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Protein

DNA polymerase beta

Gene

POLB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Mg2+By similarityNote: Binds 2 magnesium ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei72Schiff-base intermediate with DNA1
Metal bindingi101Sodium; via carbonyl oxygen1
Metal bindingi103Sodium; via carbonyl oxygen1
Metal bindingi106Sodium; via carbonyl oxygen1
Metal bindingi190Magnesium 11
Metal bindingi190Magnesium 21
Metal bindingi192Magnesium 11
Metal bindingi192Magnesium 21
Metal bindingi256Magnesium 21

GO - Molecular functioni

  • damaged DNA binding Source: Ensembl
  • DNA-(apurinic or apyrimidinic site) lyase activity Source: Reactome
  • DNA-directed DNA polymerase activity Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • lyase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • microtubule binding Source: MGI

GO - Biological processi

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

BioCyciZFISH:HS00997-MONOMER.
BRENDAi2.7.7.7. 2681.
4.2.99.B1. 2681.
ReactomeiR-HSA-110362. POLB-Dependent Long Patch Base Excision Repair.
R-HSA-110373. Resolution of AP sites via the multiple-nucleotide patch replacement pathway.
R-HSA-110381. Resolution of AP sites via the single-nucleotide replacement pathway.
R-HSA-5649702. APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
R-HSA-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-73930. Abasic sugar-phosphate removal 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
Proteomesi
  • UP000005640 Componenti: 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

  • cytoplasm Source: UniProtKB
  • microtubule Source: MGI
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • protein complex Source: MGI
  • spindle microtubule Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi35K → Q or R: Reduces DNA lyase activity slightly. 1 Publication1
Mutagenesisi39Y → Q: Abolishes DNA polymerase and DNA lyase activity. 1 Publication1
Mutagenesisi41K → R: Abolishes ubiquitination; when associated with R-61 and R-81. 1 Publication1
Mutagenesisi61K → R: Abolishes ubiquitination; when associated with R-41 and R-81. 1 Publication1
Mutagenesisi68K → Q or R: Reduces DNA lyase activity slightly. 1 Publication1
Mutagenesisi72K → Q or R: Abolishes DNA lyase activity. No effect on DNA polymerase activity. 1 Publication1
Mutagenesisi81K → R: Abolishes ubiquitination; when associated with R-41 and R-61. 1 Publication1
Mutagenesisi83R → K: Slight effect. Abolishes methylation by PRMT6 and impairs the polymerase activity; when associated with K-152. 1 Publication1
Mutagenesisi84K → R: No effect. 1 Publication1
Mutagenesisi152R → K: Slight effect. Abolishes methylation by PRMT6 and impairs the polymerase activity; when associated with K-83. 1 Publication1

Organism-specific databases

DisGeNETi5423.
OpenTargetsiENSG00000070501.
PharmGKBiPA276.

Chemistry databases

ChEMBLiCHEMBL2392.
DrugBankiDB00987. Cytarabine.

Polymorphism and mutation databases

BioMutaiPOLB.
DMDMi544186.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002187781 – 335DNA polymerase betaAdd BLAST335

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki41Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Cross-linki61Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Modified residuei72N6-acetyllysineBy similarity1
Cross-linki81Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Modified residuei83Omega-N-methylarginine; by PRMT61 Publication1
Modified residuei152Omega-N-methylarginine; by PRMT61 Publication1

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

EPDiP06746.
MaxQBiP06746.
PaxDbiP06746.
PeptideAtlasiP06746.
PRIDEiP06746.

PTM databases

iPTMnetiP06746.
PhosphoSitePlusiP06746.

Expressioni

Gene expression databases

BgeeiENSG00000070501.
CleanExiHS_POLB.
ExpressionAtlasiP06746. baseline and differential.
GenevisibleiP06746. HS.

Organism-specific databases

HPAiCAB011616.
HPA049104.

Interactioni

Subunit structurei

Monomer. Interacts with APEX1, HUWE1/ARF-BP1, STUB1/CHIP and USP47. Interacts with FAM168A (PubMed:25260657).7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TAF1DQ9H5J84EBI-713836,EBI-716128
TPP2P291443EBI-713836,EBI-1044672

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • microtubule binding Source: MGI

Protein-protein interaction databases

BioGridi111419. 39 interactors.
IntActiP06746. 17 interactors.
MINTiMINT-1393546.
STRINGi9606.ENSP00000265421.

Chemistry databases

BindingDBiP06746.

Structurei

Secondary structure

1335
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni9 – 12Combined sources4
Helixi13 – 28Combined sources16
Helixi33 – 48Combined sources16
Helixi56 – 60Combined sources5
Beta strandi62 – 64Combined sources3
Helixi67 – 79Combined sources13
Helixi83 – 90Combined sources8
Helixi92 – 100Combined sources9
Turni101 – 105Combined sources5
Helixi108 – 116Combined sources9
Helixi122 – 127Combined sources6
Helixi128 – 131Combined sources4
Helixi134 – 141Combined sources8
Helixi143 – 146Combined sources4
Helixi152 – 169Combined sources18
Beta strandi174 – 177Combined sources4
Helixi179 – 182Combined sources4
Beta strandi186 – 196Combined sources11
Beta strandi202 – 204Combined sources3
Beta strandi207 – 209Combined sources3
Helixi210 – 220Combined sources11
Beta strandi224 – 230Combined sources7
Beta strandi232 – 239Combined sources8
Beta strandi245 – 247Combined sources3
Beta strandi253 – 259Combined sources7
Helixi262 – 264Combined sources3
Helixi265 – 273Combined sources9
Helixi276 – 289Combined sources14
Beta strandi291 – 293Combined sources3
Beta strandi298 – 301Combined sources4
Beta strandi303 – 305Combined sources3
Helixi316 – 322Combined sources7
Helixi330 – 332Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4MF8X-ray2.32A7-335[»]
4MFAX-ray2.27A11-335[»]
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[»]
4O5CX-ray2.36A7-335[»]
4O5EX-ray2.53A7-335[»]
4O5KX-ray2.06A10-335[»]
4O9MX-ray2.30A1-335[»]
4P2HX-ray1.99A10-335[»]
4PGQX-ray2.30A7-335[»]
4PGXX-ray2.08A10-335[»]
4PGYX-ray2.26A7-335[»]
4PH5X-ray2.55A10-335[»]
4PHAX-ray2.52A7-335[»]
4PHDX-ray2.21A7-335[»]
4PHEX-ray2.15A7-335[»]
4PHPX-ray2.60A10-335[»]
4PPXX-ray2.08A1-335[»]
4R63X-ray1.85A1-335[»]
4R64X-ray2.20A1-335[»]
4R65X-ray1.95A1-335[»]
4R66X-ray2.25A1-335[»]
4RPXX-ray1.90A1-335[»]
4RPYX-ray1.90A1-335[»]
4RPZX-ray2.19A1-335[»]
4RQ0X-ray2.20A1-335[»]
4RQ1X-ray2.70A1-335[»]
4RQ2X-ray2.20A1-335[»]
4RQ3X-ray2.00A1-335[»]
4RQ4X-ray2.10A1-335[»]
4RQ5X-ray2.32A1-335[»]
4RQ6X-ray2.25A1-335[»]
4RQ7X-ray2.00A1-335[»]
4RQ8X-ray2.00A1-335[»]
4RT2X-ray1.92A1-335[»]
4RT3X-ray1.92A1-335[»]
4TUPX-ray1.80A7-335[»]
4TUQX-ray2.37A10-335[»]
4TURX-ray2.17A7-335[»]
4TUSX-ray2.42A10-335[»]
4UAWX-ray1.90A1-335[»]
4UAYX-ray1.98A1-335[»]
4UAZX-ray1.88A1-335[»]
4UB1X-ray2.34A1-335[»]
4UB2X-ray2.51A1-335[»]
4UB3X-ray2.06A1-335[»]
4UB4X-ray1.95A1-335[»]
4UB5X-ray2.15A1-335[»]
4UBBX-ray1.90A1-335[»]
4UBCX-ray2.00A1-335[»]
4YMMX-ray2.20A1-335[»]
4YMNX-ray2.59A1-335[»]
4YMOX-ray2.15A1-335[»]
4YN4X-ray2.24A1-335[»]
4Z6CX-ray2.68A1-335[»]
4Z6DX-ray2.51A1-335[»]
4Z6EX-ray2.75A1-335[»]
4Z6FX-ray2.44A1-335[»]
5BOLX-ray1.98A1-335[»]
5BOMX-ray2.00A1-335[»]
5BPCX-ray2.00A1-335[»]
5DB6X-ray2.83A1-335[»]
5DB7X-ray2.21A1-335[»]
5DB8X-ray2.55A1-335[»]
5DB9X-ray2.45A1-335[»]
5DBAX-ray1.97A1-335[»]
5DBBX-ray2.25A1-335[»]
5DBCX-ray2.40A1-335[»]
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06746.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni183 – 192DNA binding10

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

eggNOGiKOG2534. Eukaryota.
COG1796. LUCA.
GeneTreeiENSGT00530000063002.
HOGENOMiHOG000007787.
HOVERGENiHBG002359.
InParanoidiP06746.
KOiK02330.
OMAiADYEKNV.
OrthoDBiEOG091G0HMG.
PhylomeDBiP06746.
TreeFamiTF103002.

Family and domain databases

CDDicd00141. NT_POLXc. 1 hit.
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.
PF14716. HHH_8. 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

        10         20         30         40         50
MSKRKAPQET LNGGITDMLT ELANFEKNVS QAIHKYNAYR KAASVIAKYP
60 70 80 90 100
HKIKSGAEAK KLPGVGTKIA EKIDEFLATG KLRKLEKIRQ DDTSSSINFL
110 120 130 140 150
TRVSGIGPSA ARKFVDEGIK TLEDLRKNED KLNHHQRIGL KYFGDFEKRI
160 170 180 190 200
PREEMLQMQD IVLNEVKKVD SEYIATVCGS FRRGAESSGD MDVLLTHPSF
210 220 230 240 250
TSESTKQPKL LHQVVEQLQK VHFITDTLSK GETKFMGVCQ LPSKNDEKEY
260 270 280 290 300
PHRRIDIRLI PKDQYYCGVL YFTGSDIFNK NMRAHALEKG FTINEYTIRP
310 320 330
LGVTGVAGEP LPVDSEKDIF DYIQWKYREP KDRSE
Length:335
Mass (Da):38,178
Last modified:January 23, 2007 - v3
Checksum:iFF9A6D0E6F9A9487
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti18M → K in AAB60688 (PubMed:7914364).Curated1
Sequence conflicti228L → R in AAA60133 (PubMed:2423078).Curated1
Sequence conflicti260I → Y in AAA60133 (PubMed:2423078).Curated1
Sequence conflicti287L → K in AAA60133 (PubMed:2423078).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_018881242P → R.1 PublicationCorresponds to variant rs3136797dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
Hs.661106.

Genome annotation databases

EnsembliENST00000265421; ENSP00000265421; ENSG00000070501.
GeneIDi5423.
KEGGihsa:5423.
UCSCiuc003xoz.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
Hs.661106.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4MF8X-ray2.32A7-335[»]
4MFAX-ray2.27A11-335[»]
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[»]
4O5CX-ray2.36A7-335[»]
4O5EX-ray2.53A7-335[»]
4O5KX-ray2.06A10-335[»]
4O9MX-ray2.30A1-335[»]
4P2HX-ray1.99A10-335[»]
4PGQX-ray2.30A7-335[»]
4PGXX-ray2.08A10-335[»]
4PGYX-ray2.26A7-335[»]
4PH5X-ray2.55A10-335[»]
4PHAX-ray2.52A7-335[»]
4PHDX-ray2.21A7-335[»]
4PHEX-ray2.15A7-335[»]
4PHPX-ray2.60A10-335[»]
4PPXX-ray2.08A1-335[»]
4R63X-ray1.85A1-335[»]
4R64X-ray2.20A1-335[»]
4R65X-ray1.95A1-335[»]
4R66X-ray2.25A1-335[»]
4RPXX-ray1.90A1-335[»]
4RPYX-ray1.90A1-335[»]
4RPZX-ray2.19A1-335[»]
4RQ0X-ray2.20A1-335[»]
4RQ1X-ray2.70A1-335[»]
4RQ2X-ray2.20A1-335[»]
4RQ3X-ray2.00A1-335[»]
4RQ4X-ray2.10A1-335[»]
4RQ5X-ray2.32A1-335[»]
4RQ6X-ray2.25A1-335[»]
4RQ7X-ray2.00A1-335[»]
4RQ8X-ray2.00A1-335[»]
4RT2X-ray1.92A1-335[»]
4RT3X-ray1.92A1-335[»]
4TUPX-ray1.80A7-335[»]
4TUQX-ray2.37A10-335[»]
4TURX-ray2.17A7-335[»]
4TUSX-ray2.42A10-335[»]
4UAWX-ray1.90A1-335[»]
4UAYX-ray1.98A1-335[»]
4UAZX-ray1.88A1-335[»]
4UB1X-ray2.34A1-335[»]
4UB2X-ray2.51A1-335[»]
4UB3X-ray2.06A1-335[»]
4UB4X-ray1.95A1-335[»]
4UB5X-ray2.15A1-335[»]
4UBBX-ray1.90A1-335[»]
4UBCX-ray2.00A1-335[»]
4YMMX-ray2.20A1-335[»]
4YMNX-ray2.59A1-335[»]
4YMOX-ray2.15A1-335[»]
4YN4X-ray2.24A1-335[»]
4Z6CX-ray2.68A1-335[»]
4Z6DX-ray2.51A1-335[»]
4Z6EX-ray2.75A1-335[»]
4Z6FX-ray2.44A1-335[»]
5BOLX-ray1.98A1-335[»]
5BOMX-ray2.00A1-335[»]
5BPCX-ray2.00A1-335[»]
5DB6X-ray2.83A1-335[»]
5DB7X-ray2.21A1-335[»]
5DB8X-ray2.55A1-335[»]
5DB9X-ray2.45A1-335[»]
5DBAX-ray1.97A1-335[»]
5DBBX-ray2.25A1-335[»]
5DBCX-ray2.40A1-335[»]
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111419. 39 interactors.
IntActiP06746. 17 interactors.
MINTiMINT-1393546.
STRINGi9606.ENSP00000265421.

Chemistry databases

BindingDBiP06746.
ChEMBLiCHEMBL2392.
DrugBankiDB00987. Cytarabine.

PTM databases

iPTMnetiP06746.
PhosphoSitePlusiP06746.

Polymorphism and mutation databases

BioMutaiPOLB.
DMDMi544186.

Proteomic databases

EPDiP06746.
MaxQBiP06746.
PaxDbiP06746.
PeptideAtlasiP06746.
PRIDEiP06746.

Protocols and materials databases

DNASUi5423.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265421; ENSP00000265421; ENSG00000070501.
GeneIDi5423.
KEGGihsa:5423.
UCSCiuc003xoz.3. human.

Organism-specific databases

CTDi5423.
DisGeNETi5423.
GeneCardsiPOLB.
HGNCiHGNC:9174. POLB.
HPAiCAB011616.
HPA049104.
MIMi174760. gene.
neXtProtiNX_P06746.
OpenTargetsiENSG00000070501.
PharmGKBiPA276.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2534. Eukaryota.
COG1796. LUCA.
GeneTreeiENSGT00530000063002.
HOGENOMiHOG000007787.
HOVERGENiHBG002359.
InParanoidiP06746.
KOiK02330.
OMAiADYEKNV.
OrthoDBiEOG091G0HMG.
PhylomeDBiP06746.
TreeFamiTF103002.

Enzyme and pathway databases

BioCyciZFISH:HS00997-MONOMER.
BRENDAi2.7.7.7. 2681.
4.2.99.B1. 2681.
ReactomeiR-HSA-110362. POLB-Dependent Long Patch Base Excision Repair.
R-HSA-110373. Resolution of AP sites via the multiple-nucleotide patch replacement pathway.
R-HSA-110381. Resolution of AP sites via the single-nucleotide replacement pathway.
R-HSA-5649702. APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
R-HSA-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-73930. Abasic sugar-phosphate removal via the single-nucleotide replacement pathway.

Miscellaneous databases

EvolutionaryTraceiP06746.
GeneWikiiDNA_polymerase_beta.
GenomeRNAii5423.
PROiP06746.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000070501.
CleanExiHS_POLB.
ExpressionAtlasiP06746. baseline and differential.
GenevisibleiP06746. HS.

Family and domain databases

CDDicd00141. NT_POLXc. 1 hit.
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.
PF14716. HHH_8. 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]
ProtoNetiSearch...

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: November 2, 2016
This is version 201 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.