POLE4
Appearance
| POLE4 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | POLE4, YHHQ1, p12, polymerase (DNA) epsilon 4, accessory subunit, DNA polymerase epsilon 4, accessory subunit | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 607269; MGI: 1914229; HomoloGene: 41339; GeneCards: POLE4; OMA:POLE4 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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| Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Polymerase (DNA-directed), epsilon 4, accessory subunit is a protein that in humans is encoded by the POLE4 gene.[5]
Function
[edit]POLE4 is a histone-fold protein that interacts with other histone-fold proteins to bind DNA in a sequence-independent manner. These histone-fold protein dimers combine within larger enzymatic complexes for DNA transcription, replication, and packaging.[5]
References
[edit]- 1 2 3 GRCh38: Ensembl release 89: ENSG00000115350 – Ensembl, May 2017
- 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000030042 – Ensembl, May 2017
- ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- 1 2 "Entrez Gene: Polymerase (DNA-directed), epsilon 4, accessory subunit".
Further reading
[edit]- Post SM, Tomkinson AE, Lee EY (2003). "The human checkpoint Rad protein Rad17 is chromatin-associated throughout the cell cycle, localizes to DNA replication sites, and interacts with DNA polymerase epsilon". Nucleic Acids Res. 31 (19): 5568–75. doi:10.1093/nar/gkg765. PMC 206465. PMID 14500819.
- Li Y, Pursell ZF, Linn S (2000). "Identification and cloning of two histone fold motif-containing subunits of HeLa DNA polymerase epsilon". J. Biol. Chem. 275 (30): 23247–52. doi:10.1074/jbc.M002548200. PMID 10801849.
- Wang YL, Faiola F, Xu M, Pan S, Martinez E (2008). "Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel NC2-like histone fold module that interacts with the TATA-binding protein". J. Biol. Chem. 283 (49): 33808–15. doi:10.1074/jbc.M806936200. PMC 2590711. PMID 18838386.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.