OARD1
entrez
221443
canonical
uniprot
Q9Y530
canonical
ensembl
ENSG00000124596
resolver
ensp
ENSP00000362247
resolver
ensp
ENSP00000416829
resolver
ensp
ENSP00000418098
resolver
ensp
ENSP00000418400
resolver
ensp
ENSP00000419175
resolver
ensp
ENSP00000419875
resolver
ensp
ENSP00000420193
resolver
ensp
ENSP00000420414
resolver
ensp
ENSP00000420484
resolver
ensp
ENSP00000420601
resolver
ensp
ENSP00000487484
resolver
ensp
ENSP00000573231
resolver
ensp
ENSP00000644923
resolver
ensp
ENSP00000755264
resolver
enst
ENST00000373154
resolver
enst
ENST00000424266
resolver
enst
ENST00000463088
resolver
enst
ENST00000464633
resolver
enst
ENST00000468811
resolver
enst
ENST00000479950
resolver
enst
ENST00000480585
resolver
enst
ENST00000482515
resolver
enst
ENST00000486443
resolver
enst
ENST00000628419
resolver
enst
ENST00000903172
resolver
genesymbol
C6orf130
resolver
genesymbol
OARD1
resolver
genesymbol_syn
C6orf130
resolver
genesymbol_syn
TARG1
resolver
hgnc
HGNC:21257
resolver
uniprot
A6NEK4
resolver
uniprot
A8K4H4
resolver
uniprot
C9J5P1
resolver
uniprot
C9JA90
resolver
uniprot
C9JXC3
resolver
uniprot
Q05CR9
resolver
uniprot
Q96F23
resolver
uniprot_entry
C9J5P1_HUMAN
resolver
uniprot_entry
C9JA90_HUMAN
resolver
uniprot_entry
C9JXC3_HUMAN
resolver
uniprot_entry
OARD1_HUMAN
resolver
uniprot_entry
Q05CR9_HUMAN
resolver
uniprot_sec
A6NEK4
resolver
uniprot_sec
A8K4H4
resolver
uniprot_sec
Q96F23
resolver
activity_regulation
ACTIVITY REGULATION: Subject to competitive inhibition by the product ADP-ribose. {ECO:0000269|PubMed:21849506}.
uniprot
proteins
amino_acid_sequence
MASSLNEDPEGSRITYVKGDLFACPKTDSLAHCISEDCRMGAGIAVLFKKKFGGVQELLNQQKKSGEVAVLKRDGRYIYYLITKKRASHKPTYENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAMIEEVFEATDIKITVYTL
uniprot
proteins
disease_involvement
DISEASE: Note=Defects in OARD1 are found in patients with severe neurodegeneration (PubMed:23481255). Defects were found in an extended consanguineous family with several affected cases in two generations (PubMed:23481255). {ECO:0000269|PubMed:23481255}.
uniprot
proteins
ec_number
3.2.2.-
uniprot
proteins
ec_number
3.5.1.-
uniprot
proteins
function
FUNCTION: ADP-ribose glycohydrolase that hydrolyzes ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on glutamate and O-acetyl-ADP-D-ribose (PubMed:21849506, PubMed:23474714, PubMed:23481255). Specifically acts as a glutamate mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to glutamate residues on proteins (PubMed:23474714, PubMed:23481255). Does not act on poly-ADP-ribosylated proteins: the poly-ADP-ribose chain of poly-ADP-ribosylated glutamate residues must by hydrolyzed into mono-ADP-ribosylated glutamate by PARG to become a substrate for OARD1 (PubMed:23481255). Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins (PubMed:21849506). 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 (PubMed:21849506). {ECO:0000269|PubMed:21849506, ECO:0000269|PubMed:23474714, ECO:0000269|PubMed:23481255}.
uniprot
proteins
mass_dalton
17025
uniprot
proteins
mutagenesis
MUTAGEN 32; /note="H->A: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:21849506"; MUTAGEN 33; /note="C->S: No effect."; /evidence="ECO:0000269|PubMed:21849506"; MUTAGEN 35; /note="S->A: Reduced catalytic activity. No effect on affinity towards substrate."; /evidence="ECO:0000269|PubMed:21849506"; MUTAGEN 83; /note="T->A: Reduced catalytic activity. No effect on affinity towards substrate."; /evidence="ECO:0000269|PubMed:21849506"; MUTAGEN 84; /note="K->A: Abolishes enzyme activity and ability to form a stable covalent adduct with the ADP-ribosylated substrate."; /evidence="ECO:0000269|PubMed:23481255"; MUTAGEN 123; /note="G->E: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:21849506"; MUTAGEN 125; /note="D->A: Abolishes enzyme activity without affecting ability to form a stable covalent adduct with the ADP-ribosylated substrate."; /evidence="ECO:0000269|PubMed:21849506, ECO:0000269|PubMed:23481255
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21849506
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23474714
uniprot
proteins
pubmed
23481255
uniprot
proteins
pubmed
29712969
uniprot
proteins
pubmed
31599159
uniprot
proteins
sequence_length
152
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:23481255, ECO:0000269|PubMed:29712969}. Nucleus, nucleolus {ECO:0000269|PubMed:29712969}. Chromosome {ECO:0000269|PubMed:23481255}. Note=Localizes both in the nucleoplasm and in the nucleolus (PubMed:29712969). Relocalizes to the nucleoplasm in response to DNA damage (PubMed:29712969). Recruited to DNA lesion regions following DNA damage (PubMed:23481255). {ECO:0000269|PubMed:23481255, ECO:0000269|PubMed:29712969}.
uniprot
proteins