DPOLB_MOUSE
ID DPOLB_MOUSE Reviewed; 335 AA.
AC Q8K409; Q3UAB6; Q922Z7;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=DNA polymerase beta;
DE EC=2.7.7.7;
DE EC=4.2.99.-;
GN Name=Polb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:AAM49616.1};
RN [1] {ECO:0000312|EMBL:AAM49616.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/Ola {ECO:0000312|EMBL:AAM49616.1};
RA Poltoratsky V.P., Wilson S.H.;
RT "Sequence of mouse DNA polymerase beta.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, Bone marrow, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland, and Testis {ECO:0000312|EMBL:AAH60998.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-72, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Repair polymerase that plays a key role in base-excision
CC repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that
CC removes the 5' sugar phosphate and also acts as a DNA polymerase that
CC adds one nucleotide to the 3' end of the arising single-nucleotide gap.
CC Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion
CC rather than in a processive fashion as for other DNA polymerases (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P06766};
CC Note=Binds 2 magnesium ions per subunit.
CC {ECO:0000250|UniProtKB:P06766};
CC -!- SUBUNIT: Monomer. Interacts with APEX1, HUWE1/ARF-BP1, STUB1/CHIP and
CC USP47 (By similarity). Interacts with FAM168A (By similarity).
CC {ECO:0000250|UniProtKB:P06746}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Cytoplasmic in normal conditions. Translocates to the nucleus
CC following DNA damage (By similarity). {ECO:0000250}.
CC -!- DOMAIN: Residues 239-252 form a flexible loop which appears to affect
CC the polymerase fidelity. {ECO:0000250}.
CC -!- PTM: Methylation by PRMT6 stimulates the polymerase activity by
CC enhancing DNA binding and processivity. {ECO:0000250}.
CC -!- PTM: Ubiquitinated at Lys-41, Lys-61 and Lys-81: monoubiquitinated by
CC HUWE1/ARF-BP1. Monoubiquitinated protein is then the target of
CC STUB1/CHIP, which catalyzes polyubiquitination from monoubiquitin,
CC leading to degradation by the proteasome. USP47 mediates the
CC deubiquitination of monoubiquitinated protein, preventing
CC polyubiquitination by STUB1/CHIP and its subsequent degradation (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06681.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF513911; AAM49616.1; -; mRNA.
DR EMBL; AK077127; BAC36630.1; -; mRNA.
DR EMBL; AK146745; BAE27405.1; -; mRNA.
DR EMBL; AK151436; BAE30399.1; -; mRNA.
DR EMBL; BC006681; AAH06681.1; ALT_SEQ; mRNA.
DR EMBL; BC060998; AAH60998.1; -; mRNA.
DR CCDS; CCDS22181.1; -.
DR RefSeq; NP_035260.1; NM_011130.2.
DR AlphaFoldDB; Q8K409; -.
DR BMRB; Q8K409; -.
DR SMR; Q8K409; -.
DR BioGRID; 202289; 8.
DR IntAct; Q8K409; 1.
DR STRING; 10090.ENSMUSP00000033938; -.
DR BindingDB; Q8K409; -.
DR ChEMBL; CHEMBL4565; -.
DR iPTMnet; Q8K409; -.
DR PhosphoSitePlus; Q8K409; -.
DR EPD; Q8K409; -.
DR MaxQB; Q8K409; -.
DR PaxDb; Q8K409; -.
DR PeptideAtlas; Q8K409; -.
DR PRIDE; Q8K409; -.
DR ProteomicsDB; 279807; -.
DR Antibodypedia; 3175; 407 antibodies from 35 providers.
DR DNASU; 18970; -.
DR Ensembl; ENSMUST00000033938; ENSMUSP00000033938; ENSMUSG00000031536.
DR GeneID; 18970; -.
DR KEGG; mmu:18970; -.
DR UCSC; uc009ldk.2; mouse.
DR CTD; 5423; -.
DR MGI; MGI:97740; Polb.
DR VEuPathDB; HostDB:ENSMUSG00000031536; -.
DR eggNOG; KOG2534; Eukaryota.
DR GeneTree; ENSGT00940000156918; -.
DR HOGENOM; CLU_008698_1_0_1; -.
DR InParanoid; Q8K409; -.
DR OMA; ITDMLME; -.
DR OrthoDB; 1328151at2759; -.
DR PhylomeDB; Q8K409; -.
DR TreeFam; TF103002; -.
DR BRENDA; 4.2.99.B1; 3474.
DR Reactome; R-MMU-110362; POLB-Dependent Long Patch Base Excision Repair.
DR Reactome; R-MMU-110373; Resolution of AP sites via the multiple-nucleotide patch replacement pathway.
DR Reactome; R-MMU-110381; Resolution of AP sites via the single-nucleotide replacement pathway.
DR Reactome; R-MMU-5649702; APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
DR Reactome; R-MMU-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-73930; Abasic sugar-phosphate removal via the single-nucleotide replacement pathway.
DR BioGRID-ORCS; 18970; 10 hits in 110 CRISPR screens.
DR ChiTaRS; Polb; mouse.
DR PRO; PR:Q8K409; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8K409; protein.
DR Bgee; ENSMUSG00000031536; Expressed in spermatid and 271 other tissues.
DR ExpressionAtlas; Q8K409; baseline and differential.
DR Genevisible; Q8K409; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005876; C:spindle microtubule; ISO:MGI.
DR GO; GO:0000795; C:synaptonemal complex; TAS:MGI.
DR GO; GO:0003684; F:damaged DNA binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0016829; F:lyase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0006284; P:base-excision repair; ISS:UniProtKB.
DR GO; GO:0006287; P:base-excision repair, gap-filling; IMP:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI.
DR GO; GO:0071707; P:immunoglobulin heavy chain V-D-J recombination; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
DR GO; GO:0048535; P:lymph node development; IMP:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IGI:MGI.
DR GO; GO:0006290; P:pyrimidine dimer repair; ISO:MGI.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:MGI.
DR GO; GO:0016445; P:somatic diversification of immunoglobulins; IMP:MGI.
DR GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; IMP:MGI.
DR GO; GO:0048536; P:spleen development; IMP:MGI.
DR CDD; cd00141; NT_POLXc; 1.
DR Gene3D; 1.10.150.110; -; 1.
DR Gene3D; 3.30.210.10; -; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR002054; DNA-dir_DNA_pol_X.
DR InterPro; IPR019843; DNA_pol-X_BS.
DR InterPro; IPR010996; DNA_pol_b-like_N.
DR InterPro; IPR028207; DNA_pol_B_palm_palm.
DR InterPro; IPR018944; DNA_pol_lambd_fingers_domain.
DR InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR InterPro; IPR037160; DNA_Pol_thumb_sf.
DR InterPro; IPR022312; DNA_pol_X.
DR InterPro; IPR002008; DNA_pol_X_beta-like.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR029398; PolB_thumb.
DR PANTHER; PTHR11276; PTHR11276; 1.
DR Pfam; PF14792; DNA_pol_B_palm; 1.
DR Pfam; PF14791; DNA_pol_B_thumb; 1.
DR Pfam; PF10391; DNA_pol_lambd_f; 1.
DR Pfam; PF14716; HHH_8; 1.
DR PRINTS; PR00869; DNAPOLX.
DR PRINTS; PR00870; DNAPOLXBETA.
DR SMART; SM00278; HhH1; 2.
DR SMART; SM00483; POLXc; 1.
DR SUPFAM; SSF47802; SSF47802; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS00522; DNA_POLYMERASE_X; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; DNA damage; DNA repair; DNA replication;
KW DNA synthesis; DNA-binding; DNA-directed DNA polymerase; Isopeptide bond;
KW Lyase; Magnesium; Metal-binding; Methylation; Nucleotidyltransferase;
KW Nucleus; Reference proteome; Sodium; Transferase; Ubl conjugation.
FT CHAIN 1..335
FT /note="DNA polymerase beta"
FT /id="PRO_0000218779"
FT REGION 183..192
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 72
FT /note="Schiff-base intermediate with DNA"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 72
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 83
FT /note="Omega-N-methylarginine; by PRMT6"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT MOD_RES 152
FT /note="Omega-N-methylarginine; by PRMT6"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT CROSSLNK 41
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT CROSSLNK 61
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT CROSSLNK 81
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P06746"
SQ SEQUENCE 335 AA; 38288 MW; 41E62348DC766A39 CRC64;
MSKRKAPQET LNGGITDMLV ELANFEKNVS QAIHKYNAYR KAASVIAKYP HKIKSGAEAK
KLPGVGTKIA EKIDEFLATG KLRKLEKIRQ DDTSSSINFL TRVTGIGPSA ARKFVDEGIK
TLEDLRKNED KLNHHQRIGL KYFEDFEKRI PREEMLQMQD IVLNEIKKVD SEYIATVCGS
FRRGAESSGD MDVLLTHPNF TSESSKQPKL LHRVVEQLQK VHFITDTLSK GETKFMGVCQ
LPSEKDGKEY PHRRIDIRLI PKDQYYCGVL YFTGSDIFNK NMRAHALEKG FTINEYTIRP
LGVTGVAGEP LPVDSEQDIF DYIQWRYREP KDRSE
