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Protein

DNA polymerase delta subunit 3

Gene

POL32

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 delta (DNA polymerase III) 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.

GO - Molecular functioni

  • DNA-directed DNA polymerase activity Source: SGD

GO - Biological processi

  • base-excision repair Source: SGD
  • DNA amplification Source: SGD
  • DNA replication, removal of RNA primer Source: SGD
  • double-strand break repair via break-induced replication Source: SGD
  • lagging strand elongation Source: SGD
  • leading strand elongation Source: SGD
  • mismatch repair Source: SGD
  • nucleic acid phosphodiester bond hydrolysis Source: GOC
  • nucleotide-excision repair Source: SGD
  • postreplication repair Source: SGD
  • RNA-dependent DNA biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA replication

Enzyme and pathway databases

BioCyciYEAST:G3O-31678-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase delta subunit 3
Gene namesi
Name:POL32
Ordered Locus Names:YJR043C
ORF Names:J1626
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJR043C.
SGDiS000003804. POL32.

Subcellular locationi

GO - Cellular componenti

  • delta DNA polymerase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350DNA polymerase delta subunit 3PRO_0000186050Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei223 – 2231PhosphothreonineCombined sources
Modified residuei230 – 2301PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP47110.
PRIDEiP47110.

PTM databases

iPTMnetiP47110.

Interactioni

Subunit structurei

DNA polymerase delta is a heterotrimer of POL3, POL32 and HYS2. POL32 can form homodimers.

Protein-protein interaction databases

BioGridi33794. 284 interactions.
DIPiDIP-2523N.
IntActiP47110. 9 interactions.
MINTiMINT-477170.

Structurei

3D structure databases

ProteinModelPortaliP47110.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

HOGENOMiHOG000112262.
InParanoidiP47110.
KOiK03504.
OMAiDCFIYAF.
OrthoDBiEOG7R5765.

Sequencei

Sequence statusi: Complete.

P47110-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDQKASYFIN EKLFTEVKPV LFTDLIHHLK IGPSMAKKLM FDYYKQTTNA
60 70 80 90 100
KYNCVVICCY KDQTIKIIHD LSNIPQQDSI IDCFIYAFNP MDSFIPYYDI
110 120 130 140 150
IDQKDCLTIK NSYELKVSES SKIIERTKTL EEKSKPLVRP TARSKTTPEE
160 170 180 190 200
TTGRKSKSKD MGLRSTALLA KMKKDRDDKE TSRQNELRKR KEENLQKINK
210 220 230 240 250
QNPEREAQMK ELNNLFVEDD LDTEEVNGGS KPNSPKETDS NDKDKNNDDL
260 270 280 290 300
EDLLETTAED SLMDVPKIQQ TKPSETEHSK EPKSEEEPSS FIDEDGYIVT
310 320 330 340 350
KRPATSTPPR KPSPVVKRAL SSSKKQETPS SNKRLKKQGT LESFFKRKAK
Length:350
Mass (Da):40,310
Last modified:February 1, 1996 - v1
Checksum:iD0B9CC52F26E20B2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L36344 Genomic DNA. Translation: AAA88745.1.
Z49543 Genomic DNA. Translation: CAA89571.1.
AY557918 Genomic DNA. Translation: AAS56244.1.
BK006943 Genomic DNA. Translation: DAA08830.1.
PIRiS57062.
RefSeqiNP_012577.1. NM_001181701.1.

Genome annotation databases

EnsemblFungiiYJR043C; YJR043C; YJR043C.
GeneIDi853500.
KEGGisce:YJR043C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L36344 Genomic DNA. Translation: AAA88745.1.
Z49543 Genomic DNA. Translation: CAA89571.1.
AY557918 Genomic DNA. Translation: AAS56244.1.
BK006943 Genomic DNA. Translation: DAA08830.1.
PIRiS57062.
RefSeqiNP_012577.1. NM_001181701.1.

3D structure databases

ProteinModelPortaliP47110.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33794. 284 interactions.
DIPiDIP-2523N.
IntActiP47110. 9 interactions.
MINTiMINT-477170.

PTM databases

iPTMnetiP47110.

Proteomic databases

MaxQBiP47110.
PRIDEiP47110.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJR043C; YJR043C; YJR043C.
GeneIDi853500.
KEGGisce:YJR043C.

Organism-specific databases

EuPathDBiFungiDB:YJR043C.
SGDiS000003804. POL32.

Phylogenomic databases

HOGENOMiHOG000112262.
InParanoidiP47110.
KOiK03504.
OMAiDCFIYAF.
OrthoDBiEOG7R5765.

Enzyme and pathway databases

BioCyciYEAST:G3O-31678-MONOMER.

Miscellaneous databases

PROiP47110.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of a 42.5 kb DNA sequence of chromosome X reveals three tRNA genes and 14 new open reading frames including a gene most probably belonging to the family of ubiquitin-protein ligases."
    Huang M.-E., Chuat J.-C., Galibert F.
    Yeast 11:775-781(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Characterization of the two small subunits of Saccharomyces cerevisiae DNA polymerase delta."
    Gerik K.J., Li X., Pautz A., Burgers P.M.
    J. Biol. Chem. 273:19747-19755(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "Structure of DNA polymerase delta from Saccharomyces cerevisiae."
    Johansson E., Majka J., Burgers P.M.
    J. Biol. Chem. 276:43824-43828(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPOSITION OF THE DNA POLYMERASE DELTA COMPLEX.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-223 AND SER-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDPOD3_YEAST
AccessioniPrimary (citable) accession number: P47110
Secondary accession number(s): D6VWL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 6, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2410 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: 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.