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Pol epsilon

Protein FULL name:

Catalytic subunit of DNA polymerase (II) epsilon, a chromosomal DNA replication polymerase that exhibits processivity and proofreading exonuclease activity; also involved in DNA synthesis during DNA repair; interacts extensively with Mrc1p


Protein SHORT name:

DNA polymerase (II) epsilon, Pol2p, DUN2


Pol epsilon (Saccharomyces cerevisiae) is product of expression of POL2 gene.


Pol epsilon is involved in:

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


Keywords:



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.

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

SUBUNIT: DNA polymerase epsilon is a heterotetramer consisting of POL2, DPB2, DPB3 and DPB4.

SUBCELLULAR LOCATION: Nucleus.

DOMAIN: The DNA polymerase activity domain resides in the N- terminal half of the protein, while the C-terminus is necessary for complexing subunits B and C.

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

MISCELLANEOUS: Present with 1970 molecules/cell in log phase SD medium.

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


NCBI GenPept GI number(s): 6324067
1045247
Species: Saccharomyces cerevisiae

Links to other databases:

Database ID Link
Uniprot P21951 P21951
PFAM: - P21951 (Link - using uniprot id)
InterPro: - P21951 (Link - using uniprot id)
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MMFGKKKNNGGSSTARYSAGNKYNTLSNNYALSAQQLLNASKIDDIDSMM
GFERYVPPQYNGRFDAKDIDQIPGRVGWLTNMHATLVSQETLSSGSNGGG
NSNDGERVTTNQGISGVDFYFLDEEGGSFKSTVVYDPYFFIACNDESRVN
DVEELVKKYLESCLKSLQIIRKEDLTMDNHLLGLQKTLIKLSFVNSNQLF
EARKLLRPILQDNANNNVQRNIYNVAANGSEKVDAKHLIEDIREYDVPYH
VRVSIDKDIRVGKWYKVTQQGFIEDTRKIAFADPVVMAFDIETTKPPLKF
PDSAVDQIMMISYMIDGEGFLITNREIISEDIEDFEYTPKPEYPGFFTIF
NENDEVALLQRFFEHIRDVRPTVISTFNGDFFDWPFIHNRSKIHGLDMFD
EIGFAPDAEGEYKSSYCSHMDCFRWVKRDSYLPQGSQGLKAVTQSKLGYN
PIELDPELMTPYAFEKPQHLSEYSVSDAVATYYLYMKYVHPFIFSLCTII
PLNPDETLRKGTGTLCEMLLMVQAYQHNILLPNKHTDPIERFYDGHLLES
ETYVGGHVESLEAGVFRSDLKNEFKIDPSAIDELLQELPEALKFSVEVEN
KSSVDKVTNFEEIKNQITQKLLELKENNIRNELPLIYHVDVASMYPNIMT
TNRLQPDSIKAERDCASCDFNRPGKTCARKLKWAWRGEFFPSKMDEYNMI
KRALQNETFPNKNKFSKKKVLTFDELSYADQVIHIKKRLTEYSRKVYHRV
KVSEIVEREAIVCQRENPFYVDTVKSFRDRRYEFKGLAKTWKGNLSKIDP
SDKHARDEAKKMIVLYDSLQLAHKVILNSFYGYVMRKGSRWYSMEMAGIT
CLTGATIIQMARALVERVGRPLELDTDGIWCILPKSFPETYFFTLENGKK
LYLSYPCSMLNYRVHQKFTNHQYQELKDPLNYIYETHSENTIFFEVDGPY
KAMILPSSKEEGKGIKKRYAVFNEDGSLAELKGFELKRRGELQLIKNFQS
DIFKVFLEGDTLEGCYSAVASVCNRWLDVLDSHGLMLEDEDLVSLICENR
SMSKTLKEYEGQKSTSITTARRLGDFLGEDMVKDKGLQCKYIISSKPFNA
PVTERAIPVAIFSADIPIKRSFLRRWTLDPSLEDLDIRTIIDWGYYRERL
GSAIQKIITIPAALQGVSNPVPRVEHPDWLKRKIATKEDKFKQTSLTKFF
SKTKNVPTMGKIKDIEDLFEPTVEEDNAKIKIARTTKKKAVSKRKRNQLT
NEEDPLVLPSEIPSMDEDYVGWLNYQKIKWKIQARDRKRRDQLFGNTNSS
RERSALGSMIRKQAESYANSTWEVLQYKDSGEPGVLEVFVTINGKVQNIT
FHIPKTIYMKFKSQTMPLQKIKNCLIEKSSASLPNNPKTSNPAGGQLFKI
TLPESVFLEEKENCTSIFNDENVLGVFEGTITPHQRAIMDLGASVTFRSK
AMGALGKGIQQGFEMKDLSMAENERYLSGFSMDIGYLLHFPTSIGYEFFS
LFKSWGDTITILVLKPSNQAQEINASSLGQIYKQMFEKKKGKIETYSYLV
DIKEDINFEFVYFTDISKLYRRLSQETTKLKEERGLQFLLLLQSPFITKL
LGTIRLLNQMPIVKLSLNEVLLPQLNWQPTLLKKLVNHVLSSGSWISHLI
KLSQYSNIPICNLRLDSMDYIIDVLYARKLKKENIVLWWNEKAPLPDHGG
IQNDFDLNTSWIMNDSEFPKINNSGVYDNVVLDVGVDNLTVNTILTSALI
NDAEGSDLVNNNMGIDDKDAVINSPSEFVHDAFSNDALNVLRGMLKEWWD
EALKENSTADLLVNSLASWVQNPNAKLFDGLLRYHVHNLTKKALLQLVNE
FSALGSTIVYADRNQILIKTNKYSPENCYAYSQYMMKAVRTNPMFSYLDL
NIKRYWDLLIWMDKFNFSGLACIEIEEKENQDYTAVSQWQLKKFLSPIYQ
PEFEDWMMIILDSMLKTKQSYLKLNSGTQRPTQIVNVKKQDKEDSVENSL
NGFSHLFSKPLMKRVKKLFKNQQEFILDPQYEADYVIPVLPGSHLNVKNP
LLELVKSLCHVMLLSKSTILEIRTLRKELLKIFELREFAKVAEFKDPSLS
LVVPDFLCEYCFFISDIDFCKAAPESIFSCVRCHKAFNQVLLQEHLIQKL
RSDIESYLIQDLRCSRCHKVKRDYMSAHCPCAGAWEGTLPRESIVQKLNV
FKQVAKYYGFDILLSCIADLTI

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

Title Authors Journal
A third essential DNA polymerase in S. cerevisiae. Morrison A, Araki H, Clark AB, Hamatake RK, Sugino A Cell Sept. 21, 1990
DNA polymerase II, the probable homolog of mammalian DNA polymerase epsilon, replicates chromosomal DNA in the yeast Saccharomyces cerevisiae. Araki H, Ropp PA, Johnson AL, Johnston LH, Morrison A, Sugino A EMBO J Jan. 1, 1992
The sequence of a 24,152 bp segment from the left arm of chromosome XIV from Saccharomyces cerevisiae between the BNI1 and the POL2 genes. Sen-Gupta M, Lyck R, Fleig U, Niedenthal RK, Hegemann JH Yeast April 1, 1996
The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications. Philippsen P, Kleine K, Pohlmann R, Dusterhoft A, Hamberg K, Hegemann JH, Obermaier B, Urrestarazu LA, Aert R, Albermann K, Altmann R, Andre B, Baladron V, Ballesta JP, Becam AM, Beinhauer J, Boskovic J, Buitrago MJ, Bussereau F, Coster F, Crouzet M, D'Angelo M, Dal Pero F, De Antoni A, Hani J, et al. Nature May 1, 1997
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 Oct. 15, 2000
Fidelity of DNA polymerase epsilon holoenzyme from budding yeast Saccharomyces cerevisiae. Shimizu K, Hashimoto K, Kirchner JM, Nakai W, Nishikawa H, Resnick MA, Sugino A J Biol Chem Oct. 4, 2002
The quaternary structure of DNA polymerase epsilon from Saccharomyces cerevisiae. Chilkova O, Jonsson BH, Johansson E J Biol Chem April 18, 2003
Global analysis of protein expression in yeast. Ghaemmaghami S, Huh WK, Bower K, Howson RW, Belle A, Dephoure N, O'Shea EK, Weissman JS Nature Oct. 16, 2003
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


Last modification of this entry: Oct. 19, 2010.

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