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Reviewed, UniProtKB/Swiss-Prot O88622 (PARG_MOUSE)

Last modified October 13, 2009. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · 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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length969 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.

Sequence caution

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

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

Ontologies

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O88622-1)

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.
Isoform 2 (identifier: O88622-2)

The sequence of this isoform differs from the canonical sequence as follows:
     920-920: K → E
     921-969: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 969969Poly(ADP-ribose) glycohydrolase
PRO_0000066603

Regions

Motif10 – 167Nuclear localization signal By similarity

Amino acid modifications

Modified residue1351Phosphoserine Ref.4
Modified residue1371Phosphothreonine By similarity
Modified residue1951Phosphoserine By similarity
Modified residue1971Phosphothreonine By similarity
Modified residue2561Phosphoserine Ref.4
Modified residue2591Phosphoserine Ref.4
Modified residue3111Phosphoserine By similarity
Modified residue4961N6-acetyllysine By similarity

Natural variations

Alternative sequence9201K → E in isoform 2.
VSP_011771
Alternative sequence921 – 96949Missing in isoform 2.
VSP_011772

Experimental info

Sequence conflict13 – 142RP → A in AAC28735. Ref.1
Sequence conflict3051K → R in AAC28735. Ref.1
Sequence conflict3701A → V in BC050892. Ref.3
Sequence conflict3701A → V in BC059827. Ref.3
Sequence conflict8721A → V in BAC29519. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 25, 2004. Version 2.
Checksum: 2626996A53AC48ED

FASTA969109,324
        10         20         30         40         50         60 
MSAGPGWEPC TKRPRWGAAG TSAPTASDSR SFPGRQRRVL DPKDAPVQFR VPPSSPACVS 

        70         80         90        100        110        120 
GRAGPHRGNA TSFVFKQKTI TTWMDTKGPK TAESESKENN NTRIDSMMSS VQKDNFYPHK 

       130        140        150        160        170        180 
VEKLENVPQL NLDKSPTEKS SQYLNQQQTA SVCKWQNEGK HAEQLLASEP PAGTPLPKQL 

       190        200        210        220        230        240 
SNANIGQSPH TDDHSDTDHE EDRDNQQFLT PIKLANTKPT VGDGQARSNC KCSGSRQSVK 

       250        260        270        280        290        300 
DCTGCQQEEV DVLPESPLSD VGAEDIGTGP KNDNKLTGQE SSLGDSPPFE KESEPESPMD 

       310        320        330        340        350        360 
VDNSKNSCQD SEADEETSPV FDEQDDRSSQ TANKLSSCQA READGDLRKR YLTKGSEVRL 

       370        380        390        400        410        420 
HFQFEGENNA GTSDLNAKPS GNSSSLNVEC RSSKQHGKRD SKITDHFMRI SKSEDRRKEQ 

       430        440        450        460        470        480 
CEVRHQRTER KIPKYIPPNL PPEKKWLGTP IEEMRKMPRC GIHLPSLRPS ASHTVTVRVD 

       490        500        510        520        530        540 
LLRAGEVPKP FPTHYKDLWD NKHVKMPCSE QNLYPVEDEN GERTAGSRWE LIQTALLNKF 

       550        560        570        580        590        600 
TRPQNLKDAI LKYNVAYSKK WDFTALVDFW DKVLEEAEAQ HLYQSILPDM VKIALCLPNI 

       610        620        630        640        650        660 
CTQPIPLLKQ KMNHSVTMSQ EQIASLLANA FFCTFPRRNA KMKSEYSSYP DINFNRLFEG 

       670        680        690        700        710        720 
RSSRKPEKLK TLFCYFRRVT EKKPTGLVTF TRQSLEDFPE WERCEKPLTR LHVTYEGTIE 

       730        740        750        760        770        780 
GNGRGMLQVD FANRFVGGGV TGAGLVQEEI RFLINPELIV SRLFTEVLDH NECLIITGTE 

       790        800        810        820        830        840 
QYSEYTGYAE TYRWARSHED GSEKDDWQRR CTEIVAIDAL HFRRYLDQFV PEKVRRELNK 

       850        860        870        880        890        900 
AYCGFLRPGV PSENLSAVAT GNWGCGAFGG DARLKALIQI LAAAAAERDV VYFTFGDSEL 

       910        920        930        940        950        960 
MRDIYSMHTF LTERKLDVGK VYKLLLRYYN EECRNCSTPG PDIKLYPFIY HAVESSAETT 


DMPGQKAGT 

« Hide

Isoform 2.

Checksum: 2EA3C15C421B09A1
Show »

FASTA920103,771

References

« Hide 'large scale' references
[1]"Assignment of the poly(ADP-ribose) glycohydrolase gene (PARG) to human chromosome 10q11.23 and mouse chromosome 14B by in situ hybridization."
Ame J.-C., Apiou F., Jacobson E.L., Jacobson M.K.
Cytogenet. Cell Genet. 85:269-270(1999) [PubMed: 10449915] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Bone.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6.
Tissue: Brain.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135; SER-256 AND SER-259, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF079557 mRNA. Translation: AAC28735.1.
AK036656 mRNA. Translation: BAC29519.1.
BC050892 mRNA. No translation available.
BC059827 mRNA. No translation available.
IPIIPI00471055.
IPI00471056.
UniGeneMm.15962

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGO88622.

PTM databases

PhosphoSiteO88622.

Proteomic databases

PRIDEO88622.

Genome annotation databases

EnsemblENSMUST00000022470; ENSMUSP00000022470; ENSMUSG00000021911; Mus musculus. [Genome view]
UCSCuc007syq.1. mouse.

Organism-specific databases

MGIMGI:1347094. Parg.

Phylogenomic databases

HOGENOMO88622.
HOVERGENO88622.

Enzyme and pathway databases

BRENDA3.2.1.143. 244.

Gene expression databases

ArrayExpressO88622.
BgeeO88622.
CleanExMM_PARG.
GenevestigatorO88622.
GermOnlineENSMUSG00000021911. Mus musculus.

Family and domain databases

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

Other Resources

SOURCESearch...

Entry information

Entry namePARG_MOUSE
AccessionPrimary (citable) accession number: O88622
Secondary accession number(s): Q80YQ6, Q8CB72
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: October 25, 2004
Last modified: October 13, 2009
This is version 53 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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