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P06746

- DPOLB_HUMAN

UniProt

P06746 - DPOLB_HUMAN

Protein

DNA polymerase beta

Gene

POLB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 179 (01 Oct 2014)
      Sequence version 3 (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.4 Publications

    Catalytic activityi

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

    Cofactori

    Binds 2 magnesium ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei72 – 721Schiff-base intermediate with DNA
    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: Ensembl
    2. DNA-directed DNA polymerase activity Source: UniProtKB
    3. enzyme binding Source: UniProtKB
    4. lyase activity Source: UniProtKB
    5. metal ion binding Source: UniProtKB-KW
    6. microtubule binding Source: MGI
    7. protein binding Source: UniProtKB

    GO - Biological processi

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

    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_1357. Base-free sugar-phosphate removal via the single-nucleotide replacement pathway.
    REACT_2192. Removal of DNA patch containing abasic residue.
    REACT_933. 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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:9174. POLB.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. microtubule Source: MGI
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB
    5. spindle microtubule Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi35 – 351K → Q or R: Reduces DNA lyase activity slightly. 1 Publication
    Mutagenesisi39 – 391Y → Q: Abolishes DNA polymerase and DNA lyase activity. 1 Publication
    Mutagenesisi41 – 411K → R: Abolishes ubiquitination; when associated with R-61 and R-81. 1 Publication
    Mutagenesisi61 – 611K → R: Abolishes ubiquitination; when associated with R-41 and R-81. 1 Publication
    Mutagenesisi68 – 681K → Q or R: Reduces DNA lyase activity slightly. 1 Publication
    Mutagenesisi72 – 721K → Q or R: Abolishes DNA lyase activity. No effect on DNA polymerase activity. 1 Publication
    Mutagenesisi81 – 811K → R: Abolishes ubiquitination; when associated with R-41 and R-61. 1 Publication
    Mutagenesisi83 – 831R → K: Slight effect. Abolishes methylation by PRMT6 and impairs the polymerase activity; when associated with K-152. 1 Publication
    Mutagenesisi84 – 841K → R: No effect. 1 Publication
    Mutagenesisi152 – 1521R → K: Slight effect. Abolishes methylation by PRMT6 and impairs the polymerase activity; when associated with K-83. 1 Publication

    Organism-specific databases

    PharmGKBiPA276.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 335335DNA polymerase betaPRO_0000218778Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki41 – 41Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
    Cross-linki61 – 61Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
    Modified residuei72 – 721N6-acetyllysineBy similarity
    Cross-linki81 – 81Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
    Modified residuei83 – 831Omega-N-methylarginine; by PRMT61 Publication
    Modified residuei152 – 1521Omega-N-methylarginine; by PRMT61 Publication

    Post-translational modificationi

    Methylation by PRMT6 stimulates the polymerase activity by enhancing DNA binding and processivity.1 Publication
    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.2 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Methylation, Ubl conjugation

    Proteomic databases

    MaxQBiP06746.
    PaxDbiP06746.
    PeptideAtlasiP06746.
    PRIDEiP06746.

    PTM databases

    PhosphoSiteiP06746.

    Expressioni

    Gene expression databases

    ArrayExpressiP06746.
    BgeeiP06746.
    CleanExiHS_POLB.
    GenevestigatoriP06746.

    Organism-specific databases

    HPAiCAB011616.

    Interactioni

    Subunit structurei

    Monomer. Interacts with APEX1, HUWE1/ARF-BP1, STUB1/CHIP and USP47.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TAF1DQ9H5J84EBI-713836,EBI-716128

    Protein-protein interaction databases

    BioGridi111419. 17 interactions.
    IntActiP06746. 6 interactions.
    MINTiMINT-1393546.
    STRINGi9606.ENSP00000265421.

    Structurei

    Secondary structure

    1
    335
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni9 – 124
    Helixi13 – 2816
    Helixi33 – 4816
    Helixi56 – 605
    Beta strandi62 – 643
    Helixi67 – 7913
    Helixi83 – 908
    Helixi92 – 1009
    Turni101 – 1055
    Helixi108 – 1169
    Helixi122 – 1276
    Helixi128 – 1314
    Helixi134 – 1418
    Helixi143 – 1464
    Helixi152 – 16918
    Beta strandi174 – 1774
    Helixi179 – 1824
    Beta strandi186 – 19611
    Beta strandi202 – 2043
    Beta strandi207 – 2093
    Helixi210 – 22011
    Beta strandi224 – 2307
    Beta strandi232 – 2398
    Beta strandi245 – 2473
    Beta strandi253 – 2597
    Helixi262 – 2643
    Helixi265 – 2739
    Helixi276 – 28914
    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
    1BPXX-ray2.40A1-335[»]
    1BPYX-ray2.20A1-335[»]
    1BPZX-ray2.60A1-335[»]
    1MQ2X-ray3.10A1-335[»]
    1MQ3X-ray2.80A1-335[»]
    1TV9X-ray2.00A1-335[»]
    1TVAX-ray2.60A1-335[»]
    1ZJMX-ray2.10A1-335[»]
    1ZJNX-ray2.61A1-335[»]
    1ZQAX-ray3.20A1-335[»]
    1ZQBX-ray3.20A1-335[»]
    1ZQCX-ray3.20A1-335[»]
    1ZQDX-ray3.50A1-335[»]
    1ZQEX-ray3.70A1-335[»]
    1ZQFX-ray2.90A1-335[»]
    1ZQGX-ray3.10A1-335[»]
    1ZQHX-ray3.10A1-335[»]
    1ZQIX-ray2.70A1-335[»]
    1ZQJX-ray3.30A1-335[»]
    1ZQKX-ray3.20A1-335[»]
    1ZQLX-ray3.30A1-335[»]
    1ZQMX-ray3.20A1-335[»]
    1ZQNX-ray3.00A1-335[»]
    1ZQOX-ray3.20A1-335[»]
    1ZQPX-ray2.80A1-335[»]
    1ZQQX-ray3.30A1-335[»]
    1ZQRX-ray3.70A1-335[»]
    1ZQSX-ray3.30A1-335[»]
    1ZQTX-ray3.40A1-335[»]
    2FMPX-ray1.65A1-335[»]
    2FMQX-ray2.20A1-335[»]
    2FMSX-ray2.00A1-335[»]
    2I9GX-ray2.10A1-335[»]
    2ISOX-ray2.10A1-335[»]
    2ISPX-ray2.20A1-335[»]
    2P66X-ray2.50A1-335[»]
    2PXIX-ray2.10A1-335[»]
    3C2KX-ray2.40A1-335[»]
    3C2LX-ray2.60A1-335[»]
    3C2MX-ray2.15A1-335[»]
    3GDXX-ray2.20A10-335[»]
    3ISBX-ray2.00A1-335[»]
    3ISCX-ray2.00A1-335[»]
    3ISDX-ray2.60A1-335[»]
    3JPNX-ray2.15A1-335[»]
    3JPOX-ray2.00A1-335[»]
    3JPPX-ray2.10A1-335[»]
    3JPQX-ray1.90A1-335[»]
    3JPRX-ray2.10A1-335[»]
    3JPSX-ray2.00A1-335[»]
    3JPTX-ray2.15A1-335[»]
    3LK9X-ray2.50A1-335[»]
    3MBYX-ray2.00A1-335[»]
    3OGUX-ray1.84A1-335[»]
    3RH4X-ray1.92A1-335[»]
    3RH5X-ray2.10A1-335[»]
    3RH6X-ray2.05A1-335[»]
    3RJEX-ray2.10A1-335[»]
    3RJFX-ray2.30A1-335[»]
    3RJGX-ray2.00A1-335[»]
    3RJHX-ray2.20A1-335[»]
    3RJIX-ray2.30A1-335[»]
    3RJJX-ray2.00A1-335[»]
    3RJKX-ray2.10A1-335[»]
    3TFRX-ray2.00A1-335[»]
    3TFSX-ray2.00A1-335[»]
    4DO9X-ray2.05A1-335[»]
    4DOAX-ray2.05A1-335[»]
    4DOBX-ray2.05A1-335[»]
    4DOCX-ray1.95A1-335[»]
    4F5NX-ray1.80A1-335[»]
    4F5OX-ray2.00A1-335[»]
    4F5PX-ray1.85A1-335[»]
    4F5QX-ray2.25A1-335[»]
    4F5RX-ray2.20A/B1-335[»]
    4GXIX-ray1.95A1-335[»]
    4GXJX-ray2.20A1-335[»]
    4GXKX-ray2.00A1-335[»]
    4JWMX-ray2.00A1-335[»]
    4JWNX-ray2.39A1-335[»]
    4KLDX-ray1.92A1-335[»]
    4KLEX-ray1.97A1-335[»]
    4KLFX-ray1.85A1-335[»]
    4KLGX-ray1.70A1-335[»]
    4KLHX-ray1.88A1-335[»]
    4KLIX-ray1.60A1-335[»]
    4KLJX-ray1.80A1-335[»]
    4KLLX-ray1.84A1-335[»]
    4KLMX-ray1.75A1-335[»]
    4KLOX-ray1.84A1-335[»]
    4KLQX-ray2.00A1-335[»]
    4KLSX-ray1.98A1-335[»]
    4KLTX-ray1.98A1-335[»]
    4KLUX-ray1.97A1-335[»]
    4LVSX-ray2.00A1-335[»]
    4M2YX-ray2.27A11-335[»]
    4M47X-ray2.37A12-335[»]
    4M9GX-ray2.01A1-335[»]
    4M9HX-ray2.39A1-335[»]
    4M9JX-ray2.04A1-335[»]
    4M9LX-ray2.09A1-335[»]
    4M9NX-ray2.28A1-335[»]
    4MF2X-ray2.40A11-335[»]
    4MFCX-ray2.13A11-335[»]
    4MFFX-ray2.55A11-335[»]
    4NLKX-ray2.49A7-335[»]
    4NLNX-ray2.26A7-335[»]
    4NLZX-ray2.68A7-335[»]
    4NM1X-ray2.42A7-335[»]
    4NM2X-ray2.52A7-335[»]
    4NXZX-ray2.56A10-335[»]
    4NY8X-ray2.25A10-335[»]
    4O9MX-ray2.30A1-335[»]
    4PPXX-ray2.08A1-335[»]
    7ICEX-ray2.80A1-335[»]
    7ICFX-ray3.10A1-335[»]
    7ICGX-ray3.00A1-335[»]
    7ICHX-ray2.90A1-335[»]
    7ICIX-ray2.80A1-335[»]
    7ICJX-ray3.50A1-335[»]
    7ICKX-ray2.90A1-335[»]
    7ICLX-ray3.10A1-335[»]
    7ICMX-ray3.00A1-335[»]
    7ICNX-ray2.80A1-335[»]
    7ICOX-ray3.30A1-335[»]
    7ICPX-ray3.00A1-335[»]
    7ICQX-ray2.90A1-335[»]
    7ICRX-ray3.00A1-335[»]
    7ICSX-ray2.80A1-335[»]
    7ICTX-ray2.80A1-335[»]
    7ICUX-ray3.30A1-335[»]
    7ICVX-ray2.80A1-335[»]
    8ICAX-ray3.00A1-335[»]
    8ICBX-ray3.10A1-335[»]
    8ICCX-ray2.80A1-335[»]
    8ICEX-ray3.20A1-335[»]
    8ICFX-ray2.90A1-335[»]
    8ICGX-ray3.30A1-335[»]
    8ICHX-ray3.30A1-335[»]
    8ICIX-ray2.80A1-335[»]
    8ICJX-ray3.20A1-335[»]
    8ICKX-ray2.70A1-335[»]
    8ICLX-ray3.10A1-335[»]
    8ICMX-ray2.90A1-335[»]
    8ICNX-ray2.80A1-335[»]
    8ICOX-ray2.70A1-335[»]
    8ICPX-ray2.90A1-335[»]
    8ICQX-ray3.00A1-335[»]
    8ICRX-ray2.90A1-335[»]
    8ICSX-ray2.90A1-335[»]
    8ICTX-ray3.10A1-335[»]
    8ICUX-ray3.00A1-335[»]
    8ICVX-ray3.20A1-335[»]
    8ICWX-ray3.30A1-335[»]
    8ICXX-ray3.00A1-335[»]
    8ICYX-ray3.10A1-335[»]
    8ICZX-ray3.10A1-335[»]
    9ICAX-ray3.00A1-335[»]
    9ICBX-ray3.20A1-335[»]
    9ICCX-ray3.10A1-335[»]
    9ICEX-ray3.30A1-335[»]
    9ICFX-ray3.00A1-335[»]
    9ICGX-ray3.00A1-335[»]
    9ICHX-ray2.90A1-335[»]
    9ICIX-ray3.10A1-335[»]
    9ICJX-ray3.10A1-335[»]
    9ICKX-ray2.70A1-335[»]
    9ICLX-ray2.80A1-335[»]
    9ICMX-ray2.90A1-335[»]
    9ICNX-ray3.00A1-335[»]
    9ICOX-ray2.90A1-335[»]
    9ICPX-ray3.10A1-335[»]
    9ICQX-ray2.90A1-335[»]
    9ICRX-ray3.00A1-335[»]
    9ICSX-ray2.90A1-335[»]
    9ICTX-ray3.00A1-335[»]
    9ICUX-ray2.90A1-335[»]
    9ICVX-ray2.70A1-335[»]
    9ICWX-ray2.60A1-335[»]
    9ICXX-ray2.60A1-335[»]
    9ICYX-ray3.00A1-335[»]
    ProteinModelPortaliP06746.
    SMRiP06746. Positions 10-335.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06746.

    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.By similarity

    Sequence similaritiesi

    Belongs to the DNA polymerase type-X family.Curated

    Phylogenomic databases

    eggNOGiCOG1796.
    HOGENOMiHOG000007787.
    HOVERGENiHBG002359.
    InParanoidiP06746.
    KOiK02330.
    OMAiRYREPKD.
    PhylomeDBiP06746.
    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.

    P06746-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKRKAPQET LNGGITDMLT ELANFEKNVS QAIHKYNAYR KAASVIAKYP    50
    HKIKSGAEAK KLPGVGTKIA EKIDEFLATG KLRKLEKIRQ DDTSSSINFL 100
    TRVSGIGPSA ARKFVDEGIK TLEDLRKNED KLNHHQRIGL KYFGDFEKRI 150
    PREEMLQMQD IVLNEVKKVD SEYIATVCGS FRRGAESSGD MDVLLTHPSF 200
    TSESTKQPKL LHQVVEQLQK VHFITDTLSK GETKFMGVCQ LPSKNDEKEY 250
    PHRRIDIRLI PKDQYYCGVL YFTGSDIFNK NMRAHALEKG FTINEYTIRP 300
    LGVTGVAGEP LPVDSEKDIF DYIQWKYREP KDRSE 335
    Length:335
    Mass (Da):38,178
    Last modified:January 23, 2007 - v3
    Checksum:iFF9A6D0E6F9A9487
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181M → K in AAB60688. (PubMed:7914364)Curated
    Sequence conflicti228 – 2281L → R in AAA60133. (PubMed:2423078)Curated
    Sequence conflicti260 – 2601I → Y in AAA60133. (PubMed:2423078)Curated
    Sequence conflicti287 – 2871L → K in AAA60133. (PubMed:2423078)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti242 – 2421P → R.1 Publication
    Corresponds to variant rs3136797 [ dbSNP | Ensembl ].
    VAR_018881

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11607 mRNA. Translation: AAB59441.1.
    D29013 mRNA. Translation: BAA06099.1.
    U10526
    , U10516, U10517, U10519, U10520, U10521, U10522, U10523, U10524, U10525 Genomic DNA. Translation: AAB60688.1.
    AK314976 mRNA. Translation: BAG37475.1.
    CR536503 mRNA. Translation: CAG38741.1.
    CR541802 mRNA. Translation: CAG46601.1.
    AF491812 Genomic DNA. Translation: AAL91594.1.
    BC100288 mRNA. Translation: AAI00289.1.
    BC106909 mRNA. Translation: AAI06910.1.
    J04201 Genomic DNA. Translation: AAA60134.1.
    M13140 mRNA. Translation: AAA60133.1.
    CCDSiCCDS6129.1.
    PIRiI55273.
    S48061.
    RefSeqiNP_002681.1. NM_002690.2.
    UniGeneiHs.654484.

    Genome annotation databases

    EnsembliENST00000265421; ENSP00000265421; ENSG00000070501.
    GeneIDi5423.
    KEGGihsa:5423.
    UCSCiuc003xoz.2. human.

    Polymorphism databases

    DMDMi544186.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11607 mRNA. Translation: AAB59441.1 .
    D29013 mRNA. Translation: BAA06099.1 .
    U10526
    , U10516 , U10517 , U10519 , U10520 , U10521 , U10522 , U10523 , U10524 , U10525 Genomic DNA. Translation: AAB60688.1 .
    AK314976 mRNA. Translation: BAG37475.1 .
    CR536503 mRNA. Translation: CAG38741.1 .
    CR541802 mRNA. Translation: CAG46601.1 .
    AF491812 Genomic DNA. Translation: AAL91594.1 .
    BC100288 mRNA. Translation: AAI00289.1 .
    BC106909 mRNA. Translation: AAI06910.1 .
    J04201 Genomic DNA. Translation: AAA60134.1 .
    M13140 mRNA. Translation: AAA60133.1 .
    CCDSi CCDS6129.1.
    PIRi I55273.
    S48061.
    RefSeqi NP_002681.1. NM_002690.2.
    UniGenei Hs.654484.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BPX X-ray 2.40 A 1-335 [» ]
    1BPY X-ray 2.20 A 1-335 [» ]
    1BPZ X-ray 2.60 A 1-335 [» ]
    1MQ2 X-ray 3.10 A 1-335 [» ]
    1MQ3 X-ray 2.80 A 1-335 [» ]
    1TV9 X-ray 2.00 A 1-335 [» ]
    1TVA X-ray 2.60 A 1-335 [» ]
    1ZJM X-ray 2.10 A 1-335 [» ]
    1ZJN X-ray 2.61 A 1-335 [» ]
    1ZQA X-ray 3.20 A 1-335 [» ]
    1ZQB X-ray 3.20 A 1-335 [» ]
    1ZQC X-ray 3.20 A 1-335 [» ]
    1ZQD X-ray 3.50 A 1-335 [» ]
    1ZQE X-ray 3.70 A 1-335 [» ]
    1ZQF X-ray 2.90 A 1-335 [» ]
    1ZQG X-ray 3.10 A 1-335 [» ]
    1ZQH X-ray 3.10 A 1-335 [» ]
    1ZQI X-ray 2.70 A 1-335 [» ]
    1ZQJ X-ray 3.30 A 1-335 [» ]
    1ZQK X-ray 3.20 A 1-335 [» ]
    1ZQL X-ray 3.30 A 1-335 [» ]
    1ZQM X-ray 3.20 A 1-335 [» ]
    1ZQN X-ray 3.00 A 1-335 [» ]
    1ZQO X-ray 3.20 A 1-335 [» ]
    1ZQP X-ray 2.80 A 1-335 [» ]
    1ZQQ X-ray 3.30 A 1-335 [» ]
    1ZQR X-ray 3.70 A 1-335 [» ]
    1ZQS X-ray 3.30 A 1-335 [» ]
    1ZQT X-ray 3.40 A 1-335 [» ]
    2FMP X-ray 1.65 A 1-335 [» ]
    2FMQ X-ray 2.20 A 1-335 [» ]
    2FMS X-ray 2.00 A 1-335 [» ]
    2I9G X-ray 2.10 A 1-335 [» ]
    2ISO X-ray 2.10 A 1-335 [» ]
    2ISP X-ray 2.20 A 1-335 [» ]
    2P66 X-ray 2.50 A 1-335 [» ]
    2PXI X-ray 2.10 A 1-335 [» ]
    3C2K X-ray 2.40 A 1-335 [» ]
    3C2L X-ray 2.60 A 1-335 [» ]
    3C2M X-ray 2.15 A 1-335 [» ]
    3GDX X-ray 2.20 A 10-335 [» ]
    3ISB X-ray 2.00 A 1-335 [» ]
    3ISC X-ray 2.00 A 1-335 [» ]
    3ISD X-ray 2.60 A 1-335 [» ]
    3JPN X-ray 2.15 A 1-335 [» ]
    3JPO X-ray 2.00 A 1-335 [» ]
    3JPP X-ray 2.10 A 1-335 [» ]
    3JPQ X-ray 1.90 A 1-335 [» ]
    3JPR X-ray 2.10 A 1-335 [» ]
    3JPS X-ray 2.00 A 1-335 [» ]
    3JPT X-ray 2.15 A 1-335 [» ]
    3LK9 X-ray 2.50 A 1-335 [» ]
    3MBY X-ray 2.00 A 1-335 [» ]
    3OGU X-ray 1.84 A 1-335 [» ]
    3RH4 X-ray 1.92 A 1-335 [» ]
    3RH5 X-ray 2.10 A 1-335 [» ]
    3RH6 X-ray 2.05 A 1-335 [» ]
    3RJE X-ray 2.10 A 1-335 [» ]
    3RJF X-ray 2.30 A 1-335 [» ]
    3RJG X-ray 2.00 A 1-335 [» ]
    3RJH X-ray 2.20 A 1-335 [» ]
    3RJI X-ray 2.30 A 1-335 [» ]
    3RJJ X-ray 2.00 A 1-335 [» ]
    3RJK X-ray 2.10 A 1-335 [» ]
    3TFR X-ray 2.00 A 1-335 [» ]
    3TFS X-ray 2.00 A 1-335 [» ]
    4DO9 X-ray 2.05 A 1-335 [» ]
    4DOA X-ray 2.05 A 1-335 [» ]
    4DOB X-ray 2.05 A 1-335 [» ]
    4DOC X-ray 1.95 A 1-335 [» ]
    4F5N X-ray 1.80 A 1-335 [» ]
    4F5O X-ray 2.00 A 1-335 [» ]
    4F5P X-ray 1.85 A 1-335 [» ]
    4F5Q X-ray 2.25 A 1-335 [» ]
    4F5R X-ray 2.20 A/B 1-335 [» ]
    4GXI X-ray 1.95 A 1-335 [» ]
    4GXJ X-ray 2.20 A 1-335 [» ]
    4GXK X-ray 2.00 A 1-335 [» ]
    4JWM X-ray 2.00 A 1-335 [» ]
    4JWN X-ray 2.39 A 1-335 [» ]
    4KLD X-ray 1.92 A 1-335 [» ]
    4KLE X-ray 1.97 A 1-335 [» ]
    4KLF X-ray 1.85 A 1-335 [» ]
    4KLG X-ray 1.70 A 1-335 [» ]
    4KLH X-ray 1.88 A 1-335 [» ]
    4KLI X-ray 1.60 A 1-335 [» ]
    4KLJ X-ray 1.80 A 1-335 [» ]
    4KLL X-ray 1.84 A 1-335 [» ]
    4KLM X-ray 1.75 A 1-335 [» ]
    4KLO X-ray 1.84 A 1-335 [» ]
    4KLQ X-ray 2.00 A 1-335 [» ]
    4KLS X-ray 1.98 A 1-335 [» ]
    4KLT X-ray 1.98 A 1-335 [» ]
    4KLU X-ray 1.97 A 1-335 [» ]
    4LVS X-ray 2.00 A 1-335 [» ]
    4M2Y X-ray 2.27 A 11-335 [» ]
    4M47 X-ray 2.37 A 12-335 [» ]
    4M9G X-ray 2.01 A 1-335 [» ]
    4M9H X-ray 2.39 A 1-335 [» ]
    4M9J X-ray 2.04 A 1-335 [» ]
    4M9L X-ray 2.09 A 1-335 [» ]
    4M9N X-ray 2.28 A 1-335 [» ]
    4MF2 X-ray 2.40 A 11-335 [» ]
    4MFC X-ray 2.13 A 11-335 [» ]
    4MFF X-ray 2.55 A 11-335 [» ]
    4NLK X-ray 2.49 A 7-335 [» ]
    4NLN X-ray 2.26 A 7-335 [» ]
    4NLZ X-ray 2.68 A 7-335 [» ]
    4NM1 X-ray 2.42 A 7-335 [» ]
    4NM2 X-ray 2.52 A 7-335 [» ]
    4NXZ X-ray 2.56 A 10-335 [» ]
    4NY8 X-ray 2.25 A 10-335 [» ]
    4O9M X-ray 2.30 A 1-335 [» ]
    4PPX X-ray 2.08 A 1-335 [» ]
    7ICE X-ray 2.80 A 1-335 [» ]
    7ICF X-ray 3.10 A 1-335 [» ]
    7ICG X-ray 3.00 A 1-335 [» ]
    7ICH X-ray 2.90 A 1-335 [» ]
    7ICI X-ray 2.80 A 1-335 [» ]
    7ICJ X-ray 3.50 A 1-335 [» ]
    7ICK X-ray 2.90 A 1-335 [» ]
    7ICL X-ray 3.10 A 1-335 [» ]
    7ICM X-ray 3.00 A 1-335 [» ]
    7ICN X-ray 2.80 A 1-335 [» ]
    7ICO X-ray 3.30 A 1-335 [» ]
    7ICP X-ray 3.00 A 1-335 [» ]
    7ICQ X-ray 2.90 A 1-335 [» ]
    7ICR X-ray 3.00 A 1-335 [» ]
    7ICS X-ray 2.80 A 1-335 [» ]
    7ICT X-ray 2.80 A 1-335 [» ]
    7ICU X-ray 3.30 A 1-335 [» ]
    7ICV X-ray 2.80 A 1-335 [» ]
    8ICA X-ray 3.00 A 1-335 [» ]
    8ICB X-ray 3.10 A 1-335 [» ]
    8ICC X-ray 2.80 A 1-335 [» ]
    8ICE X-ray 3.20 A 1-335 [» ]
    8ICF X-ray 2.90 A 1-335 [» ]
    8ICG X-ray 3.30 A 1-335 [» ]
    8ICH X-ray 3.30 A 1-335 [» ]
    8ICI X-ray 2.80 A 1-335 [» ]
    8ICJ X-ray 3.20 A 1-335 [» ]
    8ICK X-ray 2.70 A 1-335 [» ]
    8ICL X-ray 3.10 A 1-335 [» ]
    8ICM X-ray 2.90 A 1-335 [» ]
    8ICN X-ray 2.80 A 1-335 [» ]
    8ICO X-ray 2.70 A 1-335 [» ]
    8ICP X-ray 2.90 A 1-335 [» ]
    8ICQ X-ray 3.00 A 1-335 [» ]
    8ICR X-ray 2.90 A 1-335 [» ]
    8ICS X-ray 2.90 A 1-335 [» ]
    8ICT X-ray 3.10 A 1-335 [» ]
    8ICU X-ray 3.00 A 1-335 [» ]
    8ICV X-ray 3.20 A 1-335 [» ]
    8ICW X-ray 3.30 A 1-335 [» ]
    8ICX X-ray 3.00 A 1-335 [» ]
    8ICY X-ray 3.10 A 1-335 [» ]
    8ICZ X-ray 3.10 A 1-335 [» ]
    9ICA X-ray 3.00 A 1-335 [» ]
    9ICB X-ray 3.20 A 1-335 [» ]
    9ICC X-ray 3.10 A 1-335 [» ]
    9ICE X-ray 3.30 A 1-335 [» ]
    9ICF X-ray 3.00 A 1-335 [» ]
    9ICG X-ray 3.00 A 1-335 [» ]
    9ICH X-ray 2.90 A 1-335 [» ]
    9ICI X-ray 3.10 A 1-335 [» ]
    9ICJ X-ray 3.10 A 1-335 [» ]
    9ICK X-ray 2.70 A 1-335 [» ]
    9ICL X-ray 2.80 A 1-335 [» ]
    9ICM X-ray 2.90 A 1-335 [» ]
    9ICN X-ray 3.00 A 1-335 [» ]
    9ICO X-ray 2.90 A 1-335 [» ]
    9ICP X-ray 3.10 A 1-335 [» ]
    9ICQ X-ray 2.90 A 1-335 [» ]
    9ICR X-ray 3.00 A 1-335 [» ]
    9ICS X-ray 2.90 A 1-335 [» ]
    9ICT X-ray 3.00 A 1-335 [» ]
    9ICU X-ray 2.90 A 1-335 [» ]
    9ICV X-ray 2.70 A 1-335 [» ]
    9ICW X-ray 2.60 A 1-335 [» ]
    9ICX X-ray 2.60 A 1-335 [» ]
    9ICY X-ray 3.00 A 1-335 [» ]
    ProteinModelPortali P06746.
    SMRi P06746. Positions 10-335.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111419. 17 interactions.
    IntActi P06746. 6 interactions.
    MINTi MINT-1393546.
    STRINGi 9606.ENSP00000265421.

    Chemistry

    BindingDBi P06746.
    ChEMBLi CHEMBL2392.
    DrugBanki DB00987. Cytarabine.

    PTM databases

    PhosphoSitei P06746.

    Polymorphism databases

    DMDMi 544186.

    Proteomic databases

    MaxQBi P06746.
    PaxDbi P06746.
    PeptideAtlasi P06746.
    PRIDEi P06746.

    Protocols and materials databases

    DNASUi 5423.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265421 ; ENSP00000265421 ; ENSG00000070501 .
    GeneIDi 5423.
    KEGGi hsa:5423.
    UCSCi uc003xoz.2. human.

    Organism-specific databases

    CTDi 5423.
    GeneCardsi GC08P042213.
    HGNCi HGNC:9174. POLB.
    HPAi CAB011616.
    MIMi 174760. gene.
    neXtProti NX_P06746.
    PharmGKBi PA276.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1796.
    HOGENOMi HOG000007787.
    HOVERGENi HBG002359.
    InParanoidi P06746.
    KOi K02330.
    OMAi RYREPKD.
    PhylomeDBi P06746.
    TreeFami TF103002.

    Enzyme and pathway databases

    Reactomei REACT_1357. Base-free sugar-phosphate removal via the single-nucleotide replacement pathway.
    REACT_2192. Removal of DNA patch containing abasic residue.
    REACT_933. Resolution of AP sites via the single-nucleotide replacement pathway.

    Miscellaneous databases

    EvolutionaryTracei P06746.
    GeneWikii DNA_polymerase_beta.
    GenomeRNAii 5423.
    NextBioi 20981.
    PROi P06746.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P06746.
    Bgeei P06746.
    CleanExi HS_POLB.
    Genevestigatori P06746.

    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. "Molecular cloning and high-level expression of human polymerase beta cDNA and comparison of the purified recombinant human and rat enzymes."
      Patterson T.A., Little W., Cheng X., Widen S.G., Kumar A., Beard W.A., Wilson S.H.
      Protein Expr. Purif. 18:100-110(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Polymorphisms in the human DNA polymerase beta gene."
      Dobashi Y., Kubota Y., Shuin T., Torigoe S., Yao M., Hosaka M.
      Hum. Genet. 95:389-390(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The human DNA polymerase beta gene structure. Evidence of alternative splicing in gene expression."
      Chyan Y.-J., Ackerman S., Shepherd N.S., McBride O.W., Widen S.G., Wilson S.H., Wood T.G.
      Nucleic Acids Res. 22:2719-2725(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Skin.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. NIEHS SNPs program
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-242.
    7. "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: Skin.
    8. "Human beta-polymerase gene. Structure of the 5'-flanking region and active promoter."
      Widen S.G., Kedar P., Wilson S.H.
      J. Biol. Chem. 263:16992-16998(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
    9. "Expression of human DNA polymerase beta in Escherichia coli and characterization of the recombinant enzyme."
      Abbotts J., Sengupta D.N., Zmudzka B., Widen S.G., Notario V., Wilson S.H.
      Biochemistry 27:901-909(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-32.
    10. "Sequence of human DNA polymerase beta mRNA obtained through cDNA cloning."
      Sengupta D.N., Zmudzka B.Z., Kumar P., Cobianchi F., Skowronski J., Wilson S.H.
      Biochem. Biophys. Res. Commun. 136:341-347(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-335.
    11. "Interaction of human apurinic endonuclease and DNA polymerase beta in the base excision repair pathway."
      Bennett R.A., Wilson D.M. III, Wong D., Demple B.
      Proc. Natl. Acad. Sci. U.S.A. 94:7166-7169(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH APEX1.
    12. "Catalytic center of DNA polymerase beta for excision of deoxyribose phosphate groups."
      Matsumoto Y., Kim K., Katz D.S., Feng J.-A.
      Biochemistry 37:6456-6464(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-35; TYR-39; LYS-68; LYS-72 AND LYS-84.
    13. "Covalent trapping of human DNA polymerase beta by the oxidative DNA lesion 2-deoxyribonolactone."
      DeMott M.S., Beyret E., Wong D., Bales B.C., Hwang J.-T., Greenberg M.M., Demple B.
      J. Biol. Chem. 277:7637-7640(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. Cited for: METHYLATION AT ARG-83 AND ARG-152 BY PRMT6, MUTAGENESIS OF ARG-83 AND ARG-152.
    15. Cited for: SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-41; LYS-61 AND LYS-81, MUTAGENESIS OF LYS-41; LYS-61 AND LYS-81.
    16. "USP47 is a deubiquitylating enzyme that regulates base excision repair by controlling steady-state levels of DNA Polymerase beta."
      Parsons J.L., Dianova I.I., Khoronenkova S.V., Edelmann M.J., Kessler B.M., Dianov G.L.
      Mol. Cell 41:609-615(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-41; LYS-61 AND LYS-81, DEUBIQUITINATION BY USP47, INTERACTION WITH USP47.
    17. "A structural basis for metal ion mutagenicity and nucleotide selectivity in human DNA polymerase beta."
      Pelletier H., Sawaya M.R., Wolfle W., Wilson S.H., Kraut J.
      Biochemistry 35:12762-12777(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH DNA; ATP AND METAL IONS.
    18. "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) IN COMPLEX WITH DNA AND METAL IONS.
    19. "Crystal structures of human DNA polymerase beta complexed with gapped and nicked DNA: evidence for an induced fit mechanism."
      Sawaya M.R., Prasad R., Wilson S.H., Kraut J., Pelletier H.
      Biochemistry 36:11205-11215(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH DNA.
    20. "Structure of DNA polymerase beta with the mutagenic DNA lesion 8-oxodeoxyguanine reveals structural insights into its coding potential."
      Krahn J.M., Beard W.A., Miller H., Grollman A.P., Wilson S.H.
      Structure 11:121-127(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH DNA.

    Entry informationi

    Entry nameiDPOLB_HUMAN
    AccessioniPrimary (citable) accession number: P06746
    Secondary accession number(s): B2RC78, Q3KP48, Q6FI34
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 179 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3