Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

DNA polymerase eta (EC 2.7.7.7) (Radiation-sensitive protein 30)

 POLH_YEAST              Reviewed;         632 AA.
Q04049; D6VT49;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
27-SEP-2017, entry version 132.
RecName: Full=DNA polymerase eta;
EC=2.7.7.7;
AltName: Full=Radiation-sensitive protein 30;
Name=RAD30; Synonyms=DBH1; OrderedLocusNames=YDR419W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
FUNCTION, AND INDUCTION.
PubMed=9409821;
McDonald J.P., Levine A.S., Woodgate R.;
"The Saccharomyces cerevisiae RAD30 gene, a homologue of Escherichia
coli dinB and umuC, is DNA damage inducible and functions in a novel
error-free postreplication repair mechanism.";
Genetics 147:1557-1568(1997).
[4]
FUNCTION, AND MUTAGENESIS OF 155-ASP-GLU-156.
PubMed=10347143; DOI=10.1074/jbc.274.23.15975;
Johnson R.E., Prakash S., Prakash L.;
"Requirement of DNA polymerase activity of yeast Rad30 protein for its
biological function.";
J. Biol. Chem. 274:15975-15977(1999).
[5]
FUNCTION.
PubMed=10601233; DOI=10.1074/jbc.274.52.36835;
Washington M.T., Johnson R.E., Prakash S., Prakash L.;
"Fidelity and processivity of Saccharomyces cerevisiae DNA polymerase
eta.";
J. Biol. Chem. 274:36835-36838(1999).
[6]
FUNCTION.
PubMed=9974380; DOI=10.1126/science.283.5404.1001;
Johnson R.E., Prakash S., Prakash L.;
"Efficient bypass of a thymine-thymine dimer by yeast DNA polymerase,
Poleta.";
Science 283:1001-1004(1999).
[7]
FUNCTION.
PubMed=10924462;
Xiao W., Chow B.L., Broomfield S., Hanna M.;
"The Saccharomyces cerevisiae RAD6 group is composed of an error-prone
and two error-free postreplication repair pathways.";
Genetics 155:1633-1641(2000).
[8]
FUNCTION.
PubMed=10713149; DOI=10.1074/jbc.275.11.8233;
Yuan F., Zhang Y., Rajpal D.K., Wu X., Guo D., Wang M., Taylor J.-S.,
Wang Z.;
"Specificity of DNA lesion bypass by the yeast DNA polymerase eta.";
J. Biol. Chem. 275:8233-8239(2000).
[9]
FUNCTION.
PubMed=11027270; DOI=10.1128/MCB.20.21.8001-8007.2000;
Haracska L., Prakash S., Prakash L.;
"Replication past O(6)-methylguanine by yeast and human DNA polymerase
eta.";
Mol. Cell. Biol. 20:8001-8007(2000).
[10]
FUNCTION.
PubMed=10932195; DOI=10.1038/78169;
Haracska L., Yu S.-L., Johnson R.E., Prakash L., Prakash S.;
"Efficient and accurate replication in the presence of 7,8-dihydro-8-
oxoguanine by DNA polymerase eta.";
Nat. Genet. 25:458-461(2000).
[11]
FUNCTION.
PubMed=10725365; DOI=10.1073/pnas.97.7.3094;
Washington M.T., Johnson R.E., Prakash S., Prakash L.;
"Accuracy of thymine-thymine dimer bypass by Saccharomyces cerevisiae
DNA polymerase eta.";
Proc. Natl. Acad. Sci. U.S.A. 97:3094-3099(2000).
[12]
FUNCTION.
PubMed=11062246; DOI=10.1074/jbc.M007867200;
Minko I.G., Washington M.T., Prakash L., Prakash S., Lloyd R.S.;
"Translesion DNA synthesis by yeast DNA polymerase eta on templates
containing N2-guanine adducts of 1,3-butadiene metabolites.";
J. Biol. Chem. 276:2517-2522(2001).
[13]
FUNCTION, DOMAIN, INTERACTION WITH POL30, AND MUTAGENESIS OF
627-PHE-PHE-628.
PubMed=11545742; DOI=10.1016/S1097-2765(01)00319-7;
Haracska L., Kondratick C.M., Unk I., Prakash S., Prakash L.;
"Interaction with PCNA is essential for yeast DNA polymerase eta
function.";
Mol. Cell 8:407-415(2001).
[14]
FUNCTION.
PubMed=11113193; DOI=10.1128/MCB.21.1.185-188.2001;
Yu S.-L., Johnson R.E., Prakash S., Prakash L.;
"Requirement of DNA polymerase eta for error-free bypass of UV-induced
CC and TC photoproducts.";
Mol. Cell. Biol. 21:185-188(2001).
[15]
FUNCTION, DOMAIN, AND MUTAGENESIS OF ASP-30; GLU-39; ASP-155 AND
GLU-156.
PubMed=11238937; DOI=10.1128/MCB.21.6.2018-2025.2001;
Kondratick C.M., Washington M.T., Prakash S., Prakash L.;
"Acidic residues critical for the activity and biological function of
yeast DNA polymerase eta.";
Mol. Cell. Biol. 21:2018-2025(2001).
[16]
FUNCTION.
PubMed=11054429; DOI=10.1074/jbc.M009049200;
Washington M.T., Johnson R.E., Prakash S., Prakash L.;
"Mismatch extension ability of yeast and human DNA polymerase eta.";
J. Biol. Chem. 276:2263-2266(2001).
[17]
FUNCTION.
PubMed=12110599; DOI=10.1093/emboj/cdf363;
Bresson A., Fuchs R.P.;
"Lesion bypass in yeast cells: Pol eta participates in a multi-DNA
polymerase process.";
EMBO J. 21:3881-3887(2002).
[18]
FUNCTION.
PubMed=11861920; DOI=10.1093/nar/30.5.1262;
Zhang H., Siede W.;
"UV-induced T-->C transition at a TT photoproduct site is dependent on
Saccharomyces cerevisiae polymerase eta in vivo.";
Nucleic Acids Res. 30:1262-1267(2002).
[19]
FUNCTION.
PubMed=12899630; DOI=10.1021/bi0345687;
Sun L., Zhang K., Zhou L., Hohler P., Kool E.T., Yuan F., Wang Z.,
Taylor J.-S.;
"Yeast pol eta holds a cis-syn thymine dimer loosely in the active
site during elongation opposite the 3'-T of the dimer, but tightly
opposite the 5'-T.";
Biochemistry 42:9431-9437(2003).
[20]
FUNCTION, AND MUTAGENESIS OF TYR-64; ARG-67 AND LYS-279.
PubMed=12665597; DOI=10.1128/MCB.23.8.3008-3012.2003;
Johnson R.E., Trincao J., Aggarwal A.K., Prakash S., Prakash L.;
"Deoxynucleotide triphosphate binding mode conserved in Y family DNA
polymerases.";
Mol. Cell. Biol. 23:3008-3012(2003).
[21]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[22]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[23]
FUNCTION.
PubMed=12888515; DOI=10.1093/nar/gkg489;
Kozmin S.G., Pavlov Y.I., Kunkel T.A., Sage E.;
"Roles of Saccharomyces cerevisiae DNA polymerases Poleta and Polzeta
in response to irradiation by simulated sunlight.";
Nucleic Acids Res. 31:4541-4552(2003).
[24]
FUNCTION.
PubMed=12692307; DOI=10.1073/pnas.0837578100;
Washington M.T., Wolfle W.T., Spratt T.E., Prakash L., Prakash S.;
"Yeast DNA polymerase eta makes functional contacts with the DNA minor
groove only at the incoming nucleoside triphosphate.";
Proc. Natl. Acad. Sci. U.S.A. 100:5113-5118(2003).
[25]
FUNCTION.
PubMed=14527996; DOI=10.1073/pnas.2134223100;
Washington M.T., Prakash L., Prakash S.;
"Mechanism of nucleotide incorporation opposite a thymine-thymine
dimer by yeast DNA polymerase eta.";
Proc. Natl. Acad. Sci. U.S.A. 100:12093-12098(2003).
[26]
FUNCTION.
PubMed=15157108; DOI=10.1021/bi0497749;
Gu C., Wang Y.;
"LC-MS/MS identification and yeast polymerase eta bypass of a novel
gamma-irradiation-induced intrastrand cross-link lesion G[8-5]C.";
Biochemistry 43:6745-6750(2004).
[27]
FUNCTION.
PubMed=15544332; DOI=10.1021/bi0489558;
Hwang H., Taylor J.-S.;
"Role of base stacking and sequence context in the inhibition of yeast
DNA polymerase eta by pyrene nucleotide.";
Biochemistry 43:14612-14623(2004).
[28]
FUNCTION.
PubMed=15284331; DOI=10.1093/nar/gkh710;
Zhao B., Xie Z., Shen H., Wang Z.;
"Role of DNA polymerase eta in the bypass of abasic sites in yeast
cells.";
Nucleic Acids Res. 32:3984-3994(2004).
[29]
FUNCTION.
PubMed=15333698; DOI=10.1093/nar/gkh777;
McCulloch S.D., Kokoska R.J., Chilkova O., Welch C.M., Johansson E.,
Burgers P.M.J., Kunkel T.A.;
"Enzymatic switching for efficient and accurate translesion DNA
replication.";
Nucleic Acids Res. 32:4665-4675(2004).
[30]
FUNCTION, AND MUTAGENESIS OF PHE-34.
PubMed=15024063; DOI=10.1128/MCB.24.7.2734-2746.2004;
Niimi A., Limsirichaikul S., Yoshida S., Iwai S., Masutani C.,
Hanaoka F., Kool E.T., Nishiyama Y., Suzuki M.;
"Palm mutants in DNA polymerases alpha and eta alter DNA replication
fidelity and translesion activity.";
Mol. Cell. Biol. 24:2734-2746(2004).
[31]
FUNCTION.
PubMed=15779911; DOI=10.1021/bi048244+;
Hwang H., Taylor J.-S.;
"Evidence for Watson-Crick and not Hoogsteen or wobble base pairing in
the selection of nucleotides for insertion opposite pyrimidines and a
thymine dimer by yeast DNA pol eta.";
Biochemistry 44:4850-4860(2005).
[32]
INDUCTION.
PubMed=15725627; DOI=10.1016/j.dnarep.2004.12.001;
Michan C., Monje-Casas F., Pueyo C.;
"Transcript copy number of genes for DNA repair and translesion
synthesis in yeast: contribution of transcription rate and mRNA
stability to the steady-state level of each mRNA along with growth in
glucose-fermentative medium.";
DNA Repair 4:469-478(2005).
[33]
FUNCTION.
PubMed=16181813; DOI=10.1016/j.dnarep.2005.08.012;
Xie Z., Zhang Y., Guliaev A.B., Shen H., Hang B., Singer B., Wang Z.;
"The p-benzoquinone DNA adducts derived from benzene are highly
mutagenic.";
DNA Repair 4:1399-1409(2005).
[34]
FUNCTION.
PubMed=15520252; DOI=10.1534/genetics.104.034611;
Gibbs P.E.M., McDonald J.P., Woodgate R., Lawrence C.W.;
"The relative roles in vivo of Saccharomyces cerevisiae Pol eta, Pol
zeta, Rev1 protein and Pol32 in the bypass and mutation induction of
an abasic site, T-T (6-4) photoadduct and T-T cis-syn cyclobutane
dimer.";
Genetics 169:575-582(2005).
[35]
FUNCTION.
PubMed=16366567; DOI=10.1021/ja0549188;
Ober M., Mueller H., Pieck C., Gierlich J., Carell T.;
"Base pairing and replicative processing of the formamidopyrimidine-dG
DNA lesion.";
J. Am. Chem. Soc. 127:18143-18149(2005).
[36]
FUNCTION.
PubMed=15743815; DOI=10.1128/MCB.25.6.2169-2176.2005;
Carlson K.D., Washington M.T.;
"Mechanism of efficient and accurate nucleotide incorporation opposite
7,8-dihydro-8-oxoguanine by Saccharomyces cerevisiae DNA polymerase
eta.";
Mol. Cell. Biol. 25:2169-2176(2005).
[37]
FUNCTION.
PubMed=16866379; DOI=10.1021/bi0602009;
Vu B., Cannistraro V.J., Sun L., Taylor J.-S.;
"DNA synthesis past a 5-methylC-containing cis-syn-cyclobutane
pyrimidine dimer by yeast pol eta is highly nonmutagenic.";
Biochemistry 45:9327-9335(2006).
[38]
FUNCTION.
PubMed=16387871; DOI=10.1534/genetics.105.052480;
Abdulovic A.L., Jinks-Robertson S.;
"The in vivo characterization of translesion synthesis across UV-
induced lesions in Saccharomyces cerevisiae: insights into Pol
zeta- and Pol eta-dependent frameshift mutagenesis.";
Genetics 172:1487-1498(2006).
[39]
FUNCTION.
PubMed=16415180; DOI=10.1093/nar/gkj446;
Zhao B., Wang J., Geacintov N.E., Wang Z.;
"Poleta, Polzeta and Rev1 together are required for G to T
transversion mutations induced by the (+)- and (-)-trans-anti-BPDE-N2-
dG DNA adducts in yeast cells.";
Nucleic Acids Res. 34:417-425(2006).
[40]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-531.
PubMed=11545743; DOI=10.1016/S1097-2765(01)00306-9;
Trincao J., Johnson R.E., Escalante C.R., Prakash S., Prakash L.,
Aggarwal A.K.;
"Structure of the catalytic core of S. cerevisiae DNA polymerase eta:
implications for translesion DNA synthesis.";
Mol. Cell 8:417-426(2001).
-!- FUNCTION: DNA polymerase specifically involved in DNA repair.
Plays an important role in translesion synthesis, where the normal
high fidelity DNA polymerases cannot proceed and DNA synthesis
stalls. Plays an important role in the repair of UV-induced
pyrimidine dimers. Depending on the context, it inserts the
correct base, but causes frequent base transitions and
transversions. Efficiently incorporates nucleotides opposite to
other UV or oxidative DNA damages like O(6)-methylguanine, 7,8-
dihydro-8-oxoguanine, 2,6-diamino-4-hydroxy-5-formamidopyrimidine
of 2'-deoxyguanosine (FaPydG), or p-benzoquinone DNA adducts.
{ECO:0000269|PubMed:10347143, ECO:0000269|PubMed:10601233,
ECO:0000269|PubMed:10713149, ECO:0000269|PubMed:10725365,
ECO:0000269|PubMed:10924462, ECO:0000269|PubMed:10932195,
ECO:0000269|PubMed:11027270, ECO:0000269|PubMed:11054429,
ECO:0000269|PubMed:11062246, ECO:0000269|PubMed:11113193,
ECO:0000269|PubMed:11238937, ECO:0000269|PubMed:11545742,
ECO:0000269|PubMed:11861920, ECO:0000269|PubMed:12110599,
ECO:0000269|PubMed:12665597, ECO:0000269|PubMed:12692307,
ECO:0000269|PubMed:12888515, ECO:0000269|PubMed:12899630,
ECO:0000269|PubMed:14527996, ECO:0000269|PubMed:15024063,
ECO:0000269|PubMed:15157108, ECO:0000269|PubMed:15284331,
ECO:0000269|PubMed:15333698, ECO:0000269|PubMed:15520252,
ECO:0000269|PubMed:15544332, ECO:0000269|PubMed:15743815,
ECO:0000269|PubMed:15779911, ECO:0000269|PubMed:16181813,
ECO:0000269|PubMed:16366567, ECO:0000269|PubMed:16387871,
ECO:0000269|PubMed:16415180, ECO:0000269|PubMed:16866379,
ECO:0000269|PubMed:9409821, ECO:0000269|PubMed:9974380}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1).
-!- SUBUNIT: Interacts with POL30. This interaction is essential for
the polymerase eta function. {ECO:0000269|PubMed:11545742}.
-!- INTERACTION:
Q04739:GAL83; NbExp=2; IntAct=EBI-36214, EBI-7244;
P38828:LSM12; NbExp=2; IntAct=EBI-36214, EBI-24700;
P15873:POL30; NbExp=3; IntAct=EBI-36214, EBI-12993;
P06782:SNF1; NbExp=2; IntAct=EBI-36214, EBI-17516;
P12904:SNF4; NbExp=2; IntAct=EBI-36214, EBI-17537;
P39990:SNU13; NbExp=2; IntAct=EBI-36214, EBI-12032;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
-!- INDUCTION: By UV radiation and heat shock. The mRNA is stabilized
during stationary phase. {ECO:0000269|PubMed:15725627,
ECO:0000269|PubMed:9409821}.
-!- MISCELLANEOUS: Present with 1860 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the DNA polymerase type-Y family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U33007; AAB64856.1; -; Genomic_DNA.
EMBL; BK006938; DAA12259.1; -; Genomic_DNA.
PIR; S69702; S69702.
RefSeq; NP_010707.3; NM_001180727.3.
PDB; 1JIH; X-ray; 2.25 A; A/B=1-513.
PDB; 2R8J; X-ray; 3.10 A; A/B=1-531.
PDB; 2R8K; X-ray; 3.30 A; A/B=1-531.
PDB; 2WTF; X-ray; 2.50 A; A/B=1-513.
PDB; 2XGP; X-ray; 2.70 A; A/B=1-513.
PDB; 2XGQ; X-ray; 2.70 A; A/B=1-513.
PDB; 3MFH; X-ray; 2.00 A; A=1-513.
PDB; 3MFI; X-ray; 1.76 A; A=1-513.
PDB; 3OHA; X-ray; 2.00 A; A=1-513.
PDB; 3OHB; X-ray; 2.00 A; A=1-513.
PDBsum; 1JIH; -.
PDBsum; 2R8J; -.
PDBsum; 2R8K; -.
PDBsum; 2WTF; -.
PDBsum; 2XGP; -.
PDBsum; 2XGQ; -.
PDBsum; 3MFH; -.
PDBsum; 3MFI; -.
PDBsum; 3OHA; -.
PDBsum; 3OHB; -.
ProteinModelPortal; Q04049; -.
SMR; Q04049; -.
BioGrid; 32477; 135.
DIP; DIP-6500N; -.
IntAct; Q04049; 21.
MINT; MINT-708283; -.
STRING; 4932.YDR419W; -.
MaxQB; Q04049; -.
PRIDE; Q04049; -.
EnsemblFungi; YDR419W; YDR419W; YDR419W.
GeneID; 852028; -.
KEGG; sce:YDR419W; -.
EuPathDB; FungiDB:YDR419W; -.
SGD; S000002827; RAD30.
HOGENOM; HOG000065930; -.
InParanoid; Q04049; -.
KO; K03509; -.
OMA; FGEESIW; -.
OrthoDB; EOG092C18P5; -.
BioCyc; YEAST:G3O-29960-MONOMER; -.
EvolutionaryTrace; Q04049; -.
PRO; PR:Q04049; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005739; C:mitochondrion; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0005657; C:replication fork; IPI:SGD.
GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:SGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007059; P:chromosome segregation; IMP:SGD.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0070987; P:error-free translesion synthesis; IDA:SGD.
GO; GO:0042276; P:error-prone translesion synthesis; IDA:SGD.
GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD.
Gene3D; 3.30.1490.100; -; 1.
InterPro; IPR017061; DNA_pol_eta/kappa/iota/IV.
InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
InterPro; IPR001126; UmuC.
Pfam; PF00817; IMS; 1.
Pfam; PF11799; IMS_C; 1.
PIRSF; PIRSF036603; DPol_eta; 1.
SUPFAM; SSF100879; SSF100879; 1.
PROSITE; PS50173; UMUC; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; DNA damage; DNA repair;
DNA replication; DNA synthesis; DNA-binding;
DNA-directed DNA polymerase; Magnesium; Metal-binding;
Mutator protein; Nucleotidyltransferase; Nucleus; Reference proteome;
Transferase.
CHAIN 1 632 DNA polymerase eta.
/FTId=PRO_0000268698.
DOMAIN 26 309 UmuC. {ECO:0000255|PROSITE-
ProRule:PRU00216}.
REGION 625 632 POL30-binding.
METAL 30 30 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00216}.
METAL 155 155 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00216}.
MUTAGEN 30 30 D->A: Abolishes DNA polymerase activity.
{ECO:0000269|PubMed:11238937}.
MUTAGEN 34 34 F->L: Alters translesion activity.
{ECO:0000269|PubMed:15024063}.
MUTAGEN 39 39 E->A: Abolishes DNA polymerase activity.
{ECO:0000269|PubMed:11238937}.
MUTAGEN 64 64 Y->F,A: Decreases efficiency of
nucleotide incorporation.
{ECO:0000269|PubMed:12665597}.
MUTAGEN 67 67 R->A: Decreases efficiency of nucleotide
incorporation.
{ECO:0000269|PubMed:12665597}.
MUTAGEN 155 155 D->A: Abolishes DNA polymerase activity
and increases UV-induced mutations.
{ECO:0000269|PubMed:11238937}.
MUTAGEN 156 156 E->A: Decreases efficiency of nucleotide
incorporation.
{ECO:0000269|PubMed:11238937}.
MUTAGEN 279 279 K->A: Decreases efficiency of nucleotide
incorporation.
{ECO:0000269|PubMed:12665597}.
MUTAGEN 627 627 F->A: Abolishes POL30-binding; when
associated with A-628.
MUTAGEN 628 628 F->A: Abolishes POL30-binding; when
associated with A-627.
STRAND 1 5 {ECO:0000244|PDB:3MFI}.
HELIX 6 10 {ECO:0000244|PDB:3MFI}.
HELIX 11 13 {ECO:0000244|PDB:3MFI}.
TURN 15 17 {ECO:0000244|PDB:3MFI}.
HELIX 18 20 {ECO:0000244|PDB:3MFI}.
STRAND 21 23 {ECO:0000244|PDB:2R8K}.
STRAND 26 31 {ECO:0000244|PDB:3MFI}.
HELIX 34 42 {ECO:0000244|PDB:3MFI}.
STRAND 51 55 {ECO:0000244|PDB:3MFI}.
STRAND 58 62 {ECO:0000244|PDB:3MFI}.
HELIX 64 67 {ECO:0000244|PDB:3MFI}.
TURN 68 70 {ECO:0000244|PDB:3MFI}.
HELIX 77 81 {ECO:0000244|PDB:3MFI}.
STRAND 88 91 {ECO:0000244|PDB:3MFI}.
STRAND 93 96 {ECO:0000244|PDB:3MFI}.
STRAND 100 103 {ECO:0000244|PDB:3OHB}.
HELIX 115 117 {ECO:0000244|PDB:3OHA}.
STRAND 123 127 {ECO:0000244|PDB:3MFI}.
HELIX 129 145 {ECO:0000244|PDB:3MFI}.
STRAND 149 153 {ECO:0000244|PDB:3MFI}.
STRAND 156 160 {ECO:0000244|PDB:3MFI}.
HELIX 162 171 {ECO:0000244|PDB:3MFI}.
STRAND 176 178 {ECO:0000244|PDB:3MFI}.
HELIX 183 186 {ECO:0000244|PDB:3MFI}.
HELIX 188 196 {ECO:0000244|PDB:3MFI}.
STRAND 203 206 {ECO:0000244|PDB:3MFI}.
HELIX 210 214 {ECO:0000244|PDB:3MFI}.
STRAND 219 221 {ECO:0000244|PDB:3MFI}.
HELIX 233 256 {ECO:0000244|PDB:3MFI}.
STRAND 260 267 {ECO:0000244|PDB:3MFI}.
HELIX 268 275 {ECO:0000244|PDB:3MFI}.
TURN 276 278 {ECO:0000244|PDB:1JIH}.
STRAND 280 285 {ECO:0000244|PDB:3MFI}.
HELIX 288 290 {ECO:0000244|PDB:3MFI}.
HELIX 291 295 {ECO:0000244|PDB:3MFI}.
STRAND 297 299 {ECO:0000244|PDB:3MFI}.
HELIX 302 304 {ECO:0000244|PDB:3MFI}.
HELIX 306 308 {ECO:0000244|PDB:1JIH}.
HELIX 311 319 {ECO:0000244|PDB:3MFI}.
STRAND 324 326 {ECO:0000244|PDB:3MFI}.
HELIX 327 334 {ECO:0000244|PDB:3MFI}.
HELIX 339 351 {ECO:0000244|PDB:3MFI}.
STRAND 352 355 {ECO:0000244|PDB:2WTF}.
TURN 357 359 {ECO:0000244|PDB:3OHA}.
HELIX 364 366 {ECO:0000244|PDB:3MFH}.
HELIX 367 377 {ECO:0000244|PDB:3MFI}.
TURN 378 380 {ECO:0000244|PDB:3MFI}.
STRAND 395 400 {ECO:0000244|PDB:3MFI}.
TURN 403 406 {ECO:0000244|PDB:3MFI}.
HELIX 409 434 {ECO:0000244|PDB:3MFI}.
STRAND 436 448 {ECO:0000244|PDB:3MFI}.
STRAND 454 460 {ECO:0000244|PDB:3MFI}.
HELIX 466 468 {ECO:0000244|PDB:3MFI}.
HELIX 469 487 {ECO:0000244|PDB:3MFI}.
TURN 488 490 {ECO:0000244|PDB:3MFI}.
STRAND 497 510 {ECO:0000244|PDB:3MFI}.
SEQUENCE 632 AA; 71515 MW; CFB1A9FBC8AFE39B CRC64;
MSKFTWKELI QLGSPSKAYE SSLACIAHID MNAFFAQVEQ MRCGLSKEDP VVCVQWNSII
AVSYAARKYG ISRMDTIQEA LKKCSNLIPI HTAVFKKGED FWQYHDGCGS WVQDPAKQIS
VEDHKVSLEP YRRESRKALK IFKSACDLVE RASIDEVFLD LGRICFNMLM FDNEYELTGD
LKLKDALSNI REAFIGGNYD INSHLPLIPE KIKSLKFEGD VFNPEGRDLI TDWDDVILAL
GSQVCKGIRD SIKDILGYTT SCGLSSTKNV CKLASNYKKP DAQTIVKNDC LLDFLDCGKF
EITSFWTLGG VLGKELIDVL DLPHENSIKH IRETWPDNAG QLKEFLDAKV KQSDYDRSTS
NIDPLKTADL AEKLFKLSRG RYGLPLSSRP VVKSMMSNKN LRGKSCNSIV DCISWLEVFC
AELTSRIQDL EQEYNKIVIP RTVSISLKTK SYEVYRKSGP VAYKGINFQS HELLKVGIKF
VTDLDIKGKN KSYYPLTKLS MTITNFDIID LQKTVVDMFG NQVHTFKSSA GKEDEEKTTS
SKADEKTPKL ECCKYQVTFT DQKALQEHAD YHLALKLSEG LNGAEESSKN LSFGEKRLLF
SRKRPNSQHT ATPQKKQVTS SKNILSFFTR KK


Related products :

Catalog number Product name Quantity
PCR-513XS Polymerase chain reaction PCR and reverse transcriptase polymerase chain reaction RT PCR products: SCRIPT One-Step RT-qPCR ProbesKit with ROX, XS pack RT-real-time-PCR Kit for highly sensitive and spe 40reactions x 25
PCR-513L Polymerase chain reaction PCR and reverse transcriptase polymerase chain reaction RT PCR products: SCRIPT One-Step RT-qPCR ProbesKit with ROX, L pack RT-real-time-PCR Kit for highly sensitive and spec 1000reactions x 25
PCR-515XS Polymerase chain reaction PCR and reverse transcriptase polymerase chain reaction RT PCR products: SCRIPT One-Step RT-qPCR GreenKit with ROX, XS pack RT-real-time-PCR Kit for highly sensitive and spec 40reactions x 25
PCR-515S Polymerase chain reaction PCR and reverse transcriptase polymerase chain reaction RT PCR products: SCRIPT One-Step RT-qPCR GreenKit with ROX, S pack RT-real-time-PCR Kit for highly sensitive and speci 200reactions x 25
PCR-515L Polymerase chain reaction PCR and reverse transcriptase polymerase chain reaction RT PCR products: SCRIPT One-Step RT-qPCR GreenKit with ROX, L pack RT-real-time-PCR Kit for highly sensitive and speci 1000reactions x 25
PCR-512XS Polymerase chain reaction PCR and reverse transcriptase polymerase chain reaction RT PCR products: SCRIPT One-Step RT-qPCR ProbesKit, XS pack RT-real-time-PCR Kit for highly sensitive and specific amp 40reactions x 25
PCR-513S Polymerase chain reaction PCR and reverse transcriptase polymerase chain reaction RT PCR products: SCRIPT One-Step RT-qPCR ProbesKit with ROX, S pack RT-real-time-PCR Kit for highly sensitive and spec 200reactions x 25
PCR-514S Polymerase chain reaction PCR and reverse transcriptase polymerase chain reaction RT PCR products: SCRIPT One-Step RT-qPCR GreenKit, S pack RT-real-time-PCR Kit for highly sensitive and specific ampli 200reactions x 25
PCR-512S Polymerase chain reaction PCR and reverse transcriptase polymerase chain reaction RT PCR products: SCRIPT One-Step RT-qPCR ProbesKit, S pack RT-real-time-PCR Kit for highly sensitive and specific ampl 200reactions x 25
PCR-512L Polymerase chain reaction PCR and reverse transcriptase polymerase chain reaction RT PCR products: SCRIPT One-Step RT-qPCR ProbesKit, L pack RT-real-time-PCR Kit for highly sensitive and specific ampl 1000reactions x 25
PCR-514L Polymerase chain reaction PCR and reverse transcriptase polymerase chain reaction RT PCR products: SCRIPT One-Step RT-qPCR GreenKit, L pack RT-real-time-PCR Kit for highly sensitive and specific ampli 1000reactions x 25
PCR-514XS Polymerase chain reaction PCR and reverse transcriptase polymerase chain reaction RT PCR products: SCRIPT One-Step RT-qPCR GreenKit, XS pack RT-real-time-PCR Kit for highly sensitive and specific ampl 40reactions x 25
PCR-509L Polymerase chain reaction PCR and reverse transcriptase polymerase chain reaction RT PCR products: SCRIPT One-Step RT-PCR Kit, L pack One-Step RT-PCR Kit for highly sensitive and specific amplificatio 500reactions x 50
PCR-509S Polymerase chain reaction PCR and reverse transcriptase polymerase chain reaction RT PCR products: SCRIPT One-Step RT-PCR Kit, S pack One-Step RT-PCR Kit for highly sensitive and specific amplificatio 100reactions x 50
PCR-509XS Polymerase chain reaction PCR and reverse transcriptase polymerase chain reaction RT PCR products: SCRIPT One-Step RT-PCR Kit, XS pack One-Step RT-PCR Kit for highly sensitive and specific amplificati 20reactions x 50
MEBE027 csm Taq DNA Polymerase Cold sensitive mutant Taq polymerases,5U μl <20KU
EIAAB27950 Erg1,NEM-sensitive fusion protein,N-ethylmaleimide-sensitive fusion protein,Nsf,Rat,Rattus norvegicus,Vesicle-fusing ATPase,Vesicular-fusion protein NSF
EIAAB27951 Homo sapiens,Human,NEM-sensitive fusion protein,N-ethylmaleimide-sensitive fusion protein,NSF,Vesicle-fusing ATPase,Vesicular-fusion protein NSF
EIAAB27952 Mouse,Mus musculus,NEM-sensitive fusion protein,N-ethylmaleimide-sensitive fusion protein,Nsf,Protein SKD2,Skd2,Suppressor of K(+) transport growth defect 2,Vesicle-fusing ATPase,Vesicular-fusion prot
EIAAB36333 28S ribosomal protein S29, mitochondrial,DAP3,DAP-3,Death-associated protein 3,Homo sapiens,Human,Ionizing radiation resistance conferring protein,MRPS29,MRP-S29,S29mt
E1131h Bovine ELISA Kit FOR X-ray radiation resistance-associated protein 1 96T
orb90215 Pfu DNA Polymerase protein Pfu DNA Polymerase is thermo-stable enzyme having Mw of about 90kDa. Pfu DNA Polymerase is derived from E.coli that and cloned from Pyrococcus furiosus strain Vc1 DSM3638. P 100 U
CSB-EL026237BO Bovine X-ray radiation resistance-associated protein 1(XRRA1) ELISA kit 96T
CSB-EL026237HU Human X-ray radiation resistance-associated protein 1(XRRA1) ELISA kit 96T
EIAAB46598 Bos taurus,Bovine,X-ray radiation resistance-associated protein 1,XRRA1


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur