PRIM2
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Primase, polypeptide 2A, 58kDa
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Identifiers | ||||||||||||||
Symbol(s) | PRIM2A; p58; MGC75142; PRIM2 | |||||||||||||
External IDs | OMIM: 176636 MGI: 97758 HomoloGene: 731 | |||||||||||||
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RNA expression pattern | ||||||||||||||
Orthologs | ||||||||||||||
Human | Mouse | |||||||||||||
Entrez | 5558 | 19076 | ||||||||||||
Ensembl | ENSG00000146143 | ENSMUSG00000026134 | ||||||||||||
Uniprot | P49643 | Q3THK0 | ||||||||||||
Refseq | XM_001134297 (mRNA) XP_001134297 (protein) |
NM_008922 (mRNA) NP_032948 (protein) |
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Location | Chr 6: 57.29 - 57.62 Mb | Chr 1: 33.4 - 33.61 Mb | ||||||||||||
Pubmed search | [1] | [2] |
Primase, polypeptide 2A, 58kDa, also known as PRIM2A, is a human gene.[1]
The replication of DNA in eukaryotic cells is carried out by a complex chromosomal replication apparatus, in which DNA polymerase alpha and primase are two key enzymatic components. Primase, which is a heterodimer of a small subunit and a large subunit, synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication. The protein encoded by this gene is the large, 58 kDa primase subunit.[1]
[edit] References
[edit] Further reading
- Stadlbauer F, Brueckner A, Rehfuess C, et al. (1994). "DNA replication in vitro by recombinant DNA-polymerase-alpha-primase.". Eur. J. Biochem. 222 (3): 781–93. PMID 8026492.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
- Shiratori A, Okumura K, Nogami M, et al. (1996). "Assignment of the 49-kDa (PRIM1) and 58-kDa (PRIM2A and PRIM2B) subunit genes of the human DNA primase to chromosome bands 1q44 and 6p11.1-p12.". Genomics 28 (2): 350–3. PMID 8530050.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
- Coll JM, Hickey RJ, Cronkey EA, et al. (1998). "Mapping specific protein-protein interactions within the core component of the breast cell DNA synthesome.". Oncol. Res. 9 (11-12): 629–39. PMID 9563011.
- Schneider A, Smith RW, Kautz AR, et al. (1998). "Primase activity of human DNA polymerase alpha-primase. Divalent cations stabilize the enzyme activity of the p48 subunit.". J. Biol. Chem. 273 (34): 21608–15. PMID 9705292.
- Arezi B, Kirk BW, Copeland WC, Kuchta RD (1999). "Interactions of DNA with human DNA primase monitored with photoactivatable cross-linking agents: implications for the role of the p58 subunit.". Biochemistry 38 (39): 12899–907. PMID 10504261.
- Smith RW, Nasheuer HP (2002). "Control of complex formation of DNA polymerase alpha-primase and cell-free DNA replication by the C-terminal amino acids of the largest subunit p180.". FEBS Lett. 527 (1-3): 143–6. PMID 12220650.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi: . PMID 12477932.
- Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6.". Nature 425 (6960): 805–11. doi: . PMID 14574404.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi: . PMID 15489334.
- Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.". Nat. Biotechnol. 23 (1): 94–101. doi: . PMID 15592455.