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P06766

- DPOLB_RAT

UniProt

P06766 - DPOLB_RAT

Protein

DNA polymerase beta

Gene

Polb

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases.

    Catalytic activityi

    Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

    Cofactori

    Binds 2 magnesium ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei72 – 721Schiff-base intermediate with DNABy similarity
    Metal bindingi101 – 1011Sodium; via carbonyl oxygen
    Metal bindingi103 – 1031Sodium; via carbonyl oxygen
    Metal bindingi106 – 1061Sodium; via carbonyl oxygen
    Metal bindingi190 – 1901Magnesium 1
    Metal bindingi190 – 1901Magnesium 2
    Metal bindingi192 – 1921Magnesium 1
    Metal bindingi192 – 1921Magnesium 2
    Metal bindingi256 – 2561Magnesium 2

    GO - Molecular functioni

    1. damaged DNA binding Source: RGD
    2. DNA binding Source: UniProtKB
    3. DNA-directed DNA polymerase activity Source: UniProtKB
    4. lyase activity Source: UniProtKB
    5. metal ion binding Source: UniProtKB
    6. protein binding Source: RGD

    GO - Biological processi

    1. base-excision repair Source: UniProtKB
    2. base-excision repair, gap-filling Source: RGD
    3. cellular response to DNA damage stimulus Source: UniProtKB
    4. DNA biosynthetic process Source: RGD
    5. DNA-dependent DNA replication Source: GOC
    6. intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
    7. neuron apoptotic process Source: Ensembl
    8. pyrimidine dimer repair Source: RGD
    9. response to ethanol Source: RGD

    Keywords - Molecular functioni

    DNA-directed DNA polymerase, Lyase, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    DNA damage, DNA repair, DNA replication, DNA synthesis

    Keywords - Ligandi

    DNA-binding, Magnesium, Metal-binding, Sodium

    Enzyme and pathway databases

    ReactomeiREACT_225345. Resolution of AP sites via the single-nucleotide replacement pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA polymerase beta (EC:2.7.7.7, EC:4.2.99.-)
    Gene namesi
    Name:Polb
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 16

    Organism-specific databases

    RGDi3363. Polb.

    Subcellular locationi

    Nucleus. Cytoplasm By similarity
    Note: Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: RGD
    3. spindle microtubule Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi190 – 1901D → E or S: Loss of activity. 1 Publication
    Mutagenesisi191 – 1911M → I: No loss of activity.
    Mutagenesisi191 – 1911M → T: 50% loss of activity.
    Mutagenesisi192 – 1921D → E or S: Loss of activity. 1 Publication
    Mutagenesisi246 – 2461D → V: Misincorporates T nucleotide opposite G/C template. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 335335DNA polymerase betaPRO_0000218780Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki41 – 41Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki61 – 61Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei72 – 721N6-acetyllysineBy similarity
    Cross-linki81 – 81Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei83 – 831Omega-N-methylarginine; by PRMT6By similarity
    Modified residuei152 – 1521Omega-N-methylarginine; by PRMT6By similarity

    Post-translational modificationi

    Methylation by PRMT6 stimulates the polymerase activity by enhancing DNA binding and processivity.By similarity
    Ubiquitinated at Lys-41, Lys-61 and Lys-81: monoubiquitinated by HUWE1/ARF-BP1. Monoubiquitinated protein is then the target of STUB1/CHIP, which catalyzes polyubiquitination from monoubiquitin, leading to degradation by the proteasome. USP47 mediates the deubiquitination of monoubiquitinated protein, preventing polyubiquitination by STUB1/CHIP and its subsequent degradation By similarity.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Methylation, Ubl conjugation

    Proteomic databases

    PaxDbiP06766.
    PRIDEiP06766.

    PTM databases

    PhosphoSiteiP06766.

    Expressioni

    Gene expression databases

    GenevestigatoriP06766.

    Interactioni

    Subunit structurei

    Interacts with APEX1, HUWE1/ARF-BP1, STUB1/CHIP and USP47 By similarity. Monomer.By similarity

    Protein-protein interaction databases

    DIPiDIP-44707N.
    MINTiMINT-1504350.

    Structurei

    Secondary structure

    1
    335
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi13 – 2816
    Beta strandi29 – 313
    Helixi33 – 4816
    Helixi56 – 616
    Beta strandi62 – 643
    Helixi67 – 7610
    Beta strandi79 – 813
    Helixi83 – 908
    Helixi92 – 1009
    Turni101 – 1044
    Helixi108 – 1158
    Turni116 – 1183
    Helixi122 – 1265
    Helixi129 – 1313
    Helixi134 – 1418
    Turni142 – 1443
    Helixi145 – 1473
    Helixi152 – 16918
    Beta strandi174 – 1774
    Helixi179 – 1824
    Beta strandi186 – 19611
    Turni202 – 2043
    Helixi208 – 22013
    Beta strandi224 – 2307
    Beta strandi232 – 2398
    Beta strandi244 – 2474
    Beta strandi253 – 2597
    Helixi262 – 2643
    Helixi265 – 2739
    Helixi276 – 28813
    Beta strandi291 – 2933
    Beta strandi298 – 3014
    Beta strandi303 – 3053
    Helixi316 – 3227
    Helixi330 – 3323

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BNONMR-A1-87[»]
    1BNPNMR-A1-87[»]
    1BPBX-ray2.30A88-335[»]
    1BPDX-ray3.60A1-335[»]
    1BPEX-ray2.90A1-335[»]
    1DK2NMR-A2-87[»]
    1DK3NMR-A1-87[»]
    1HUOX-ray2.60A/B1-335[»]
    1HUZX-ray2.60A/B1-335[»]
    1JN3X-ray2.35A85-335[»]
    1NOMX-ray3.00A88-335[»]
    1RPLX-ray2.30A85-335[»]
    1ZQUX-ray2.60A88-335[»]
    1ZQVX-ray2.70A88-335[»]
    1ZQWX-ray2.30A88-335[»]
    1ZQXX-ray2.50A88-335[»]
    1ZQYX-ray2.30A88-335[»]
    1ZQZX-ray2.70A88-335[»]
    2BPCX-ray2.80A88-335[»]
    2BPFX-ray2.90A1-335[»]
    2BPGX-ray3.60A/B1-335[»]
    2VANX-ray2.10A91-335[»]
    3K75X-ray2.95D/E91-335[»]
    3LQCX-ray2.35B142-335[»]
    3UXNX-ray2.50A/B1-335[»]
    3UXOX-ray2.10A/B1-335[»]
    3UXPX-ray2.72A/B1-335[»]
    3V72X-ray2.49A1-335[»]
    3V7JX-ray2.25A4-335[»]
    3V7KX-ray2.27A4-335[»]
    3V7LX-ray2.66A4-335[»]
    ProteinModelPortaliP06766.
    SMRiP06766. Positions 10-334.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06766.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni183 – 19210DNA binding

    Domaini

    Residues 239-252 form a flexible loop which appears to affect the polymerase fidelity.

    Sequence similaritiesi

    Belongs to the DNA polymerase type-X family.Curated

    Phylogenomic databases

    eggNOGiCOG1796.
    GeneTreeiENSGT00530000063002.
    HOGENOMiHOG000007787.
    HOVERGENiHBG002359.
    InParanoidiP06766.
    KOiK02330.
    OMAiRYREPKD.
    OrthoDBiEOG7RJPRK.
    PhylomeDBiP06766.
    TreeFamiTF103002.

    Family and domain databases

    Gene3Di1.10.8.310. 1 hit.
    3.30.210.10. 1 hit.
    InterProiIPR002054. DNA-dir_DNA_pol_X.
    IPR019843. DNA_pol-X_BS.
    IPR010996. DNA_pol_b-like_N.
    IPR028207. DNA_pol_B_palm_palm.
    IPR018944. DNA_pol_lambd_fingers_domain.
    IPR022312. DNA_pol_X.
    IPR002008. DNA_pol_X_beta-like.
    IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
    IPR027420. PolB_N.
    IPR029398. PolB_thumb.
    [Graphical view]
    PfamiPF14792. DNA_pol_B_palm. 1 hit.
    PF14791. DNA_pol_B_thumb. 1 hit.
    PF10391. DNA_pol_lambd_f. 1 hit.
    [Graphical view]
    PRINTSiPR00869. DNAPOLX.
    PR00870. DNAPOLXBETA.
    SMARTiSM00278. HhH1. 2 hits.
    SM00483. POLXc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47802. SSF47802. 1 hit.
    PROSITEiPS00522. DNA_POLYMERASE_X. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P06766-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKRKAPQET LNGGITDMLV ELANFEKNVS QAIHKYNAYR KAASVIAKYP    50
    HKIKSGAEAK KLPGVGTKIA EKIDEFLATG KLRKLEKIRQ DDTSSSINFL 100
    TRVTGIGPSA ARKLVDEGIK TLEDLRKNED KLNHHQRIGL KYFEDFEKRI 150
    PREEMLQMQD IVLNEVKKLD PEYIATVCGS FRRGAESSGD MDVLLTHPNF 200
    TSESSKQPKL LHRVVEQLQK VRFITDTLSK GETKFMGVCQ LPSENDENEY 250
    PHRRIDIRLI PKDQYYCGVL YFTGSDIFNK NMRAHALEKG FTINEYTIRP 300
    LGVTGVAGEP LPVDSEQDIF DYIQWRYREP KDRSE 335
    Length:335
    Mass (Da):38,327
    Last modified:January 23, 2007 - v4
    Checksum:iBBF8498C0D3FBFC9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti228 – 2281L → R in AAA41901. (PubMed:3597402)Curated
    Sequence conflicti228 – 2281L → R in AAB00389. 1 PublicationCurated
    Sequence conflicti228 – 2281L → R in AAA41900. (PubMed:2873575)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02776 mRNA. Translation: AAA41901.1.
    U38801 mRNA. Translation: AAB00389.1.
    BC098668 mRNA. Translation: AAH98668.1.
    M13961 mRNA. Translation: AAA41900.1.
    PIRiA27112.
    RefSeqiNP_058837.2. NM_017141.2.
    UniGeneiRn.9346.

    Genome annotation databases

    EnsembliENSRNOT00000026039; ENSRNOP00000026039; ENSRNOG00000019150.
    GeneIDi29240.
    KEGGirno:29240.
    UCSCiRGD:3363. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02776 mRNA. Translation: AAA41901.1 .
    U38801 mRNA. Translation: AAB00389.1 .
    BC098668 mRNA. Translation: AAH98668.1 .
    M13961 mRNA. Translation: AAA41900.1 .
    PIRi A27112.
    RefSeqi NP_058837.2. NM_017141.2.
    UniGenei Rn.9346.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BNO NMR - A 1-87 [» ]
    1BNP NMR - A 1-87 [» ]
    1BPB X-ray 2.30 A 88-335 [» ]
    1BPD X-ray 3.60 A 1-335 [» ]
    1BPE X-ray 2.90 A 1-335 [» ]
    1DK2 NMR - A 2-87 [» ]
    1DK3 NMR - A 1-87 [» ]
    1HUO X-ray 2.60 A/B 1-335 [» ]
    1HUZ X-ray 2.60 A/B 1-335 [» ]
    1JN3 X-ray 2.35 A 85-335 [» ]
    1NOM X-ray 3.00 A 88-335 [» ]
    1RPL X-ray 2.30 A 85-335 [» ]
    1ZQU X-ray 2.60 A 88-335 [» ]
    1ZQV X-ray 2.70 A 88-335 [» ]
    1ZQW X-ray 2.30 A 88-335 [» ]
    1ZQX X-ray 2.50 A 88-335 [» ]
    1ZQY X-ray 2.30 A 88-335 [» ]
    1ZQZ X-ray 2.70 A 88-335 [» ]
    2BPC X-ray 2.80 A 88-335 [» ]
    2BPF X-ray 2.90 A 1-335 [» ]
    2BPG X-ray 3.60 A/B 1-335 [» ]
    2VAN X-ray 2.10 A 91-335 [» ]
    3K75 X-ray 2.95 D/E 91-335 [» ]
    3LQC X-ray 2.35 B 142-335 [» ]
    3UXN X-ray 2.50 A/B 1-335 [» ]
    3UXO X-ray 2.10 A/B 1-335 [» ]
    3UXP X-ray 2.72 A/B 1-335 [» ]
    3V72 X-ray 2.49 A 1-335 [» ]
    3V7J X-ray 2.25 A 4-335 [» ]
    3V7K X-ray 2.27 A 4-335 [» ]
    3V7L X-ray 2.66 A 4-335 [» ]
    ProteinModelPortali P06766.
    SMRi P06766. Positions 10-334.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-44707N.
    MINTi MINT-1504350.

    Chemistry

    BindingDBi P06766.
    ChEMBLi CHEMBL4343.

    PTM databases

    PhosphoSitei P06766.

    Proteomic databases

    PaxDbi P06766.
    PRIDEi P06766.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000026039 ; ENSRNOP00000026039 ; ENSRNOG00000019150 .
    GeneIDi 29240.
    KEGGi rno:29240.
    UCSCi RGD:3363. rat.

    Organism-specific databases

    CTDi 5423.
    RGDi 3363. Polb.

    Phylogenomic databases

    eggNOGi COG1796.
    GeneTreei ENSGT00530000063002.
    HOGENOMi HOG000007787.
    HOVERGENi HBG002359.
    InParanoidi P06766.
    KOi K02330.
    OMAi RYREPKD.
    OrthoDBi EOG7RJPRK.
    PhylomeDBi P06766.
    TreeFami TF103002.

    Enzyme and pathway databases

    Reactomei REACT_225345. Resolution of AP sites via the single-nucleotide replacement pathway.

    Miscellaneous databases

    EvolutionaryTracei P06766.
    NextBioi 608510.
    PROi P06766.

    Gene expression databases

    Genevestigatori P06766.

    Family and domain databases

    Gene3Di 1.10.8.310. 1 hit.
    3.30.210.10. 1 hit.
    InterProi IPR002054. DNA-dir_DNA_pol_X.
    IPR019843. DNA_pol-X_BS.
    IPR010996. DNA_pol_b-like_N.
    IPR028207. DNA_pol_B_palm_palm.
    IPR018944. DNA_pol_lambd_fingers_domain.
    IPR022312. DNA_pol_X.
    IPR002008. DNA_pol_X_beta-like.
    IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
    IPR027420. PolB_N.
    IPR029398. PolB_thumb.
    [Graphical view ]
    Pfami PF14792. DNA_pol_B_palm. 1 hit.
    PF14791. DNA_pol_B_thumb. 1 hit.
    PF10391. DNA_pol_lambd_f. 1 hit.
    [Graphical view ]
    PRINTSi PR00869. DNAPOLX.
    PR00870. DNAPOLXBETA.
    SMARTi SM00278. HhH1. 2 hits.
    SM00483. POLXc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47802. SSF47802. 1 hit.
    PROSITEi PS00522. DNA_POLYMERASE_X. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Homology between mammalian DNA polymerase beta and terminal deoxynucleotidyltransferase."
      Matsukage A., Nishikawa K., Ooi T., Seto Y., Yamaguchi M.
      J. Biol. Chem. 262:8960-8962(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Konopinski R., Nowak R., Siedlecki J.A.
      Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Wistar.
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Thymus.
    4. "Structure of rat DNA polymerase beta revealed by partial amino acid sequencing and cDNA cloning."
      Zmudzka B.Z., Sengupta D., Matsukage A., Cobianchi F., Kumar P., Wilson S.H.
      Proc. Natl. Acad. Sci. U.S.A. 83:5106-5110(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-335.
    5. "Studies of the domain structure of mammalian DNA polymerase beta. Identification of a discrete template binding domain."
      Kumar P., Widen S.G., Williams K.R., Kedar P., Karpel R.L., Wilson S.H.
      J. Biol. Chem. 265:2124-2131(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, SEQUENCE REVISION TO 228.
    6. "Site-directed mutagenesis of recombinant rat DNA polymerase beta: involvement of arginine-183 in primer recognition."
      Date T., Yamamoto S., Tanihara K., Nishimoto Y., Liu N., Matsukage A.
      Biochemistry 29:5027-5034(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: IMPORTANCE OF ARG-183 IN PRIMER BINDING.
    7. "Aspartic acid residues at positions 190 and 192 of rat DNA polymerase beta are involved in primer binding."
      Date T., Yamamoto S., Tanihara K., Nishimoto Y., Matsukage A.
      Biochemistry 30:5286-5292(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-190 AND ASP-192, IMPORTANCE OF ASP-190 AND ASP-192 IN PRIMER BINDING.
    8. "Mammalian DNA polymerase beta: characterization of a 16-kDa transdomain fragment containing the nucleic acid-binding activities of the native enzyme."
      Casas-Finet J.R., Kumar A., Karpel R.L., Wilson S.H.
      Biochemistry 31:10272-10280(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING REGION.
    9. "The D246V mutant of DNA polymerase beta misincorporates nucleotides: evidence for a role for the flexible loop in DNA positioning within the active site."
      Dalal S., Kosa J.L., Sweasy J.B.
      J. Biol. Chem. 279:577-584(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-246, IMPORTANCE OF ASP-246 IN FIDELITY.
    10. "2.3-A crystal structure of the catalytic domain of DNA polymerase beta."
      Davies J.F. II, Almassy R.J., Hostomska Z., Ferre R.A., Hostomsky Z.
      Cell 76:1123-1133(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    11. "Crystal structure of rat DNA polymerase beta: evidence for a common polymerase mechanism."
      Sawaya M.R., Pelletier H., Kumar A., Wilson S.H., Kraut J.
      Science 264:1930-1935(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    12. "Characterization of the metal ion binding helix-hairpin-helix motifs in human DNA polymerase beta by X-ray structural analysis."
      Pelletier H., Sawaya M.R.
      Biochemistry 35:12778-12787(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
    13. "Insight into the catalytic mechanism of DNA polymerase beta: structures of intermediate complexes."
      Arndt J.W., Gong W., Zhong X., Showalter A.K., Liu J., Dunlap C.A., Lin Z., Paxson C., Tsai M.-D., Chan M.K.
      Biochemistry 40:5368-5375(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
    14. "Three-dimensional solution structure of the N-terminal domain of DNA polymerase beta and mapping of the ssDNA interaction interface."
      Liu D., Prasad R., Wilson S.H., DeRose E.F., Mullen G.P.
      Biochemistry 35:6188-6200(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-87.
    15. "Backbone dynamics and refined solution structure of the N-terminal domain of DNA polymerase beta. Correlation with DNA binding and dRP lyase activity."
      Maciejewski M.W., Liu D., Prasad R., Wilson S.H., Mullen G.P.
      J. Mol. Biol. 296:229-253(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-87.

    Entry informationi

    Entry nameiDPOLB_RAT
    AccessioniPrimary (citable) accession number: P06766
    Secondary accession number(s): Q4G081
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 152 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3