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Protein

DNA polymerase epsilon catalytic subunit A

Gene

POL2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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

DNA polymerase epsilon (DNA polymerase II) participates in chromosomal DNA replication. It is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair.1 Publication

Miscellaneous

In eukaryotes there are five DNA polymerases: alpha, beta, gamma, delta, and epsilon which are responsible for different reactions of DNA synthesis.
Present with 1970 molecules/cell in log phase SD medium.1 Publication

<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] cluster1 PublicationNote: Binds 1 [4Fe-4S] cluster.1 Publication

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 bindingi2108ZincBy similarity1
Metal bindingi2111ZincBy similarity1
Metal bindingi2130ZincBy similarity1
Metal bindingi2133ZincBy similarity1
Metal bindingi2164Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi2167Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi2179Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi2181Iron-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 fingeri2108 – 2133CysA-typeAdd BLAST26

<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

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • DNA binding Source: GO_Central
  • DNA-directed DNA polymerase activity Source: SGD
  • double-stranded DNA binding Source: SGD
  • nucleotide binding Source: InterPro
  • single-stranded DNA 3'-5' exodeoxyribonuclease activity Source: SGD
  • single-stranded DNA binding Source: SGD
  • zinc ion binding Source: InterPro

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

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-33258-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-110314 Recognition of DNA damage by PCNA-containing replication complex
R-SCE-174430 Telomere C-strand synthesis initiation
R-SCE-5651801 PCNA-Dependent Long Patch Base Excision Repair
R-SCE-5656169 Termination of translesion DNA synthesis
R-SCE-5696400 Dual Incision in GG-NER
R-SCE-6782135 Dual incision in TC-NER
R-SCE-68952 DNA replication initiation
R-SCE-68962 Activation of the pre-replicative complex

<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 epsilon catalytic subunit A (EC:2.7.7.7)
Alternative name(s):
DNA polymerase II subunit A
<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:POL2
Synonyms:DUN2
Ordered Locus Names:YNL262W
ORF Names:N0825
<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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<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 identifieri559292 [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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<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
  • UP000002311 <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 XIV

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000005206 POL2

<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 Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi644M → I in POL2-9; temperature-sensitive mutant. 1 Publication1
Mutagenesisi710P → S in POL2-18; temperature-sensitive mutant. 1 Publication1

<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_00000464671 – 2222DNA polymerase epsilon catalytic subunit AAdd BLAST2222

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P21951

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

More...
PaxDbi
P21951

PRoteomics IDEntifications database

More...
PRIDEi
P21951

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P21951

<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

DNA polymerase epsilon is a heterotetramer consisting of POL2, DPB2, DPB3 and DPB4.1 Publication

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

WithEntry#Exp.IntActNotes
DPB2P244827EBI-6140,EBI-6071

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
35577, 599 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2110 DNA polymerase epsilon complex

Database of interacting proteins

More...
DIPi
DIP-2532N

Protein interaction database and analysis system

More...
IntActi
P21951, 20 interactors

Molecular INTeraction database

More...
MINTi
P21951

STRING: functional protein association networks

More...
STRINGi
4932.YNL262W

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

Secondary structure

12222
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P21951

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

More...
SMRi
P21951

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

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>Motifi2164 – 2181CysB motifAdd BLAST18

<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 DNA polymerase activity domain resides in the N-terminal half of the protein, while the C-terminus is necessary for complexing subunits B and C.
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 fingeri2108 – 2133CysA-typeAdd BLAST26

Keywords - Domaini

Zinc-finger

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000010194

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000196287

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P21951

KEGG Orthology (KO)

More...
KOi
K02324

Identification of Orthologs from Complete Genome Data

More...
OMAi
IIQMARQ

Database of Orthologous Groups

More...
OrthoDBi
EOG092C00WD

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.420.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006172 DNA-dir_DNA_pol_B
IPR006133 DNA-dir_DNA_pol_B_exonuc
IPR006134 DNA-dir_DNA_pol_B_multi_dom
IPR013697 DNA_pol_e_suA_C
IPR029703 POL2
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf

The PANTHER Classification System

More...
PANTHERi
PTHR10670 PTHR10670, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00136 DNA_pol_B, 1 hit
PF03104 DNA_pol_B_exo1, 1 hit
PF08490 DUF1744, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01159 DUF1744, 1 hit
SM00486 POLBc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53098 SSF53098, 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.

P21951-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MMFGKKKNNG GSSTARYSAG NKYNTLSNNY ALSAQQLLNA SKIDDIDSMM
60 70 80 90 100
GFERYVPPQY NGRFDAKDID QIPGRVGWLT NMHATLVSQE TLSSGSNGGG
110 120 130 140 150
NSNDGERVTT NQGISGVDFY FLDEEGGSFK STVVYDPYFF IACNDESRVN
160 170 180 190 200
DVEELVKKYL ESCLKSLQII RKEDLTMDNH LLGLQKTLIK LSFVNSNQLF
210 220 230 240 250
EARKLLRPIL QDNANNNVQR NIYNVAANGS EKVDAKHLIE DIREYDVPYH
260 270 280 290 300
VRVSIDKDIR VGKWYKVTQQ GFIEDTRKIA FADPVVMAFD IETTKPPLKF
310 320 330 340 350
PDSAVDQIMM ISYMIDGEGF LITNREIISE DIEDFEYTPK PEYPGFFTIF
360 370 380 390 400
NENDEVALLQ RFFEHIRDVR PTVISTFNGD FFDWPFIHNR SKIHGLDMFD
410 420 430 440 450
EIGFAPDAEG EYKSSYCSHM DCFRWVKRDS YLPQGSQGLK AVTQSKLGYN
460 470 480 490 500
PIELDPELMT PYAFEKPQHL SEYSVSDAVA TYYLYMKYVH PFIFSLCTII
510 520 530 540 550
PLNPDETLRK GTGTLCEMLL MVQAYQHNIL LPNKHTDPIE RFYDGHLLES
560 570 580 590 600
ETYVGGHVES LEAGVFRSDL KNEFKIDPSA IDELLQELPE ALKFSVEVEN
610 620 630 640 650
KSSVDKVTNF EEIKNQITQK LLELKENNIR NELPLIYHVD VASMYPNIMT
660 670 680 690 700
TNRLQPDSIK AERDCASCDF NRPGKTCARK LKWAWRGEFF PSKMDEYNMI
710 720 730 740 750
KRALQNETFP NKNKFSKKKV LTFDELSYAD QVIHIKKRLT EYSRKVYHRV
760 770 780 790 800
KVSEIVEREA IVCQRENPFY VDTVKSFRDR RYEFKGLAKT WKGNLSKIDP
810 820 830 840 850
SDKHARDEAK KMIVLYDSLQ LAHKVILNSF YGYVMRKGSR WYSMEMAGIT
860 870 880 890 900
CLTGATIIQM ARALVERVGR PLELDTDGIW CILPKSFPET YFFTLENGKK
910 920 930 940 950
LYLSYPCSML NYRVHQKFTN HQYQELKDPL NYIYETHSEN TIFFEVDGPY
960 970 980 990 1000
KAMILPSSKE EGKGIKKRYA VFNEDGSLAE LKGFELKRRG ELQLIKNFQS
1010 1020 1030 1040 1050
DIFKVFLEGD TLEGCYSAVA SVCNRWLDVL DSHGLMLEDE DLVSLICENR
1060 1070 1080 1090 1100
SMSKTLKEYE GQKSTSITTA RRLGDFLGED MVKDKGLQCK YIISSKPFNA
1110 1120 1130 1140 1150
PVTERAIPVA IFSADIPIKR SFLRRWTLDP SLEDLDIRTI IDWGYYRERL
1160 1170 1180 1190 1200
GSAIQKIITI PAALQGVSNP VPRVEHPDWL KRKIATKEDK FKQTSLTKFF
1210 1220 1230 1240 1250
SKTKNVPTMG KIKDIEDLFE PTVEEDNAKI KIARTTKKKA VSKRKRNQLT
1260 1270 1280 1290 1300
NEEDPLVLPS EIPSMDEDYV GWLNYQKIKW KIQARDRKRR DQLFGNTNSS
1310 1320 1330 1340 1350
RERSALGSMI RKQAESYANS TWEVLQYKDS GEPGVLEVFV TINGKVQNIT
1360 1370 1380 1390 1400
FHIPKTIYMK FKSQTMPLQK IKNCLIEKSS ASLPNNPKTS NPAGGQLFKI
1410 1420 1430 1440 1450
TLPESVFLEE KENCTSIFND ENVLGVFEGT ITPHQRAIMD LGASVTFRSK
1460 1470 1480 1490 1500
AMGALGKGIQ QGFEMKDLSM AENERYLSGF SMDIGYLLHF PTSIGYEFFS
1510 1520 1530 1540 1550
LFKSWGDTIT ILVLKPSNQA QEINASSLGQ IYKQMFEKKK GKIETYSYLV
1560 1570 1580 1590 1600
DIKEDINFEF VYFTDISKLY RRLSQETTKL KEERGLQFLL LLQSPFITKL
1610 1620 1630 1640 1650
LGTIRLLNQM PIVKLSLNEV LLPQLNWQPT LLKKLVNHVL SSGSWISHLI
1660 1670 1680 1690 1700
KLSQYSNIPI CNLRLDSMDY IIDVLYARKL KKENIVLWWN EKAPLPDHGG
1710 1720 1730 1740 1750
IQNDFDLNTS WIMNDSEFPK INNSGVYDNV VLDVGVDNLT VNTILTSALI
1760 1770 1780 1790 1800
NDAEGSDLVN NNMGIDDKDA VINSPSEFVH DAFSNDALNV LRGMLKEWWD
1810 1820 1830 1840 1850
EALKENSTAD LLVNSLASWV QNPNAKLFDG LLRYHVHNLT KKALLQLVNE
1860 1870 1880 1890 1900
FSALGSTIVY ADRNQILIKT NKYSPENCYA YSQYMMKAVR TNPMFSYLDL
1910 1920 1930 1940 1950
NIKRYWDLLI WMDKFNFSGL ACIEIEEKEN QDYTAVSQWQ LKKFLSPIYQ
1960 1970 1980 1990 2000
PEFEDWMMII LDSMLKTKQS YLKLNSGTQR PTQIVNVKKQ DKEDSVENSL
2010 2020 2030 2040 2050
NGFSHLFSKP LMKRVKKLFK NQQEFILDPQ YEADYVIPVL PGSHLNVKNP
2060 2070 2080 2090 2100
LLELVKSLCH VMLLSKSTIL EIRTLRKELL KIFELREFAK VAEFKDPSLS
2110 2120 2130 2140 2150
LVVPDFLCEY CFFISDIDFC KAAPESIFSC VRCHKAFNQV LLQEHLIQKL
2160 2170 2180 2190 2200
RSDIESYLIQ DLRCSRCHKV KRDYMSAHCP CAGAWEGTLP RESIVQKLNV
2210 2220
FKQVAKYYGF DILLSCIADL TI
Length:2,222
Mass (Da):255,671
Last modified:August 1, 1991 - 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:iCBCDDE2AB147D65B
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M60416 Genomic DNA Translation: AAA88711.1
X92494 Genomic DNA Translation: CAA63235.1
Z71538 Genomic DNA Translation: CAA96169.1
BK006947 Genomic DNA Translation: DAA10297.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A36028

NCBI Reference Sequences

More...
RefSeqi
NP_014137.1, NM_001183100.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YNL262W_mRNA; YNL262W_mRNA; YNL262W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
855459

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YNL262W

<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
M60416 Genomic DNA Translation: AAA88711.1
X92494 Genomic DNA Translation: CAA63235.1
Z71538 Genomic DNA Translation: CAA96169.1
BK006947 Genomic DNA Translation: DAA10297.1
PIRiA36028
RefSeqiNP_014137.1, NM_001183100.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4M8OX-ray2.20A1-1228[»]
4PTFX-ray2.81A1-1187[»]
5OKIX-ray4.50A/B1-524[»]
ProteinModelPortaliP21951
SMRiP21951
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35577, 599 interactors
ComplexPortaliCPX-2110 DNA polymerase epsilon complex
DIPiDIP-2532N
IntActiP21951, 20 interactors
MINTiP21951
STRINGi4932.YNL262W

PTM databases

iPTMnetiP21951

Proteomic databases

MaxQBiP21951
PaxDbiP21951
PRIDEiP21951

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL262W_mRNA; YNL262W_mRNA; YNL262W
GeneIDi855459
KEGGisce:YNL262W

Organism-specific databases

SGDiS000005206 POL2

Phylogenomic databases

GeneTreeiENSGT00390000010194
HOGENOMiHOG000196287
InParanoidiP21951
KOiK02324
OMAiIIQMARQ
OrthoDBiEOG092C00WD

Enzyme and pathway databases

BioCyciYEAST:G3O-33258-MONOMER
ReactomeiR-SCE-110314 Recognition of DNA damage by PCNA-containing replication complex
R-SCE-174430 Telomere C-strand synthesis initiation
R-SCE-5651801 PCNA-Dependent Long Patch Base Excision Repair
R-SCE-5656169 Termination of translesion DNA synthesis
R-SCE-5696400 Dual Incision in GG-NER
R-SCE-6782135 Dual incision in TC-NER
R-SCE-68952 DNA replication initiation
R-SCE-68962 Activation of the pre-replicative complex

Miscellaneous databases

Protein Ontology

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PROi
PR:P21951

Family and domain databases

Gene3Di3.30.420.10, 1 hit
InterProiView protein in InterPro
IPR006172 DNA-dir_DNA_pol_B
IPR006133 DNA-dir_DNA_pol_B_exonuc
IPR006134 DNA-dir_DNA_pol_B_multi_dom
IPR013697 DNA_pol_e_suA_C
IPR029703 POL2
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
PANTHERiPTHR10670 PTHR10670, 1 hit
PfamiView protein in Pfam
PF00136 DNA_pol_B, 1 hit
PF03104 DNA_pol_B_exo1, 1 hit
PF08490 DUF1744, 1 hit
SMARTiView protein in SMART
SM01159 DUF1744, 1 hit
SM00486 POLBc, 1 hit
SUPFAMiSSF53098 SSF53098, 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 nameiDPOE_YEAST
<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: P21951
Secondary accession number(s): D6W0T1
<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: August 1, 1991
Last sequence update: August 1, 1991
Last modified: December 5, 2018
This is version 182 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 programFungal Protein Annotation Program

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

Keywords - Technical termi

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

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names
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