UniProt Accession

 ARHL2_HUMAN; Q9NX46; Q53G94; Q6IAB8; Q9BY47 

Genbank Protein ID

 AJ313333; AJ427295; AF212236; AK000453; CR457237; AK223037; AL138787; BC014169 

Genbank Nucleotide ID

 CAC85940.1; CAD20316.1; AAK14922.1; BAA91174.1; CAG33518.1; BAD96757.1; CAC21453.1; AAH14169.1 

Protein Name

 Poly(ADP-ribose) glycohydrolase ARH3 

Protein Synonyms/Alias

 ADP-ribosylhydrolase 3; [Protein ADP-ribosylarginine] hydrolase-like protein 2 

Gene Name

 ADPRHL2 

Gene Synonyms/Alias

 ARH3 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
92	LVQSLLAKEAFDEVD	ubiquitination	[1]
109	HRFAQEYKKDPDRGY	acetylation	[2]
131	FKKLLNPKCRDVFEP	ubiquitination	[1]
146	ARAQFNGKGSYGNGG	ubiquitination	[1]
172	SSVQDVQKFARLSAQ	ubiquitination	[1]
248	PYSSRLKKIGELLDQ	ubiquitination	[1]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 

Functional Description

 Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. Poly(ADP-ribose) metabolism may be required for maintenance of the normal function of neuronal cells. Generates ADP-ribose from poly-(ADP-ribose), but does not hydrolyze ADP- ribose-arginine, -cysteine, -diphthamide, or -asparagine bonds. Due to catalytic inactivity of PARG mitochondrial isoforms, ARH3 is the only PAR hydrolyzing enzyme in mitochondria. 

Sequence Annotation

 METAL 41 41 Magnesium 2.
 METAL 76 76 Magnesium 1.
 METAL 77 77 Magnesium 1.
 METAL 78 78 Magnesium 1.
 METAL 314 314 Magnesium 2.
 METAL 316 316 Magnesium 1.
 METAL 316 316 Magnesium 2.
 METAL 317 317 Magnesium 2.
 BINDING 254 254 Substrate (By similarity).  

Keyword

 3D-structure; Complete proteome; Cytoplasm; Hydrolase; Magnesium; Metal-binding; Mitochondrion; Nucleus; Polymorphism; Reference proteome; Transit peptide. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 363 AA 

Protein Sequence

Gene Ontology

 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004649; F:poly(ADP-ribose) glycohydrolase activity; IEA:EC. 

Interpro

 IPR005502; Ribosyl_crysJ1. 

Pfam

 PF03747; ADP_ribosyl_GH 

SMART

  

PROSITE

  

PRINTS