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Protein

DNA polymerase epsilon subunit B

Gene

DPB2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • DNA-dependent DNA replication Source: SGD
  • DNA-dependent DNA replication maintenance of fidelity Source: SGD
  • error-prone translesion synthesis Source: SGD
  • heterochromatin organization involved in chromatin silencing Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

Cell cycle, DNA replication

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-34302-MONOMER.
ReactomeiR-SCE-174430. Telomere C-strand synthesis initiation.
R-SCE-68952. DNA replication initiation.
R-SCE-68962. Activation of the pre-replicative complex.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase epsilon subunit B (EC:2.7.7.7)
Alternative name(s):
DNA polymerase II subunit 2
Gene namesi
Name:DPB2
Ordered Locus Names:YPR175W
ORF Names:P9705.7
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPR175W.
SGDiS000006379. DPB2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • epsilon DNA polymerase complex Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000715731 – 689DNA polymerase epsilon subunit BAdd BLAST689

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei122PhosphoserineCombined sources1
Modified residuei141Phosphoserine; by CDC281 Publication1
Modified residuei613Phosphoserine1 Publication1

Post-translational modificationi

Phosphorylated in a cell cycle dependent manner during late G1 phase. Phosphorylation may facilitate the interaction with POL2 or the activity of DNA polymerase II. Phosphorylation is independent of DNA replication but dependent upon CDC28 in vivo. Both Ser-141 and Ser-613 are phosphorylated in vivo, but in vitro only Ser-141 is phosphorylated by CDC28.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP24482.
PRIDEiP24482.

PTM databases

iPTMnetiP24482.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi36348. 61 interactors.
DIPiDIP-2533N.
IntActiP24482. 23 interactors.
MINTiMINT-532205.

Structurei

3D structure databases

ProteinModelPortaliP24482.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000012435.
HOGENOMiHOG000246706.
InParanoidiP24482.
KOiK02325.
OMAiFVPGDND.
OrthoDBiEOG092C2QT9.

Family and domain databases

InterProiIPR007185. DNA_pol_alpha/epsilon_bsu.
[Graphical view]
PfamiPF04042. DNA_pol_E_B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P24482-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFGSGNVLPV KIQPPLLRPL AYRVLSRKYG LSIKSDGLSA LAEFVGTNIG
60 70 80 90 100
ANWRQGPATI KFLEQFAAVW KQQERGLFID QSGVKEVIQE MKEREKVEWS
110 120 130 140 150
HEHPIQHEEN ILGRTDDDEN NSDDEMPIAA DSSLQNVSLS SPMRQPTERD
160 170 180 190 200
EYKQPFKPES SKALDWRDYF KVINASQQQR FSYNPHKMQF IFVPNKKQNG
210 220 230 240 250
LGGIAGFLPD IEDKVQMFLT RYYLTNDRVM RNENFQNSDM FNPLSSMVSL
260 270 280 290 300
QNELSNTNRQ QQSSSMSITP IKNLLGRDAQ NFLLLGLLNK NFKGNWSLED
310 320 330 340 350
PSGSVEIDIS QTIPTQGHYY VPGCMVLVEG IYYSVGNKFH VTSMTLPPGE
360 370 380 390 400
RREITLETIG NLDLLGIHGI SNNNFIARLD KDLKIRLHLL EKELTDHKFV
410 420 430 440 450
ILGANLFLDD LKIMTALSKI LQKLNDDPPT LLIWQGSFTS VPVFASMSSR
460 470 480 490 500
NISSSTQFKN NFDALATLLS RFDNLTENTT MIFIPGPNDL WGSMVSLGAS
510 520 530 540 550
GTLPQDPIPS AFTKKINKVC KNVVWSSNPT RIAYLSQEIV IFRDDLSGRF
560 570 580 590 600
KRHRLEFPFN ESEDVYTEND NMMSKDTDIV PIDELVKEPD QLPQKVQETR
610 620 630 640 650
KLVKTILDQG HLSPFLDSLR PISWDLDHTL TLCPIPSTMV LCDTTSAQFD
660 670 680
LTYNGCKVIN PGSFIHNRRA RYMEYVPSSK KTIQEEIYI
Length:689
Mass (Da):78,340
Last modified:January 10, 2006 - v3
Checksum:i0936E3FC90552788
GO

Sequence cautioni

The sequence AAA34576 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAB68109 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti458F → Y in AAA34576 (PubMed:2052544).Curated1
Sequence conflicti521K → R in AAA34576 (PubMed:2052544).Curated1
Sequence conflicti565V → F in AAA34576 (PubMed:2052544).Curated1
Sequence conflicti584E → Q in AAA34576 (PubMed:2052544).Curated1
Sequence conflicti644T → I in AAA34576 (PubMed:2052544).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61710 Genomic DNA. Translation: AAA34576.1. Different initiation.
U25842 Genomic DNA. Translation: AAB68109.1. Different initiation.
BK006949 Genomic DNA. Translation: DAA11592.1.
PIRiS59833.
RefSeqiNP_015501.2. NM_001184272.1.

Genome annotation databases

EnsemblFungiiYPR175W; YPR175W; YPR175W.
GeneIDi856305.
KEGGisce:YPR175W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61710 Genomic DNA. Translation: AAA34576.1. Different initiation.
U25842 Genomic DNA. Translation: AAB68109.1. Different initiation.
BK006949 Genomic DNA. Translation: DAA11592.1.
PIRiS59833.
RefSeqiNP_015501.2. NM_001184272.1.

3D structure databases

ProteinModelPortaliP24482.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36348. 61 interactors.
DIPiDIP-2533N.
IntActiP24482. 23 interactors.
MINTiMINT-532205.

PTM databases

iPTMnetiP24482.

Proteomic databases

MaxQBiP24482.
PRIDEiP24482.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR175W; YPR175W; YPR175W.
GeneIDi856305.
KEGGisce:YPR175W.

Organism-specific databases

EuPathDBiFungiDB:YPR175W.
SGDiS000006379. DPB2.

Phylogenomic databases

GeneTreeiENSGT00390000012435.
HOGENOMiHOG000246706.
InParanoidiP24482.
KOiK02325.
OMAiFVPGDND.
OrthoDBiEOG092C2QT9.

Enzyme and pathway databases

BioCyciYEAST:G3O-34302-MONOMER.
ReactomeiR-SCE-174430. Telomere C-strand synthesis initiation.
R-SCE-68952. DNA replication initiation.
R-SCE-68962. Activation of the pre-replicative complex.

Miscellaneous databases

PROiP24482.

Family and domain databases

InterProiIPR007185. DNA_pol_alpha/epsilon_bsu.
[Graphical view]
PfamiPF04042. DNA_pol_E_B. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDPB2_YEAST
AccessioniPrimary (citable) accession number: P24482
Secondary accession number(s): D6W4H6, Q06622
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 10, 2006
Last modified: November 2, 2016
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3110 +/- 251 molecules/cell in log phase SD medium.1 Publication
In eukaryotes there are five DNA polymerases: alpha, beta, gamma, delta, and epsilon which are responsible for different reactions of DNA synthesis.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.