Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot O02776 (PARG_BOVIN)

Last modified October 13, 2009. Version 47. 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
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length977 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.

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 componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionpoly(ADP-ribose) glycohydrolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 977977Poly(ADP-ribose) glycohydrolase
PRO_0000066601

Regions

Motif10 – 167Nuclear localization signal By similarity

Amino acid modifications

Modified residue1381Phosphoserine By similarity
Modified residue1981Phosphoserine By similarity
Modified residue2001Phosphothreonine By similarity
Modified residue2621Phosphoserine By similarity
Modified residue2651Phosphoserine By similarity
Modified residue3171Phosphoserine By similarity
Modified residue5041N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O02776-1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 87D2100F979DF377

FASTA977110,837
        10         20         30         40         50         60 
MSAGPGCEPC TKRPRWDAAA TSPPAASDAR SFPGRQRRVL DSKDAPVQFR VPPSSSGCAL 

        70         80         90        100        110        120 
GRAGQHRGSA TSLVFKQKTI TSWMDTKGIK TVESESLHSK ENNNTREESM MSSVQKDNFY 

       130        140        150        160        170        180 
QHNMEKLENV SQLGFDKSPV EKGTQYLKQH QTAAMCKWQN EGPHSERLLE SEPPAVTLVP 

       190        200        210        220        230        240 
EQFSNANVDQ SSPKDDHSDT NSEESRDNQQ FLTHVKLANA KQTMEDEQGR EARSHQKCGK 

       250        260        270        280        290        300 
ACHPAEACAG CQQEETDVVS ESPLSDTGSE DVGTGLKNAN RLNRQESSLG NSPPFEKESE 

       310        320        330        340        350        360 
PESPMDVDNS KNSCQDSEAD EETSPGFDEQ EDSSSAQTAN KPSRFQPREA DTELRKRSSA 

       370        380        390        400        410        420 
KGGEIRLHFQ FEGGESRAGM NDVNAKRPGS TSSLNVECRN SKQHGRKDSK ITDHFMRVPK 

       430        440        450        460        470        480 
AEDKRKEQCE MKHQRTERKI PKYIPPHLSP DKKWLGTPIE EMRRMPRCGI RLPPLRPSAN 

       490        500        510        520        530        540 
HTVTIRVDLL RIGEVPKPFP THFKDLWDNK HVKMPCSEQN LYPVEDENGE RAAGSRWELI 

       550        560        570        580        590        600 
QTALLNRLTR PQNLKDAILK YNVAYSKKWD FTALIDFWDK VLEEAEAQHL YQSILPDMVK 

       610        620        630        640        650        660 
IALCLPNICT QPIPLLKQKM NHSITMSQEQ IASLLANAFF CTFPRRNAKM KSEYSSYPDI 

       670        680        690        700        710        720 
NFNRLFEGRS SRKPEKLKTL FCYFRRVTEK KPTGLVTFTR QSLEDFPEWE RCEKLLTRLH 

       730        740        750        760        770        780 
VTYEGTIEGN GQGMLQVDFA NRFVGGGVTS AGLVQEEIRF LINPELIVSR LFTEVLDHNE 

       790        800        810        820        830        840 
CLIITGTEQY SEYTGYAETY RWARSHEDRS ERDDWQRRTT EIVAIDALHF RRYLDQFVPE 

       850        860        870        880        890        900 
KIRRELNKAY CGFLRPGVSS ENLSAVATGN WGCGAFGGDA RLKALIQILA AAVAERDVVY 

       910        920        930        940        950        960 
FTFGDSELMR DIYSMHTFLT ERKLTVGEVY KLLLRYYNEE CRNCSTPGPD IKLYPFIYHA 

       970 
VESCTQTTNQ PGQRTGA 

« Hide

References

[1]"Isolation and characterization of the cDNA encoding bovine poly(ADP-ribose) glycohydrolase."
Lin W., Ame J.-C., Aboul-Ela N., Jacobson E.L., Jacobson M.K.
J. Biol. Chem. 272:11895-11901(1997) [PubMed: 9115250] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 601-616; 760-801 AND 849-877.
Tissue: Thymus.

Cross-references

Sequence databases

U78975 mRNA. Translation: AAB53370.1.
IPIIPI00700481.
RefSeqNP_776563.1.
UniGeneBt.65122

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGO02776.

Genome annotation databases

EnsemblENSBTAT00000031269; ENSBTAP00000031225; ENSBTAG00000023018; Bos taurus. [Genome view]
GeneID281377.
KEGGbta:281377.

Organism-specific databases

CTD281377.

Phylogenomic databases

HOVERGENO02776.

Enzyme and pathway databases

BRENDA3.2.1.143. 251.

Family and domain databases

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

Entry information

Entry namePARG_BOVIN
AccessionPrimary (citable) accession number: O02776
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: July 1, 1997
Last modified: October 13, 2009
This is version 47 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