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Protein

O-acetyl-ADP-ribose deacetylase 1

Gene

OARD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei21 – 211Substrate; via amide nitrogen
Active sitei125 – 1251Proton acceptor1 Publication
Binding sitei152 – 1521Substrate; via carboxylate

GO - Molecular functioni

  1. deacetylase activity Source: UniProtKB
  2. purine nucleoside binding Source: UniProtKB

GO - Biological processi

  1. purine nucleoside metabolic process Source: UniProtKB
Complete GO annotation...

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 Componenti: 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.

Polymorphism and mutation databases

BioMutaiOARD1.
DMDMi38258957.

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

BgeeiQ9Y530.
CleanExiHS_C6orf130.
ExpressionAtlasiQ9Y530. baseline and differential.
GenevestigatoriQ9Y530.

Organism-specific databases

HPAiHPA029036.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi128727. 4 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 – 196Combined sources
Helixi21 – 233Combined sources
Beta strandi28 – 358Combined sources
Beta strandi41 – 433Combined sources
Helixi45 – 528Combined sources
Helixi55 – 617Combined sources
Beta strandi67 – 737Combined sources
Beta strandi76 – 8611Combined sources
Helixi93 – 11018Combined sources
Beta strandi114 – 1174Combined sources
Helixi123 – 1253Combined sources
Helixi129 – 14012Combined sources
Beta strandi146 – 1516Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000006988.
HOGENOMiHOG000012894.
HOVERGENiHBG050914.
InParanoidiQ9Y530.
OMAiEAMKTHC.
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

        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. 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 and mutation databases

BioMutaiOARD1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi128727. 4 interactions.
IntActiQ9Y530. 2 interactions.
STRINGi9606.ENSP00000416829.

PTM databases

PhosphoSiteiQ9Y530.

Polymorphism and mutation databases

BioMutaiOARD1.
DMDMi38258957.

Proteomic databases

MaxQBiQ9Y530.
PaxDbiQ9Y530.
PRIDEiQ9Y530.

Protocols and materials databases

DNASUi221443.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi221443.
GeneCardsiGC06M041001.
H-InvDBHIX0005859.
HGNCiHGNC:21257. OARD1.
HPAiHPA029036.
MIMi614393. gene.
neXtProtiNX_Q9Y530.
PharmGKBiPA134879529.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG72109.
GeneTreeiENSGT00390000006988.
HOGENOMiHOG000012894.
HOVERGENiHBG050914.
InParanoidiQ9Y530.
OMAiEAMKTHC.
PhylomeDBiQ9Y530.
TreeFamiTF324128.

Miscellaneous databases

EvolutionaryTraceiQ9Y530.
GenomeRNAii221443.
NextBioi91343.
PROiQ9Y530.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y530.
CleanExiHS_C6orf130.
ExpressionAtlasiQ9Y530. baseline and differential.
GenevestigatoriQ9Y530.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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: April 29, 2015
This is version 111 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.