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P06746 (DPOLB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 177. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA polymerase beta

EC=2.7.7.7
EC=4.2.99.-
Gene names
Name:POLB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11 Ref.12 Ref.13 Ref.16

Catalytic activity

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

Cofactor

Binds 2 magnesium ions per subunit By similarity.

Subunit structure

Monomer. Interacts with APEX1, HUWE1/ARF-BP1, STUB1/CHIP and USP47. Ref.11 Ref.16

Subcellular location

Nucleus. Cytoplasm. Note: Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage. Ref.15 Ref.16

Domain

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

Post-translational modification

Methylation by PRMT6 stimulates the polymerase activity by enhancing DNA binding and processivity. Ref.14

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. Ref.15 Ref.16

Sequence similarities

Belongs to the DNA polymerase type-X family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
DNA replication
DNA synthesis
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   LigandDNA-binding
Magnesium
Metal-binding
Sodium
   Molecular functionDNA-directed DNA polymerase
Lyase
Nucleotidyltransferase
Transferase
   PTMAcetylation
Isopeptide bond
Methylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA biosynthetic process

Inferred from electronic annotation. Source: Ensembl

DNA repair

Traceable author statement. Source: Reactome

DNA-dependent DNA replication

Traceable author statement PubMed 8168825. Source: ProtInc

base-excision repair

Inferred from direct assay Ref.14. Source: UniProtKB

base-excision repair, gap-filling

Inferred from electronic annotation. Source: Ensembl

cellular response to DNA damage stimulus

Inferred from mutant phenotype Ref.16. Source: UniProtKB

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from electronic annotation. Source: Ensembl

neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

pyrimidine dimer repair

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay Ref.15Ref.16. Source: UniProtKB

microtubule

Inferred from direct assay PubMed 15725623. Source: MGI

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.15Ref.16. Source: UniProtKB

spindle microtubule

Inferred from direct assay PubMed 15725623. Source: MGI

   Molecular_functionDNA-directed DNA polymerase activity

Inferred from direct assay Ref.14Ref.11. Source: UniProtKB

damaged DNA binding

Inferred from electronic annotation. Source: Ensembl

enzyme binding

Inferred from physical interaction Ref.14Ref.15Ref.16. Source: UniProtKB

lyase activity

Inferred from direct assay Ref.14. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule binding

Inferred from direct assay PubMed 15725623. Source: MGI

protein binding

Inferred from physical interaction Ref.11. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TAF1DQ9H5J84EBI-713836,EBI-716128

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 335335DNA polymerase beta
PRO_0000218778

Regions

Region183 – 19210DNA binding

Sites

Active site721Schiff-base intermediate with DNA
Metal binding1011Sodium; via carbonyl oxygen
Metal binding1031Sodium; via carbonyl oxygen
Metal binding1061Sodium; via carbonyl oxygen
Metal binding1901Magnesium 1
Metal binding1901Magnesium 2
Metal binding1921Magnesium 1
Metal binding1921Magnesium 2
Metal binding2561Magnesium 2

Amino acid modifications

Modified residue721N6-acetyllysine By similarity
Modified residue831Omega-N-methylarginine; by PRMT6 Ref.14
Modified residue1521Omega-N-methylarginine; by PRMT6 Ref.14
Cross-link41Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.15 Ref.16
Cross-link61Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.15 Ref.16
Cross-link81Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.15 Ref.16

Natural variations

Natural variant2421P → R. Ref.6
Corresponds to variant rs3136797 [ dbSNP | Ensembl ].
VAR_018881

Experimental info

Mutagenesis351K → Q or R: Reduces DNA lyase activity slightly. Ref.12
Mutagenesis391Y → Q: Abolishes DNA polymerase and DNA lyase activity. Ref.12
Mutagenesis411K → R: Abolishes ubiquitination; when associated with R-61 and R-81. Ref.15
Mutagenesis611K → R: Abolishes ubiquitination; when associated with R-41 and R-81. Ref.15
Mutagenesis681K → Q or R: Reduces DNA lyase activity slightly. Ref.12
Mutagenesis721K → Q or R: Abolishes DNA lyase activity. No effect on DNA polymerase activity. Ref.12
Mutagenesis811K → R: Abolishes ubiquitination; when associated with R-41 and R-61. Ref.15
Mutagenesis831R → K: Slight effect. Abolishes methylation by PRMT6 and impairs the polymerase activity; when associated with K-152. Ref.14
Mutagenesis841K → R: No effect. Ref.12
Mutagenesis1521R → K: Slight effect. Abolishes methylation by PRMT6 and impairs the polymerase activity; when associated with K-83. Ref.14
Sequence conflict181M → K in AAB60688. Ref.3
Sequence conflict2281L → R in AAA60133. Ref.10
Sequence conflict2601I → Y in AAA60133. Ref.10
Sequence conflict2871L → K in AAA60133. Ref.10

Secondary structure

.............................................................. 335
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06746 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: FF9A6D0E6F9A9487

FASTA33538,178
        10         20         30         40         50         60 
MSKRKAPQET LNGGITDMLT ELANFEKNVS QAIHKYNAYR KAASVIAKYP HKIKSGAEAK 

        70         80         90        100        110        120 
KLPGVGTKIA EKIDEFLATG KLRKLEKIRQ DDTSSSINFL TRVSGIGPSA ARKFVDEGIK 

       130        140        150        160        170        180 
TLEDLRKNED KLNHHQRIGL KYFGDFEKRI PREEMLQMQD IVLNEVKKVD SEYIATVCGS 

       190        200        210        220        230        240 
FRRGAESSGD MDVLLTHPSF TSESTKQPKL LHQVVEQLQK VHFITDTLSK GETKFMGVCQ 

       250        260        270        280        290        300 
LPSKNDEKEY PHRRIDIRLI PKDQYYCGVL YFTGSDIFNK NMRAHALEKG FTINEYTIRP 

       310        320        330 
LGVTGVAGEP LPVDSEKDIF DYIQWKYREP KDRSE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Arginine methylation regulates DNA polymerase beta."
El-Andaloussi N., Valovka T., Toueille M., Steinacher R., Focke F., Gehrig P., Covic M., Hassa P.O., Schaer P., Huebscher U., Hottiger M.O.
Mol. Cell 22:51-62(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT ARG-83 AND ARG-152 BY PRMT6, MUTAGENESIS OF ARG-83 AND ARG-152.
[15]"Ubiquitin ligase ARF-BP1/Mule modulates base excision repair."
Parsons J.L., Tait P.S., Finch D., Dianova I.I., Edelmann M.J., Khoronenkova S.V., Kessler B.M., Sharma R.A., McKenna W.G., Dianov G.L.
EMBO J. 28:3207-3215(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L11607 mRNA. Translation: AAB59441.1.
D29013 mRNA. Translation: BAA06099.1.
U10526 expand/collapse EMBL AC list , 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.
CCDSCCDS6129.1.
PIRI55273.
S48061.
RefSeqNP_002681.1. NM_002690.2.
UniGeneHs.654484.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP06746.
SMRP06746. Positions 10-335.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111419. 17 interactions.
IntActP06746. 6 interactions.
MINTMINT-1393546.
STRING9606.ENSP00000265421.

Chemistry

BindingDBP06746.
ChEMBLCHEMBL2392.
DrugBankDB00987. Cytarabine.

PTM databases

PhosphoSiteP06746.

Polymorphism databases

DMDM544186.

Proteomic databases

MaxQBP06746.
PaxDbP06746.
PeptideAtlasP06746.
PRIDEP06746.

Protocols and materials databases

DNASU5423.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265421; ENSP00000265421; ENSG00000070501.
GeneID5423.
KEGGhsa:5423.
UCSCuc003xoz.2. human.

Organism-specific databases

CTD5423.
GeneCardsGC08P042213.
HGNCHGNC:9174. POLB.
HPACAB011616.
MIM174760. gene.
neXtProtNX_P06746.
PharmGKBPA276.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1796.
HOGENOMHOG000007787.
HOVERGENHBG002359.
InParanoidP06746.
KOK02330.
OMARYREPKD.
PhylomeDBP06746.
TreeFamTF103002.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.

Gene expression databases

ArrayExpressP06746.
BgeeP06746.
CleanExHS_POLB.
GenevestigatorP06746.

Family and domain databases

Gene3D1.10.8.310. 1 hit.
3.30.210.10. 1 hit.
InterProIPR002054. 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]
PfamPF14792. DNA_pol_B_palm. 1 hit.
PF14791. DNA_pol_B_thumb. 1 hit.
PF10391. DNA_pol_lambd_f. 1 hit.
[Graphical view]
PRINTSPR00869. DNAPOLX.
PR00870. DNAPOLXBETA.
SMARTSM00278. HhH1. 2 hits.
SM00483. POLXc. 1 hit.
[Graphical view]
SUPFAMSSF47802. SSF47802. 1 hit.
SSF81585. SSF81585. 1 hit.
PROSITEPS00522. DNA_POLYMERASE_X. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06746.
GeneWikiDNA_polymerase_beta.
GenomeRNAi5423.
NextBio20981.
PROP06746.
SOURCESearch...

Entry information

Entry nameDPOLB_HUMAN
AccessionPrimary (citable) accession number: P06746
Secondary accession number(s): B2RC78, Q3KP48, Q6FI34
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 177 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM