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Pol3p

Protein FULL name:

Catalytic subunit of DNA polymerase delta; required for chromosomal DNA replication during mitosis and meiosis, intragenic recombination, repair of double strand DNA breaks, and DNA replication during nucleotide excision repair (NER)


Protein SHORT name:

POL3, CDC2, HPR6, TEX1


Pol3p (Saccharomyces cerevisiae) is product of expression of POL3 gene.


Pol3p is involved in:

MMR in Saccharomyces cerevisiae BER in Saccharomyces cerevisiae HRR in Saccharomyces cerevisiae NER in Saccharomyces cerevisiae




FUNCTION: 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. POL3 contains the polymerase active site and most likely the active site for the 3'- 5' exonuclease activity.

CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

SUBUNIT: DNA polymerase delta is a heterotrimer of POL3, POL32 and HYS2.

INTERACTION: P46957:HYS2; NbExp=2; IntAct=EBI-6134, EBI-6080;

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.

SIMILARITY: Belongs to the DNA polymerase type-B family.


NCBI GenPept GI number(s): 6320101
1199547
Species: Saccharomyces cerevisiae

Links to other databases:

Database ID Link
Uniprot P15436 P15436
PFAM: - P15436 (Link - using uniprot id)
InterPro: - P15436 (Link - using uniprot id)
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MSEKRSLPMVDVKIDDEDTPQLEKKIKRQSIDHGVGSEPVSTIEIIPSDS
FRKYNSQGFKAKDTDLMGTQLESTFEQDVSQMEHDMADQEEHDLSSFERK
KLPTDFDPSLYDISFQQIDAEQSVLNGIKDENTSTVVRFFGVTSEGHSVL
CNVTGFKNYLYVPAPNSSDANDQEQINKFVHYLNETFDHAIDSIEVVSKQ
SIWGYSGDTKLPFWKIYVTYPHMVNKLRTAFERGHLSFNSWFSNGTTTYD
NIAYTLRLMVDCGIVGMSWITLPKGKYSMIEPNNRVSSCQLEVSINYRNL
IAHPAEGDWSHTAPLRIMSFDIECAGRIGVFPEPEYDPVIQIANVVSIAG
AKKPFIRNVFTLNTCSPITGSMIFSHATEEEMLSNWRNFIIKVDPDVIIG
YNTTNFDIPYLLNRAKALKVNDFPYFGRLKTVKQEIKESVFSSKAYGTRE
TKNVNIDGRLQLDLLQFIQREYKLRSYTLNAVSAHFLGEQKEDVHYSIIS
DLQNGDSETRRRLAVYCLKDAYLPLRLMEKLMALVNYTEMARVTGVPFSY
LLARGQQIKVVSQLFRKCLEIDTVIPNMQSQASDDQYEGATVIEPIRGYY
DVPIATLDFNSLYPSIMMAHNLCYTTLCNKATVERLNLKIDEDYVITPNG
DYFVTTKRRRGILPIILDELISARKRAKKDLRDEKDPFKRDVLNGRQLAL
KISANSVYGFTGATVGKLPCLAISSSVTAYGRTMILKTKTAVQEKYCIKN
GYKHDAVVVYGDTDSVMVKFGTTDLKEAMDLGTEAAKYVSTLFKHPINLE
FEKAYFPYLLINKKRYAGLFWTNPDKFDKLDQKGLASVRRDSCSLVSIVM
NKVLKKILIERNVDGALAFVRETINDILHNRVDISKLIISKTLAPNYTNP
QPHAVLAERMKRREGVGPNVGDRVDYVIIGGNDKLYNRAEDPLFVLENNI
QVDSRYYLTNQLQNPIISIVAPIIGDKQANGMFVVKSIKINTGSQKGGLM
SFIKKVEACKSCKGPLRKGEGPLCSNCLARSGELYIKALYDVRDLEEKYS
RLWTQCQRCAGNLHSEVLCSNKNCDIFYMRVKVKKELQEKVEQLSKW

Pol3p (Saccharomyces cerevisiae) is able to recognize following damages:
Pol3p (Saccharomyces cerevisiae) belongs to following protein families:
References:

Title Authors Journal
Structure and function of the Saccharomyces cerevisiae CDC2 gene encoding the large subunit of DNA polymerase III. Boulet A, Simon M, Faye G, Bauer GA, Burgers PM EMBO J June 1, 1989
The 3' to 5' exonuclease activity located in the DNA polymerase delta subunit of Saccharomyces cerevisiae is required for accurate replication. Simon M, Giot L, Faye G EMBO J Aug. 1, 1991
Nucleotide sequence of the POL3 gene encoding DNA polymerase III (delta) of Saccharomyces cerevisiae. Morrison A, Sugino A Nucleic Acids Res Feb. 25, 1992
The sequence of a 20.3 kb DNA fragment from the left arm of Saccharomyces cerevisiae chromosome IV contains the KIN28, MSS2, PHO2, POL3 and DUN1 genes, and six new open reading frames. Saiz JE, Buitrago MJ, Garcia R, Revuelta JL, Del Rey F Yeast Sept. 1, 1996
The nucleotide sequence of Saccharomyces cerevisiae chromosome IV. Jacq C, Alt-Morbe J, Andre B, Arnold W, Bahr A, Ballesta JP, Bargues M, Baron L, Becker A, Biteau N, Blocker H, Blugeon C, Boskovic J, Brandt P, Bruckner M, Buitrago MJ, Coster F, Delaveau T, del Rey F, Dujon B, Eide LG, Garcia-Cantalejo JM, Goffeau A, Gomez-Peris A, Zaccaria P, et al. Nature May 1, 1997
Structure of DNA polymerase delta from Saccharomyces cerevisiae. Johansson E, Majka J, Burgers PM J Biol Chem Nov. 23, 2001
Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry. Chi A, Huttenhower C, Geer LY, Coon JJ, Syka JE, Bai DL, Shabanowitz J, Burke DJ, Troyanskaya OG, Hunt DF Proc Natl Acad Sci U S A Jan. 13, 2007
Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae. Li X, Gerber SA, Rudner AD, Beausoleil SA, Haas W, Villen J, Elias JE, Gygi SP J Proteome Res March 1, 2007
Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases. Smolka MB, Albuquerque CP, Chen SH, Zhou H Proc Natl Acad Sci U S A June 19, 2007
A multidimensional chromatography technology for in-depth phosphoproteome analysis. Albuquerque CP, Smolka MB, Payne SH, Bafna V, Eng J, Zhou H Mol Cell Proteomics July 1, 2008


Last modification of this entry: Oct. 6, 2010.

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