ID DPOLB_RAT Reviewed; 335 AA.
AC P06766; Q4G081;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 24-JAN-2024, entry version 212.
DE RecName: Full=DNA polymerase beta {ECO:0000250|UniProtKB:P06746};
DE EC=2.7.7.7 {ECO:0000250|UniProtKB:P06746};
DE AltName: Full=5'-deoxyribose-phosphate lyase {ECO:0000250|UniProtKB:P06746};
DE Short=5'-dRP lyase {ECO:0000250|UniProtKB:P06746};
DE EC=4.2.99.- {ECO:0000250|UniProtKB:P06746};
DE AltName: Full=AP lyase {ECO:0000250|UniProtKB:P06746};
DE EC=4.2.99.18 {ECO:0000250|UniProtKB:P06746};
GN Name=Polb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3597402; DOI=10.1016/s0021-9258(18)48029-5;
RA Matsukage A., Nishikawa K., Ooi T., Seto Y., Yamaguchi M.;
RT "Homology between mammalian DNA polymerase beta and terminal
RT deoxynucleotidyltransferase.";
RL J. Biol. Chem. 262:8960-8962(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RA Konopinski R., Nowak R., Siedlecki J.A.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 18-335.
RX PubMed=2873575; DOI=10.1073/pnas.83.14.5106;
RA Zmudzka B.Z., Sengupta D., Matsukage A., Cobianchi F., Kumar P.,
RA Wilson S.H.;
RT "Structure of rat DNA polymerase beta revealed by partial amino acid
RT sequencing and cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:5106-5110(1986).
RN [5]
RP PARTIAL PROTEIN SEQUENCE, AND SEQUENCE REVISION TO 228.
RX PubMed=2404980; DOI=10.1016/s0021-9258(19)39949-1;
RA Kumar P., Widen S.G., Williams K.R., Kedar P., Karpel R.L., Wilson S.H.;
RT "Studies of the domain structure of mammalian DNA polymerase beta.
RT Identification of a discrete template binding domain.";
RL J. Biol. Chem. 265:2124-2131(1990).
RN [6]
RP IMPORTANCE OF ARG-183 IN PRIMER BINDING.
RX PubMed=2198936; DOI=10.1021/bi00473a005;
RA Date T., Yamamoto S., Tanihara K., Nishimoto Y., Liu N., Matsukage A.;
RT "Site-directed mutagenesis of recombinant rat DNA polymerase beta:
RT involvement of arginine-183 in primer recognition.";
RL Biochemistry 29:5027-5034(1990).
RN [7]
RP MUTAGENESIS OF ASP-190 AND ASP-192, AND IMPORTANCE OF ASP-190 AND ASP-192
RP IN PRIMER BINDING.
RX PubMed=2036395; DOI=10.1021/bi00235a023;
RA Date T., Yamamoto S., Tanihara K., Nishimoto Y., Matsukage A.;
RT "Aspartic acid residues at positions 190 and 192 of rat DNA polymerase beta
RT are involved in primer binding.";
RL Biochemistry 30:5286-5292(1991).
RN [8]
RP DNA-BINDING REGION.
RX PubMed=1420147; DOI=10.1021/bi00157a014;
RA Casas-Finet J.R., Kumar A., Karpel R.L., Wilson S.H.;
RT "Mammalian DNA polymerase beta: characterization of a 16-kDa transdomain
RT fragment containing the nucleic acid-binding activities of the native
RT enzyme.";
RL Biochemistry 31:10272-10280(1992).
RN [9]
RP MUTAGENESIS OF ASP-246, AND IMPORTANCE OF ASP-246 IN FIDELITY.
RX PubMed=14563842; DOI=10.1074/jbc.m309607200;
RA Dalal S., Kosa J.L., Sweasy J.B.;
RT "The D246V mutant of DNA polymerase beta misincorporates nucleotides:
RT evidence for a role for the flexible loop in DNA positioning within the
RT active site.";
RL J. Biol. Chem. 279:577-584(2004).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=8137427; DOI=10.1016/0092-8674(94)90388-3;
RA Davies J.F. II, Almassy R.J., Hostomska Z., Ferre R.A., Hostomsky Z.;
RT "2.3-A crystal structure of the catalytic domain of DNA polymerase beta.";
RL Cell 76:1123-1133(1994).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=7516581; DOI=10.1126/science.7516581;
RA Sawaya M.R., Pelletier H., Kumar A., Wilson S.H., Kraut J.;
RT "Crystal structure of rat DNA polymerase beta: evidence for a common
RT polymerase mechanism.";
RL Science 264:1930-1935(1994).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=8841120; DOI=10.1021/bi960790i;
RA Pelletier H., Sawaya M.R.;
RT "Characterization of the metal ion binding helix-hairpin-helix motifs in
RT human DNA polymerase beta by X-ray structural analysis.";
RL Biochemistry 35:12778-12787(1996).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=11330999; DOI=10.1021/bi002176j;
RA Arndt J.W., Gong W., Zhong X., Showalter A.K., Liu J., Dunlap C.A., Lin Z.,
RA Paxson C., Tsai M.-D., Chan M.K.;
RT "Insight into the catalytic mechanism of DNA polymerase beta: structures of
RT intermediate complexes.";
RL Biochemistry 40:5368-5375(2001).
RN [14]
RP STRUCTURE BY NMR OF 1-87.
RX PubMed=8639559; DOI=10.1021/bi952656o;
RA Liu D., Prasad R., Wilson S.H., DeRose E.F., Mullen G.P.;
RT "Three-dimensional solution structure of the N-terminal domain of DNA
RT polymerase beta and mapping of the ssDNA interaction interface.";
RL Biochemistry 35:6188-6200(1996).
RN [15]
RP STRUCTURE BY NMR OF 1-87.
RX PubMed=10656829; DOI=10.1006/jmbi.1999.3455;
RA Maciejewski M.W., Liu D., Prasad R., Wilson S.H., Mullen G.P.;
RT "Backbone dynamics and refined solution structure of the N-terminal domain
RT of DNA polymerase beta. Correlation with DNA binding and dRP lyase
RT activity.";
RL J. Mol. Biol. 296:229-253(2000).
CC -!- FUNCTION: Repair polymerase that plays a key role in base-excision
CC repair. During this process, the damaged base is excised by specific
CC DNA glycosylases, the DNA backbone is nicked at the abasic site by an
CC apurinic/apyrimidic (AP) endonuclease, and POLB removes 5'-deoxyribose-
CC phosphate from the preincised AP site acting as a 5'-deoxyribose-
CC phosphate lyase (5'-dRP lyase); through its DNA polymerase activity, it
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. It is
CC also able to cleave sugar-phosphate bonds 3' to an intact AP site,
CC acting as an AP lyase. {ECO:0000250|UniProtKB:P06746}.
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 Evidence={ECO:0000250|UniProtKB:P06746};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end 2'-deoxyribose-2'-deoxyribonucleotide-DNA = (2E,4S)-
CC 4-hydroxypenten-2-al-5-phosphate + a 5'-end 5'-monophospho-2'-
CC deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:76255, Rhea:RHEA-
CC COMP:13180, Rhea:RHEA-COMP:18657, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:136412, ChEBI:CHEBI:195194, ChEBI:CHEBI:195195;
CC Evidence={ECO:0000250|UniProtKB:P06746};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC 2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC ChEBI:CHEBI:167181; EC=4.2.99.18;
CC Evidence={ECO:0000250|UniProtKB:P06746};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P06746};
CC Note=Binds 2 magnesium ions per subunit.
CC {ECO:0000250|UniProtKB:P06746};
CC -!- SUBUNIT: Monomer (By similarity). Binds single-stranded DNA (ssDNA) (By
CC similarity). Interacts with APEX1, LIG1, LIG3, FEN1, PCNA and XRCC1 (By
CC similarity). Interacts with HUWE1/ARF-BP1, STUB1/CHIP and USP47 (By
CC similarity). Interacts with FAM168A (By similarity).
CC {ECO:0000250|UniProtKB:P06746}.
CC -!- INTERACTION:
CC P06766; P18887: XRCC1; Xeno; NbExp=4; IntAct=EBI-15845002, EBI-947466;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P06746}. Cytoplasm
CC {ECO:0000250|UniProtKB:P06746}. Note=Cytoplasmic in normal conditions.
CC Translocates to the nucleus following DNA damage.
CC {ECO:0000250|UniProtKB:P06746}.
CC -!- DOMAIN: Residues 239-252 form a flexible loop which appears to affect
CC the polymerase fidelity.
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}.
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DR EMBL; J02776; AAA41901.1; -; mRNA.
DR EMBL; U38801; AAB00389.1; -; mRNA.
DR EMBL; BC098668; AAH98668.1; -; mRNA.
DR EMBL; M13961; AAA41900.1; -; mRNA.
DR PIR; A27112; A27112.
DR RefSeq; NP_058837.2; NM_017141.2.
DR PDB; 1BNO; NMR; -; A=1-87.
DR PDB; 1BNP; NMR; -; A=1-87.
DR PDB; 1BPB; X-ray; 2.30 A; A=88-335.
DR PDB; 1BPD; X-ray; 3.60 A; A=1-335.
DR PDB; 1BPE; X-ray; 2.90 A; A=1-335.
DR PDB; 1DK2; NMR; -; A=2-87.
DR PDB; 1DK3; NMR; -; A=1-87.
DR PDB; 1HUO; X-ray; 2.60 A; A/B=1-335.
DR PDB; 1HUZ; X-ray; 2.60 A; A/B=1-335.
DR PDB; 1JN3; X-ray; 2.35 A; A=85-335.
DR PDB; 1NOM; X-ray; 3.00 A; A=88-335.
DR PDB; 1RPL; X-ray; 2.30 A; A=85-335.
DR PDB; 1ZQU; X-ray; 2.60 A; A=88-335.
DR PDB; 1ZQV; X-ray; 2.70 A; A=88-335.
DR PDB; 1ZQW; X-ray; 2.30 A; A=88-335.
DR PDB; 1ZQX; X-ray; 2.50 A; A=88-335.
DR PDB; 1ZQY; X-ray; 2.30 A; A=88-335.
DR PDB; 1ZQZ; X-ray; 2.70 A; A=88-335.
DR PDB; 2BPC; X-ray; 2.80 A; A=88-335.
DR PDB; 2BPF; X-ray; 2.90 A; A=1-335.
DR PDB; 2BPG; X-ray; 3.60 A; A/B=1-335.
DR PDB; 2VAN; X-ray; 2.10 A; A=91-335.
DR PDB; 3K75; X-ray; 2.95 A; D/E=91-335.
DR PDB; 3LQC; X-ray; 2.35 A; B=142-335.
DR PDB; 3UXN; X-ray; 2.50 A; A/B=1-335.
DR PDB; 3UXO; X-ray; 2.10 A; A/B=1-335.
DR PDB; 3UXP; X-ray; 2.72 A; A/B=1-335.
DR PDB; 3V72; X-ray; 2.49 A; A=1-335.
DR PDB; 3V7J; X-ray; 2.25 A; A=4-335.
DR PDB; 3V7K; X-ray; 2.27 A; A=4-335.
DR PDB; 3V7L; X-ray; 2.66 A; A=4-335.
DR PDBsum; 1BNO; -.
DR PDBsum; 1BNP; -.
DR PDBsum; 1BPB; -.
DR PDBsum; 1BPD; -.
DR PDBsum; 1BPE; -.
DR PDBsum; 1DK2; -.
DR PDBsum; 1DK3; -.
DR PDBsum; 1HUO; -.
DR PDBsum; 1HUZ; -.
DR PDBsum; 1JN3; -.
DR PDBsum; 1NOM; -.
DR PDBsum; 1RPL; -.
DR PDBsum; 1ZQU; -.
DR PDBsum; 1ZQV; -.
DR PDBsum; 1ZQW; -.
DR PDBsum; 1ZQX; -.
DR PDBsum; 1ZQY; -.
DR PDBsum; 1ZQZ; -.
DR PDBsum; 2BPC; -.
DR PDBsum; 2BPF; -.
DR PDBsum; 2BPG; -.
DR PDBsum; 2VAN; -.
DR PDBsum; 3K75; -.
DR PDBsum; 3LQC; -.
DR PDBsum; 3UXN; -.
DR PDBsum; 3UXO; -.
DR PDBsum; 3UXP; -.
DR PDBsum; 3V72; -.
DR PDBsum; 3V7J; -.
DR PDBsum; 3V7K; -.
DR PDBsum; 3V7L; -.
DR AlphaFoldDB; P06766; -.
DR BMRB; P06766; -.
DR SMR; P06766; -.
DR DIP; DIP-44707N; -.
DR IntAct; P06766; 1.
DR STRING; 10116.ENSRNOP00000026039; -.
DR BindingDB; P06766; -.
DR ChEMBL; CHEMBL4343; -.
DR iPTMnet; P06766; -.
DR PhosphoSitePlus; P06766; -.
DR jPOST; P06766; -.
DR PaxDb; 10116-ENSRNOP00000026039; -.
DR Ensembl; ENSRNOT00000113772.1; ENSRNOP00000094599.1; ENSRNOG00000019150.6.
DR Ensembl; ENSRNOT00055012865; ENSRNOP00055010253; ENSRNOG00055007682.
DR Ensembl; ENSRNOT00060048617; ENSRNOP00060040531; ENSRNOG00060027954.
DR Ensembl; ENSRNOT00065013936; ENSRNOP00065010380; ENSRNOG00065008755.
DR GeneID; 29240; -.
DR KEGG; rno:29240; -.
DR UCSC; RGD:3363; rat.
DR AGR; RGD:3363; -.
DR CTD; 5423; -.
DR RGD; 3363; Polb.
DR eggNOG; KOG2534; Eukaryota.
DR GeneTree; ENSGT00940000156918; -.
DR HOGENOM; CLU_008698_1_0_1; -.
DR InParanoid; P06766; -.
DR OMA; YKYNAYR; -.
DR OrthoDB; 49764at2759; -.
DR PhylomeDB; P06766; -.
DR TreeFam; TF103002; -.
DR Reactome; R-RNO-110362; POLB-Dependent Long Patch Base Excision Repair.
DR Reactome; R-RNO-110373; Resolution of AP sites via the multiple-nucleotide patch replacement pathway.
DR Reactome; R-RNO-110381; Resolution of AP sites via the single-nucleotide replacement pathway.
DR Reactome; R-RNO-5649702; APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
DR Reactome; R-RNO-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR Reactome; R-RNO-73930; Abasic sugar-phosphate removal via the single-nucleotide replacement pathway.
DR EvolutionaryTrace; P06766; -.
DR PRO; PR:P06766; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000019150; Expressed in testis and 20 other cell types or tissues.
DR Genevisible; P06766; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005876; C:spindle microtubule; ISO:RGD.
DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; ISO:RGD.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; ISO:RGD.
DR GO; GO:0003684; F:damaged DNA binding; IDA:RGD.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0016829; F:lyase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR GO; GO:0006284; P:base-excision repair; ISS:UniProtKB.
DR GO; GO:0006287; P:base-excision repair, gap-filling; IDA:RGD.
DR GO; GO:0006974; P:DNA damage response; 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; ISO:RGD.
DR GO; GO:0071707; P:immunoglobulin heavy chain V-D-J recombination; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:RGD.
DR GO; GO:0048535; P:lymph node development; ISO:RGD.
DR GO; GO:0051402; P:neuron apoptotic process; ISO:RGD.
DR GO; GO:0006290; P:pyrimidine dimer repair; IDA:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0010332; P:response to gamma radiation; IEP:RGD.
DR GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR GO; GO:0007435; P:salivary gland morphogenesis; ISO:RGD.
DR GO; GO:0016445; P:somatic diversification of immunoglobulins; ISO:RGD.
DR GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; ISO:RGD.
DR GO; GO:0048536; P:spleen development; ISO:RGD.
DR CDD; cd00141; NT_POLXc; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.150.110; DNA polymerase beta, N-terminal domain-like; 1.
DR Gene3D; 3.30.210.10; DNA polymerase, thumb domain; 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:SF42; DNA POLYMERASE BETA; 1.
DR PANTHER; PTHR11276; DNA POLYMERASE TYPE-X FAMILY MEMBER; 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; DNA polymerase beta, N-terminal domain-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81585; PsbU/PolX domain-like; 1.
DR PROSITE; PS00522; DNA_POLYMERASE_X; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW DNA damage; DNA repair; DNA replication; DNA synthesis; DNA-binding;
KW DNA-directed DNA polymerase; Isopeptide bond; Lyase; Magnesium;
KW Metal-binding; Methylation; Nucleotidyltransferase; Nucleus; Potassium;
KW Reference proteome; Sodium; Transferase; Ubl conjugation.
FT CHAIN 1..335
FT /note="DNA polymerase beta"
FT /id="PRO_0000218780"
FT REGION 183..192
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT ACT_SITE 72
FT /note="Nucleophile; Schiff-base intermediate with DNA; for
FT 5'-dRP lyase activity"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT BINDING 60
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT BINDING 60
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT BINDING 62
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT BINDING 62
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT BINDING 65
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT BINDING 65
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT BINDING 101
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT BINDING 101
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT BINDING 103
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT BINDING 103
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT BINDING 106
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT BINDING 106
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT BINDING 149
FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61560"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT BINDING 180
FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61560"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT BINDING 183
FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61560"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT BINDING 189
FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61560"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT BINDING 190
FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61560"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT BINDING 256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT MOD_RES 72
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8K409"
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"
FT MUTAGEN 190
FT /note="D->E,S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:2036395"
FT MUTAGEN 191
FT /note="M->I: No loss of activity."
FT MUTAGEN 191
FT /note="M->T: 50% loss of activity."
FT MUTAGEN 192
FT /note="D->E,S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:2036395"
FT MUTAGEN 246
FT /note="D->V: Misincorporates T nucleotide opposite G/C
FT template."
FT /evidence="ECO:0000269|PubMed:14563842"
FT CONFLICT 228
FT /note="L -> R (in Ref. 1; AAA41901, 2; AAB00389 and 4;
FT AAA41900)"
FT /evidence="ECO:0000305"
FT HELIX 13..28
FT /evidence="ECO:0007829|PDB:3UXO"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1DK2"
FT HELIX 33..48
FT /evidence="ECO:0007829|PDB:3UXO"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:3UXO"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:3V7L"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:3UXO"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:3UXO"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:3UXO"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:2VAN"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:3V7L"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:2VAN"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:2VAN"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:2VAN"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:2VAN"
FT HELIX 134..141
FT /evidence="ECO:0007829|PDB:2VAN"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:2VAN"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:2VAN"
FT HELIX 152..169
FT /evidence="ECO:0007829|PDB:2VAN"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:2VAN"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:2VAN"
FT STRAND 186..196
FT /evidence="ECO:0007829|PDB:2VAN"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:1BPB"
FT HELIX 208..220
FT /evidence="ECO:0007829|PDB:2VAN"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:2VAN"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:2VAN"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:3V7J"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:2VAN"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:2VAN"
FT HELIX 265..273
FT /evidence="ECO:0007829|PDB:2VAN"
FT HELIX 276..288
FT /evidence="ECO:0007829|PDB:2VAN"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:2VAN"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:2VAN"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:3UXO"
FT HELIX 316..322
FT /evidence="ECO:0007829|PDB:2VAN"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:2VAN"
SQ SEQUENCE 335 AA; 38327 MW; BBF8498C0D3FBFC9 CRC64;
MSKRKAPQET LNGGITDMLV ELANFEKNVS QAIHKYNAYR KAASVIAKYP HKIKSGAEAK
KLPGVGTKIA EKIDEFLATG KLRKLEKIRQ DDTSSSINFL TRVTGIGPSA ARKLVDEGIK
TLEDLRKNED KLNHHQRIGL KYFEDFEKRI PREEMLQMQD IVLNEVKKLD PEYIATVCGS
FRRGAESSGD MDVLLTHPNF TSESSKQPKL LHRVVEQLQK VRFITDTLSK GETKFMGVCQ
LPSENDENEY PHRRIDIRLI PKDQYYCGVL YFTGSDIFNK NMRAHALEKG FTINEYTIRP
LGVTGVAGEP LPVDSEQDIF DYIQWRYREP KDRSE
//
