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Q9JJN0 (POLH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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):
RAD30 homolog A
Xeroderma pigmentosum variant type protein homolog
Gene names
Name:Polh
Synonyms:Rad30a, Xpv
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length694 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. 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. Ref.1

Catalytic activity

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

Cofactor

Divalent metal cations. Prefers magnesium, but can also use manganese By similarity.

Subunit structure

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. Ref.3

Subcellular location

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

Tissue specificity

Ubiquitous. Ref.1

Induction

Up-regulated in proliferating cultured fibroblasts. Ref.1

Domain

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.

Post-translational modification

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

Sequence similarities

Belongs to the DNA polymerase type-Y family.

Contains 1 umuC domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 694694DNA polymerase eta
PRO_0000173987

Regions

Domain9 – 258250UmuC

Sites

Metal binding131Magnesium By similarity
Metal binding1151Magnesium By similarity

Amino acid modifications

Cross-link663Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link667Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link675Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link690Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9JJN0 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 727895AB5DB84BC8

FASTA69476,167
        10         20         30         40         50         60 
MAPGQNRVVA LVDMDCFFVQ VEQRQNPHLR NKPCAVVQYK SWKGGGIIAV SYEARAFGVT 

        70         80         90        100        110        120 
RNMWADDAKK LCPDLLLAQV RESRGKANLT KYREASVEVM EIMSYFAVIE RASIDEAYID 

       130        140        150        160        170        180 
LTSAVQERLQ KLQGQPISAD LLPSTYIEGL PRGPTVEETV QKEAIRKQGL LQWLDSLQSD 

       190        200        210        220        230        240 
DPTSPDLRLT VGAMIVEEMR AAIESKTGFQ CSAGISHNKV LAKLACGLNK PNRQTLVSHG 

       250        260        270        280        290        300 
SVPQLFSQMP IRKIRSLGGK LGASVIEVLG IEYMGDLTQF TESQLQSHFG EKNGSWLYAM 

       310        320        330        340        350        360 
CRGIEHDPVK PRQLPKTIGC SKNFPGKTAL ATREQVQWWL LQLALELEER LTKDRNDNDR 

       370        380        390        400        410        420 
VATQLVVSIR FQGDRRLSSL RRCCALPRYD AHKMSQDAFA AIRNCNTSGI QTEWSPPLTM 

       430        440        450        460        470        480 
LFLCATKFSA AAPPACTDIT AFLSSDSSCQ PKVPIASSET RTQGSGPAVP TSKEAATSLA 

       490        500        510        520        530        540 
SFFQKAAKKQ RMKETSFVPL NTATEKLSSK PSLVFQSSQT TGSQSFFKQK SLLLQHTQLS 

       550        560        570        580        590        600 
NSAAPDPPQA SPAAQPSCLP AECVDSGPDD GAVKPVSSKA VSTEMNVAGD SPNVLDSPAY 

       610        620        630        640        650        660 
NSQEVTQRAT EDQVLCEKCD SLVPVWDMPE HTDYHFALEL QKSFLQPCTS KPQAIPAVSP 

       670        680        690 
QGKRNPKSPS ASSSKRLRPH GMQTLESFFK PLTH 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB027128 mRNA. Translation: BAA97570.1.
AB037184 mRNA. Translation: BAA97585.1.
AK036296 mRNA. Translation: BAC29375.1.
CCDSCCDS28822.1.
RefSeqNP_109640.1. NM_030715.3.
UniGeneMm.311585.

3D structure databases

ProteinModelPortalQ9JJN0.
SMRQ9JJN0. Positions 1-431, 611-643.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid219842. 3 interactions.
IntActQ9JJN0. 1 interaction.

PTM databases

PhosphoSiteQ9JJN0.

Proteomic databases

PaxDbQ9JJN0.
PRIDEQ9JJN0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000024749; ENSMUSP00000024749; ENSMUSG00000023953.
GeneID80905.
KEGGmmu:80905.
UCSCuc008crx.1. mouse.

Organism-specific databases

CTD5429.
MGIMGI:1891457. Polh.

Phylogenomic databases

eggNOGCOG0389.
GeneTreeENSGT00530000062942.
HOGENOMHOG000115605.
HOVERGENHBG053633.
InParanoidQ9JJN0.
KOK03509.
OMASPPLTML.
OrthoDBEOG7N63M8.
PhylomeDBQ9JJN0.
TreeFamTF103010.

Gene expression databases

BgeeQ9JJN0.
CleanExMM_POLH.
GenevestigatorQ9JJN0.

Family and domain databases

Gene3D3.30.1490.100. 1 hit.
InterProIPR017061. DNA_pol_eta.
IPR017961. 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]
PIRSFPIRSF036603. DPol_eta. 1 hit.
SUPFAMSSF100879. SSF100879. 1 hit.
PROSITEPS50173. UMUC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio350254.
PROQ9JJN0.
SOURCESearch...

Entry information

Entry namePOLH_MOUSE
AccessionPrimary (citable) accession number: Q9JJN0
Secondary accession number(s): Q9JJJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot