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UniProt functional annotation for A1Z1Q3 | ||
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| UniProt code: A1Z1Q3. |
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| Organism: | |
Homo sapiens (Human). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. |
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| Function: | |
Removes ADP-ribose from asparatate and glutamate residues in proteins bearing a single ADP-ribose moiety (PubMed:23474714, PubMed:23474712). Inactive towards proteins bearing poly-ADP-ribose (PubMed:23474714, PubMed:23474712). Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins (PubMed:21257746). {ECO:0000269|PubMed:21257746, ECO:0000269|PubMed:23474712, ECO:0000269|PubMed:23474714}. |
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| Catalytic activity: | |
Reaction=2''-O-acetyl-ADP-D-ribose + H2O = acetate + ADP-D-ribose + H(+); Xref=Rhea:RHEA:57060, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57967, ChEBI:CHEBI:83767; Evidence={ECO:0000305|PubMed:21257746}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57061; Evidence={ECO:0000305|PubMed:21257746}; |
| Catalytic activity: | |
Reaction=4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-ribose + H(+) + L-aspartyl-[protein]; Xref=Rhea:RHEA:54428, Rhea:RHEA- COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29961, ChEBI:CHEBI:57967, ChEBI:CHEBI:138102; Evidence={ECO:0000269|PubMed:23474714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54429; Evidence={ECO:0000269|PubMed:23474714}; |
| Catalytic activity: | |
Reaction=5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + H2O = ADP-D-ribose + H(+) + L-glutamyl-[protein]; Xref=Rhea:RHEA:58248, Rhea:RHEA- COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:57967, ChEBI:CHEBI:142540; Evidence={ECO:0000269|PubMed:23474712, ECO:0000269|PubMed:23474714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58249; Evidence={ECO:0000269|PubMed:23474712, ECO:0000269|PubMed:23474714}; |
| Activity regulation: | |
Subject to product inhibition by ADP-ribose. {ECO:0000269|PubMed:23474712}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=107 uM for O-acetyl-ADP-ribose {ECO:0000269|PubMed:21257746}; |
| Subunit: | |
Interacts with ADP-ribosylated PARP1. {ECO:0000269|PubMed:23474712}. |
| Subcellular location: | |
Nucleus {ECO:0000269|PubMed:23474712}. Note=Recruited to DNA lesions, probably via mono-APD-ribosylated proteins. {ECO:0000269|PubMed:23474712}. |
| Sequence caution: | |
Sequence=BAD18504.1; Type=Frameshift; Evidence={ECO:0000305}; |
Annotations taken from UniProtKB at the EBI.