471081 Genomic DNA. Translation: EAX04011.1.
    BC011709 mRNA. Translation: AAH11709.1.
    CCDSiCCDS34445.1.
    RefSeqiNP_659500.1. NM_145063.2.
    UniGeneiHs.227457.

    Genome annotation databases

    EnsembliENST00000424266; ENSP00000416829; ENSG00000124596.
    ENST00000463088; ENSP00000420193; ENSG00000124596.
    ENST00000468811; ENSP00000420601; ENSG00000124596.
    ENST00000479950; ENSP00000420484; ENSG00000124596.
    GeneIDi221443.
    KEGGihsa:221443.
    UCSCiuc003opm.3. human.

    Polymorphism databases

    DMDMi38258957.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK290939 mRNA. Translation: BAF83628.1 .
    AK313361 mRNA. Translation: BAG36161.1 .
    AL031778 Genomic DNA. Translation: CAI20285.1 .
    CH471081 Genomic DNA. Translation: EAX04011.1 .
    BC011709 mRNA. Translation: AAH11709.1 .
    CCDSi CCDS34445.1.
    RefSeqi NP_659500.1. NM_145063.2.
    UniGenei Hs.227457.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EEE NMR - A 11-152 [» ]
    2L8R NMR - A 3-152 [» ]
    2LGR NMR - A 2-152 [» ]
    4J5Q X-ray 1.35 A 7-152 [» ]
    4J5R X-ray 1.25 A/B 11-152 [» ]
    4J5S X-ray 1.55 A/B/C/D 11-152 [» ]
    ProteinModelPortali Q9Y530.
    SMRi Q9Y530. Positions 12-152.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 128727. 5 interactions.
    IntActi Q9Y530. 2 interactions.
    STRINGi 9606.ENSP00000416829.

    PTM databases

    PhosphoSitei Q9Y530.

    Polymorphism databases

    DMDMi 38258957.

    Proteomic databases

    MaxQBi Q9Y530.
    PaxDbi Q9Y530.
    PRIDEi Q9Y530.

    Protocols and materials databases

    DNASUi 221443.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000424266 ; ENSP00000416829 ; ENSG00000124596 .
    ENST00000463088 ; ENSP00000420193 ; ENSG00000124596 .
    ENST00000468811 ; ENSP00000420601 ; ENSG00000124596 .
    ENST00000479950 ; ENSP00000420484 ; ENSG00000124596 .
    GeneIDi 221443.
    KEGGi hsa:221443.
    UCSCi uc003opm.3. human.

    Organism-specific databases

    CTDi 221443.
    GeneCardsi GC06M041001.
    H-InvDB HIX0005859.
    HGNCi HGNC:21257. OARD1.
    HPAi HPA029036.
    MIMi 614393. gene.
    neXtProti NX_Q9Y530.
    PharmGKBi PA134879529.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG72109.
    HOGENOMi HOG000012894.
    HOVERGENi HBG050914.
    InParanoidi Q9Y530.
    OMAi WENVSAI.
    PhylomeDBi Q9Y530.
    TreeFami TF324128.

    Miscellaneous databases

    EvolutionaryTracei Q9Y530.
    GenomeRNAii 221443.
    NextBioi 91343.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y530.
    Bgeei Q9Y530.
    CleanExi HS_C6orf130.
    Genevestigatori Q9Y530.

    Family and domain databases

    InterProi IPR002589. Macro_dom.
    [Graphical view ]
    Pfami PF01661. Macro. 1 hit.
    [Graphical view ]
    PROSITEi PS51154. MACRO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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].
    2. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
      Tissue: Lung.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    7. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Solution structure of the A1PP domain from human protein C6orf130."
      RIKEN structural genomics initiative (RSGI)
      Submitted (AUG-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 11-152.
    10. "Solution structure of human C6orf130, a putative Macro domain."
      Center for eukaryotic structural genomics (CESG)
      Submitted (APR-2008) to the PDB data bank
      Cited for: STRUCTURE BY NMR.
    11. "Orphan macrodomain (human C6ORF130) is an o-acyl-ADP-ribose deacylase: solution structure and catalytic properties."
      Peterson F.C., Chen D., Lytle B.L., Rossi M.N., Ahel I., Denu J.M., Volkman B.F.
      J. Biol. Chem. 286:35955-35965(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR IN COMPLEX WITH ADENOSINE-5-DIPHOSPHORIBOSE, CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF HIS-32; CYS-33; SER-35; GLY-123 AND ASP-125, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.

    Entry informationi

    Entry nameiOARD1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y530
    Secondary accession number(s): A6NEK4, A8K4H4, Q96F23
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 7, 2003
    Last modified: October 1, 2014
    This is version 106 of the entry and version 2 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 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
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3