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P06746

- DPOLB_HUMAN

UniProt

P06746 - DPOLB_HUMAN

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Protein
DNA polymerase beta
Gene
POLB
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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. DNA-directed DNA polymerase activity Source: UniProtKB
  2. damaged DNA binding Source: Ensembl
  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
Complete GO annotation...

GO - Biological processi

  1. DNA repair Source: Reactome
  2. DNA-dependent DNA replication Source: ProtInc
  3. base-excision repair Source: UniProtKB
  4. base-excision repair, gap-filling Source: Ensembl
  5. cellular response to DNA damage stimulus Source: UniProtKB
  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
Complete GO annotation...

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.2 Publications

GO - Cellular componenti

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

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 beta
PRO_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-acetyllysine By 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 USP47.2 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

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.

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

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

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181M → K in AAB60688. 1 Publication
Sequence conflicti228 – 2281L → R in AAA60133. 1 Publication
Sequence conflicti260 – 2601I → Y in AAA60133. 1 Publication
Sequence conflicti287 – 2871L → K in AAA60133. 1 Publication

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 178 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

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