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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
Keywords:
- mismatch repair (MMR)
- transcription-coupled repair NER (TCR-NER)
- nucleotide excision repair (NER)
- base excision repair (BER)
- long path BER (LP-BER)
- homologous recombination repair (HRR)
- global genome repair NER (GGR-NER)
- DNA polymerase
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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