Q04049 (POLH_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA polymerase eta
EC=2.7.7.7

Alternative name(s):
Radiation-sensitive protein 30

Gene names

Name:	RAD30
Synonyms:	DBH1
Ordered Locus Names:	YDR419W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	632 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39
Catalytic activity	Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Subunit structure	Interacts with POL30. This interaction is essential for the polymerase eta function. Ref.13
Subcellular location	Nucleus Ref.21.
Induction	By UV radiation and heat shock. The mRNA is stabilized during stationary phase. Ref.3 Ref.32
Miscellaneous	Present with 1860 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the DNA polymerase type-Y family. Contains 1 umuC domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair DNA replication DNA synthesis
Cellular component	Nucleus
Ligand	DNA-binding Magnesium Metal-binding
Molecular function	DNA-directed DNA polymerase Mutator protein Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW error-free translesion synthesis Inferred from direct assay Ref.8Ref.10Ref.9Ref.6. Source: SGD error-prone translesion synthesis Inferred from direct assay Ref.8. Source: SGD
Cellular_component	mitochondrion Inferred from direct assay PubMed 23313845. Source: SGD nucleus Inferred from direct assay PubMed 23313845. Source: SGD replication fork Inferred from physical interaction Ref.13. Source: SGD
Molecular_function	DNA-directed DNA polymerase activity Inferred from direct assay Ref.5Ref.6. Source: SGD damaged DNA binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
POL30	P15873	3	EBI-36214,EBI-12993

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 632

632

DNA polymerase eta

PRO_0000268698

Regions

Domain

26 – 309

284

UmuC

Region

625 – 632

8

POL30-binding

Sites

Metal binding

30

1

Magnesium By similarity

Metal binding

155

1

Magnesium By similarity

Experimental info

Mutagenesis

30

1

D → A: Abolishes DNA polymerase activity. Ref.4 Ref.13 Ref.15

Mutagenesis

34

1

F → L: Alters translesion activity. Ref.4 Ref.13 Ref.30

Mutagenesis

39

1

E → A: Abolishes DNA polymerase activity. Ref.4 Ref.13 Ref.15

Mutagenesis

64

1

Y → F or A: Decreases efficiency of nucleotide incorporation. Ref.4 Ref.13 Ref.20

Mutagenesis

67

1

R → A: Decreases efficiency of nucleotide incorporation. Ref.4 Ref.13 Ref.20

Mutagenesis

155

1

D → A: Abolishes DNA polymerase activity and increases UV-induced mutations. Ref.4 Ref.13 Ref.15

Mutagenesis

156

1

E → A: Decreases efficiency of nucleotide incorporation. Ref.4 Ref.13 Ref.15

Mutagenesis

279

1

K → A: Decreases efficiency of nucleotide incorporation. Ref.4 Ref.13 Ref.20

Mutagenesis

627

1

F → A: Abolishes POL30-binding; when associated with A-628. Ref.4 Ref.13

Mutagenesis

628

1

F → A: Abolishes POL30-binding; when associated with A-627. Ref.4 Ref.13

Secondary structure

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632

Helix Strand Turn

Details...

Beta strand

1 – 5

5

Helix

6 – 10

5

Helix

11 – 13

3

Turn

15 – 17

3

Helix

18 – 20

3

Beta strand

21 – 23

3

Beta strand

26 – 31

6

Helix

34 – 42

9

Beta strand

51 – 55

5

Beta strand

58 – 62

5

Helix

64 – 67

4

Turn

68 – 70

3

Helix

77 – 81

5

Beta strand

88 – 91

4

Beta strand

93 – 96

4

Beta strand

100 – 103

4

Helix

115 – 117

3

Beta strand

123 – 127

5

Helix

129 – 145

17

Beta strand

149 – 153

5

Beta strand

156 – 160

5

Helix

162 – 171

10

Beta strand

176 – 178

3

Helix

183 – 186

4

Helix

188 – 196

9

Beta strand

203 – 206

4

Helix

210 – 214

5

Beta strand

219 – 221

3

Helix

233 – 256

24

Beta strand

260 – 267

8

Helix

268 – 275

8

Turn

276 – 278

3

Beta strand

280 – 285

6

Helix

288 – 290

3

Helix

291 – 295

5

Beta strand

297 – 299

3

Helix

302 – 304

3

Helix

306 – 308

3

Helix

311 – 319

9

Beta strand

324 – 326

3

Helix

327 – 334

8

Helix

339 – 351

13

Beta strand

352 – 355

4

Turn

357 – 359

3

Helix

364 – 366

3

Helix

367 – 377

11

Turn

378 – 380

3

Beta strand

395 – 400

6

Turn

403 – 406

4

Helix

409 – 434

26

Beta strand

436 – 448

13

Beta strand

454 – 460

7

Helix

466 – 468

3

Helix

469 – 487

19

Turn

488 – 490

3

Beta strand

497 – 510

14

Sequences

	Sequence		Length	Mass (Da)
	Q04049 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: CFB1A9FBC8AFE39B	FASTA	632	71,515
	10 20 30 40 50 60 MSKFTWKELI QLGSPSKAYE SSLACIAHID MNAFFAQVEQ MRCGLSKEDP VVCVQWNSII 70 80 90 100 110 120 AVSYAARKYG ISRMDTIQEA LKKCSNLIPI HTAVFKKGED FWQYHDGCGS WVQDPAKQIS 130 140 150 160 170 180 VEDHKVSLEP YRRESRKALK IFKSACDLVE RASIDEVFLD LGRICFNMLM FDNEYELTGD 190 200 210 220 230 240 LKLKDALSNI REAFIGGNYD INSHLPLIPE KIKSLKFEGD VFNPEGRDLI TDWDDVILAL 250 260 270 280 290 300 GSQVCKGIRD SIKDILGYTT SCGLSSTKNV CKLASNYKKP DAQTIVKNDC LLDFLDCGKF 310 320 330 340 350 360 EITSFWTLGG VLGKELIDVL DLPHENSIKH IRETWPDNAG QLKEFLDAKV KQSDYDRSTS 370 380 390 400 410 420 NIDPLKTADL AEKLFKLSRG RYGLPLSSRP VVKSMMSNKN LRGKSCNSIV DCISWLEVFC 430 440 450 460 470 480 AELTSRIQDL EQEYNKIVIP RTVSISLKTK SYEVYRKSGP VAYKGINFQS HELLKVGIKF 490 500 510 520 530 540 VTDLDIKGKN KSYYPLTKLS MTITNFDIID LQKTVVDMFG NQVHTFKSSA GKEDEEKTTS 550 560 570 580 590 600 SKADEKTPKL ECCKYQVTFT DQKALQEHAD YHLALKLSEG LNGAEESSKN LSFGEKRLLF 610 620 630 SRKRPNSQHT ATPQKKQVTS SKNILSFFTR KK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." 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. Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"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." McDonald J.P., Levine A.S., Woodgate R. Genetics 147:1557-1568(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION.
[4]	"Requirement of DNA polymerase activity of yeast Rad30 protein for its biological function." Johnson R.E., Prakash S., Prakash L. J. Biol. Chem. 274:15975-15977(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF 155-ASP-GLU-156.
[5]	"Fidelity and processivity of Saccharomyces cerevisiae DNA polymerase eta." Washington M.T., Johnson R.E., Prakash S., Prakash L. J. Biol. Chem. 274:36835-36838(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Efficient bypass of a thymine-thymine dimer by yeast DNA polymerase, Poleta." Johnson R.E., Prakash S., Prakash L. Science 283:1001-1004(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"The Saccharomyces cerevisiae RAD6 group is composed of an error-prone and two error-free postreplication repair pathways." Xiao W., Chow B.L., Broomfield S., Hanna M. Genetics 155:1633-1641(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Specificity of DNA lesion bypass by the yeast DNA polymerase eta." Yuan F., Zhang Y., Rajpal D.K., Wu X., Guo D., Wang M., Taylor J.-S., Wang Z. J. Biol. Chem. 275:8233-8239(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"Replication past O(6)-methylguanine by yeast and human DNA polymerase eta." Haracska L., Prakash S., Prakash L. Mol. Cell. Biol. 20:8001-8007(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"Efficient and accurate replication in the presence of 7,8-dihydro-8-oxoguanine by DNA polymerase eta." Haracska L., Yu S.-L., Johnson R.E., Prakash L., Prakash S. Nat. Genet. 25:458-461(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Accuracy of thymine-thymine dimer bypass by Saccharomyces cerevisiae DNA polymerase eta." Washington M.T., Johnson R.E., Prakash S., Prakash L. Proc. Natl. Acad. Sci. U.S.A. 97:3094-3099(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Translesion DNA synthesis by yeast DNA polymerase eta on templates containing N2-guanine adducts of 1,3-butadiene metabolites." Minko I.G., Washington M.T., Prakash L., Prakash S., Lloyd R.S. J. Biol. Chem. 276:2517-2522(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Interaction with PCNA is essential for yeast DNA polymerase eta function." Haracska L., Kondratick C.M., Unk I., Prakash S., Prakash L. Mol. Cell 8:407-415(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DOMAIN, INTERACTION WITH POL30, MUTAGENESIS OF 627-PHE-PHE-628.
[14]	"Requirement of DNA polymerase eta for error-free bypass of UV-induced CC and TC photoproducts." Yu S.-L., Johnson R.E., Prakash S., Prakash L. Mol. Cell. Biol. 21:185-188(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"Acidic residues critical for the activity and biological function of yeast DNA polymerase eta." Kondratick C.M., Washington M.T., Prakash S., Prakash L. Mol. Cell. Biol. 21:2018-2025(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DOMAIN, MUTAGENESIS OF ASP-30; GLU-39; ASP-155 AND GLU-156.
[16]	"Mismatch extension ability of yeast and human DNA polymerase eta." Washington M.T., Johnson R.E., Prakash S., Prakash L. J. Biol. Chem. 276:2263-2266(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[17]	"Lesion bypass in yeast cells: Pol eta participates in a multi-DNA polymerase process." Bresson A., Fuchs R.P. EMBO J. 21:3881-3887(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[18]	"UV-induced T-->C transition at a TT photoproduct site is dependent on Saccharomyces cerevisiae polymerase eta in vivo." Zhang H., Siede W. Nucleic Acids Res. 30:1262-1267(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[19]	"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." Sun L., Zhang K., Zhou L., Hohler P., Kool E.T., Yuan F., Wang Z., Taylor J.-S. Biochemistry 42:9431-9437(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[20]	"Deoxynucleotide triphosphate binding mode conserved in Y family DNA polymerases." Johnson R.E., Trincao J., Aggarwal A.K., Prakash S., Prakash L. Mol. Cell. Biol. 23:3008-3012(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF TYR-64; ARG-67 AND LYS-279.
[21]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[22]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[23]	"Roles of Saccharomyces cerevisiae DNA polymerases Poleta and Polzeta in response to irradiation by simulated sunlight." Kozmin S.G., Pavlov Y.I., Kunkel T.A., Sage E. Nucleic Acids Res. 31:4541-4552(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[24]	"Yeast DNA polymerase eta makes functional contacts with the DNA minor groove only at the incoming nucleoside triphosphate." Washington M.T., Wolfle W.T., Spratt T.E., Prakash L., Prakash S. Proc. Natl. Acad. Sci. U.S.A. 100:5113-5118(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[25]	"Mechanism of nucleotide incorporation opposite a thymine-thymine dimer by yeast DNA polymerase eta." Washington M.T., Prakash L., Prakash S. Proc. Natl. Acad. Sci. U.S.A. 100:12093-12098(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[26]	"LC-MS/MS identification and yeast polymerase eta bypass of a novel gamma-irradiation-induced intrastrand cross-link lesion G[8-5]C." Gu C., Wang Y. Biochemistry 43:6745-6750(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[27]	"Role of base stacking and sequence context in the inhibition of yeast DNA polymerase eta by pyrene nucleotide." Hwang H., Taylor J.-S. Biochemistry 43:14612-14623(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[28]	"Role of DNA polymerase eta in the bypass of abasic sites in yeast cells." Zhao B., Xie Z., Shen H., Wang Z. Nucleic Acids Res. 32:3984-3994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[29]	"Enzymatic switching for efficient and accurate translesion DNA replication." McCulloch S.D., Kokoska R.J., Chilkova O., Welch C.M., Johansson E., Burgers P.M.J., Kunkel T.A. Nucleic Acids Res. 32:4665-4675(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[30]	"Palm mutants in DNA polymerases alpha and eta alter DNA replication fidelity and translesion activity." Niimi A., Limsirichaikul S., Yoshida S., Iwai S., Masutani C., Hanaoka F., Kool E.T., Nishiyama Y., Suzuki M. Mol. Cell. Biol. 24:2734-2746(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF PHE-34.
[31]	"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." Hwang H., Taylor J.-S. Biochemistry 44:4850-4860(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[32]	"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." Michan C., Monje-Casas F., Pueyo C. DNA Repair 4:469-478(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[33]	"The p-benzoquinone DNA adducts derived from benzene are highly mutagenic." Xie Z., Zhang Y., Guliaev A.B., Shen H., Hang B., Singer B., Wang Z. DNA Repair 4:1399-1409(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[34]	"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." Gibbs P.E.M., McDonald J.P., Woodgate R., Lawrence C.W. Genetics 169:575-582(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[35]	"Base pairing and replicative processing of the formamidopyrimidine-dG DNA lesion." Ober M., Mueller H., Pieck C., Gierlich J., Carell T. J. Am. Chem. Soc. 127:18143-18149(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[36]	"Mechanism of efficient and accurate nucleotide incorporation opposite 7,8-dihydro-8-oxoguanine by Saccharomyces cerevisiae DNA polymerase eta." Carlson K.D., Washington M.T. Mol. Cell. Biol. 25:2169-2176(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[37]	"DNA synthesis past a 5-methylC-containing cis-syn-cyclobutane pyrimidine dimer by yeast pol eta is highly nonmutagenic." Vu B., Cannistraro V.J., Sun L., Taylor J.-S. Biochemistry 45:9327-9335(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[38]	"The in vivo characterization of translesion synthesis across UV-induced lesions in Saccharomyces cerevisiae: insights into Pol zeta- and Pol eta-dependent frameshift mutagenesis." Abdulovic A.L., Jinks-Robertson S. Genetics 172:1487-1498(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[39]	"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." Zhao B., Wang J., Geacintov N.E., Wang Z. Nucleic Acids Res. 34:417-425(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[40]	"Structure of the catalytic core of S. cerevisiae DNA polymerase eta: implications for translesion DNA synthesis." Trincao J., Johnson R.E., Escalante C.R., Prakash S., Prakash L., Aggarwal A.K. Mol. Cell 8:417-426(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-531.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U33007 Genomic DNA. Translation: AAB64856.1.
BK006938 Genomic DNA. Translation: DAA12259.1.

PIR

S69702.

RefSeq

NP_010707.3. NM_001180727.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JIH	X-ray	2.25	A/B	1-513	[»]
2R8J	X-ray	3.10	A/B	1-531	[»]
2R8K	X-ray	3.30	A/B	1-531	[»]
2WTF	X-ray	2.50	A/B	1-513	[»]
2XGP	X-ray	2.70	A/B	1-513	[»]
2XGQ	X-ray	2.70	A/B	1-513	[»]
3MFH	X-ray	2.00	A	1-513	[»]
3MFI	X-ray	1.76	A	1-513	[»]
3OHA	X-ray	2.00	A	1-513	[»]
3OHB	X-ray	2.00	A	1-513	[»]

ProteinModelPortal

Q04049.

SMR

Q04049. Positions 1-512.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6500N.

IntAct

Q04049. 9 interactions.

MINT

MINT-708283.

STRING

4932.YDR419W.

Proteomic databases

PaxDb

Q04049.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR419W; YDR419W; YDR419W.

GeneID

852028.

KEGG

sce:YDR419W.
sce:YDR423C.

Organism-specific databases

CYGD

YDR419w.

SGD

S000002827. RAD30.

Phylogenomic databases

eggNOG

COG0389.

HOGENOM

HOG000065930.

KO

K03509.
K09043.

OMA

IPIHTAV.

OrthoDB

EOG4M0J8V.

Gene expression databases

Genevestigator

Q04049.

GermOnline

YDR419W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.30.1490.100. 1 hit.

InterPro

IPR017961. DNA_pol_Y-fam_little_finger.
IPR001126. DNA_repair_prot_UmuC-like.
IPR017963. DNA_repair_prot_UmuC-like_N.
[Graphical view]

Pfam

PF00817. IMS. 1 hit.
PF11799. IMS_C. 1 hit.
[Graphical view]

SUPFAM

SSF100879. DNA_pol_Y-fam_little_finger. 1 hit.

PROSITE

PS50173. UMUC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q04049.

NextBio

970255.

Entry information

Entry name

POLH_YEAST

Accession

Primary (citable) accession number: Q04049
Secondary accession number(s): D6VT49

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program