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Protein

DNA polymerase eta

Gene

Polh

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. May play a role in hypermutation at immunoglobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity. Targets POLI to replication foci (By similarity).By similarity

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Divalent metal cations. Prefers Mg(2+), but can also use Mn2+.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi13 – 131MagnesiumPROSITE-ProRule annotation
Metal bindingi115 – 1151MagnesiumPROSITE-ProRule annotation

GO - Molecular functioni

  • damaged DNA binding Source: InterPro
  • DNA-directed DNA polymerase activity Source: MGI
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cellular response to UV-C Source: MGI
  • DNA replication Source: UniProtKB-KW
  • DNA synthesis involved in DNA repair Source: MGI
  • postreplication repair Source: MGI
  • pyrimidine dimer repair Source: MGI
  • response to UV-C Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Mutator protein, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA damage, DNA repair, DNA replication, DNA synthesis

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding, Schiff base

Enzyme and pathway databases

ReactomeiREACT_332983. Translesion Synthesis by POLH.
REACT_362050. Termination of translesion DNA synthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase eta (EC:2.7.7.7)
Alternative name(s):
RAD30 homolog A
Xeroderma pigmentosum variant type protein homolog
Gene namesi
Name:Polh
Synonyms:Rad30a, Xpv
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1891457. Polh.

Subcellular locationi

  • Nucleus By similarity

  • Note: Accumulates at replication forks after DNA damage.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 694694DNA polymerase etaPRO_0000173987Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki663 – 663Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki667 – 667Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki675 – 675Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki690 – 690Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

Monoubiquitinated by RCHY1/PIRH2; ubiquitination inhibits the ability of PolH to interact with PCNA and to bypass UV-induced lesions.By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiQ9JJN0.
PRIDEiQ9JJN0.

PTM databases

PhosphoSiteiQ9JJN0.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Inductioni

Up-regulated in proliferating cultured fibroblasts.1 Publication

Gene expression databases

BgeeiQ9JJN0.
CleanExiMM_POLH.
GenevisibleiQ9JJN0. MM.

Interactioni

Subunit structurei

Interacts with REV1. Interacts with monoubiquitinated PCNA, but not unmodified PCNA. Interacts with POLI. Interacts with PALB2 and BRCA2; the interactions are direct and are involved in POLH localization at collapsed replication forks and DNA polymerization activity.1 Publication

Protein-protein interaction databases

BioGridi219842. 3 interactions.
IntActiQ9JJN0. 1 interaction.
STRINGi10090.ENSMUSP00000024749.

Structurei

3D structure databases

ProteinModelPortaliQ9JJN0.
SMRiQ9JJN0. Positions 1-431, 611-643.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 258250UmuCPROSITE-ProRule annotationAdd
BLAST

Domaini

The catalytic core consists of fingers, palm and thumb subdomains, but the fingers and thumb subdomains are much smaller than in high-fidelity polymerases; residues from five sequence motifs of the Y-family cluster around an active site cleft that can accommodate DNA and nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation and low processivity.

Sequence similaritiesi

Belongs to the DNA polymerase type-Y family.Curated
Contains 1 umuC domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0389.
GeneTreeiENSGT00530000062942.
HOGENOMiHOG000115605.
HOVERGENiHBG053633.
InParanoidiQ9JJN0.
KOiK03509.
OMAiRNKPCAV.
OrthoDBiEOG7N63M8.
PhylomeDBiQ9JJN0.
TreeFamiTF103010.

Family and domain databases

Gene3Di3.30.1490.100. 1 hit.
InterProiIPR017061. DNA_pol_eta/kappa.
IPR017961. DNA_pol_Y-fam_little_finger.
IPR001126. DNA_repair_prot_UmuC-like.
IPR017963. DNA_repair_prot_UmuC-like_N.
[Graphical view]
PfamiPF00817. IMS. 1 hit.
PF11799. IMS_C. 1 hit.
[Graphical view]
PIRSFiPIRSF036603. DPol_eta. 1 hit.
SUPFAMiSSF100879. SSF100879. 1 hit.
PROSITEiPS50173. UMUC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JJN0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPGQNRVVA LVDMDCFFVQ VEQRQNPHLR NKPCAVVQYK SWKGGGIIAV
60 70 80 90 100
SYEARAFGVT RNMWADDAKK LCPDLLLAQV RESRGKANLT KYREASVEVM
110 120 130 140 150
EIMSYFAVIE RASIDEAYID LTSAVQERLQ KLQGQPISAD LLPSTYIEGL
160 170 180 190 200
PRGPTVEETV QKEAIRKQGL LQWLDSLQSD DPTSPDLRLT VGAMIVEEMR
210 220 230 240 250
AAIESKTGFQ CSAGISHNKV LAKLACGLNK PNRQTLVSHG SVPQLFSQMP
260 270 280 290 300
IRKIRSLGGK LGASVIEVLG IEYMGDLTQF TESQLQSHFG EKNGSWLYAM
310 320 330 340 350
CRGIEHDPVK PRQLPKTIGC SKNFPGKTAL ATREQVQWWL LQLALELEER
360 370 380 390 400
LTKDRNDNDR VATQLVVSIR FQGDRRLSSL RRCCALPRYD AHKMSQDAFA
410 420 430 440 450
AIRNCNTSGI QTEWSPPLTM LFLCATKFSA AAPPACTDIT AFLSSDSSCQ
460 470 480 490 500
PKVPIASSET RTQGSGPAVP TSKEAATSLA SFFQKAAKKQ RMKETSFVPL
510 520 530 540 550
NTATEKLSSK PSLVFQSSQT TGSQSFFKQK SLLLQHTQLS NSAAPDPPQA
560 570 580 590 600
SPAAQPSCLP AECVDSGPDD GAVKPVSSKA VSTEMNVAGD SPNVLDSPAY
610 620 630 640 650
NSQEVTQRAT EDQVLCEKCD SLVPVWDMPE HTDYHFALEL QKSFLQPCTS
660 670 680 690
KPQAIPAVSP QGKRNPKSPS ASSSKRLRPH GMQTLESFFK PLTH
Length:694
Mass (Da):76,167
Last modified:October 1, 2000 - v1
Checksum:i727895AB5DB84BC8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB027128 mRNA. Translation: BAA97570.1.
AB037184 mRNA. Translation: BAA97585.1.
AK036296 mRNA. Translation: BAC29375.1.
CCDSiCCDS28822.1.
RefSeqiNP_109640.1. NM_030715.3.
UniGeneiMm.311585.

Genome annotation databases

EnsembliENSMUST00000024749; ENSMUSP00000024749; ENSMUSG00000023953.
GeneIDi80905.
KEGGimmu:80905.
UCSCiuc008crx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB027128 mRNA. Translation: BAA97570.1.
AB037184 mRNA. Translation: BAA97585.1.
AK036296 mRNA. Translation: BAC29375.1.
CCDSiCCDS28822.1.
RefSeqiNP_109640.1. NM_030715.3.
UniGeneiMm.311585.

3D structure databases

ProteinModelPortaliQ9JJN0.
SMRiQ9JJN0. Positions 1-431, 611-643.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi219842. 3 interactions.
IntActiQ9JJN0. 1 interaction.
STRINGi10090.ENSMUSP00000024749.

PTM databases

PhosphoSiteiQ9JJN0.

Proteomic databases

PaxDbiQ9JJN0.
PRIDEiQ9JJN0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024749; ENSMUSP00000024749; ENSMUSG00000023953.
GeneIDi80905.
KEGGimmu:80905.
UCSCiuc008crx.1. mouse.

Organism-specific databases

CTDi5429.
MGIiMGI:1891457. Polh.

Phylogenomic databases

eggNOGiCOG0389.
GeneTreeiENSGT00530000062942.
HOGENOMiHOG000115605.
HOVERGENiHBG053633.
InParanoidiQ9JJN0.
KOiK03509.
OMAiRNKPCAV.
OrthoDBiEOG7N63M8.
PhylomeDBiQ9JJN0.
TreeFamiTF103010.

Enzyme and pathway databases

ReactomeiREACT_332983. Translesion Synthesis by POLH.
REACT_362050. Termination of translesion DNA synthesis.

Miscellaneous databases

NextBioi350254.
PROiQ9JJN0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JJN0.
CleanExiMM_POLH.
GenevisibleiQ9JJN0. MM.

Family and domain databases

Gene3Di3.30.1490.100. 1 hit.
InterProiIPR017061. DNA_pol_eta/kappa.
IPR017961. DNA_pol_Y-fam_little_finger.
IPR001126. DNA_repair_prot_UmuC-like.
IPR017963. DNA_repair_prot_UmuC-like_N.
[Graphical view]
PfamiPF00817. IMS. 1 hit.
PF11799. IMS_C. 1 hit.
[Graphical view]
PIRSFiPIRSF036603. DPol_eta. 1 hit.
SUPFAMiSSF100879. SSF100879. 1 hit.
PROSITEiPS50173. UMUC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complementation of defective translesion synthesis and UV light-sensitivity in xeroderma pigmentosum variant cells by human and mouse DNA polymerase eta."
    Yamada A., Masutani C., Iwai S., Hanaoka F.
    Nucleic Acids Res. 28:2473-2480(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, TISSUE SPECIFICITY.
    Strain: 129/Sv.
    Tissue: Embryo.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  3. "Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis."
    Guo C., Fischhaber P.L., Luk-Paszyc M.J., Masuda Y., Zhou J., Kamiya K., Kisker C., Friedberg E.C.
    EMBO J. 22:6621-6630(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH REV1.

Entry informationi

Entry nameiPOLH_MOUSE
AccessioniPrimary (citable) accession number: Q9JJN0
Secondary accession number(s): Q9JJJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: October 1, 2000
Last modified: July 22, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.