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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

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.
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_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 ‘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 bindingi1287ZincBy similarity1
Metal bindingi1290ZincBy similarity1
Metal bindingi1314ZincBy similarity1
Metal bindingi1319ZincBy similarity1
Metal bindingi1352Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1357Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1375Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1378Iron-sulfur (4Fe-4S)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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

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, 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-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_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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 X

Organism-specific databases

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

More...
MGIi
MGI:99660 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; 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

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.<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

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

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000006678 Expressed in 213 organ(s), highest expression level in embryonic stem cell

CleanEx database of gene expression profiles

More...
CleanExi
MM_POLA1

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_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

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
202287, 2 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

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P33609

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

More...
SMRi
P33609

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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>Regioni654 – 719DNA-binding regionSequence analysisAdd BLAST66
Regioni1249 – 1380DNA-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>Motifi1352 – 1378CysB 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 fingeri1287 – 1317CysA-typeAdd BLAST31

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0970 Eukaryota
COG0417 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00550000074891

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000163524

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG080008

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P33609

KEGG Orthology (KO)

More...
KOi
K02320

Identification of Orthologs from Complete Genome Data

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OMAi
FPYDFKE

Database of Orthologous Groups

More...
OrthoDBi
EOG091G00RR

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P33609

TreeFam database of animal gene trees

More...
TreeFami
TF103001

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
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
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>.<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.

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

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EMBLi

GenBank nucleotide sequence database

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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

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PIRi
S45628

NCBI Reference Sequences

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RefSeqi
NP_032918.1, NM_008892.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.1923

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000006856; ENSMUSP00000006856; ENSMUSG00000006678

Database of genes from NCBI RefSeq genomes

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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
UniGeneiMm.1923

3D structure databases

ProteinModelPortaliP33609
SMRiP33609
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202287, 2 interactors
ComplexPortaliCPX-2088 DNA polymerase alpha:primase complex
CORUMiP33609
IntActiP33609, 4 interactors
STRINGi10090.ENSMUSP00000006856

Chemistry databases

ChEMBLiCHEMBL2797

PTM databases

iPTMnetiP33609
PhosphoSitePlusiP33609

Proteomic databases

EPDiP33609
MaxQBiP33609
PaxDbiP33609
PeptideAtlasiP33609
PRIDEiP33609

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
5422
MGIiMGI:99660 Pola1

Phylogenomic databases

eggNOGiKOG0970 Eukaryota
COG0417 LUCA
GeneTreeiENSGT00550000074891
HOGENOMiHOG000163524
HOVERGENiHBG080008
InParanoidiP33609
KOiK02320
OMAiFPYDFKE
OrthoDBiEOG091G00RR
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

Protein Ontology

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PROi
PR:P33609

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSMUSG00000006678 Expressed in 213 organ(s), highest expression level in embryonic stem cell
CleanExiMM_POLA1
GenevisibleiP33609 MM

Family and domain databases

Gene3Di1.10.3200.20, 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
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

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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 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_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: February 1, 1994
Last sequence update: June 1, 1994
Last modified: December 5, 2018
This is version 160 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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