CPLM-016265

Genbank Nucleotide ID

Poly(ADP-ribose) glycohydrolase

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
503	KPFPTHYKDLWDNKH	acetylation	[1, 2]
546	IQTALLNKFTRPQNL	ubiquitination	[3, 4, 5]
616	TQPIPLLKQKMNHSI	ubiquitination	[6]
618	PIPLLKQKMNHSITM	ubiquitination	[6]
650	PRRNAKMKSEYSSYP	ubiquitination	[6]

[1] 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]
[2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[4] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
[5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[6] 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]

Functional Description

Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. PARG acts both as an endo- and exoglycosidase, releasing PAR of different length as well as ADP-ribose monomers. Required for retinoid acid-dependent gene transactivation, probably by dePARsylating histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters.

REGION 1 456 A-domain.
REGION 610 795 Catalytic.
REGION 726 727 Substrate binding (By similarity).
REGION 869 874 Substrate binding (By similarity).
MOTIF 10 16 Nuclear localization signal.
MOTIF 76 83 PIP-box (PCNA interacting peptide).
ACT_SITE 737 737 By similarity.
ACT_SITE 755 755 By similarity.
ACT_SITE 756 756 By similarity.
BINDING 740 740 Substrate (By similarity).
BINDING 754 754 Substrate; via amide nitrogen (By
BINDING 795 795 Substrate (By similarity).
MOD_RES 133 133 Phosphoserine.
MOD_RES 137 137 Phosphoserine.
MOD_RES 197 197 Phosphoserine.
MOD_RES 199 199 Phosphothreonine.
MOD_RES 261 261 Phosphoserine (By similarity).
MOD_RES 264 264 Phosphoserine (By similarity).
MOD_RES 298 298 Phosphoserine.
MOD_RES 302 302 Phosphoserine.

3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Hydrolase; Mitochondrion; Nucleus; Phosphoprotein; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; TAS:ProtInc.
GO:0005829; C:cytosol; IEA:Compara.
GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO:0005634; C:nucleus; IDA:HPA.
GO:0004649; F:poly(ADP-ribose) glycohydrolase activity; IDA:UniProtKB.
GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO:0016045; P:detection of bacterium; IEA:Compara.
GO:0006974; P:response to DNA damage stimulus; IEA:Compara.

IPR007724; Poly_GlycHdrlase.