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Poly(ADP-ribose) glycohydrolase (EC 3.2.1.143)

 PARG_HUMAN              Reviewed;         976 AA.
Q86W56; A5YBK3; B2RC24; B4DIU5; B4DYR4; I6RUV3; Q6E4P6; Q6E4P7;
Q7Z742; Q9Y4W7;
25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
30-AUG-2017, entry version 129.
RecName: Full=Poly(ADP-ribose) glycohydrolase;
EC=3.2.1.143;
Name=PARG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Skin;
PubMed=14527731; DOI=10.1016/S0378-1119(03)00738-8;
Meyer R.G., Meyer-Ficca M.L., Jacobson E.L., Jacobson M.K.;
"Human poly(ADP-ribose) glycohydrolase (PARG) gene and the common
promoter sequence it shares with inner mitochondrial membrane
translocase 23 (TIM23).";
Gene 314:181-190(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), MUTAGENESIS OF LYS-12;
ARG-13; ARG-36 AND ARG-37, AND NUCLEAR LOCALIZATION SIGNAL.
TISSUE=Skin;
PubMed=15212953; DOI=10.1016/j.yexcr.2004.03.050;
Meyer-Ficca M.L., Meyer R.G., Coyle D.L., Jacobson E.L.,
Jacobson M.K.;
"Human poly(ADP-ribose) glycohydrolase is expressed in alternative
splice variants yielding isoforms that localize to different cell
compartments.";
Exp. Cell Res. 297:521-532(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10449915;
Ame J.-C., Apiou F., Jacobson E.L., Jacobson M.K.;
"Assignment of the poly(ADP-ribose) glycohydrolase gene (PARG) to
human chromosome 10q11.23 and mouse chromosome 14B by in situ
hybridization.";
Cytogenet. Cell Genet. 85:269-270(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND SUBCELLULAR LOCATION.
TISSUE=Testis;
PubMed=17509564; DOI=10.1016/j.yexcr.2007.03.043;
Meyer R.G., Meyer-Ficca M.L., Whatcott C.J., Jacobson E.L.,
Jacobson M.K.;
"Two small enzyme isoforms mediate mammalian mitochondrial poly(ADP-
ribose) glycohydrolase (PARG) activity.";
Exp. Cell Res. 313:2920-2936(2007).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE SPLICING (ISOFORMS
4 AND 5), ABSENCE OF CATALYTIC ACTIVITY (ISOFORMS 4 AND 5), AND
SUBCELLULAR LOCATION.
TISSUE=Peripheral blood monocyte;
PubMed=22433848; DOI=10.1074/jbc.M112.349183;
Niere M., Mashimo M., Agledal L., Dolle C., Kasamatsu A., Kato J.,
Moss J., Ziegler M.;
"ADP-ribosylhydrolase 3 (ARH3), not poly(ADP-ribose) glycohydrolase
(PARG) isoforms, is responsible for degradation of mitochondrial
matrix-associated poly(ADP-ribose).";
J. Biol. Chem. 287:16088-16102(2012).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Brain cortex, Hippocampus, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
SUBCELLULAR LOCATION (ISOFORMS 1 AND 2).
PubMed=16460818; DOI=10.1016/j.bbamcr.2005.11.015;
Haince J.F., Ouellet M.E., McDonald D., Hendzel M.J., Poirier G.G.;
"Dynamic relocation of poly(ADP-ribose) glycohydrolase isoforms during
radiation-induced DNA damage.";
Biochim. Biophys. Acta 1763:226-237(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; SER-137; SER-197
AND THR-199, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
PHOSPHORYLATION AT SER-197; THR-199 AND SER-298.
PubMed=19105632; DOI=10.1021/pr800810n;
Gagne J.P., Moreel X., Gagne P., Labelle Y., Droit A.,
Chevalier-Pare M., Bourassa S., McDonald D., Hendzel M.J., Prigent C.,
Poirier G.G.;
"Proteomic investigation of phosphorylation sites in poly(ADP-ribose)
polymerase-1 and poly(ADP-ribose) glycohydrolase.";
J. Proteome Res. 8:1014-1029(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND THR-199, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
SUBCELLULAR LOCATION (ISOFORM 1), AND INTERACTION WITH PCNA.
PubMed=21398629; DOI=10.1093/nar/gkr099;
Mortusewicz O., Fouquerel E., Ame J.C., Leonhardt H., Schreiber V.;
"PARG is recruited to DNA damage sites through poly(ADP-ribose)- and
PCNA-dependent mechanisms.";
Nucleic Acids Res. 39:5045-5056(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[17]
FUNCTION.
PubMed=23102699; DOI=10.1016/j.molcel.2012.09.021;
Le May N., Iltis I., Ame J.C., Zhovmer A., Biard D., Egly J.M.,
Schreiber V., Coin F.;
"Poly (ADP-ribose) glycohydrolase regulates retinoic acid receptor-
mediated gene expression.";
Mol. Cell 48:785-798(2012).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-68; SER-133;
SER-137; THR-139; SER-286; SER-291; SER-302; SER-316 AND SER-448, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261 AND SER-264, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
FUNCTION, AND INTERACTION WITH NUDT5.
PubMed=27257257; DOI=10.1126/science.aad9335;
Wright R.H., Lioutas A., Le Dily F., Soronellas D., Pohl A., Bonet J.,
Nacht A.S., Samino S., Font-Mateu J., Vicent G.P., Wierer M.,
Trabado M.A., Schelhorn C., Carolis C., Macias M.J., Yanes O.,
Oliva B., Beato M.;
"ADP-ribose-derived nuclear ATP synthesis by NUDIX5 is required for
chromatin remodeling.";
Science 352:1221-1225(2016).
[22]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 448-976 ALONE AND IN COMPLEX
WITH INHIBITORS, ACTIVE SITE, AND SUBSTRATE-BINDING SITES.
PubMed=23251397; DOI=10.1371/journal.pone.0050889;
Tucker J.A., Bennett N., Brassington C., Durant S.T., Hassall G.,
Holdgate G., McAlister M., Nissink J.W., Truman C., Watson M.;
"Structures of the human poly (ADP-ribose) glycohydrolase catalytic
domain confirm catalytic mechanism and explain inhibition by ADP-HPD
derivatives.";
PLoS ONE 7:E50889-E50889(2012).
-!- FUNCTION: Poly(ADP-ribose) synthesized after DNA damage is only
present transiently and is rapidly degraded by poly(ADP-ribose)
glycohydrolase (PubMed:23102699). PARG acts both as an endo- and
exoglycosidase, releasing PAR of different length as well as ADP-
ribose monomers (PubMed:23102699). Required for retinoid acid-
dependent gene transactivation, probably by dePARsylating histone
demethylase KDM4D, allowing chromatin derepression at RAR-
dependent gene promoters (PubMed:23102699). Involved in the
synthesis of ATP in the nucleus, together with PARP1, NMNAT1 and
NUDT5 (PubMed:27257257). Nuclear ATP generation is required for
extensive chromatin remodeling events that are energy-consuming
(PubMed:27257257). {ECO:0000269|PubMed:23102699,
ECO:0000269|PubMed:27257257}.
-!- CATALYTIC ACTIVITY: Hydrolyzes poly(ADP-D-ribose) at glycosidic
(1''-2') linkage of ribose-ribose bond to produce free ADP-D-
ribose.
-!- SUBUNIT: Interacts with PCNA (PubMed:21398629). Interacts with
NUDT5 (PubMed:27257257). {ECO:0000269|PubMed:21398629,
ECO:0000269|PubMed:27257257}.
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus
{ECO:0000269|PubMed:16460818, ECO:0000269|PubMed:21398629}.
Note=Colocalizes with PCNA at replication foci. Relocalizes to the
cytoplasm in response to DNA damage.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm
{ECO:0000269|PubMed:16460818}. Note=Translocates to the nucleus in
response to DNA damage.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform 4: Cytoplasm. Mitochondrion.
-!- SUBCELLULAR LOCATION: Isoform 5: Mitochondrion matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=hPARG111;
IsoId=Q86W56-1; Sequence=Displayed;
Name=2; Synonyms=hPARG102;
IsoId=Q86W56-2; Sequence=VSP_011769;
Note=Contains a N-acetylmethionine at position 1.
{ECO:0000244|PubMed:22814378};
Name=3; Synonyms=hPARG99;
IsoId=Q86W56-3; Sequence=VSP_011770;
Name=4; Synonyms=hPARG60;
IsoId=Q86W56-4; Sequence=VSP_044675, VSP_044676, VSP_044677;
Note=Catalytically inactive.;
Name=5; Synonyms=hPARG55;
IsoId=Q86W56-5; Sequence=VSP_044674, VSP_044677;
Note=Catalytically inactive.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:14527731}.
-!- DOMAIN: The PIP-box mediates interaction with PCNA and
localization to replication foci.
-!- SIMILARITY: Belongs to the poly(ADP-ribose) glycohydrolase family.
{ECO:0000305}.
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EMBL; AY258587; AAP83314.1; -; mRNA.
EMBL; AY575848; AAT66421.1; -; mRNA.
EMBL; AY575849; AAT66422.1; -; mRNA.
EMBL; AF005043; AAB61614.1; -; mRNA.
EMBL; EF382674; ABR10027.1; -; mRNA.
EMBL; JQ890226; AFM56043.1; -; mRNA.
EMBL; AK295786; BAG58607.1; -; mRNA.
EMBL; AK302560; BAG63826.1; -; mRNA.
EMBL; AK314909; BAG37421.1; -; mRNA.
EMBL; BC050560; AAH50560.1; -; mRNA.
EMBL; BC052966; AAH52966.1; -; mRNA.
CCDS; CCDS73130.1; -. [Q86W56-1]
RefSeq; NP_001289706.1; NM_001302777.1.
RefSeq; NP_001290415.1; NM_001303486.1. [Q86W56-2]
RefSeq; NP_001290416.1; NM_001303487.1. [Q86W56-3]
RefSeq; NP_001311310.1; NM_001324381.1. [Q86W56-2]
RefSeq; NP_003622.2; NM_003631.3. [Q86W56-1]
UniGene; Hs.10136; -.
UniGene; Hs.535298; -.
UniGene; Hs.732225; -.
PDB; 4A0D; X-ray; 1.75 A; A=448-976.
PDB; 4B1G; X-ray; 1.83 A; A=448-976.
PDB; 4B1H; X-ray; 2.00 A; A=448-976.
PDB; 4B1I; X-ray; 2.14 A; A=448-976.
PDB; 4B1J; X-ray; 2.08 A; A=448-976.
PDB; 5A7R; X-ray; 1.95 A; A=448-976.
PDB; 5LHB; X-ray; 2.23 A; A=448-976.
PDBsum; 4A0D; -.
PDBsum; 4B1G; -.
PDBsum; 4B1H; -.
PDBsum; 4B1I; -.
PDBsum; 4B1J; -.
PDBsum; 5A7R; -.
PDBsum; 5LHB; -.
ProteinModelPortal; Q86W56; -.
SMR; Q86W56; -.
BioGrid; 114077; 7.
IntAct; Q86W56; 2.
STRING; 9606.ENSP00000384408; -.
BindingDB; Q86W56; -.
ChEMBL; CHEMBL1795143; -.
iPTMnet; Q86W56; -.
PhosphoSitePlus; Q86W56; -.
BioMuta; PARG; -.
DMDM; 56417893; -.
EPD; Q86W56; -.
MaxQB; Q86W56; -.
PaxDb; Q86W56; -.
PeptideAtlas; Q86W56; -.
PRIDE; Q86W56; -.
Ensembl; ENST00000402038; ENSP00000384408; ENSG00000227345. [Q86W56-1]
Ensembl; ENST00000616448; ENSP00000484285; ENSG00000227345. [Q86W56-1]
GeneID; 670; -.
GeneID; 8505; -.
KEGG; hsa:8505; -.
UCSC; uc057tfe.1; human. [Q86W56-1]
CTD; 670; -.
CTD; 8505; -.
DisGeNET; 670; -.
DisGeNET; 8505; -.
GeneCards; PARG; -.
H-InvDB; HIX0127080; -.
HGNC; HGNC:8605; PARG.
HPA; HPA021819; -.
HPA; HPA053007; -.
MIM; 603501; gene.
neXtProt; NX_Q86W56; -.
OpenTargets; ENSG00000227345; -.
PharmGKB; PA32940; -.
eggNOG; KOG2064; Eukaryota.
eggNOG; ENOG410XT3Y; LUCA.
GeneTree; ENSGT00390000003652; -.
HOVERGEN; HBG053510; -.
InParanoid; Q86W56; -.
KO; K07759; -.
OMA; NAGPGCE; -.
OrthoDB; EOG091G01FM; -.
PhylomeDB; Q86W56; -.
TreeFam; TF323527; -.
BRENDA; 3.2.1.143; 2681.
Reactome; R-HSA-110362; POLB-Dependent Long Patch Base Excision Repair.
ChiTaRS; PARG; human.
GeneWiki; PARG; -.
PMAP-CutDB; Q86W56; -.
PRO; PR:Q86W56; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000227345; -.
CleanEx; HS_PARG; -.
ExpressionAtlas; Q86W56; baseline and differential.
Genevisible; Q86W56; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:CACAO.
GO; GO:0004649; F:poly(ADP-ribose) glycohydrolase activity; IDA:UniProtKB.
GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; IDA:UniProtKB.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
InterPro; IPR007724; Poly_GlycHdrlase.
PANTHER; PTHR12837; PTHR12837; 1.
Pfam; PF05028; PARG_cat; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Hydrolase; Mitochondrion; Nucleus; Phosphoprotein;
Reference proteome.
CHAIN 1 976 Poly(ADP-ribose) glycohydrolase.
/FTId=PRO_0000066602.
REGION 1 456 A-domain.
REGION 610 795 Catalytic.
REGION 726 727 Substrate binding.
REGION 869 874 Substrate binding.
MOTIF 10 16 Nuclear localization signal.
{ECO:0000269|PubMed:15212953}.
MOTIF 76 83 PIP-box (PCNA interacting peptide).
ACT_SITE 737 737 {ECO:0000269|PubMed:23251397}.
ACT_SITE 755 755 {ECO:0000269|PubMed:23251397}.
ACT_SITE 756 756 {ECO:0000269|PubMed:23251397}.
BINDING 740 740 Substrate.
BINDING 754 754 Substrate; via amide nitrogen.
BINDING 795 795 Substrate. {ECO:0000250}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 68 68 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 133 133 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 137 137 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 139 139 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 197 197 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:19105632}.
MOD_RES 199 199 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:19105632}.
MOD_RES 261 261 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 264 264 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 286 286 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 291 291 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 298 298 Phosphoserine.
{ECO:0000269|PubMed:19105632}.
MOD_RES 302 302 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 316 316 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 340 340 N6-acetyllysine.
{ECO:0000250|UniProtKB:O88622}.
MOD_RES 448 448 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 460 Missing (in isoform 5).
{ECO:0000303|PubMed:17509564}.
/FTId=VSP_044674.
VAR_SEQ 1 108 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15212953}.
/FTId=VSP_011770.
VAR_SEQ 1 82 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15212953}.
/FTId=VSP_011769.
VAR_SEQ 1 15 MNAGPGCEPCTKRPR -> MVQAGAEKDAQSISL (in
isoform 4).
{ECO:0000303|PubMed:22433848}.
/FTId=VSP_044675.
VAR_SEQ 16 423 Missing (in isoform 4).
{ECO:0000303|PubMed:22433848}.
/FTId=VSP_044676.
VAR_SEQ 485 526 RVDLLRAGEVPKPFPTHYKDLWDNKHVKMPCSEQNLYPVED
E -> W (in isoform 4 and isoform 5).
{ECO:0000303|PubMed:17509564,
ECO:0000303|PubMed:22433848}.
/FTId=VSP_044677.
MUTAGEN 12 12 K->A: Abolishes nuclear targeting; when
associated with G-13.
{ECO:0000269|PubMed:15212953}.
MUTAGEN 13 13 R->G: Abolishes nuclear targeting; when
associated with A-12.
{ECO:0000269|PubMed:15212953}.
MUTAGEN 36 36 R->A: No effect.
{ECO:0000269|PubMed:15212953}.
MUTAGEN 37 37 R->G: No effect.
{ECO:0000269|PubMed:15212953}.
CONFLICT 13 14 RP -> AT (in Ref. 3; AAB61614).
{ECO:0000305}.
CONFLICT 61 61 R -> Q (in Ref. 3; AAB61614).
{ECO:0000305}.
CONFLICT 127 127 E -> V (in Ref. 3; AAB61614).
{ECO:0000305}.
CONFLICT 138 138 P -> L (in Ref. 3; AAB61614).
{ECO:0000305}.
CONFLICT 227 227 Q -> H (in Ref. 3; AAB61614).
{ECO:0000305}.
CONFLICT 242 242 D -> H (in Ref. 3; AAB61614).
{ECO:0000305}.
CONFLICT 260 260 E -> K (in Ref. 3; AAB61614).
{ECO:0000305}.
CONFLICT 275 275 P -> S (in Ref. 3; AAB61614).
{ECO:0000305}.
CONFLICT 282 282 T -> I (in Ref. 3; AAB61614).
{ECO:0000305}.
CONFLICT 414 414 F -> L (in Ref. 3; AAB61614).
{ECO:0000305}.
CONFLICT 466 466 R -> Q (in Ref. 5; AFM56043).
{ECO:0000305}.
CONFLICT 484 484 I -> V (in Ref. 5; AFM56043).
{ECO:0000305}.
CONFLICT 814 815 WQ -> CE (in Ref. 3; AAB61614).
{ECO:0000305}.
CONFLICT 817 817 R -> H (in Ref. 7; AAH52966).
{ECO:0000305}.
STRAND 452 456 {ECO:0000244|PDB:4A0D}.
HELIX 458 460 {ECO:0000244|PDB:4A0D}.
TURN 464 467 {ECO:0000244|PDB:4A0D}.
STRAND 480 482 {ECO:0000244|PDB:4A0D}.
HELIX 486 488 {ECO:0000244|PDB:4A0D}.
STRAND 497 501 {ECO:0000244|PDB:4A0D}.
STRAND 520 522 {ECO:0000244|PDB:4A0D}.
STRAND 532 534 {ECO:0000244|PDB:4A0D}.
HELIX 535 543 {ECO:0000244|PDB:4A0D}.
HELIX 550 559 {ECO:0000244|PDB:4A0D}.
HELIX 562 564 {ECO:0000244|PDB:4A0D}.
TURN 565 567 {ECO:0000244|PDB:4A0D}.
HELIX 571 579 {ECO:0000244|PDB:4A0D}.
HELIX 583 591 {ECO:0000244|PDB:4A0D}.
HELIX 593 602 {ECO:0000244|PDB:4A0D}.
HELIX 604 607 {ECO:0000244|PDB:4A0D}.
STRAND 621 626 {ECO:0000244|PDB:4A0D}.
HELIX 627 638 {ECO:0000244|PDB:4A0D}.
TURN 652 655 {ECO:0000244|PDB:4A0D}.
HELIX 662 665 {ECO:0000244|PDB:4A0D}.
HELIX 672 688 {ECO:0000244|PDB:4A0D}.
STRAND 694 701 {ECO:0000244|PDB:4A0D}.
HELIX 708 710 {ECO:0000244|PDB:4A0D}.
STRAND 718 724 {ECO:0000244|PDB:4A0D}.
HELIX 726 729 {ECO:0000244|PDB:4A0D}.
TURN 730 732 {ECO:0000244|PDB:4A0D}.
STRAND 733 739 {ECO:0000244|PDB:4A0D}.
TURN 743 750 {ECO:0000244|PDB:4A0D}.
HELIX 754 761 {ECO:0000244|PDB:4A0D}.
HELIX 763 767 {ECO:0000244|PDB:4A0D}.
HELIX 768 771 {ECO:0000244|PDB:4A0D}.
STRAND 779 784 {ECO:0000244|PDB:4A0D}.
STRAND 790 793 {ECO:0000244|PDB:4A0D}.
HELIX 796 798 {ECO:0000244|PDB:4A0D}.
STRAND 800 804 {ECO:0000244|PDB:4A0D}.
STRAND 815 818 {ECO:0000244|PDB:5A7R}.
STRAND 820 825 {ECO:0000244|PDB:4A0D}.
HELIX 832 836 {ECO:0000244|PDB:4A0D}.
HELIX 838 852 {ECO:0000244|PDB:4A0D}.
HELIX 859 861 {ECO:0000244|PDB:4A0D}.
STRAND 865 868 {ECO:0000244|PDB:4A0D}.
HELIX 873 875 {ECO:0000244|PDB:4B1G}.
HELIX 879 892 {ECO:0000244|PDB:4A0D}.
STRAND 897 900 {ECO:0000244|PDB:4A0D}.
HELIX 905 920 {ECO:0000244|PDB:4A0D}.
HELIX 925 939 {ECO:0000244|PDB:4A0D}.
TURN 940 942 {ECO:0000244|PDB:4A0D}.
STRAND 945 947 {ECO:0000244|PDB:4A0D}.
HELIX 952 961 {ECO:0000244|PDB:4A0D}.
SEQUENCE 976 AA; 111110 MW; D6646353C6D0180E CRC64;
MNAGPGCEPC TKRPRWGAAT TSPAASDARS FPSRQRRVLD PKDAHVQFRV PPSSPACVPG
RAGQHRGSAT SLVFKQKTIT SWMDTKGIKT AESESLDSKE NNNTRIESMM SSVQKDNFYQ
HNVEKLENVS QLSLDKSPTE KSTQYLNQHQ TAAMCKWQNE GKHTEQLLES EPQTVTLVPE
QFSNANIDRS PQNDDHSDTD SEENRDNQQF LTTVKLANAK QTTEDEQARE AKSHQKCSKS
CDPGEDCASC QQDEIDVVPE SPLSDVGSED VGTGPKNDNK LTRQESCLGN SPPFEKESEP
ESPMDVDNSK NSCQDSEADE ETSPGFDEQE DGSSSQTANK PSRFQARDAD IEFRKRYSTK
GGEVRLHFQF EGGESRTGMN DLNAKLPGNI SSLNVECRNS KQHGKKDSKI TDHFMRLPKA
EDRRKEQWET KHQRTERKIP KYVPPHLSPD KKWLGTPIEE MRRMPRCGIR LPLLRPSANH
TVTIRVDLLR AGEVPKPFPT HYKDLWDNKH VKMPCSEQNL YPVEDENGER TAGSRWELIQ
TALLNKFTRP QNLKDAILKY NVAYSKKWDF TALIDFWDKV LEEAEAQHLY QSILPDMVKI
ALCLPNICTQ PIPLLKQKMN HSITMSQEQI ASLLANAFFC TFPRRNAKMK SEYSSYPDIN
FNRLFEGRSS RKPEKLKTLF CYFRRVTEKK PTGLVTFTRQ SLEDFPEWER CEKPLTRLHV
TYEGTIEENG QGMLQVDFAN RFVGGGVTSA GLVQEEIRFL INPELIISRL FTEVLDHNEC
LIITGTEQYS EYTGYAETYR WSRSHEDGSE RDDWQRRCTE IVAIDALHFR RYLDQFVPEK
MRRELNKAYC GFLRPGVSSE NLSAVATGNW GCGAFGGDAR LKALIQILAA AAAERDVVYF
TFGDSELMRD IYSMHIFLTE RKLTVGDVYK LLLRYYNEEC RNCSTPGPDI KLYPFIYHAV
ESCAETADHS GQRTGT


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