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Q04049 (POLH_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length632 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

POL30P158733EBI-36214,EBI-12993

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 632632DNA polymerase eta
PRO_0000268698

Regions

Domain26 – 309284UmuC
Region625 – 6328POL30-binding

Sites

Metal binding301Magnesium By similarity
Metal binding1551Magnesium By similarity

Experimental info

Mutagenesis301D → A: Abolishes DNA polymerase activity. Ref.4 Ref.13 Ref.15
Mutagenesis341F → L: Alters translesion activity. Ref.4 Ref.13 Ref.30
Mutagenesis391E → A: Abolishes DNA polymerase activity. Ref.4 Ref.13 Ref.15
Mutagenesis641Y → F or A: Decreases efficiency of nucleotide incorporation. Ref.4 Ref.13 Ref.20
Mutagenesis671R → A: Decreases efficiency of nucleotide incorporation. Ref.4 Ref.13 Ref.20
Mutagenesis1551D → A: Abolishes DNA polymerase activity and increases UV-induced mutations. Ref.4 Ref.13 Ref.15
Mutagenesis1561E → A: Decreases efficiency of nucleotide incorporation. Ref.4 Ref.13 Ref.15
Mutagenesis2791K → A: Decreases efficiency of nucleotide incorporation. Ref.4 Ref.13 Ref.20
Mutagenesis6271F → A: Abolishes POL30-binding; when associated with A-628. Ref.4 Ref.13
Mutagenesis6281F → A: Abolishes POL30-binding; when associated with A-627. Ref.4 Ref.13

Secondary structure

.................................................................................................. 632
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q04049 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: CFB1A9FBC8AFE39B

FASTA63271,515
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
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.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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.
PIRS69702.
RefSeqNP_010707.3. NM_001180727.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JIHX-ray2.25A/B1-513[»]
2R8JX-ray3.10A/B1-531[»]
2R8KX-ray3.30A/B1-531[»]
2WTFX-ray2.50A/B1-513[»]
2XGPX-ray2.70A/B1-513[»]
2XGQX-ray2.70A/B1-513[»]
3MFHX-ray2.00A1-513[»]
3MFIX-ray1.76A1-513[»]
3OHAX-ray2.00A1-513[»]
3OHBX-ray2.00A1-513[»]
ProteinModelPortalQ04049.
SMRQ04049. Positions 1-512.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32477. 84 interactions.
DIPDIP-6500N.
IntActQ04049. 8 interactions.
MINTMINT-708283.
STRING4932.YDR419W.

Proteomic databases

MaxQBQ04049.
PaxDbQ04049.
PRIDEQ04049.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR419W; YDR419W; YDR419W.
GeneID852028.
KEGGsce:YDR419W.

Organism-specific databases

CYGDYDR419w.
SGDS000002827. RAD30.

Phylogenomic databases

eggNOGCOG0389.
HOGENOMHOG000065930.
KOK03509.
OMAGYTTSCG.
OrthoDBEOG7RFTT2.

Enzyme and pathway databases

BioCycYEAST:G3O-29960-MONOMER.

Gene expression databases

GenevestigatorQ04049.

Family and domain databases

Gene3D3.30.1490.100. 1 hit.
InterProIPR017961. DNA_pol_Y-fam_little_finger.
IPR001126. DNA_repair_prot_UmuC-like.
IPR017963. DNA_repair_prot_UmuC-like_N.
[Graphical view]
PfamPF00817. IMS. 1 hit.
PF11799. IMS_C. 1 hit.
[Graphical view]
SUPFAMSSF100879. SSF100879. 1 hit.
PROSITEPS50173. UMUC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ04049.
NextBio970255.
PROQ04049.

Entry information

Entry namePOLH_YEAST
AccessionPrimary (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: June 11, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references