DNA polymerase epsilon subunit C - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Contribute

Send feedback

Read comments (?) or add your own

P27344 (DPB3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 107. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
DNA polymerase epsilon subunit C
EC=2.7.7.7

Alternative name(s):
DNA polymerase II subunit C

Gene names

Name:	DPB3
Ordered Locus Names:	YBR278W
ORF Names:	YBR2015

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	201 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.6
Catalytic activity	Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Subunit structure	DNA polymerase epsilon is a heterotetramer consisting of POL2, DPB2, DPB3 and DPB4. Ref.5
Subcellular location	Nucleus Ref.5.
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 784 molecules/cell in log phase SD medium.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Nucleus
Molecular function	DNA-directed DNA polymerase Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	error-prone translesion synthesis Inferred from direct assay PubMed 19776424. Source: SGD heterochromatin organization involved in chromatin silencing Inferred from mutant phenotype PubMed 14673157 PubMed 19629037. Source: SGD leading strand elongation Inferred from mutant phenotype PubMed 21124948. Source: SGD replicative senescence Inferred from mutant phenotype PubMed 21321081. Source: SGD
Cellular_component	epsilon DNA polymerase complex Inferred from direct assay Ref.7 PubMed 2406268. Source: SGD
Molecular_function	DNA-directed DNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DPB4	Q04603	3	EBI-6076,EBI-29938

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 201

201

DNA polymerase epsilon subunit C

PRO_0000208350

Regions

Compositional bias

120 – 154

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

166

Phosphoserine Ref.12

Modified residue

169

Phosphoserine Ref.12

Modified residue

186

Phosphoserine Ref.9 Ref.10 Ref.11 Ref.12

Modified residue

188

Phosphoserine Ref.11 Ref.12

Modified residue

189

Phosphoserine Ref.10 Ref.11 Ref.12

Experimental info

Sequence conflict

196

T → M in CAA41403. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P27344 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: 288913917D49C7F9
Show »

FASTA

201

22,665

        10         20         30         40         50         60 
MSNLVKEKAP VFPISKVKKI AKCDPEYVIT SNVAISATAF AAELFVQNLV EESLVLAQLN 

        70         80         90        100        110        120 
SKGKTSLRLS LNSIEECVEK RDNFRFLEDA IKQLKKNSAL DKKRELNMQP GRSDQEVVIE 

       130        140        150        160        170        180 
EPELHEDDGV EEEEEEDEVS EEEEPVHNEE LLDDSKDQQN DKSTRSVASL LSRFQYKSAL 

       190        200 
DVGEHSDSSD IEVDHTKSTD P

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning DPB3, the gene encoding the third subunit of DNA polymerase II of Saccharomyces cerevisiae." Araki H., Hamatake R.K., Morrison A., Johnson A.L., Johnston L.H., Sugino A. Nucleic Acids Res. 19:4867-4872(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204626 / S288c / A364A.
[2]	"The sequence of a 32,420 bp segment located on the right arm of chromosome II from Saccharomyces cerevisiae." Holmstroem K., Brandt T., Kallesoe T. Yeast 10:S47-S62(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. Kleine K. EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Structure and function of the fourth subunit (Dpb4p) of DNA polymerase epsilon in Saccharomyces cerevisiae." Ohya T., Maki S., Kawasaki Y., Sugino A. Nucleic Acids Res. 28:3846-3852(2000) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, SUBCELLULAR LOCATION.
[6]	"Fidelity of DNA polymerase epsilon holoenzyme from budding yeast Saccharomyces cerevisiae." Shimizu K., Hashimoto K., Kirchner J.M., Nakai W., Nishikawa H., Resnick M.A., Sugino A. J. Biol. Chem. 277:37422-37429(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"The quaternary structure of DNA polymerase epsilon from Saccharomyces cerevisiae." Chilkova O., Jonsson B.-H., Johansson E. J. Biol. Chem. 278:14082-14086(2003) [PubMed] [Europe PMC] [Abstract] Cited for: COMPOSITION OF THE DNA POLYMERASE EPSILON COMPLEX.
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, MASS SPECTROMETRY. Strain: ADR376.
[10]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186 AND SER-189, MASS SPECTROMETRY.
[11]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186; SER-188 AND SER-189, MASS SPECTROMETRY.
[12]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166; SER-169; SER-186; SER-188 AND SER-189, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X58500 Genomic DNA. Translation: CAA41403.1. X76053 Genomic DNA. Translation: CAA53641.1. Z36146 Genomic DNA. Translation: CAA85242.1. BK006936 Genomic DNA. Translation: DAA07393.1.
PIR	S44540.
RefSeq	NP_009837.1. NM_001178626.1.
3D structure databases
ProteinModelPortal	P27344.
SMR	P27344. Positions 12-93.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4803N.
IntAct	P27344. 13 interactions.
MINT	MINT-482796.
STRING	4932.YBR278W.
Proteomic databases
PaxDb	P27344.
PeptideAtlas	P27344.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YBR278W; YBR278W; YBR278W.
GeneID	852580.
KEGG	sce:YBR278W.
Organism-specific databases
CYGD	YBR278w.
SGD	S000000482. DPB3.
Phylogenomic databases
eggNOG	NOG309481.
GeneTree	ENSGT00530000067039.
KO	K03506.
OMA	DYIFLED.
OrthoDB	EOG46QB3B.
Gene expression databases
Genevestigator	P27344.
GermOnline	YBR278W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.10.20.10. 1 hit.
InterPro	IPR009072. Histone-fold. [Graphical view]
SUPFAM	SSF47113. Histone-fold. 1 hit.
ProtoNet	Search...
Other
NextBio	971724.

Entry information

Entry name

DPB3_YEAST

Accession

Primary (citable) accession number: P27344
Secondary accession number(s): D6VQS3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	October 1, 1994
Last modified:	April 3, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents