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P56282 (DPOE2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA polymerase epsilon subunit 2

EC=2.7.7.7
Alternative name(s):
DNA polymerase II subunit 2
DNA polymerase epsilon subunit B
Gene names
Name:POLE2
Synonyms:DPE2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length527 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Participates in DNA repair and in chromosomal DNA replication.

Catalytic activity

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Subunit structure

Component of the epsilon DNA polymerase complex consisting of four subunits: POLE, POLE2, POLE3 and POLE4. Ref.8

Subcellular location

Nucleus.

Miscellaneous

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

Sequence similarities

Belongs to the DNA polymerase epsilon subunit B family.

Ontologies

Keywords
   Biological processDNA replication
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandDNA-binding
   Molecular functionDNA-directed DNA polymerase
Nucleotidyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Traceable author statement. Source: Reactome

DNA replication

Traceable author statement Ref.1. Source: ProtInc

DNA replication initiation

Traceable author statement. Source: Reactome

G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

nucleotide-excision repair

Traceable author statement. Source: Reactome

nucleotide-excision repair, DNA gap filling

Traceable author statement. Source: Reactome

telomere maintenance

Traceable author statement. Source: Reactome

telomere maintenance via recombination

Traceable author statement. Source: Reactome

telomere maintenance via semi-conservative replication

Traceable author statement. Source: Reactome

transcription-coupled nucleotide-excision repair

Traceable author statement. Source: Reactome

   Cellular_componentepsilon DNA polymerase complex

Inferred from direct assay Ref.8. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-directed DNA polymerase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P56282-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P56282-2)

The sequence of this isoform differs from the canonical sequence as follows:
     83-108: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P56282-3)

The sequence of this isoform differs from the canonical sequence as follows:
     500-527: GSFPRSGFSFKVFYPSNKTVEDSKLQGF → VRM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 527527DNA polymerase epsilon subunit 2
PRO_0000071562

Natural variations

Alternative sequence83 – 10826Missing in isoform 2.
VSP_042551
Alternative sequence500 – 52728GSFPR…KLQGF → VRM in isoform 3.
VSP_043796
Natural variant841H → P. Ref.4
Corresponds to variant rs34857719 [ dbSNP | Ensembl ].
VAR_044379
Natural variant4561L → V.
Corresponds to variant rs34574266 [ dbSNP | Ensembl ].
VAR_044380
Natural variant5141P → L. Ref.4
Corresponds to variant rs45515094 [ dbSNP | Ensembl ].
VAR_044381

Experimental info

Sequence conflict111L → P in AAC51920. Ref.1
Sequence conflict3591Missing in AAC51920. Ref.1

Secondary structure

............. 527
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: AFA7AF7C2C0BFF15

FASTA52759,537
        10         20         30         40         50         60 
MAPERLRSRA LSAFKLRGLL LRGEAIKYLT EALQSISELE LEDKLEKIIN AVEKQPLSSN 

        70         80         90        100        110        120 
MIERSVVEAA VQECSQSVDE TIEHVFNIIG AFDIPRFVYN SERKKFLPLL MTNHPAPNLF 

       130        140        150        160        170        180 
GTPRDKAEMF RERYTILHQR THRHELFTPP VIGSHPDESG SKFQLKTIET LLGSTTKIGD 

       190        200        210        220        230        240 
AIVLGMITQL KEGKFFLEDP TGTVQLDLSK AQFHSGLYTE ACFVLAEGWF EDQVFHVNAF 

       250        260        270        280        290        300 
GFPPTEPSST TRAYYGNINF FGGPSNTSVK TSAKLKQLEE ENKDAMFVFL SDVWLDQVEV 

       310        320        330        340        350        360 
LEKLRIMFAG YSPAPPTCFI LCGNFSSAPY GKNQVQALKD SLKTLADIIC EYPDIHQSSR 

       370        380        390        400        410        420 
FVFVPGPEDP GFGSILPRPP LAESITNEFR QRVPFSVFTT NPCRIQYCTQ EITVFREDLV 

       430        440        450        460        470        480 
NKMCRNCVRF PSSNLAIPNH FVKTILSQGH LTPLPLYVCP VYWAYDYALR VYPVPDLLVI 

       490        500        510        520 
ADKYDPFTTT NTECLCINPG SFPRSGFSFK VFYPSNKTVE DSKLQGF 

« Hide

Isoform 2 [UniParc].

Checksum: ECB4BFD1E2FDAE1C
Show »

FASTA50156,418
Isoform 3 [UniParc].

Checksum: 0F3391E93AB14483
Show »

FASTA50256,784

References

« Hide 'large scale' references
[1]"Purification, cDNA cloning, and gene mapping of the small subunit of human DNA polymerase epsilon."
Li Y., Asahara H., Patel V.S., Zhou S., Linn S.
J. Biol. Chem. 272:32337-32344(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The small subunits of human and mouse DNA polymerase epsilon are homologous to the second largest subunit of the yeast Saccharomyces cerevisiae DNA polymerase epsilon."
Jokela M., Makiniemi M., Lehtonen S., Szpirer C., Hellman U., Syvaeoja J.E.
Nucleic Acids Res. 26:730-734(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"E2F mediates induction of the Sp1-controlled promoter of the human DNA polymerase varepsilon B-subunit gene POLE2."
Huang D., Jokela M., Tuusa J., Skog S., Poikonen K., Syvaoja J.E.
Nucleic Acids Res. 29:2810-2821(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]NIEHS SNPs program
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-84 AND LEU-514.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Tissue: Embryonic stem cell.
[8]"Identification and cloning of two histone fold motif-containing subunits of HeLa DNA polymerase epsilon."
Li Y., Pursell Z.F., Linn S.
J. Biol. Chem. 275:23247-23252(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN EPSILON DNA POLYMERASE COMPLEX.
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF025840 mRNA. Translation: AAC51920.1.
AF036899 mRNA. Translation: AAC39610.1.
AF387034 expand/collapse EMBL AC list , AF387021, AF387022, AF387023, AF387024, AF387025, AF387026, AF387027, AF387028, AF387029, AF387030, AF387031, AF387032, AF387033 Genomic DNA. Translation: AAK72254.1.
EF506887 Genomic DNA. Translation: ABO43040.1.
AK293163 mRNA. Translation: BAG56707.1.
AL139099 Genomic DNA. No translation available.
AL591767 Genomic DNA. No translation available.
BC112962 mRNA. Translation: AAI12963.1.
BC126218 mRNA. Translation: AAI26219.1.
BC126220 mRNA. Translation: AAI26221.1.
RefSeqNP_001184259.1. NM_001197330.1.
NP_001184260.1. NM_001197331.1.
NP_002683.2. NM_002692.3.
UniGeneHs.162777.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V6ZNMR-M1-73[»]
ProteinModelPortalP56282.
SMRP56282. Positions 1-75.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111423. 12 interactions.
IntActP56282. 7 interactions.
MINTMINT-1377461.
STRING9606.ENSP00000216367.

PTM databases

PhosphoSiteP56282.

Polymorphism databases

DMDM3915676.

Proteomic databases

PaxDbP56282.
PRIDEP56282.

Protocols and materials databases

DNASU5427.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216367; ENSP00000216367; ENSG00000100479. [P56282-1]
ENST00000539565; ENSP00000446313; ENSG00000100479. [P56282-2]
ENST00000554396; ENSP00000451621; ENSG00000100479. [P56282-3]
GeneID5427.
KEGGhsa:5427.
UCSCuc001wwu.3. human. [P56282-1]
uc010ano.3. human. [P56282-3]
uc021rsr.1. human. [P56282-2]

Organism-specific databases

CTD5427.
GeneCardsGC14M050110.
HGNCHGNC:9178. POLE2.
HPAHPA027555.
MIM602670. gene.
neXtProtNX_P56282.
PharmGKBPA278.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG311342.
HOGENOMHOG000265254.
HOVERGENHBG061290.
InParanoidP56282.
KOK02325.
OMAILQQRTH.
OrthoDBEOG725DH7.
PhylomeDBP56282.
TreeFamTF103007.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_216. DNA Repair.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpressP56282.
BgeeP56282.
CleanExHS_POLE2.
GenevestigatorP56282.

Family and domain databases

InterProIPR007185. DNA_pol_alpha/epsilon_bsu.
IPR016266. DNA_pol_e_bsu.
IPR024639. DNA_pol_e_bsu_N.
[Graphical view]
PfamPF04042. DNA_pol_E_B. 1 hit.
PF12213. Dpoe2NT. 1 hit.
[Graphical view]
PIRSFPIRSF000799. DNA_pol_eps_2. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP56282.
GeneWikiPOLE2.
GenomeRNAi5427.
NextBio20997.
PROP56282.
SOURCESearch...

Entry information

Entry nameDPOE2_HUMAN
AccessionPrimary (citable) accession number: P56282
Secondary accession number(s): A0AV55 expand/collapse secondary AC list , A4FU92, A4LBB7, A6NH58, B4DDE6, O43560
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 15, 1998
Last modified: April 16, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM