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Description:
DNA polymerase epsilon subunit B (EC 2.7.7.7) (DNA polymerase IIsubunit B).
Molecular weight: 78340
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
nucleotide-excision repair (and GO:0045001, a synonym)( GO:0006289 ) mismatch repair( GO:0006298 )
Important dates:
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
10-JAN-2006, sequence version 3.
07-MAR-2006, entry version 50.
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 DPB2_YEAST:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | M61710 | AAA34576.1 | ALT_INIT |
| EMBL | U25842 | AAB68109.1 | ALT_INIT |
| PIR | S59833 | S59833. | |
| IntAct | P24482 | -.1 | |
| GermOnline | 144440 | -.1 | |
| Ensembl | YPR175W | Saccharomyces cerevisiae.1 | |
| GenomeReviews | U00094_GR | YPR175W.1 | |
| SGD | S000006379 | DPB2. | |
| BioCyc | SCER-S28-01:SCER-S28-01-006328-MONOMER | -.1 | |
| LinkHub | P24482 | -.1 | |
| GO | GO:0005737 | C:cytoplasm | IDA. |
| GO | GO:0008622 | C:epsilon DNA polymerase complex | IDA. |
| GO | GO:0005634 | C:nucleus | IDA. |
| GO | GO:0005657 | C:replication fork | TAS. |
| GO | GO:0003893 | F:epsilon DNA polymerase activity | TAS. |
| 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. |
Keywords:
Cell cycle; Complete proteome; Direct protein sequencing; DNA replication; DNA-binding; DNA-directed DNA polymerase; Nuclear protein; Nucleotidyltransferase; Phosphorylation; Transferase.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=YHA8;
RX MEDLINE=91271241; PubMed=2052544;
RA Araki H., Hamatake R.K., Johnston L.H., Sugino A.;
RT "DPB2, the gene encoding DNA polymerase II subunit B, is required for
RT chromosome replication in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4601-4605(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S288c / AB972;
RX MEDLINE=97313271; PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
RA Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
RA Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
RA Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
RA Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
RA Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
RA Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
RA Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
RA Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
RA Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
RA Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
RA Zollner A., Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP PROTEIN SEQUENCE OF 132-144 AND 606-622, PHOSPHORYLATION SITE SER-141
RP AND SER-613, AND MASS SPECTROMETRY.
RX PubMed=14747467; DOI=10.1074/jbc.M313289200;
RA Kesti T., McDonald W.H., Yates J.R. III, Wittenberg C.;
RT "Cell cycle-dependent phosphorylation of the DNA polymerase epsilon
RT subunit, Dpb2, by the Cdc28 cyclin-dependent protein kinase.";
RL J. Biol. Chem. 279:14245-14255(2004).
RN [4]
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 [5]
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 [6]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX MEDLINE=22633889; PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [7]
RP SUBCELLULAR LOCATION.
RX MEDLINE=22923954; PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
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 1 689 DNA polymerase epsilon subunit B.
/FTId=PRO_0000071573.
MOD_RES 141 141 Phosphoserine (by CDC28).
MOD_RES 613 613 Phosphoserine.
CONFLICT 458 458 F -> Y (in Ref. 1).
CONFLICT 521 521 K -> R (in Ref. 1).
CONFLICT 565 565 V -> F (in Ref. 1).
CONFLICT 584 584 E -> Q (in Ref. 1).
CONFLICT 644 644 T -> I (in Ref. 1).
Comments:
-!- FUNCTION: DNA polymerase II participates in chromosomal DNA
replication. DPB2 is essential for cell growth. May have a role in
DNA synthesis.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1).
-!- SUBUNIT: Heterotetramer. Consists of four subunits: POL2, DPB2,
DPB3 and DPB4.
-!- SUBCELLULAR LOCATION: Nuclear and cytoplasmic.
-!- PTM: Phosphorylated in a cell cycle dependent manner during late
G1 phase. Phosphorylation may facilitate the interaction with POL2
or the activity of DNA polymerase II. Phosphorylation is
independent of DNA replication but dependent upon CDC28 in vivo.
Both Ser-141 and Ser-613 are phosphorylated in vivo, but in vitro
only Ser-141 is phosphorylated by CDC28.
-!- MISCELLANEOUS: Present with 3110 +/- 251 molecules/cell.
-!- 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 epsilon subunit B
family.
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Sequence length: 689
MFGSGNVLPV KIQPPLLRPL AYRVLSRKYG LSIKSDGLSA LAEFVGTNIG ANWRQGPATI
KFLEQFAAVW KQQERGLFID QSGVKEVIQE MKEREKVEWS HEHPIQHEEN ILGRTDDDEN
NSDDEMPIAA DSSLQNVSLS SPMRQPTERD EYKQPFKPES SKALDWRDYF KVINASQQQR
FSYNPHKMQF IFVPNKKQNG LGGIAGFLPD IEDKVQMFLT RYYLTNDRVM RNENFQNSDM
FNPLSSMVSL QNELSNTNRQ QQSSSMSITP IKNLLGRDAQ NFLLLGLLNK NFKGNWSLED
PSGSVEIDIS QTIPTQGHYY VPGCMVLVEG IYYSVGNKFH VTSMTLPPGE RREITLETIG
NLDLLGIHGI SNNNFIARLD KDLKIRLHLL EKELTDHKFV ILGANLFLDD LKIMTALSKI
LQKLNDDPPT LLIWQGSFTS VPVFASMSSR NISSSTQFKN NFDALATLLS RFDNLTENTT
MIFIPGPNDL WGSMVSLGAS GTLPQDPIPS AFTKKINKVC KNVVWSSNPT RIAYLSQEIV
IFRDDLSGRF KRHRLEFPFN ESEDVYTEND NMMSKDTDIV PIDELVKEPD QLPQKVQETR
KLVKTILDQG HLSPFLDSLR PISWDLDHTL TLCPIPSTMV LCDTTSAQFD LTYNGCKVIN
PGSFIHNRRA RYMEYVPSSK KTIQEEIYI