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UniProtKB - P06746 (DPOLB_HUMAN)

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Protein

DNA polymerase beta

Gene

POLB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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) endonuclease 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
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionDNA-binding, DNA-directed DNA polymerase, Lyase, Nucleotidyltransferase, Transferase
Biological processDNA damage, DNA repair, DNA replication, DNA synthesis
LigandMagnesium, Metal-binding, Sodium

Enzyme and pathway databases

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
SIGNORiP06746

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

EuPathDBiHostDB:ENSG00000070501.11
HGNCiHGNC:9174 POLB
MIMi174760 gene
neXtProtiNX_P06746

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
DrugBankiDB03222 2'-Deoxyadenosine 5'-Triphosphate
DB00987 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
ProteomicsDBi51926

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

Show more details

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • microtubule binding Source: MGI
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi111419, 39 interactors
CORUMiP06746
IntActiP06746, 17 interactors
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[»]
5EOZX-ray2.09A1-335[»]
5HHHX-ray2.36A9-335[»]
5HHIX-ray2.52A7-335[»]
5J0OX-ray2.00A1-335[»]
5J0PX-ray2.20A1-335[»]
5J0QX-ray2.00A1-335[»]
5J0RX-ray2.00A1-335[»]
5J0SX-ray2.00A1-335[»]
5J0TX-ray2.00A1-335[»]
5J0UX-ray2.10A1-335[»]
5J0WX-ray2.40A1-335[»]
5J0XX-ray2.00A1-335[»]
5J0YX-ray2.00A1-335[»]
5J29X-ray2.20A1-335[»]
5J2AX-ray2.50A1-335[»]
5J2BX-ray2.50A1-335[»]
5J2CX-ray2.10A1-335[»]
5J2DX-ray2.10A1-335[»]
5J2EX-ray2.10A1-335[»]
5J2FX-ray2.10A1-335[»]
5J2GX-ray2.10A1-335[»]
5J2HX-ray2.30A1-335[»]
5J2IX-ray2.40A1-335[»]
5J2JX-ray2.20A1-335[»]
5J2KX-ray2.10A1-335[»]
5TB8X-ray2.00A1-335[»]
5TB9X-ray2.49A1-335[»]
5TBAX-ray2.49A1-335[»]
5TBBX-ray2.39A1-335[»]
5TBCX-ray1.85A1-335[»]
5TZVX-ray2.00A1-335[»]
5U2RX-ray1.80A1-335[»]
5U2SX-ray2.30A1-335[»]
5U2TX-ray1.79A1-335[»]
5U8GX-ray2.17A1-335[»]
5U8HX-ray2.15A1-335[»]
5U8IX-ray2.45A1-335[»]
5U9HX-ray1.85A1-335[»]
5UGNX-ray2.00A1-335[»]
5UGOX-ray1.90A1-335[»]
5UGPX-ray1.96A1-335[»]
5V1FX-ray2.18A1-335[»]
5V1GX-ray1.80A1-335[»]
5V1HX-ray1.95A1-335[»]
5V1IX-ray2.04A1-335[»]
5V1JX-ray2.62A1-335[»]
5V1NX-ray2.00A1-335[»]
5V1OX-ray1.80A1-335[»]
5V1PX-ray1.99A1-335[»]
5V1RX-ray2.08A1-335[»]
5VEZX-ray2.04A1-335[»]
5VRWX-ray2.58A1-335[»]
5VRXX-ray2.20A1-335[»]
5VRYX-ray1.90A1-335[»]
5VRZX-ray2.05A1-335[»]
5VS0X-ray2.10A1-335[»]
5VS1X-ray2.50A1-335[»]
5VS2X-ray2.33A1-335[»]
5VS3X-ray1.70A1-335[»]
5VS4X-ray1.87A1-335[»]
5WNXX-ray2.55A1-335[»]
5WNYX-ray2.10A1-335[»]
5WNZX-ray2.20A1-335[»]
5WO0X-ray1.60A1-335[»]
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
OMAiDLFNKNM
OrthoDBiEOG091G0HMG
PhylomeDBiP06746
TreeFamiTF103002

Family and domain databases

CDDicd00141 NT_POLXc, 1 hit
Gene3Di1.10.150.110, 1 hit
3.30.210.10, 1 hit
InterProiView protein in InterPro
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
IPR027421 DNA_pol_lamdba_lyase_dom_sf
IPR037160 DNA_Pol_thumb_sf
IPR022312 DNA_pol_X
IPR002008 DNA_pol_X_beta-like
IPR003583 Hlx-hairpin-Hlx_DNA-bd_motif
IPR029398 PolB_thumb
PfamiView protein in Pfam
PF14792 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
PRINTSiPR00869 DNAPOLX
PR00870 DNAPOLXBETA
SMARTiView protein in SMART
SM00278 HhH1, 2 hits
SM00483 POLXc, 1 hit
SUPFAMiSSF47802 SSF47802, 1 hit
PROSITEiView protein in PROSITE
PS00522 DNA_POLYMERASE_X, 1 hit

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 → R1 PublicationCorresponds to variant dbSNP:rs3136797Ensembl.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

Similar proteinsi

Entry informationi

Entry nameiDPOLB_HUMAN
AccessioniPrimary (citable) accession number: P06746
Secondary accession number(s): B2RC78, Q3KP48, Q6FI34
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 217 of the entry and version 3 of the sequence. See 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

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