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Protein

Poly(ADP-ribose) glycohydrolase

Gene

Parg

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei733 – 7331By similarity
Binding sitei736 – 7361Substrate
Binding sitei750 – 7501Substrate; via amide nitrogen
Active sitei751 – 7511By similarity
Active sitei752 – 7521By similarity
Binding sitei791 – 7911Substrate

GO - Molecular functioni

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

GO - Biological processi

  • carbohydrate metabolic process Source: InterPro
  • positive regulation of DNA repair Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Poly(ADP-ribose) glycohydrolase (EC:3.2.1.143)
Gene namesi
Name:Parg
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620387. Parg.

Subcellular locationi

  • Nucleus By similarity

  • Note: Colocalizes with PCNA at replication foci. Relocalizes to the cytoplasm in response to DNA damage (By similarity).By similarity

GO - Cellular componenti

  • chromatin Source: RGD
  • intracellular membrane-bounded organelle Source: RGD
  • nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3317337.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 972972Poly(ADP-ribose) glycohydrolasePRO_0000066604Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei69 – 691PhosphoserineBy similarity
Modified residuei135 – 1351PhosphoserineBy similarity
Modified residuei137 – 1371PhosphothreonineBy similarity
Modified residuei195 – 1951PhosphoserineBy similarity
Modified residuei197 – 1971PhosphothreonineBy similarity
Modified residuei256 – 2561PhosphoserineCombined sources
Modified residuei259 – 2591PhosphoserineCombined sources
Modified residuei281 – 2811PhosphoserineBy similarity
Modified residuei286 – 2861PhosphoserineCombined sources
Modified residuei293 – 2931PhosphoserineBy similarity
Modified residuei297 – 2971PhosphoserineBy similarity
Modified residuei311 – 3111PhosphoserineBy similarity
Modified residuei337 – 3371N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9QYM2.
PRIDEiQ9QYM2.

PTM databases

iPTMnetiQ9QYM2.
PhosphoSiteiQ9QYM2.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Interactioni

Subunit structurei

Interacts with PCNA. Interacts with NUDT5.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027071.

Structurei

Secondary structure

1
972
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi448 – 4525Combined sources
Helixi454 – 4563Combined sources
Turni460 – 4634Combined sources
Beta strandi476 – 4783Combined sources
Helixi482 – 4843Combined sources
Beta strandi493 – 4975Combined sources
Beta strandi503 – 5064Combined sources
Beta strandi516 – 5205Combined sources
Beta strandi522 – 5243Combined sources
Beta strandi526 – 5305Combined sources
Helixi531 – 5399Combined sources
Helixi546 – 55510Combined sources
Helixi558 – 5603Combined sources
Turni561 – 5633Combined sources
Helixi567 – 5748Combined sources
Helixi579 – 5879Combined sources
Helixi589 – 59810Combined sources
Helixi600 – 6034Combined sources
Beta strandi617 – 6226Combined sources
Helixi623 – 63412Combined sources
Beta strandi644 – 6463Combined sources
Turni648 – 6514Combined sources
Helixi658 – 6614Combined sources
Helixi668 – 68417Combined sources
Beta strandi690 – 6978Combined sources
Helixi704 – 7063Combined sources
Beta strandi714 – 7207Combined sources
Helixi722 – 7254Combined sources
Turni726 – 7283Combined sources
Beta strandi729 – 7357Combined sources
Turni739 – 7446Combined sources
Helixi750 – 7578Combined sources
Helixi759 – 7635Combined sources
Helixi764 – 7674Combined sources
Beta strandi775 – 7806Combined sources
Beta strandi786 – 7905Combined sources
Helixi792 – 7943Combined sources
Beta strandi796 – 8005Combined sources
Beta strandi816 – 8216Combined sources
Helixi828 – 8325Combined sources
Helixi834 – 84815Combined sources
Helixi855 – 8573Combined sources
Beta strandi861 – 8644Combined sources
Helixi875 – 88814Combined sources
Beta strandi893 – 8964Combined sources
Helixi901 – 91616Combined sources
Helixi921 – 93515Combined sources
Turni936 – 9383Combined sources
Beta strandi941 – 9433Combined sources
Helixi948 – 95710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UEKX-ray1.95A385-972[»]
3UELX-ray3.00A/B/C385-972[»]
ProteinModelPortaliQ9QYM2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 452452A-domainBy similarityAdd
BLAST
Regioni605 – 790186CatalyticBy similarityAdd
BLAST
Regioni722 – 7232Substrate binding
Regioni865 – 8706Substrate binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi10 – 167Nuclear localization signalBy similarity
Motifi77 – 848PIP-box (PCNA interacting peptide)By similarity

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2064. Eukaryota.
ENOG410XT3Y. LUCA.
HOGENOMiHOG000168457.
HOVERGENiHBG053510.
InParanoidiQ9QYM2.
KOiK07759.
PhylomeDBiQ9QYM2.

Family and domain databases

InterProiIPR007724. Poly_GlycHdrlase.
[Graphical view]
PANTHERiPTHR12837. PTHR12837. 1 hit.
PfamiPF05028. PARG_cat. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9QYM2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAGPGCEPC TKRPRWGAAG TSAPTASDSR SFPGRQKRVL DPKDAPVQFR
60 70 80 90 100
VPPSSSACVS GRAGPHRGSV TSFVFKQKPI TTWMDTKGPK TAESESKENN
110 120 130 140 150
NTRTDPMMSS VQKDNFYPHK VEKLGNVPQL NLDKSPTEKS TPYLNQQQTA
160 170 180 190 200
GVCKWHSAGE RAEQLSASEP SAVTQAPKQL SNANIDQSPP TDGHSDTDHE
210 220 230 240 250
EDRDNQQFLT PVKLANAKQT VGDGQARSNC KCSASCQCGQ DCAGCQREEA
260 270 280 290 300
DVIPESPLSD VGAEDIGTGS KNDNKLTGQE SGLGDSPPFE KESEPESPMD
310 320 330 340 350
VDNSKTSCQD SEADEEASPV FDEQDDQDDR SSQTANKLSS RQAREVDGDL
360 370 380 390 400
RKRYLTKGSE IRLHFQFEGG SNAGTSDLNA KPSGNSSSLN VDGRSSKQHG
410 420 430 440 450
KRDSKITDHF VRIPKSEDKR KEQCEVRHQR AERKIPKYVP PNLPPDKKWL
460 470 480 490 500
GTPIEEMRKM PRCGVRLPLL RPSASHTVTV RVDLLRAGEV PKPFPTHYKD
510 520 530 540 550
LWDNKHVKMP CSEQNLYPVE DENGERTAGS RWELIQTALL NKFTRPQNLK
560 570 580 590 600
DAILKYNVAY SKKWDFTALV DFWDKVLEEA EAQHLYQSIL PDMVKIALCL
610 620 630 640 650
PNICTQPIPL LKQKMNHSVT MSQEQIASLL ANAFFCTFPR RNAKMKSEYS
660 670 680 690 700
SYPDINFNRL FEGRSSRKPE KLKTLFCYFR RVTEKKPTGL VTFTRQSLED
710 720 730 740 750
FPEWERCDKP LTRLHVTYEG TIEGNGRGML QVDFANRFVG GGVTGAGLVQ
760 770 780 790 800
EEIRFLINPE LIVSRLFTEV LDHNECLIIT GTEQYSEYTG YAETYRWARS
810 820 830 840 850
HEDGSEKDDW QRCCTEIVAI DALHFRRYLD QFVPEKVRRE LNKAYCGFLR
860 870 880 890 900
PGVPPENLSA VATGNWGCGA FGGDARLKAL IQLLAAAAAE RDVVYFTFGD
910 920 930 940 950
SELMRDIYSM HTFLTERKLN VGKVYRLLLR YYREECRDCS SPGPDTKLYP
960 970
FIYHAAESSA ETSDQPGQRT GT
Length:972
Mass (Da):109,003
Last modified:May 1, 2000 - v1
Checksum:i3DED7885684F59E9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB019366 mRNA. Translation: BAA87901.1.
RefSeqiNP_112629.1. NM_031339.1.
UniGeneiRn.13634.

Genome annotation databases

GeneIDi83507.
KEGGirno:83507.
UCSCiRGD:620387. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB019366 mRNA. Translation: BAA87901.1.
RefSeqiNP_112629.1. NM_031339.1.
UniGeneiRn.13634.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UEKX-ray1.95A385-972[»]
3UELX-ray3.00A/B/C385-972[»]
ProteinModelPortaliQ9QYM2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027071.

Chemistry

ChEMBLiCHEMBL3317337.

PTM databases

iPTMnetiQ9QYM2.
PhosphoSiteiQ9QYM2.

Proteomic databases

PaxDbiQ9QYM2.
PRIDEiQ9QYM2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi83507.
KEGGirno:83507.
UCSCiRGD:620387. rat.

Organism-specific databases

CTDi8505.
RGDi620387. Parg.

Phylogenomic databases

eggNOGiKOG2064. Eukaryota.
ENOG410XT3Y. LUCA.
HOGENOMiHOG000168457.
HOVERGENiHBG053510.
InParanoidiQ9QYM2.
KOiK07759.
PhylomeDBiQ9QYM2.

Miscellaneous databases

PROiQ9QYM2.

Family and domain databases

InterProiIPR007724. Poly_GlycHdrlase.
[Graphical view]
PANTHERiPTHR12837. PTHR12837. 1 hit.
PfamiPF05028. PARG_cat. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPARG_RAT
AccessioniPrimary (citable) accession number: Q9QYM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: May 1, 2000
Last modified: September 7, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.