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UniProtKB - O89042 (DPOLA_RAT)

Entry version 147 (05 Jun 2019)
Sequence version 1 (01 Nov 1998)
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Protein

DNA polymerase alpha catalytic subunit

Gene

Pola1

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 transcript 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

Plays an essential role in the initiation of DNA replication. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1/p180, a regulatory subunit POLA2/p70 and two primase subunits PRIM1/p49 and PRIM2/p58) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1. The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively. The reason this transfer occurs is because the polymerase alpha has limited processivity and lacks intrinsic 3' exonuclease activity for proofreading error, and therefore is not well suited for replicating long complexes. In the cytosol, responsible for a substantial proportion of the physiological concentration of cytosolic RNA:DNA hybrids, which are necessary to prevent spontaneous activation of type I interferon responses.By similarity

Miscellaneous

In eukaryotes there are five DNA polymerases: alpha, beta, gamma, delta, and epsilon which are responsible for different reactions of DNA synthesis.

<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

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi1290ZincBy similarity1
Metal bindingi1293ZincBy similarity1
Metal bindingi1317ZincBy similarity1
Metal bindingi1322ZincBy similarity1
Metal bindingi1355Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1360Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1378Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1381Iron-sulfur (4Fe-4S)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri1290 – 1320CysA-typeAdd BLAST31

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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, Nucleotidyltransferase, Transferase
Biological processDNA replication
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-113501 Inhibition of replication initiation of damaged DNA by RB1/E2F1
R-RNO-174411 Polymerase switching on the C-strand of the telomere
R-RNO-174430 Telomere C-strand synthesis initiation
R-RNO-68952 DNA replication initiation
R-RNO-68962 Activation of the pre-replicative complex
R-RNO-69091 Polymerase switching
R-RNO-69166 Removal of the Flap Intermediate
R-RNO-69183 Processive synthesis on the lagging strand

<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 alpha catalytic subunit (EC:2.7.7.7)
Alternative name(s):
DNA polymerase alpha catalytic subunit p180
<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:Pola1
Synonyms:Pola
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<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: Unplaced

Organism-specific databases

Rat genome database

More...RGDi		621816 Pola1

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<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_00000464301 – ›1451DNA polymerase alpha catalytic subunitAdd BLAST›1451

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei192PhosphoserineBy similarity1
Modified residuei196PhosphoserineBy similarity1
Modified residuei215PhosphoserineBy similarity1
Modified residuei230N6-acetyllysineBy similarity1
Modified residuei413PhosphothreonineBy similarity1
Modified residuei977N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		O89042

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

More...PaxDbi		O89042

PRoteomics IDEntifications database

More...PRIDEi		O89042

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O89042

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

More...PhosphoSitePlusi		O89042

<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

The DNA polymerase alpha complex is composed of four subunits: the catalytic subunit POLA1, the regulatory subunit POLA2, and the small and the large primase subunits PRIM1 and PRIM2 respectively.

Interacts with PARP1; this interaction functions as part of the control of replication fork progression.

Interacts with MCM10 and WDHD1; these interactions recruit the polymerase alpha complex to the pre-replicative complex bound to DNA.

Interacts with RPA1; this interaction stabilizes the replicative complex and reduces the misincorporation rate of DNA polymerase alpha by acting as a fidelity clamp (By similarity).

By similarity

Protein-protein interaction databases

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-2089 DNA polymerase alpha:primase complex

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000018147

<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

3D structure databases

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

More...SMRi		O89042

Database of comparative protein structure models

More...ModBasei		Search...

<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>Regioni657 – 722DNA-binding regionSequence analysisAdd BLAST66
Regioni1252 – 1383DNA-binding regionSequence analysisAdd BLAST132

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1355 – 1381CysB motifAdd BLAST27

<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

The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes.By similarity

<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-B family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1290 – 1320CysA-typeAdd BLAST31

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0970 Eukaryota
COG0417 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000163524

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O89042

KEGG Orthology (KO)

More...KOi		K02320

Database of Orthologous Groups

More...OrthoDBi		293315at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		O89042

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.132.60, 1 hit
1.10.3200.20, 1 hit
3.30.420.10, 1 hit
3.90.1600.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR006172 DNA-dir_DNA_pol_B
IPR017964 DNA-dir_DNA_pol_B_CS
IPR006133 DNA-dir_DNA_pol_B_exonuc
IPR006134 DNA-dir_DNA_pol_B_multi_dom
IPR024647 DNA_pol_a_cat_su_N
IPR042087 DNA_pol_B_C
IPR023211 DNA_pol_palm_dom_sf
IPR038256 Pol_alpha_znc_sf
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
IPR015088 Znf_DNA-dir_DNA_pol_B_alpha

Pfam protein domain database

More...Pfami		View protein in Pfam
PF12254 DNA_pol_alpha_N, 1 hit
PF00136 DNA_pol_B, 1 hit
PF03104 DNA_pol_B_exo1, 1 hit
PF08996 zf-DNA_Pol, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00106 DNAPOLB

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00486 POLBc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53098 SSF53098, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00116 DNA_POLYMERASE_B, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<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: Fragment.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

O89042-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAPVHGDDCK LETSAVSDSG SFVASRARRE KKSKKGRQEA LERLKKAKAG 
        60         70         80         90        100
EKYKYEVEDL TSVYEEVDEE QYSKLVQARQ DDDWIVDDDG IGYVEDGREI 
       110        120        130        140        150
FDDDLEDDAL DTCGEGSDGK AHRKDRKDVK KPSVTKPNNI KAMFIASAGK 
       160        170        180        190        200
KTTDKTVDLS KDDLLGDILQ DLNTETPQIA PPPVLIPKKK RSTGASPNPF 
       210        220        230        240        250
SVHTATAVPS GKIASPVSRK EPPLTPVPLK RAEFAGDLAQ PECPEDEQES 
       260        270        280        290        300
GVIEFEDGDF DEPMDTEEVD EEEPVTAKIW DQESEPVEGV KHEADPETGT 
       310        320        330        340        350
TSFLDSFLPD VSCWDIDQKD ENSFLLQEVQ VDSNHLPLVK GADDEQVFQF 
       360        370        380        390        400
YWLDAYEDPY NQPGVVFLFG KVWVESAKTH VSCCVMVKNI ERTLYFLPRE 
       410        420        430        440        450
MKIDLNTGKE TATPITMKDV YEEFDSKISA KYKIMKFKSK IVEKNYAFEI 
       460        470        480        490        500
PDVPEKSEYL EVRYSAEVPQ LPQNLKGETF SHVFGTNTSS LELFLMNRKI 
       510        520        530        540        550
KGPCWLEVKN PQLLNQPISW CKFEAMALKP DLVNVIKDVS PPPLVVMSFS 
       560        570        580        590        600
MKTMQNVQNH QHEIIAMAAL VHHNFPLDKA PPKPPFQTHF CVVSKPKDCI 
       610        620        630        640        650
FPCAFKEVIK KKNMEVEVAA TERTLLGFFL AKVHKLDPDI LVGHNICGFE 
       660        670        680        690        700
LEVLLQRINE CKVPFWSKIG RLRRSNMPKL GSRSGFGERN ATCGRMICDV 
       710        720        730        740        750
EISVKELIHC KSYHLSELVQ QILKTERIVI PTENIRNMYS EPSHLLYLLE 
       760        770        780        790        800
HIWKDARFIL QIMCELNVLP LALQITNIAG NIMSRTLMGG RSERNEFLLL 
       810        820        830        840        850
HAFYENNYIV PDKQIFRKPQ QKPGDEDEEI DGDTNKYKKG RKKAAYAGGL 
       860        870        880        890        900
VLDPKVGFYD KFILLLDFNS LYPSIIQEFN ICFTTVQRVA SETLKATEDE 
       910        920        930        940        950
EQEQIPELPD PNLDMGILPR EIRKLVERRK QVKQLMKQQD LNPDLVLQYD 
       960        970        980        990       1000
IRQKALKLTA NSMYGCLGFS YSRFYAKPLA ALVTYKGREI LMHTKEMVQK 
      1010       1020       1030       1040       1050
MNLEVIYGDT DSIMINTNST NLEEVFKLGN KVKNEVNKLY KLLEIDIDGV 
      1060       1070       1080       1090       1100
FKSLLLLKKK KYAALVVEPT SDGNYITKQE LKGLDIVRRD WCDLAKDTGN 
      1110       1120       1130       1140       1150
FVIGQILSDQ SRDTIVENIQ KRLIEIGENV LNGSVPVSQF EINKALTKDP 
      1160       1170       1180       1190       1200
QDYPDKKSLP HVHVALWINS QGGRKVKAGD TVSYVICQDG SNLPATQRAY 
      1210       1220       1230       1240       1250
APEQLQKQDN LAIDTQYYLA QQIHPVVARI CEPIDGIDAV LIALWLGLDS 
      1260       1270       1280       1290       1300
TQFRVHQYHK DEENDALLGG PAQLTDEEKY KDCEKFKCLC PSCGTENIYD 
      1310       1320       1330       1340       1350
NVFEGSGMDM EPSLNRCSNI DCKASPATFM VQLSNKLIMD IRRCIKKYYD 
      1360       1370       1380       1390       1400
GWLICEEPTC RNRIRRLPLH FSRNGPLCPA CMKAVLRPEY SDKSLYTQLC 
      1410       1420       1430       1440       1450
FYRYIFDADC ALEKLPEHEK DKLKKQFFTP RVLQDYRKVK NIAEHFLSWS 

G
Length:1,451
Mass (Da):165,306
Last modified:November 1, 1998 - v1
<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:iF0E1B16F8B8D5CD2
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F1LRJ6F1LRJ6_RAT
DNA polymerase
Pola1
1,340Annotation score:

Annotation score:3 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>
A0A096MK13A0A096MK13_RAT
DNA polymerase
Pola1
957Annotation score:

Annotation score:3 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>
A0A096MJL5A0A096MJL5_RAT
DNA polymerase alpha catalytic subu...
Pola1
465Annotation score:

Annotation score:1 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section is used for sequence fragments to indicate that the residue at the extremity of the sequence is not the actual terminal residue in the complete protein sequence.<p><a href='/help/non_ter' target='_top'>More...</a></p>Non-terminal residuei14511

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AJ011605 mRNA Translation: CAA09720.1

NCBI Reference Sequences

More...RefSeqi		NP_445931.1, NM_053479.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		85241

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:85241

<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
AJ011605 mRNA Translation: CAA09720.1
RefSeqiNP_445931.1, NM_053479.1

3D structure databases

SMRiO89042
ModBaseiSearch...

Protein-protein interaction databases

ComplexPortaliCPX-2089 DNA polymerase alpha:primase complex
STRINGi10116.ENSRNOP00000018147

PTM databases

iPTMnetiO89042
PhosphoSitePlusiO89042

Proteomic databases

jPOSTiO89042
PaxDbiO89042
PRIDEiO89042

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi85241
KEGGirno:85241

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5422
RGDi621816 Pola1

Phylogenomic databases

eggNOGiKOG0970 Eukaryota
COG0417 LUCA
HOGENOMiHOG000163524
InParanoidiO89042
KOiK02320
OrthoDBi293315at2759
PhylomeDBiO89042

Enzyme and pathway databases

ReactomeiR-RNO-113501 Inhibition of replication initiation of damaged DNA by RB1/E2F1
R-RNO-174411 Polymerase switching on the C-strand of the telomere
R-RNO-174430 Telomere C-strand synthesis initiation
R-RNO-68952 DNA replication initiation
R-RNO-68962 Activation of the pre-replicative complex
R-RNO-69091 Polymerase switching
R-RNO-69166 Removal of the Flap Intermediate
R-RNO-69183 Processive synthesis on the lagging strand

Family and domain databases

Gene3Di1.10.132.60, 1 hit
1.10.3200.20, 1 hit
3.30.420.10, 1 hit
3.90.1600.10, 1 hit
InterProiView protein in InterPro
IPR006172 DNA-dir_DNA_pol_B
IPR017964 DNA-dir_DNA_pol_B_CS
IPR006133 DNA-dir_DNA_pol_B_exonuc
IPR006134 DNA-dir_DNA_pol_B_multi_dom
IPR024647 DNA_pol_a_cat_su_N
IPR042087 DNA_pol_B_C
IPR023211 DNA_pol_palm_dom_sf
IPR038256 Pol_alpha_znc_sf
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
IPR015088 Znf_DNA-dir_DNA_pol_B_alpha
PfamiView protein in Pfam
PF12254 DNA_pol_alpha_N, 1 hit
PF00136 DNA_pol_B, 1 hit
PF03104 DNA_pol_B_exo1, 1 hit
PF08996 zf-DNA_Pol, 1 hit
PRINTSiPR00106 DNAPOLB
SMARTiView protein in SMART
SM00486 POLBc, 1 hit
SUPFAMiSSF53098 SSF53098, 1 hit
PROSITEiView protein in PROSITE
PS00116 DNA_POLYMERASE_B, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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 nameiDPOLA_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: O89042
<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: December 15, 1998
Last sequence update: November 1, 1998
Last modified: June 5, 2019
This is version 147 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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