P06746 (DPOLB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA polymerase beta
EC=2.7.7.7
EC=4.2.99.-

Gene names

Name:

POLB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	335 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	DNA damage DNA repair DNA replication DNA synthesis
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding Magnesium Metal-binding Sodium
Molecular function	DNA-directed DNA polymerase Lyase Nucleotidyltransferase Transferase
PTM	Isopeptide bond Methylation Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA-dependent DNA replication Traceable author statement PubMed 8168825. Source: ProtInc base-excision repair Inferred from direct assay Ref.14. Source: UniProtKB cell death Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara pyrimidine dimer repair Inferred from electronic annotation. Source: Compara response to ethanol Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from direct assay Ref.15Ref.16. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome spindle microtubule Inferred from direct assay PubMed 15725623. Source: MGI
Molecular_function	DNA-directed DNA polymerase activity Inferred from direct assay Ref.14Ref.11. Source: UniProtKB damaged DNA binding Inferred from electronic annotation. Source: Compara 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TAF1D	Q9H5J8	4	EBI-713836,EBI-716128

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 335

334

DNA polymerase beta

PRO_0000218778

Regions

Region

183 – 192

10

DNA binding

Sites

Active site

72

1

Schiff-base intermediate with DNA

Metal binding

101

1

Sodium; via carbonyl oxygen

Metal binding

103

1

Sodium; via carbonyl oxygen

Metal binding

106

1

Sodium; via carbonyl oxygen

Metal binding

190

1

Magnesium 1

Metal binding

190

1

Magnesium 2

Metal binding

192

1

Magnesium 1

Metal binding

192

1

Magnesium 2

Metal binding

256

1

Magnesium 2

Amino acid modifications

Modified residue

83

1

Omega-N-methylarginine; by PRMT6 Ref.14

Modified residue

152

1

Omega-N-methylarginine; by PRMT6 Ref.14

Cross-link

41

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.15 Ref.16

Cross-link

61

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.15 Ref.16

Cross-link

81

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.15 Ref.16

Natural variations

Natural variant

242

1

P → R. Ref.6
Corresponds to variant rs3136797 [ dbSNP | Ensembl ].

VAR_018881

Experimental info

Mutagenesis

35

1

K → Q or R: Reduces DNA lyase activity slightly. Ref.12

Mutagenesis

39

1

Y → Q: Abolishes DNA polymerase and DNA lyase activity. Ref.12

Mutagenesis

41

1

K → R: Abolishes ubiquitination; when associated with R-61 and R-81. Ref.15

Mutagenesis

61

1

K → R: Abolishes ubiquitination; when associated with R-41 and R-81. Ref.15

Mutagenesis

68

1

K → Q or R: Reduces DNA lyase activity slightly. Ref.12

Mutagenesis

72

1

K → Q or R: Abolishes DNA lyase activity. No effect on DNA polymerase activity. Ref.12

Mutagenesis

81

1

K → R: Abolishes ubiquitination; when associated with R-41 and R-61. Ref.15

Mutagenesis

83

1

R → K: Slight effect. Abolishes methylation by PRMT6 and impairs the polymerase activity; when associated with K-152. Ref.14

Mutagenesis

84

1

K → R: No effect. Ref.12

Mutagenesis

152

1

R → K: Slight effect. Abolishes methylation by PRMT6 and impairs the polymerase activity; when associated with K-83. Ref.14

Sequence conflict

18

1

M → K in AAB60688. Ref.3

Sequence conflict

228

1

L → R in AAA60133. Ref.10

Sequence conflict

260

1

I → Y in AAA60133. Ref.10

Sequence conflict

287

1

L → K in AAA60133. Ref.10

Secondary structure

1

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335

Helix Strand Turn

Details...

Turn

9 – 12

4

Helix

13 – 28

16

Helix

33 – 48

16

Helix

56 – 60

5

Beta strand

62 – 64

3

Helix

67 – 79

13

Helix

83 – 90

8

Helix

92 – 100

9

Turn

101 – 105

5

Helix

108 – 116

9

Helix

122 – 126

5

Helix

129 – 131

3

Helix

134 – 141

8

Helix

143 – 146

4

Helix

152 – 169

18

Beta strand

174 – 177

4

Helix

179 – 182

4

Beta strand

186 – 196

11

Beta strand

202 – 204

3

Beta strand

207 – 209

3

Helix

210 – 220

11

Beta strand

223 – 230

8

Beta strand

232 – 239

8

Beta strand

245 – 247

3

Beta strand

253 – 259

7

Helix

262 – 264

3

Helix

265 – 273

9

Helix

276 – 288

13

Beta strand

291 – 293

3

Beta strand

298 – 300

3

Beta strand

303 – 305

3

Helix

316 – 322

7

Helix

330 – 332

3

Sequences

	Sequence		Length	Mass (Da)
	P06746 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: FF9A6D0E6F9A9487	FASTA	335	38,178
	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

References

	« Hide 'large scale' referencesShow '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. , 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

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00219538.

PIR

I55273.
S48061.

RefSeq

NP_002681.1. NM_002690.2.

UniGene

Hs.654484.

3D structure databases

PDBe
RCSB PDB
PDBj

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	2-334	[»]
2FMQ	X-ray	2.20	A	2-334	[»]
2FMS	X-ray	2.00	A	2-334	[»]
2I9G	X-ray	2.10	A	1-334	[»]
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	3-335	[»]
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	[»]
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	2-334	[»]
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	2-334	[»]
9ICX	X-ray	2.60	A	2-334	[»]
9ICY	X-ray	3.00	A	2-334	[»]

ProteinModelPortal

P06746.

ModBase

Search...

Protein-protein interaction databases

IntAct

P06746. 4 interactions.

MINT

MINT-1393546.

STRING

9606.ENSP00000265421.

PTM databases

PhosphoSite

P06746.

Polymorphism databases

DMDM

544186.

Proteomic databases

PaxDb

P06746.

PeptideAtlas

P06746.

PRIDE

P06746.

Protocols and materials databases

DNASU

5423.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265421; ENSP00000265421; ENSG00000070501.

GeneID

5423.

KEGG

hsa:5423.

UCSC

uc003xoz.2. human.

Organism-specific databases

CTD

5423.

GeneCards

GC08P042213.

HGNC

HGNC:9174. POLB.

HPA

CAB011616.

MIM

174760. gene.

neXtProt

NX_P06746.

PharmGKB

PA276.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1796.

HOGENOM

HOG000007787.

HOVERGEN

HBG002359.

InParanoid

P06746.

KO

K02330.

OMA

GKEYPHR.

OrthoDB

EOG43FGX8.

PhylomeDB

P06746.

Enzyme and pathway databases

Reactome

REACT_216. DNA Repair.

Gene expression databases

ArrayExpress

P06746.

Bgee

P06746.

CleanEx

HS_POLB.

Genevestigator

P06746.

GermOnline

ENSG00000070501. Homo sapiens.

Family and domain databases

InterPro

IPR002054. DNA-dir_DNA_pol_X.
IPR019843. DNA_pol-X_BS.
IPR010996. DNA_pol_b-like_N.
IPR018944. DNA_pol_lambd_fingers_domain.
IPR022312. DNA_pol_X.
IPR002008. DNA_pol_X_beta-like.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
[Graphical view]

Pfam

PF10391. DNA_pol_lambd_f. 1 hit.
[Graphical view]

PRINTS

PR00869. DNAPOLX.
PR00870. DNAPOLXBETA.

SMART

SM00278. HhH1. 2 hits.
SM00483. POLXc. 1 hit.
[Graphical view]

SUPFAM

SSF81585. DNA_pol_lambd_fingers_domain. 1 hit.
SSF47802. DNApol_B_N_like. 1 hit.

PROSITE

PS00522. DNA_POLYMERASE_X. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P06746.

ChEMBL

CHEMBL2392.

DrugBank

DB00987. Cytarabine.

EvolutionaryTrace

P06746.

GenomeRNAi

5423.

NextBio

20981.

SOURCE

Search...

Entry information

Entry name

DPOLB_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 163 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.