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Protein

DNA polymerase beta

Gene

Polb

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+Note: Binds 2 magnesium ions per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei72Schiff-base intermediate with DNABy similarity1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>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

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-110362 POLB-Dependent Long Patch Base Excision Repair
R-RNO-110373 Resolution of AP sites via the multiple-nucleotide patch replacement pathway
R-RNO-110381 Resolution of AP sites via the single-nucleotide replacement pathway
R-RNO-5649702 APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway
R-RNO-5651801 PCNA-Dependent Long Patch Base Excision Repair
R-RNO-5689880 Ub-specific processing proteases
R-RNO-73930 Abasic sugar-phosphate removal via the single-nucleotide replacement pathway

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DNA polymerase beta (EC:2.7.7.7, EC:4.2.99.-)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Polb
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 16

Organism-specific databases

Rat genome database

More...
RGDi
3363 Polb

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi190D → E or S: Loss of activity. 1 Publication1
Mutagenesisi191M → I: No loss of activity. 1
Mutagenesisi191M → T: 50% loss of activity. 1
Mutagenesisi192D → E or S: Loss of activity. 1 Publication1
Mutagenesisi246D → V: Misincorporates T nucleotide opposite G/C template. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4343

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002187801 – 335DNA polymerase betaAdd BLAST335

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki41Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki61Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei72N6-acetyllysineBy similarity1
Cross-linki81Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei83Omega-N-methylarginine; by PRMT6By similarity1
Modified residuei152Omega-N-methylarginine; by PRMT6By similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Methylation by PRMT6 stimulates the polymerase activity by enhancing DNA binding and processivity.By similarity
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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Ubl conjugation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P06766

PRoteomics IDEntifications database

More...
PRIDEi
P06766

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P06766

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P06766

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000019150 Expressed in 10 organ(s), highest expression level in testis

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P06766 RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with APEX1, HUWE1/ARF-BP1, STUB1/CHIP and USP47 (By similarity). Monomer. Interacts with FAM168A (By similarity).By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
XRCC1P188874EBI-15845002,EBI-947466From Homo sapiens.

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

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DIPi
DIP-44707N

Protein interaction database and analysis system

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IntActi
P06766, 1 interactor

STRING: functional protein association networks

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STRINGi
10116.ENSRNOP00000026039

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P06766

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1335
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P06766

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P06766

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P06766

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni183 – 192DNA binding10

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the DNA polymerase type-X family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2534 Eukaryota
COG1796 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156918

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000007787

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG002359

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P06766

KEGG Orthology (KO)

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KOi
K02330

Identification of Orthologs from Complete Genome Data

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OMAi
ITDMLME

Database of Orthologous Groups

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OrthoDBi
EOG091G0HMG

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P06766

TreeFam database of animal gene trees

More...
TreeFami
TF103002

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00141 NT_POLXc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.150.110, 1 hit
3.30.210.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View 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

Pfam protein domain database

More...
Pfami
View 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

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00869 DNAPOLX
PR00870 DNAPOLXBETA

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00278 HhH1, 2 hits
SM00483 POLXc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47802 SSF47802, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00522 DNA_POLYMERASE_X, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P06766-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSKRKAPQET LNGGITDMLV ELANFEKNVS QAIHKYNAYR KAASVIAKYP
60 70 80 90 100
HKIKSGAEAK KLPGVGTKIA EKIDEFLATG KLRKLEKIRQ DDTSSSINFL
110 120 130 140 150
TRVTGIGPSA ARKLVDEGIK TLEDLRKNED KLNHHQRIGL KYFEDFEKRI
160 170 180 190 200
PREEMLQMQD IVLNEVKKLD PEYIATVCGS FRRGAESSGD MDVLLTHPNF
210 220 230 240 250
TSESSKQPKL LHRVVEQLQK VRFITDTLSK GETKFMGVCQ LPSENDENEY
260 270 280 290 300
PHRRIDIRLI PKDQYYCGVL YFTGSDIFNK NMRAHALEKG FTINEYTIRP
310 320 330
LGVTGVAGEP LPVDSEQDIF DYIQWRYREP KDRSE
Length:335
Mass (Da):38,327
Last modified:January 23, 2007 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iBBF8498C0D3FBFC9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti228L → R in AAA41901 (PubMed:3597402).Curated1
Sequence conflicti228L → R in AAB00389 (Ref. 2) Curated1
Sequence conflicti228L → R in AAA41900 (PubMed:2873575).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
J02776 mRNA Translation: AAA41901.1
U38801 mRNA Translation: AAB00389.1
BC098668 mRNA Translation: AAH98668.1
M13961 mRNA Translation: AAA41900.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A27112

NCBI Reference Sequences

More...
RefSeqi
NP_058837.2, NM_017141.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Rn.9346

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000026039; ENSRNOP00000026039; ENSRNOG00000019150

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
29240

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:29240

UCSC genome browser

More...
UCSCi
RGD:3363 rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02776 mRNA Translation: AAA41901.1
U38801 mRNA Translation: AAB00389.1
BC098668 mRNA Translation: AAH98668.1
M13961 mRNA Translation: AAA41900.1
PIRiA27112
RefSeqiNP_058837.2, NM_017141.2
UniGeneiRn.9346

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BNONMR-A1-87[»]
1BNPNMR-A1-87[»]
1BPBX-ray2.30A88-335[»]
1BPDX-ray3.60A1-335[»]
1BPEX-ray2.90A1-335[»]
1DK2NMR-A2-87[»]
1DK3NMR-A1-87[»]
1HUOX-ray2.60A/B1-335[»]
1HUZX-ray2.60A/B1-335[»]
1JN3X-ray2.35A85-335[»]
1NOMX-ray3.00A88-335[»]
1RPLX-ray2.30A85-335[»]
1ZQUX-ray2.60A88-335[»]
1ZQVX-ray2.70A88-335[»]
1ZQWX-ray2.30A88-335[»]
1ZQXX-ray2.50A88-335[»]
1ZQYX-ray2.30A88-335[»]
1ZQZX-ray2.70A88-335[»]
2BPCX-ray2.80A88-335[»]
2BPFX-ray2.90A1-335[»]
2BPGX-ray3.60A/B1-335[»]
2VANX-ray2.10A91-335[»]
3K75X-ray2.95D/E91-335[»]
3LQCX-ray2.35B142-335[»]
3UXNX-ray2.50A/B1-335[»]
3UXOX-ray2.10A/B1-335[»]
3UXPX-ray2.72A/B1-335[»]
3V72X-ray2.49A1-335[»]
3V7JX-ray2.25A4-335[»]
3V7KX-ray2.27A4-335[»]
3V7LX-ray2.66A4-335[»]
ProteinModelPortaliP06766
SMRiP06766
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-44707N
IntActiP06766, 1 interactor
STRINGi10116.ENSRNOP00000026039

Chemistry databases

BindingDBiP06766
ChEMBLiCHEMBL4343

PTM databases

iPTMnetiP06766
PhosphoSitePlusiP06766

Proteomic databases

PaxDbiP06766
PRIDEiP06766

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026039; ENSRNOP00000026039; ENSRNOG00000019150
GeneIDi29240
KEGGirno:29240
UCSCiRGD:3363 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5423
RGDi3363 Polb

Phylogenomic databases

eggNOGiKOG2534 Eukaryota
COG1796 LUCA
GeneTreeiENSGT00940000156918
HOGENOMiHOG000007787
HOVERGENiHBG002359
InParanoidiP06766
KOiK02330
OMAiITDMLME
OrthoDBiEOG091G0HMG
PhylomeDBiP06766
TreeFamiTF103002

Enzyme and pathway databases

ReactomeiR-RNO-110362 POLB-Dependent Long Patch Base Excision Repair
R-RNO-110373 Resolution of AP sites via the multiple-nucleotide patch replacement pathway
R-RNO-110381 Resolution of AP sites via the single-nucleotide replacement pathway
R-RNO-5649702 APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway
R-RNO-5651801 PCNA-Dependent Long Patch Base Excision Repair
R-RNO-5689880 Ub-specific processing proteases
R-RNO-73930 Abasic sugar-phosphate removal via the single-nucleotide replacement pathway

Miscellaneous databases

EvolutionaryTraceiP06766

Protein Ontology

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PROi
PR:P06766

Gene expression databases

BgeeiENSRNOG00000019150 Expressed in 10 organ(s), highest expression level in testis
GenevisibleiP06766 RN

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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDPOLB_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P06766
Secondary accession number(s): Q4G081
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 187 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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