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Polh |
Protein FULL name:
DNA polymerase eta [Mus musculus].
Polh (Mus musculus) is product of expression of Polh gene.
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).
CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
COFACTOR: Divalent metal cations. Prefers magnesium, but can also use manganese (By similarity).
SUBUNIT: Binds POLI (By similarity). Binds REV1L. Binds monoubiquitinated PCNA, but not unmodified PCNA.
SUBCELLULAR LOCATION: Nucleus (By similarity). Note=Accumulates at replication forks after DNA damage (By similarity).
TISSUE SPECIFICITY: Ubiquitous.
INDUCTION: Up-regulated in proliferating cultured fibroblasts.
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.
SIMILARITY: Belongs to the DNA polymerase type-Y family.
SIMILARITY: Contains 1 umuC domain.
| NCBI GenPept GI number(s): |
17105328 |
| Species: | Mus musculus |
Links to other databases:
| Database | ID | Link |
| Uniprot | Q9JJN0 |
Q9JJN0 |
| PFAM: | - |
Q9JJN0 (Link - using uniprot id) |
| InterPro: | - |
Q9JJN0 (Link - using uniprot id) |
| CATH: | - | - |
| SCOP: | - | - |
| PDB: | - | - |
Protein sequence:
|
MAPGQNRVVALVDMDCFFVQVEQRQNPHLRNKPCAVVQYKSWKGGGIIAV SYEARAFGVTRNMWADDAKKLCPDLLLAQVRESRGKANLTKYREASVEVM EIMSYFAVIERASIDEAYIDLTSAVQERLQKLQGQPISADLLPSTYIEGL PRGPTVEETVQKEAIRKQGLLQWLDSLQSDDPTSPDLRLTVGAMIVEEMR AAIESKTGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMP IRKIRSLGGKLGASVIEVLGIEYMGDLTQFTESQLQSHFGEKNGSWLYAM CRGIEHDPVKPRQLPKTIGCSKNFPGKTALATREQVQWWLLQLALELEER LTKDRNDNDRVATQLVVSIRFQGDRRLSSLRRCCALPRYDAHKMSQDAFA AIRNCNTSGIQTEWSPPLTMLFLCATKFSAAAPPACTDITAFLSSDSSCQ PKVPIASSETRTQGSGPAVPTSKEAATSLASFFQKAAKKQRMKETSFVPL NTATEKLSSKPSLVFQSSQTTGSQSFFKQKSLLLQHTQLSNSAAPDPPQA SPAAQPSCLPAECVDSGPDDGAVKPVSSKAVSTEMNVAGDSPNVLDSPAY NSQEVTQRATEDQVLCEKCDSLVPVWDMPEHTDYHFALELQKSFLQPCTS KPQAIPAVSPQGKRNPKSPSASSSKRLRPHGMQTLESFFKPLTH |
Polh (Mus musculus) is able to recognize following damages:
Polh (Mus musculus) belongs to following protein families:
References:
| Title | Authors | Journal |
| 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 July 1, 2000 |
| Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis. | Guo C, Fischhaber PL, Luk-Paszyc MJ, Masuda Y, Zhou J, Kamiya K, Kisker C, Friedberg EC | EMBO J Dec. 15, 2003 |
| The transcriptional landscape of the mammalian genome. | Carninci P, Kasukawa T, Katayama S, Gough J, Frith MC, Maeda N, Oyama R, Ravasi T, Lenhard B, Wells C, Kodzius R, Shimokawa K, Bajic VB, Brenner SE, Batalov S, Forrest AR, Zavolan M, Davis MJ, Wilming LG, Aidinis V, Allen JE, Ambesi-Impiombato A, Apweiler R, Aturaliya RN, Bailey TL, Bansal M, Baxter L, Beisel KW, Bersano T, Bono H, Chalk AM, Chiu KP, Choudhary V, Christoffels A, Clutterbuck DR, Crowe ML, Dalla E, Dalrymple BP, de Bono B, Della Gatta G, di Bernardo D, Down T, Engstrom P, Fagiolini M, Faulkner G, Fletcher CF, Fukushima T, Furuno M, Futaki S, Gariboldi M, Georgii-Hemming P, Gingeras TR, Gojobori T, Green RE, Gustincich S, Harbers M, Hayashi Y, Hensch TK, 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 SP, Kruger A, Kummerfeld SK, Kurochkin IV, Lareau LF, 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 KC, Pavan WJ, Pavesi G, Pesole G, Petrovsky N, Piazza S, Reed J, Reid JF, Ring BZ, Ringwald M, Rost B, Ruan Y, Salzberg SL, Sandelin A, Schneider C, Schonbach C, Sekiguchi K, Semple CA, 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 SL, Tang S, Taylor MS, Tegner J, Teichmann SA, Ueda HR, van Nimwegen E, Verardo R, Wei CL, Yagi K, Yamanishi H, Zabarovsky E, Zhu S, Zimmer A, Hide W, Bult C, Grimmond SM, Teasdale RD, Liu ET, Brusic V, Quackenbush J, Wahlestedt C, Mattick JS, Hume DA, 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 Sept. 2, 2005 |
Last modification of this entry: Oct. 6, 2010.
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