PARG
entrez
8505
canonical
uniprot
Q86W56
canonical
ensembl
ENSG00000227345
resolver
ensp
ENSP00000484285
resolver
ensp
ENSP00000611236
resolver
genesymbol
PARG
resolver
hgnc
HGNC:8605
resolver
uniprot
A5YBK3
resolver
uniprot
B2RC24
resolver
uniprot
B4DIU5
resolver
uniprot
B4DYR4
resolver
uniprot
I6RUV3
resolver
uniprot
Q6E4P6
resolver
uniprot
Q6E4P7
resolver
uniprot
Q7Z742
resolver
uniprot
Q9Y4W7
resolver
uniprot_entry
PARG_HUMAN
resolver
uniprot_sec
A5YBK3
resolver
uniprot_sec
B2RC24
resolver
uniprot_sec
B4DIU5
resolver
uniprot_sec
B4DYR4
resolver
uniprot_sec
I6RUV3
resolver
uniprot_sec
Q6E4P6
resolver
uniprot_sec
Q6E4P7
resolver
uniprot_sec
Q7Z742
resolver
uniprot_sec
Q9Y4W7
resolver
amino_acid_sequence
MNAGPGCEPCTKRPRWGAATTSPAASDARSFPSRQRRVLDPKDAHVQFRVPPSSPACVPGRAGQHRGSATSLVFKQKTITSWMDTKGIKTAESESLDSKENNNTRIESMMSSVQKDNFYQHNVEKLENVSQLSLDKSPTEKSTQYLNQHQTAAMCKWQNEGKHTEQLLESEPQTVTLVPEQFSNANIDRSPQNDDHSDTDSEENRDNQQFLTTVKLANAKQTTEDEQAREAKSHQKCSKSCDPGEDCASCQQDEIDVVPESPLSDVGSEDVGTGPKNDNKLTRQESCLGNSPPFEKESEPESPMDVDNSKNSCQDSEADEETSPGFDEQEDGSSSQTANKPSRFQARDADIEFRKRYSTKGGEVRLHFQFEGGESRTGMNDLNAKLPGNISSLNVECRNSKQHGKKDSKITDHFMRLPKAEDRRKEQWETKHQRTERKIPKYVPPHLSPDKKWLGTPIEEMRRMPRCGIRLPLLRPSANHTVTIRVDLLRAGEVPKPFPTHYKDLWDNKHVKMPCSEQNLYPVEDENGERTAGSRWELIQTALLNKFTRPQNLKDAILKYNVAYSKKWDFTALIDFWDKVLEEAEAQHLYQSILPDMVKIALCLPNICTQPIPLLKQKMNHSITMSQEQIASLLANAFFCTFPRRNAKMKSEYSSYPDINFNRLFEGRSSRKPEKLKTLFCYFRRVTEKKPTGLVTFTRQSLEDFPEWERCEKPLTRLHVTYEGTIEENGQGMLQVDFANRFVGGGVTSAGLVQEEIRFLINPELIISRLFTEVLDHNECLIITGTEQYSEYTGYAETYRWSRSHEDGSERDDWQRRCTEIVAIDALHFRRYLDQFVPEKMRRELNKAYCGFLRPGVSSENLSAVATGNWGCGAFGGDARLKALIQILAAAAAERDVVYFTFGDSELMRDIYSMHIFLTERKLTVGDVYKLLLRYYNEECRNCSTPGPDIKLYPFIYHAVESCAETADHSGQRTGT
uniprot
proteins
ec_number
3.2.1.143
uniprot
proteins
function
FUNCTION: Poly(ADP-ribose) glycohydrolase that degrades poly(ADP-ribose) by hydrolyzing the ribose-ribose bonds present in poly(ADP-ribose) (PubMed:15450800, PubMed:21892188, PubMed:23102699, PubMed:23474714, PubMed:33186521, PubMed:34019811, PubMed:34321462). Mainly acts as an exo-glycohydrolase but can act as an endo-glycohydrolase at low efficiency, releasing poly(ADP-ribose) of different length as well as ADP-ribose monomers (PubMed:23102699, PubMed:23481255, PubMed:37268618). It is however unable to cleave the ester bond between the terminal ADP-ribose and ADP-ribosylated residues, leaving proteins that are mono-ADP-ribosylated (PubMed:21892188, PubMed:23474714, PubMed:33186521, PubMed:37268618). Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by PARG (PubMed:23102699, PubMed:34019811). Required to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged replicative stress, while it is not required for recovery from transient replicative stress (PubMed:24906880). Responsible for the prevalence of mono-ADP-ribosylated proteins in cells, thanks to its ability to degrade poly(ADP-ribose) without cleaving the terminal protein-ribose bond (PubMed:33186521). Required for retinoid acid-dependent gene transactivation, probably by removing poly(ADP-ribose) from histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters (PubMed:23102699). Involved in the synthesis of ATP in the nucleus, together with PARP1, NMNAT1 and NUDT5 (PubMed:27257257). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (PubMed:27257257). {ECO:0000269|PubMed:15450800, ECO:0000269|PubMed:21892188, ECO:0000269|PubMed:23102699, ECO:0000269|PubMed:23474714, ECO:0000269|PubMed:23481255, ECO:0000269|PubMed:24906880, ECO:0000269|PubMed:27257257, ECO:0000269|PubMed:33186521, ECO:0000269|PubMed:34019811, ECO:0000269|PubMed:34321462, ECO:0000269|PubMed:37268618}.
uniprot
proteins
mass_dalton
111110
uniprot
proteins
mutagenesis
MUTAGEN 1..619; /note="Missing: Reduces protein stability but does not abrogate poly(ADP-ribose) glycohydrolase activity."; /evidence="ECO:0000269|PubMed:22673905"; MUTAGEN 12..13; /note="KR->AG: Abolishes nuclear targeting."; /evidence="ECO:0000269|PubMed:15212953"; MUTAGEN 36; /note="R->A: No effect on poly(ADP-ribose) glycohydrolase activity."; /evidence="ECO:0000269|PubMed:15212953"; MUTAGEN 37; /note="R->G: No effect on poly(ADP-ribose) glycohydrolase activity."; /evidence="ECO:0000269|PubMed:15212953"; MUTAGEN 653; /note="Y->F: No effect on poly(ADP-ribose) glycohydrolase activity."; /evidence="ECO:0000269|PubMed:22673905"; MUTAGEN 671; /note="R->A: No effect on poly(ADP-ribose) glycohydrolase activity."; /evidence="ECO:0000269|PubMed:37268618"; MUTAGEN 671; /note="R->K: Slightly reduces poly(ADP-ribose) glycohydrolase activity."; /evidence="ECO:0000269|PubMed:37268618"; MUTAGEN 726; /note="I->P: Severly reduces poly(ADP-ribose) glycohydrolase activity."; /evidence="ECO:0000269|PubMed:37268618"; MUTAGEN 727; /note="E->A: Severly reduces poly(ADP-ribose) glycohydrolase activity."; /evidence="ECO:0000269|PubMed:37268618"; MUTAGEN 740; /note="N->A: Severly reduces poly(ADP-ribose) glycohydrolase activity."; /evidence="ECO:0000269|PubMed:21892188, ECO:0000269|PubMed:22673905"; MUTAGEN 745; /note="G->A: Abolishes poly(ADP-ribose) glycohydrolase activity."; /evidence="ECO:0000269|PubMed:22673905"; MUTAGEN 746; /note="G->S: No effect on poly(ADP-ribose) glycohydrolase activity."; /evidence="ECO:0000269|PubMed:22673905"; MUTAGEN 749; /note="S->N: No effect on poly(ADP-ribose) glycohydrolase activity."; /evidence="ECO:0000269|PubMed:22673905"; MUTAGEN 753; /note="V->I: No effect on poly(ADP-ribose) glycohydrolase activity."; /evidence="ECO:0000269|PubMed:37268618"; MUTAGEN 755; /note="E->A: Abolishes poly(ADP-ribose) glycohydrolase activity."; /evidence="ECO:0000269|PubMed:21892188, ECO:0000269|PubMed:22673905"; MUTAGEN 756; /note="E->A: Abolishes poly(ADP-ribose) glycohydrolase activity."; /evidence="ECO:0000269|PubMed:21892188, ECO:0000269|PubMed:22673905"; MUTAGEN 756; /note="E->N: Reduces hydrolase activity."; /evidence="ECO:0000269|PubMed:34321462"; MUTAGEN 756; /note="E->Q: Abolishes poly(ADP-ribose) glycohydrolase activity."; /evidence="ECO:0000269|PubMed:37268618"; MUTAGEN 795; /note="Y->A: Reduces poly(ADP-ribose) glycohydrolase activity."; /evidence="ECO:0000269|PubMed:22673905"; MUTAGEN 869; /note="N->A: Reduces poly(ADP-ribose) glycohydrolase activity."; /evidence="ECO:0000269|PubMed:22673905"; MUTAGEN 874; /note="A->W: Reduced poly(ADP-ribose) glycohydrolase activity."; /evidence="ECO:0000269|PubMed:21892188"; MUTAGEN 875; /note="F->A: Abolishes poly(ADP-ribose) glycohydrolase activity."; /evidence="ECO:0000269|PubMed:21892188, ECO:0000269|PubMed:22673905"; MUTAGEN 902; /note="F->G: Slightly increases poly(ADP-ribose) glycohydrolase efficiency and facilitates endo-glycohydrolytic action."; /evidence="ECO:0000269|PubMed:37268618"; MUTAGEN 904; /note="D->W: Severly reduces poly(ADP-ribose) glycohydrolase activity."; /evidence="ECO:0000269|PubMed:22673905
uniprot
proteins
protein_family
Poly(ADP-ribose) glycohydrolase family
uniprot
proteins
pubmed
10449915
uniprot
proteins
pubmed
14527731
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15212953
uniprot
proteins
pubmed
15450800
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16460818
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17509564
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19105632
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21398629
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21892188
uniprot
proteins
pubmed
22433848
uniprot
proteins
pubmed
22673905
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23102699
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23251397
uniprot
proteins
pubmed
23474714
uniprot
proteins
pubmed
23481255
uniprot
proteins
pubmed
23917065
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24906880
uniprot
proteins
pubmed
27257257
uniprot
proteins
pubmed
30472116
uniprot
proteins
pubmed
33186521
uniprot
proteins
pubmed
34019811
uniprot
proteins
pubmed
34321462
uniprot
proteins
pubmed
37268618
uniprot
proteins
sequence_length
976
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000269|PubMed:16460818, ECO:0000269|PubMed:21398629}. Note=Colocalizes with PCNA at replication foci (PubMed:21398629). Relocalizes to the cytoplasm in response to DNA damage (PubMed:16460818). {ECO:0000269|PubMed:16460818, ECO:0000269|PubMed:21398629}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:15212953, ECO:0000269|PubMed:16460818}. Note=Translocates to the nucleus in response to DNA damage. {ECO:0000269|PubMed:16460818}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:15212953}.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm {ECO:0000269|PubMed:22433848}. Mitochondrion {ECO:0000269|PubMed:22433848}.; SUBCELLULAR LOCATION: [Isoform 5]: Mitochondrion matrix {ECO:0000269|PubMed:17509564}.
uniprot
proteins