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Description:
DNA polymerase epsilon, catalytic subunit A (EC 2.7.7.7) (DNApolymerase II subunit A).
Molecular weight: 2556
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair synthesis( GO:0000731 ) nucleotide-excision repair (and GO:0045001, a synonym)( GO:0006289 ) mismatch repair( GO:0006298 )
Important dates:
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-AUG-1991, sequence version 1.
07-MAR-2006, entry version 60.
Phylogenetic order:
Eukaryota Fungi Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein DPOE_YEAST:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | M60416 | AAA88711.1 | - |
| EMBL | X92494 | CAA63235.1 | - |
| EMBL | Z71538 | CAA96169.1 | - |
| PIR | A36028 | A36028. | |
| IntAct | P21951 | -.1 | |
| GermOnline | 143268 | -.1 | |
| Ensembl | YNL262W | Saccharomyces cerevisiae.1 | |
| GenomeReviews | Y13139_GR | YNL262W.1 | |
| SGD | S000005206 | POL2. | |
| BioCyc | SCER-S28-01:SCER-S28-01-005119-MONOMER | -.1 | |
| LinkHub | P21951 | -.1 | |
| GO | GO:0008622 | C:epsilon DNA polymerase complex | IDA. |
| GO | GO:0005657 | C:replication fork | IDA. |
| GO | GO:0003893 | F:epsilon DNA polymerase activity | TAS. |
| GO | GO:0006348 | P:chromatin silencing at telomere | IMP. |
| GO | GO:0000731 | P:DNA synthesis during DNA repair | IMP. |
| GO | GO:0006273 | P:lagging strand elongation | TAS. |
| GO | GO:0006272 | P:leading strand elongation | TAS. |
| GO | GO:0006298 | P:mismatch repair | TAS. |
| GO | GO:0006289 | P:nucleotide-excision repair | TAS. |
| InterPro | IPR006172 | DNA_pol_B. | |
| InterPro | IPR006133 | DNA_pol_B_exo. | |
| InterPro | IPR006134 | DNA_pol_B_region. | |
| InterPro | IPR012337 | RNaseH_fold. | |
| Pfam | PF00136 | DNA_pol_B | 1. |
| Pfam | PF03104 | DNA_pol_B_exo | 1. |
| SMART | SM00486 | POLBc | 1. |
| PROSITE | PS00116 | DNA_POLYMERASE_B | FALSE_NEG. |
Keywords:
Complete proteome; Direct protein sequencing; DNA replication; DNA-binding; DNA-directed DNA polymerase; Metal-binding; Nuclear protein; Nucleotidyltransferase; Transferase; Zinc; Zinc-finger.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1214-1221.
RX MEDLINE=90381771; PubMed=2169349; DOI=10.1016/0092-8674(90)90391-Q;
RA Morrison A., Araki H., Clark A.B., Hamatake R.K., Sugino A.;
RT "A third essential DNA polymerase in S. cerevisiae.";
RL Cell 62:1143-1151(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX MEDLINE=97313269; PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
RA Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
RA Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
RA Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
RA Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
RA Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
RA Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
RA Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
RA Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
RA Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
RA Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
RA Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
RA Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
RA Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
RT and its evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2221.
RC STRAIN=S288c / FY1679;
RX MEDLINE=96310631; PubMed=8740425;
RX DOI=10.1002/(SICI)1097-0061(199604)12:5<505::AID-YEA932>3.0.CO;2-F;
RA Sen-Gupta M., Lyck R., Fleig U., Niedenthal R.K., Hegemann J.H.;
RT "The sequence of a 24,152 bp segment from the left arm of chromosome
RT XIV from Saccharomyces cerevisiae between the BNI1 and the POL2
RT genes.";
RL Yeast 12:505-514(1996).
RN [4]
RP MUTAGENESIS OF MET-644 AND PRO-710.
RX MEDLINE=92164663; PubMed=1537345;
RA Araki H., Ropp P.A., Johnson A.L., Johnston L.H., Morrison A.,
RA Sugino A.;
RT "DNA polymerase II, the probable homolog of mammalian DNA polymerase
RT epsilon, replicates chromosomal DNA in the yeast Saccharomyces
RT cerevisiae.";
RL EMBO J. 11:733-740(1992).
RN [5]
RP SUBUNIT.
RX MEDLINE=20482200; PubMed=11024162; DOI=10.1093/nar/28.20.3846;
RA Ohya T., Maki S., Kawasaki Y., Sugino A.;
RT "Structure and function of the fourth subunit (Dpb4p) of DNA
RT polymerase epsilon in Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 28:3846-3852(2000).
RN [6]
RP SUBUNIT.
RX PubMed=12571237; DOI=10.1074/jbc.M211818200;
RA Chilkova O., Jonsson B.-H., Johansson E.;
RT "The quaternary structure of DNA polymerase epsilon from Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 278:14082-14086(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION.
RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA Dephoure N., O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
Feature:
CHAIN 1 2222 DNA polymerase epsilon, catalytic subunit
A.
/FTId=PRO_0000046467.
ZN_FING 2108 2181 C4-type (Potential).
MUTAGEN 644 644 M->I: In POL2-9; temperature-sensitive
mutant.
MUTAGEN 710 710 P->S: In POL2-18; temperature-sensitive
mutant.
Comments:
-!- FUNCTION: DNA polymerase II participates in chromosomal DNA
replication.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1).
-!- SUBUNIT: Heterotetramer. Consists of 4 subunits: POL2, DPB2, DPB3
and DPB4 (By similarity).
-!- 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.
-!- SIMILARITY: Belongs to the DNA polymerase type-B family.
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Sequence length: 2222
MMFGKKKNNG GSSTARYSAG NKYNTLSNNY ALSAQQLLNA SKIDDIDSMM GFERYVPPQY
NGRFDAKDID QIPGRVGWLT NMHATLVSQE TLSSGSNGGG NSNDGERVTT NQGISGVDFY
FLDEEGGSFK STVVYDPYFF IACNDESRVN DVEELVKKYL ESCLKSLQII RKEDLTMDNH
LLGLQKTLIK LSFVNSNQLF EARKLLRPIL QDNANNNVQR NIYNVAANGS EKVDAKHLIE
DIREYDVPYH VRVSIDKDIR VGKWYKVTQQ GFIEDTRKIA FADPVVMAFD IETTKPPLKF
PDSAVDQIMM ISYMIDGEGF LITNREIISE DIEDFEYTPK PEYPGFFTIF NENDEVALLQ
RFFEHIRDVR PTVISTFNGD FFDWPFIHNR SKIHGLDMFD EIGFAPDAEG EYKSSYCSHM
DCFRWVKRDS YLPQGSQGLK AVTQSKLGYN PIELDPELMT PYAFEKPQHL SEYSVSDAVA
TYYLYMKYVH PFIFSLCTII PLNPDETLRK GTGTLCEMLL MVQAYQHNIL LPNKHTDPIE
RFYDGHLLES ETYVGGHVES LEAGVFRSDL KNEFKIDPSA IDELLQELPE ALKFSVEVEN
KSSVDKVTNF EEIKNQITQK LLELKENNIR NELPLIYHVD VASMYPNIMT TNRLQPDSIK
AERDCASCDF NRPGKTCARK LKWAWRGEFF PSKMDEYNMI KRALQNETFP NKNKFSKKKV
LTFDELSYAD QVIHIKKRLT EYSRKVYHRV KVSEIVEREA IVCQRENPFY VDTVKSFRDR
RYEFKGLAKT WKGNLSKIDP SDKHARDEAK KMIVLYDSLQ LAHKVILNSF YGYVMRKGSR
WYSMEMAGIT CLTGATIIQM ARALVERVGR PLELDTDGIW CILPKSFPET YFFTLENGKK
LYLSYPCSML NYRVHQKFTN HQYQELKDPL NYIYETHSEN TIFFEVDGPY KAMILPSSKE
EGKGIKKRYA VFNEDGSLAE LKGFELKRRG ELQLIKNFQS DIFKVFLEGD TLEGCYSAVA
SVCNRWLDVL DSHGLMLEDE DLVSLICENR SMSKTLKEYE GQKSTSITTA RRLGDFLGED
MVKDKGLQCK YIISSKPFNA PVTERAIPVA IFSADIPIKR SFLRRWTLDP SLEDLDIRTI
IDWGYYRERL GSAIQKIITI PAALQGVSNP VPRVEHPDWL KRKIATKEDK FKQTSLTKFF
SKTKNVPTMG KIKDIEDLFE PTVEEDNAKI KIARTTKKKA VSKRKRNQLT NEEDPLVLPS
EIPSMDEDYV GWLNYQKIKW KIQARDRKRR DQLFGNTNSS RERSALGSMI RKQAESYANS
TWEVLQYKDS GEPGVLEVFV TINGKVQNIT FHIPKTIYMK FKSQTMPLQK IKNCLIEKSS
ASLPNNPKTS NPAGGQLFKI TLPESVFLEE KENCTSIFND ENVLGVFEGT ITPHQRAIMD
LGASVTFRSK AMGALGKGIQ QGFEMKDLSM AENERYLSGF SMDIGYLLHF PTSIGYEFFS
LFKSWGDTIT ILVLKPSNQA QEINASSLGQ IYKQMFEKKK GKIETYSYLV DIKEDINFEF
VYFTDISKLY RRLSQETTKL KEERGLQFLL LLQSPFITKL LGTIRLLNQM PIVKLSLNEV
LLPQLNWQPT LLKKLVNHVL SSGSWISHLI KLSQYSNIPI CNLRLDSMDY IIDVLYARKL
KKENIVLWWN EKAPLPDHGG IQNDFDLNTS WIMNDSEFPK INNSGVYDNV VLDVGVDNLT
VNTILTSALI NDAEGSDLVN NNMGIDDKDA VINSPSEFVH DAFSNDALNV LRGMLKEWWD
EALKENSTAD LLVNSLASWV QNPNAKLFDG LLRYHVHNLT KKALLQLVNE FSALGSTIVY
ADRNQILIKT NKYSPENCYA YSQYMMKAVR TNPMFSYLDL NIKRYWDLLI WMDKFNFSGL
ACIEIEEKEN QDYTAVSQWQ LKKFLSPIYQ PEFEDWMMII LDSMLKTKQS YLKLNSGTQR
PTQIVNVKKQ DKEDSVENSL NGFSHLFSKP LMKRVKKLFK NQQEFILDPQ YEADYVIPVL
PGSHLNVKNP LLELVKSLCH VMLLSKSTIL EIRTLRKELL KIFELREFAK VAEFKDPSLS
LVVPDFLCEY CFFISDIDFC KAAPESIFSC VRCHKAFNQV LLQEHLIQKL RSDIESYLIQ
DLRCSRCHKV KRDYMSAHCP CAGAWEGTLP RESIVQKLNV FKQVAKYYGF DILLSCIADL
TI