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Reviewed, UniProtKB/Swiss-Prot Q9QYM2 (PARG_RAT)

Last modified October 13, 2009. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Poly(ADP-ribose) glycohydrolase
    EC=3.2.1.143
Gene names
Name: Parg
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length972 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. Poly(ADP-ribose) metabolism may be required for maintenance of the normal function of neuronal cells.

Catalytic activity

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

Subcellular location

Nucleus By similarity.

Tissue specificity

Ubiquitously expressed. Ref.1

Sequence similarities

Belongs to the poly(ADP-ribose) glycohydrolase family.

Ontologies

Keywords
   Cellular componentNucleus
   Molecular functionHydrolase
   PTMAcetylation
Phosphoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentchromatin

Inferred from direct assay. Source: RGD

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionchromatin binding

Inferred from direct assay. Source: RGD

poly(ADP-ribose) glycohydrolase activity

Inferred from direct assay. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 972972Poly(ADP-ribose) glycohydrolase
PRO_0000066604

Regions

Motif10 – 167Nuclear localization signal By similarity

Amino acid modifications

Modified residue1351Phosphoserine By similarity
Modified residue1371Phosphothreonine By similarity
Modified residue1951Phosphoserine By similarity
Modified residue1971Phosphothreonine By similarity
Modified residue2561Phosphoserine By similarity
Modified residue2591Phosphoserine By similarity
Modified residue3111Phosphoserine By similarity
Modified residue4991N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9QYM2-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 3DED7885684F59E9

FASTA972109,003
        10         20         30         40         50         60 
MSAGPGCEPC TKRPRWGAAG TSAPTASDSR SFPGRQKRVL DPKDAPVQFR VPPSSSACVS 

        70         80         90        100        110        120 
GRAGPHRGSV TSFVFKQKPI TTWMDTKGPK TAESESKENN NTRTDPMMSS VQKDNFYPHK 

       130        140        150        160        170        180 
VEKLGNVPQL NLDKSPTEKS TPYLNQQQTA GVCKWHSAGE RAEQLSASEP SAVTQAPKQL 

       190        200        210        220        230        240 
SNANIDQSPP TDGHSDTDHE EDRDNQQFLT PVKLANAKQT VGDGQARSNC KCSASCQCGQ 

       250        260        270        280        290        300 
DCAGCQREEA DVIPESPLSD VGAEDIGTGS KNDNKLTGQE SGLGDSPPFE KESEPESPMD 

       310        320        330        340        350        360 
VDNSKTSCQD SEADEEASPV FDEQDDQDDR SSQTANKLSS RQAREVDGDL RKRYLTKGSE 

       370        380        390        400        410        420 
IRLHFQFEGG SNAGTSDLNA KPSGNSSSLN VDGRSSKQHG KRDSKITDHF VRIPKSEDKR 

       430        440        450        460        470        480 
KEQCEVRHQR AERKIPKYVP PNLPPDKKWL GTPIEEMRKM PRCGVRLPLL RPSASHTVTV 

       490        500        510        520        530        540 
RVDLLRAGEV PKPFPTHYKD LWDNKHVKMP CSEQNLYPVE DENGERTAGS RWELIQTALL 

       550        560        570        580        590        600 
NKFTRPQNLK DAILKYNVAY SKKWDFTALV DFWDKVLEEA EAQHLYQSIL PDMVKIALCL 

       610        620        630        640        650        660 
PNICTQPIPL LKQKMNHSVT MSQEQIASLL ANAFFCTFPR RNAKMKSEYS SYPDINFNRL 

       670        680        690        700        710        720 
FEGRSSRKPE KLKTLFCYFR RVTEKKPTGL VTFTRQSLED FPEWERCDKP LTRLHVTYEG 

       730        740        750        760        770        780 
TIEGNGRGML QVDFANRFVG GGVTGAGLVQ EEIRFLINPE LIVSRLFTEV LDHNECLIIT 

       790        800        810        820        830        840 
GTEQYSEYTG YAETYRWARS HEDGSEKDDW QRCCTEIVAI DALHFRRYLD QFVPEKVRRE 

       850        860        870        880        890        900 
LNKAYCGFLR PGVPPENLSA VATGNWGCGA FGGDARLKAL IQLLAAAAAE RDVVYFTFGD 

       910        920        930        940        950        960 
SELMRDIYSM HTFLTERKLN VGKVYRLLLR YYREECRDCS SPGPDTKLYP FIYHAAESSA 

       970 
ETSDQPGQRT GT 

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References

[1]"Isolation and cloning of rat poly(ADP-ribose) glycohydrolase: presence of a potential nuclear export signal conserved in mammalian orthologs."
Shimokawa T., Masutani M., Nagasawa S., Nozaki T., Ikota N., Aoki Y., Nakagama H., Sugimura T.
J. Biochem. 126:748-755(1999) [PubMed: 10502684] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 543-550; 556-562 AND 948-957, TISSUE SPECIFICITY.
Strain: Buffalo.
Tissue: Colon.
+Additional computationally mapped references.

Cross-references

Sequence databases

AB019366 mRNA. Translation: BAA87901.1.
IPIIPI00214269.
RefSeqNP_112629.1.
UniGeneRn.13634

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ9QYM2.

Genome annotation databases

EnsemblENSRNOT00000027071; ENSRNOP00000027071; ENSRNOG00000019978; Rattus norvegicus. [Genome view]
GeneID83507.
KEGGrno:83507.
UCSCNM_031339. rat.

Organism-specific databases

CTD83507.
RGD620387. Parg.

Phylogenomic databases

HOVERGENQ9QYM2.

Enzyme and pathway databases

BRENDA3.2.1.143. 248.

Gene expression databases

ArrayExpressQ9QYM2.
GenevestigatorQ9QYM2.
GermOnlineENSRNOG00000019978. Rattus norvegicus.

Family and domain databases

InterProIPR007724. Poly_GlycHdrlase.
[Graphical view]
PANTHERPTHR12837. Poly_glchydro. 1 hit.
PfamPF05028. PARG_cat. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio615942.

Entry information

Entry namePARG_RAT
AccessionPrimary (citable) accession number: Q9QYM2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: May 1, 2000
Last modified: October 13, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents