Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
We will be switching to the new UniProt website soon. Please explore and share your feedback. Take me to the new website.

UniProtKB - P33609 (DPOLA_MOUSE)

Entry version 177 (23 Feb 2022)
Sequence version 2 (01 Jun 1994)
Previous versions | rss
Add a publicationFeedback
Protein

DNA polymerase alpha catalytic subunit

Gene

Pola1

Organism
Mus musculus (Mouse)
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

Catalytic subunit of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex) which plays an essential role in the initiation of DNA synthesis (PubMed:8253737, PubMed:8026492).

During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1, a regulatory subunit POLA2 and two primase subunits PRIM1 and PRIM2) 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 similarity2 Publications

Miscellaneous

In eukaryotes there are five DNA polymerases: alpha, beta, gamma, delta, and epsilon which are responsible for different reactions of DNA synthesis.
Conserved regions II, IV, III and I are thought to be involved in substrate recognition, binding or PP(i) hydrolysis.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi1287Zinc 1By similarity1
Metal bindingi1290Zinc 1By similarity1
Metal bindingi1314Zinc 1By similarity1
Metal bindingi1319Zinc 1By similarity1
Metal bindingi1352Zinc 2By similarity1
Metal bindingi1357Zinc 2By similarity1
Metal bindingi1375Zinc 2By similarity1
Metal bindingi1378Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 fingeri1287 – 1317CysA-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
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-113501, Inhibition of replication initiation of damaged DNA by RB1/E2F1
R-MMU-174411, Polymerase switching on the C-strand of the telomere
R-MMU-174430, Telomere C-strand synthesis initiation
R-MMU-68952, DNA replication initiation
R-MMU-68962, Activation of the pre-replicative complex
R-MMU-69091, Polymerase switching
R-MMU-69166, Removal of the Flap Intermediate
R-MMU-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%5Fand%5Ftaxonomy%5Fsection">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:2.7.7.72 Publications)
Alternative name(s):
DNA polymerase alpha catalytic subunit p180
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 X

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:99660, Pola1

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSMUSG00000006678

<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

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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi1008D → N: Results in loss of primer extension catalytic activity but retains ability to bind to the primase complex. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2797

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000464291 – 1465DNA polymerase alpha catalytic subunitAdd BLAST1465

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 residuei180PhosphothreonineBy similarity1
Modified residuei192PhosphoserineBy similarity1
Modified residuei215PhosphoserineCombined sources1
Modified residuei230N6-acetyllysineCombined sources1
Modified residuei974N6-succinyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P33609

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P33609

MaxQB - The MaxQuant DataBase

More...MaxQBi		P33609

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

More...PaxDbi		P33609

PeptideAtlas

More...PeptideAtlasi		P33609

PRoteomics IDEntifications database

More...PRIDEi		P33609

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		279570

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P33609

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

More...PhosphoSitePlusi		P33609

<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

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in those zones containing proliferating cells in the developing embryonic neocortex, as well as in the lateral and medial ganglionic eminences. After birth, expressed in cells that remain proliferating in the ventricular and subventricular zone of the striatum.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000006678, Expressed in embryonic stem cell and 239 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P33609, MM

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the alpha DNA polymerase complex (also known as the alpha DNA polymerase-primase complex) consisting of four subunits: the catalytic subunit POLA1, the regulatory subunit POLA2, and the primase complex subunits PRIM1 and PRIM2 respectively (PubMed:8253737, PubMed:8026492). Within the complex, POLA1 directly interacts with PRIM2 (PubMed:8253737).

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 similarity2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		202287, 3 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-2088, DNA polymerase alpha:primase complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P33609

Protein interaction database and analysis system

More...IntActi		P33609, 4 interactors

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000006856

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P33609, protein

<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		P33609

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>Regioni20 – 39DisorderedSequence analysisAdd BLAST20
Regioni105 – 135DisorderedSequence analysisAdd BLAST31
Regioni261 – 297DisorderedSequence analysisAdd BLAST37
Regioni654 – 719DNA-bindingSequence analysisAdd BLAST66
Regioni1249 – 1380DNA-bindingSequence 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>Motifi1352 – 1378CysB motifAdd BLAST27

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi110 – 134Basic and acidic residuesSequence analysisAdd BLAST25
Compositional biasi265 – 297Basic and acidic residuesSequence analysisAdd BLAST33

<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 fingeri1287 – 1317CysA-typeAdd BLAST31

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0970, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00550000074891

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_001718_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P33609

Identification of Orthologs from Complete Genome Data

More...OMAi		WLKIEDA

Database of Orthologous Groups

More...OrthoDBi		293315at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P33609

TreeFam database of animal gene trees

More...TreeFami		TF103001

Family and domain databases

Conserved Domains Database

More...CDDi		cd05532, POLBc_alpha, 1 hit

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
IPR043502, DNA/RNA_pol_sf
IPR024647, DNA_pol_a_cat_su_N
IPR042087, DNA_pol_B_thumb
IPR023211, DNA_pol_palm_dom_sf
IPR038256, Pol_alpha_znc_sf
IPR045846, POLBc_alpha
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
SSF56672, SSF56672, 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%5Flength">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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P33609-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAPMHEEDCK LEASAVSDSG SFAASRARRE KKSKKGRQEA LERLKKAKAG 
        60         70         80         90        100
EKYKYEVEDL TSVYEEVDEE QYSKLVQARQ DDDWIVDDDG IGYVEDGREI 
       110        120        130        140        150
FDDDLEDDAL DTCGKGSDGK AHRKDRKDVK KPSVTKPNNI KAMFIASAGK 
       160        170        180        190        200
KTTDKAVDLS KDDLLGDILQ DLNTETAQIT PPPVLIPKKK RSTGALLNPF 
       210        220        230        240        250
SVHTPKAIPS GKPASPVLRN EPLLTPIPLK RAELAGELAQ PECPEDEQEL 
       260        270        280        290        300
GVMEFEDGDF DESMDTEKVD EKPVTAKTWD QETEPVERVE HEADPERGTT 
       310        320        330        340        350
SYLENFLPDV SCWDIDQDDE SIPQEVQVDS SNLPLVKGAD DEQVFQFYWL 
       360        370        380        390        400
DAYEDPYNQP GVVFLFGKVW IESVKTHVSC CVMVKNIERT LYFLPREMKF 
       410        420        430        440        450
DLNTGKETAI PVTMKDVYEE FDSKISAKYK IMKFKSKIVE KNYAFEIPDV 
       460        470        480        490        500
PEKSEYLEVR YSAEVPQLPQ NLKGETFSHV FGTNTSSLEL FLMNRKIKGP 
       510        520        530        540        550
CWLEVKNPQL LNQPISWCKF EVMALKPDLV NVIKDVSPPP LVVMSFSMKT 
       560        570        580        590        600
MQNVQNHQHE IIAMAALVHH SFALDKAPPE PPFQTHFCVV SKPKDCIFPC 
       610        620        630        640        650
DFKEVISKKN MKVEIAATER TLIGFFLAKV HKIDPDILVG HNICSFELEV 
       660        670        680        690        700
LLQRINECKV PYWSKIGRLR RSNMPKLGSR SGFGERNATC GRMICDVEIS 
       710        720        730        740        750
AKELIHCKSY HLSELVQQIL KTERIVIPTE NIRNMYSESS YLLYLLEHIW 
       760        770        780        790        800
KDARFILQIM CELNVLPLAL QITNIAGNIM SRTLMGGRSE RNEFLLLHAF 
       810        820        830        840        850
YENNYIVPDK QIFRKPQQKL GDEDEEIDGD TNKYKKGRKK ATYAGGLVLD 
       860        870        880        890        900
PKVGFYDKFI LLLDFNSLYP SIIQEFNICF TTVQRVTSEV QKATEDEEQE 
       910        920        930        940        950
QIPELPDPNL EMGILPREIR KLVERRKQVK QLMKQQDLNP DLVLQYDIRQ 
       960        970        980        990       1000
KALKLTANSM YGCLGFSYSR FYAKPLAALV TYKGREILMH TKDMVQKMNL 
      1010       1020       1030       1040       1050
EVIYGDTDSI MINTNSTNLE EVFKLGNKVK SEVNKLYKLL EIDIDAVFKS 
      1060       1070       1080       1090       1100
LLLLKKKKYA ALVVEPTSDG NYITKQELKG LDIVRRDWCD LAKDTGNFVI 
      1110       1120       1130       1140       1150
GQILSDQSRD TIVENIQKRL IEIGENVLNG SVPVSQFEIN KALTKDPQDY 
      1160       1170       1180       1190       1200
PDRKSLPHVH VALWINSQGG RKVKAGDTVS YVICQDGSNL TATQRAYAPE 
      1210       1220       1230       1240       1250
QLQKLDNLAI DTQYYLAQQI HPVVARICEP IDGIDAVLIA LWLGLDSTQF 
      1260       1270       1280       1290       1300
RVHQYHKDEE NDALLGGPAQ LTDEEKYKDC EKFKCLCPSC GTENIYDNVF 
      1310       1320       1330       1340       1350
EGSGLDMEPS LYRCSNVDCK VSPLTFMVQL SNKLIMDIRR CIKKYYDGWL 
      1360       1370       1380       1390       1400
ICEEPTCCSR LRRLPLHFSR NGPLCPVCMK AVLRPEYSDK SLYTQLCFYR 
      1410       1420       1430       1440       1450
YIFDADCALE KLTEHEKDKL KKQFFPLRVL QDYRKVKNIA EQFLSWSGYS 
      1460 
EVNLSKLFAN YAGKS
Length:1,465
Mass (Da):167,340
Last modified:June 1, 1994 - v2
<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:i46D1A9818A7944A3
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti1180S → F in temperature-sensitive FT20 cell line; defective activity. 1 Publication1

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
D13543 mRNA Translation: BAA40003.1
D17384 mRNA Translation: BAA04202.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS30272.1

Protein sequence database of the Protein Information Resource

More...PIRi		S45628

NCBI Reference Sequences

More...RefSeqi		NP_032918.1, NM_008892.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000006856; ENSMUSP00000006856; ENSMUSG00000006678

Database of genes from NCBI RefSeq genomes

More...GeneIDi		18968

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:18968

UCSC genome browser

More...UCSCi		uc009tss.2, mouse

<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
D13543 mRNA Translation: BAA40003.1
D17384 mRNA Translation: BAA04202.1
CCDSiCCDS30272.1
PIRiS45628
RefSeqiNP_032918.1, NM_008892.2

3D structure databases

SMRiP33609
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi202287, 3 interactors
ComplexPortaliCPX-2088, DNA polymerase alpha:primase complex
CORUMiP33609
IntActiP33609, 4 interactors
STRINGi10090.ENSMUSP00000006856

Chemistry databases

ChEMBLiCHEMBL2797

PTM databases

iPTMnetiP33609
PhosphoSitePlusiP33609

Proteomic databases

EPDiP33609
jPOSTiP33609
MaxQBiP33609
PaxDbiP33609
PeptideAtlasiP33609
PRIDEiP33609
ProteomicsDBi279570

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		498, 186 antibodies from 27 providers

The DNASU plasmid repository

More...DNASUi		18968

Genome annotation databases

EnsembliENSMUST00000006856; ENSMUSP00000006856; ENSMUSG00000006678
GeneIDi18968
KEGGimmu:18968
UCSCiuc009tss.2, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5422
MGIiMGI:99660, Pola1
VEuPathDBiHostDB:ENSMUSG00000006678

Phylogenomic databases

eggNOGiKOG0970, Eukaryota
GeneTreeiENSGT00550000074891
HOGENOMiCLU_001718_0_0_1
InParanoidiP33609
OMAiWLKIEDA
OrthoDBi293315at2759
PhylomeDBiP33609
TreeFamiTF103001

Enzyme and pathway databases

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

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		18968, 31 hits in 101 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		Pola1, mouse

Protein Ontology

More...PROi		PR:P33609
RNActiP33609, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000006678, Expressed in embryonic stem cell and 239 other tissues
GenevisibleiP33609, MM

Family and domain databases

CDDicd05532, POLBc_alpha, 1 hit
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
IPR043502, DNA/RNA_pol_sf
IPR024647, DNA_pol_a_cat_su_N
IPR042087, DNA_pol_B_thumb
IPR023211, DNA_pol_palm_dom_sf
IPR038256, Pol_alpha_znc_sf
IPR045846, POLBc_alpha
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
SSF56672, SSF56672, 1 hit
PROSITEiView protein in PROSITE
PS00116, DNA_POLYMERASE_B, 1 hit

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_MOUSE
<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: P33609
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: June 1, 1994
Last modified: February 23, 2022
This is version 177 of the entry and version 2 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

Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again