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Protein

Poly(ADP-ribose) glycohydrolase

Gene

Parg

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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. Involved in the synthesis of ATP in the nucleus, together with PARP1, NMNAT1 and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming.By similarity

Catalytic activityi

Hydrolyzes poly(ADP-D-ribose) at glycosidic (1''-2') linkage of ribose-ribose bond to produce free ADP-D-ribose.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei730By similarity1
Binding sitei733SubstrateBy similarity1
Binding sitei747Substrate; via amide nitrogenBy similarity1
Active sitei748By similarity1
Active sitei749By similarity1
Binding sitei788SubstrateBy similarity1

GO - Molecular functioni

  • chromatin binding Source: MGI
  • poly(ADP-ribose) glycohydrolase activity Source: MGI

GO - Biological processi

Keywordsi

Molecular functionHydrolase

Enzyme and pathway databases

ReactomeiR-MMU-110362 POLB-Dependent Long Patch Base Excision Repair

Names & Taxonomyi

Protein namesi
Recommended name:
Poly(ADP-ribose) glycohydrolase (EC:3.2.1.143)
Gene namesi
Name:Parg
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1347094 Parg

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000666031 – 969Poly(ADP-ribose) glycohydrolaseAdd BLAST969

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei135PhosphoserineCombined sources1
Modified residuei137PhosphothreonineCombined sources1
Modified residuei195PhosphoserineBy similarity1
Modified residuei197PhosphothreonineBy similarity1
Modified residuei256PhosphoserineCombined sources1
Modified residuei259PhosphoserineCombined sources1
Modified residuei281PhosphoserineBy similarity1
Modified residuei286PhosphoserineCombined sources1
Modified residuei293PhosphoserineCombined sources1
Modified residuei297PhosphoserineCombined sources1
Modified residuei311PhosphoserineBy similarity1
Modified residuei334N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO88622
MaxQBiO88622
PaxDbiO88622
PeptideAtlasiO88622
PRIDEiO88622

PTM databases

iPTMnetiO88622
PhosphoSitePlusiO88622

Expressioni

Gene expression databases

BgeeiENSMUSG00000021911 Expressed in 282 organ(s), highest expression level in pineal body
CleanExiMM_PARG
ExpressionAtlasiO88622 baseline and differential

Interactioni

Subunit structurei

Interacts with PCNA. Interacts with NUDT5.By similarity

Protein-protein interaction databases

IntActiO88622, 2 interactors
STRINGi10090.ENSMUSP00000022470

Structurei

Secondary structure

1969
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliO88622
SMRiO88622
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 449A-domainBy similarityAdd BLAST449
Regioni602 – 787CatalyticBy similarityAdd BLAST186
Regioni719 – 720Substrate bindingBy similarity2
Regioni862 – 867Substrate bindingBy similarity6

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi10 – 16Nuclear localization signalBy similarity7
Motifi77 – 84PIP-box (PCNA interacting peptide)By similarity8

Domaini

The PIP-box mediates interaction with PCNA and localization to replication foci.By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2064 Eukaryota
ENOG410XT3Y LUCA
GeneTreeiENSGT00390000003652
HOGENOMiHOG000168457
HOVERGENiHBG053510
InParanoidiO88622
PhylomeDBiO88622

Family and domain databases

InterProiView protein in InterPro
IPR007724 Poly_GlycHdrlase
PANTHERiPTHR12837 PTHR12837, 1 hit
PfamiView protein in Pfam
PF05028 PARG_cat, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O88622-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MSAGPGWEPC TKRPRWGAAG TSAPTASDSR SFPGRQRRVL DPKDAPVQFR
60 70 80 90 100
VPPSSPACVS GRAGPHRGNA TSFVFKQKTI TTWMDTKGPK TAESESKENN
110 120 130 140 150
NTRIDSMMSS VQKDNFYPHK VEKLENVPQL NLDKSPTEKS SQYLNQQQTA
160 170 180 190 200
SVCKWQNEGK HAEQLLASEP PAGTPLPKQL SNANIGQSPH TDDHSDTDHE
210 220 230 240 250
EDRDNQQFLT PIKLANTKPT VGDGQARSNC KCSGSRQSVK DCTGCQQEEV
260 270 280 290 300
DVLPESPLSD VGAEDIGTGP KNDNKLTGQE SSLGDSPPFE KESEPESPMD
310 320 330 340 350
VDNSKNSCQD SEADEETSPV FDEQDDRSSQ TANKLSSCQA READGDLRKR
360 370 380 390 400
YLTKGSEVRL HFQFEGENNA GTSDLNAKPS GNSSSLNVEC RSSKQHGKRD
410 420 430 440 450
SKITDHFMRI SKSEDRRKEQ CEVRHQRTER KIPKYIPPNL PPEKKWLGTP
460 470 480 490 500
IEEMRKMPRC GIHLPSLRPS ASHTVTVRVD LLRAGEVPKP FPTHYKDLWD
510 520 530 540 550
NKHVKMPCSE QNLYPVEDEN GERTAGSRWE LIQTALLNKF TRPQNLKDAI
560 570 580 590 600
LKYNVAYSKK WDFTALVDFW DKVLEEAEAQ HLYQSILPDM VKIALCLPNI
610 620 630 640 650
CTQPIPLLKQ KMNHSVTMSQ EQIASLLANA FFCTFPRRNA KMKSEYSSYP
660 670 680 690 700
DINFNRLFEG RSSRKPEKLK TLFCYFRRVT EKKPTGLVTF TRQSLEDFPE
710 720 730 740 750
WERCEKPLTR LHVTYEGTIE GNGRGMLQVD FANRFVGGGV TGAGLVQEEI
760 770 780 790 800
RFLINPELIV SRLFTEVLDH NECLIITGTE QYSEYTGYAE TYRWARSHED
810 820 830 840 850
GSEKDDWQRR CTEIVAIDAL HFRRYLDQFV PEKVRRELNK AYCGFLRPGV
860 870 880 890 900
PSENLSAVAT GNWGCGAFGG DARLKALIQI LAAAAAERDV VYFTFGDSEL
910 920 930 940 950
MRDIYSMHTF LTERKLDVGK VYKLLLRYYN EECRNCSTPG PDIKLYPFIY
960
HAVESSAETT DMPGQKAGT
Length:969
Mass (Da):109,324
Last modified:October 25, 2004 - v2
Checksum:i2626996A53AC48ED
GO
Isoform 2 (identifier: O88622-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     920-920: K → E
     921-969: Missing.

Note: No experimental confirmation available.
Show »
Length:920
Mass (Da):103,771
Checksum:i2EA3C15C421B09A1
GO

Computationally mapped potential isoform sequencesi

There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3X8U8G3X8U8_MOUSE
Poly (ADP-ribose) glycohydrolase, i...
Parg mCG_117129
961Annotation score:
E9Q088E9Q088_MOUSE
Cytosolic poly(ADP-ribose) glycohyd...
Parg
456Annotation score:
A0A2I3BRU5A0A2I3BRU5_MOUSE
Poly(ADP-ribose) glycohydrolase
Parg
661Annotation score:
E9Q7T9E9Q7T9_MOUSE
Poly(ADP-ribose) glycohydrolase
Parg
43Annotation score:
E9Q3C4E9Q3C4_MOUSE
Poly(ADP-ribose) glycohydrolase
Parg
95Annotation score:
E9Q954E9Q954_MOUSE
Poly(ADP-ribose) glycohydrolase
Parg
186Annotation score:

Sequence cautioni

The sequence BC050892 differs from that shown. Reason: Erroneous termination at position 962. Translated as Met.Curated
The sequence BC059827 differs from that shown. Reason: Erroneous termination at position 962. Translated as Met.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti13 – 14RP → A in AAC28735 (PubMed:10449915).Curated2
Sequence conflicti305K → R in AAC28735 (PubMed:10449915).Curated1
Sequence conflicti370A → V in BC050892 (PubMed:15489334).Curated1
Sequence conflicti370A → V in BC059827 (PubMed:15489334).Curated1
Sequence conflicti872A → V in BAC29519 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_011771920K → E in isoform 2. 1 Publication1
Alternative sequenceiVSP_011772921 – 969Missing in isoform 2. 1 PublicationAdd BLAST49

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079557 mRNA Translation: AAC28735.1
AK036656 mRNA Translation: BAC29519.1
BC050892 mRNA No translation available.
BC059827 mRNA No translation available.
UniGeneiMm.15962
Mm.458144

Genome annotation databases

EnsembliENSMUST00000163350; ENSMUSP00000131566; ENSMUSG00000021911 [O88622-2]
UCSCiuc007syp.1 mouse [O88622-1]
uc007syq.1 mouse [O88622-2]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079557 mRNA Translation: AAC28735.1
AK036656 mRNA Translation: BAC29519.1
BC050892 mRNA No translation available.
BC059827 mRNA No translation available.
UniGeneiMm.15962
Mm.458144

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4FC2X-ray1.91A/B/C/D439-959[»]
4N9YX-ray2.30A439-959[»]
4N9ZX-ray1.90A/B439-959[»]
4NA0X-ray2.40A/B/C439-959[»]
4NA4X-ray2.50A/B/C439-959[»]
4NA5X-ray2.00A439-959[»]
4NA6X-ray2.48A/B439-959[»]
ProteinModelPortaliO88622
SMRiO88622
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO88622, 2 interactors
STRINGi10090.ENSMUSP00000022470

PTM databases

iPTMnetiO88622
PhosphoSitePlusiO88622

Proteomic databases

EPDiO88622
MaxQBiO88622
PaxDbiO88622
PeptideAtlasiO88622
PRIDEiO88622

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000163350; ENSMUSP00000131566; ENSMUSG00000021911 [O88622-2]
UCSCiuc007syp.1 mouse [O88622-1]
uc007syq.1 mouse [O88622-2]

Organism-specific databases

MGIiMGI:1347094 Parg

Phylogenomic databases

eggNOGiKOG2064 Eukaryota
ENOG410XT3Y LUCA
GeneTreeiENSGT00390000003652
HOGENOMiHOG000168457
HOVERGENiHBG053510
InParanoidiO88622
PhylomeDBiO88622

Enzyme and pathway databases

ReactomeiR-MMU-110362 POLB-Dependent Long Patch Base Excision Repair

Miscellaneous databases

PROiPR:O88622
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000021911 Expressed in 282 organ(s), highest expression level in pineal body
CleanExiMM_PARG
ExpressionAtlasiO88622 baseline and differential

Family and domain databases

InterProiView protein in InterPro
IPR007724 Poly_GlycHdrlase
PANTHERiPTHR12837 PTHR12837, 1 hit
PfamiView protein in Pfam
PF05028 PARG_cat, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPARG_MOUSE
AccessioniPrimary (citable) accession number: O88622
Secondary accession number(s): Q80YQ6, Q8CB72
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: October 25, 2004
Last modified: November 7, 2018
This is version 106 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
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