Primary Information |
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| BoMiProt ID | Bomi8123 |
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| Protein Name | Poly(ADP-ribose) glycohydrolase |
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| Organism | Bos taurus |
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| Uniprot ID | O02776 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_776563.1 |
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| Aminoacid Length | 977 |
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| Molecular Weight | 110837 |
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| FASTA Sequence |
Download |
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| Gene Name | PARG |
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| Gene ID | 281377 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | involved in DNA replication and repair.hydrolysing the ribose-ribose bonds present in poly(ADP-ribose).PARG depleted/inhibited cells show increased sensitivity to DNA damaging agents. PARG is thought to play an important role in preventing the accumulation of cytoplasmic PAR and therefore parthanatos, a caspase-independent PAR-mediated type of cell death. |
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| Biochemical Properties | both endo-glycohydrolase and exo-glycohydrolase activity, preferentially performing the latter by binding to the two most distal ADP-ribose residues within the PAR chain.These different modes of catalysis produce free PAR and mono ADP-ribose moieties, respectively. The free mono ADP-ribose is then metabolized into AMP and ribose 5′ phosphate by ADP-ribose pyrophosphohydrolases. |
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| PTMs | Acetylation and phosphorylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|O02776|PARG_BOVIN Poly(ADP-ribose) glycohydrolase OS=Bos taurus OX=9913 GN=PARG PE=1 SV=1
MSAGPGCEPCTKRPRWDAAATSPPAASDARSFPGRQRRVLDSKDAPVQFRVPPSSSGCAL
GRAGQHRGS*69ATSLVFKQKTITSWMDTKGIKTVESESLHSKENNNTREESMMSSVQKDNFY
QHNMEKLENVSQLGFDKS*138PVEKGTQYLKQHQTAAMCKWQNEGPHSERLLESEPPAVTLVP
EQFSNANVDQSSPKDDHS*198DT*200NSEESRDNQQFLTHVKLANAKQTMEDEQGREARSHQKCGK
ACHPAEACAGCQQEETDVVSES*262PLS*265DTGSEDVGTGLKNANRLNRQES*287SLGNS*292PPFEKES*299EPES*303PMDVDNSKNSCQDS*317EADEETSPGFDEQEDSSSAQTANKPSRFQPREADTELRKRSSAKGGEIRLHFQFEGGESRAGMNDVNAKRPGSTSSLNVECRNSKQHGRKDSKITDHFMRVPK
AEDKRKEQCEMKHQRTERKIPKYIPPHLS*449PDKKWLGTPIEEMRRMPRCGIRLPPLRPSAN
HTVTIRVDLLRIGEVPKPFPTHFKDLWDNKHVKMPCSEQNLYPVEDENGERAAGSRWELI
QTALLNRLTRPQNLKDAILKYNVAYSKKWDFTALIDFWDKVLEEAEAQHLYQSILPDMVK
IALCLPNICTQPIPLLKQKMNHSITMSQEQIASLLANAFFCTFPRRNAKMKSEYSSYPDI
NFNRLFEGRSSRKPEKLKTLFCYFRRVTEKKPTGLVTFTRQSLEDFPEWERCEKLLTRLH
VTYEGTIEGNGQGMLQVDFANRFVGGGVTSAGLVQEEIRFLINPELIVSRLFTEVLDHNE
CLIITGTEQYSEYTGYAETYRWARSHEDRSERDDWQRRTTEIVAIDALHFRRYLDQFVPE
KIRRELNKAYCGFLRPGVSSENLSAVATGNWGCGAFGGDARLKALIQILAAAVAERDVVY
FTFGDSELMRDIYSMHTFLTERKLTVGEVYKLLLRYYNEECRNCSTPGPDIKLYPFIYHA
VESCTQTTNQPGQRTGA
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| Predicted Disorder Regions | (19-29), (170-360) |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Bibliography | Harrision D, Gravells P, Thompson R, Bryant HE. Poly(ADP-Ribose) Glycohydrolase (PARG) vs. Poly(ADP-Ribose) Polymerase (PARP) - Function in Genome Maintenance and Relevance of Inhibitors for Anti-cancer Therapy. Front Mol Biosci. 2020 Aug 28;7:191. doi: 10.3389/fmolb.2020.00191. PMID: 33005627; PMCID: PMC7485115. |
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