TP53RK
Template:PBB TP53-regulating kinase, also known as PRPK is an enzyme that in humans is encoded by the TP53RK gene.[1][2][3] This protein is a serine/threonine protein kinase that phosphorylates p53 at Ser15.
PRPK is part of the KEOPS/EKC complex, which participates in transcription control,[4] telomere regulation [5] and tRNA modification.[6]
Model organisms
Model organisms have been used in the study of TP53RK function. A conditional knockout mouse line called Trp53rktm1a(EUCOMM)Wtsi was generated at the Wellcome Trust Sanger Institute.[7] Male and female animals underwent a standardized phenotypic screen[8] to determine the effects of deletion.[9][10][11][12] Additional screens performed: - In-depth immunological phenotyping[13]
| Characteristic | Phenotype |
|---|---|
| All data available at.[8][13] | |
| Insulin | Normal |
| Homozygous viability at P14 | Normal |
| Recessive lethal study | Normal |
| Homozygous Fertility | Normal |
| Body weight | Normal |
| Neurological assessment | Normal |
| Grip strength | Normal |
| Dysmorphology | Normal |
| Indirect calorimetry | Normal |
| Glucose tolerance test | Normal |
| Auditory brainstem response | Normal |
| DEXA | Normal |
| Radiography | Normal |
| Eye morphology | Normal |
| Clinical chemistry | Normal |
| Haematology 16 Weeks | Normal |
| Peripheral blood leukocytes 16 Weeks | Normal |
| Heart weight | Normal |
| Salmonella infection | Normal |
| Cytotoxic T Cell Function | Normal |
| Spleen Immunophenotyping | Normal |
| Mesenteric Lymph Node Immunophenotyping | Normal |
| Epidermal Immune Composition | Normal |
References
- ^ Abe Y, Matsumoto S, Wei S, Nezu K, Miyoshi A, Kito K, Ueda N, Shigemoto K, Hitsumoto Y, Nikawa J, Enomoto Y (Nov 2001). "Cloning and characterization of a p53-related protein kinase expressed in interleukin-2-activated cytotoxic T-cells, epithelial tumor cell lines, and the testes". The Journal of Biological Chemistry. 276 (47): 44003–11. doi:10.1074/jbc.M105669200. PMID 11546806.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Facchin S, Lopreiato R, Ruzzene M, Marin O, Sartori G, Götz C, Montenarh M, Carignani G, Pinna LA (Aug 2003). "Functional homology between yeast piD261/Bud32 and human PRPK: both phosphorylate p53 and PRPK partially complements piD261/Bud32 deficiency". FEBS Letters. 549 (1–3): 63–6. doi:10.1016/S0014-5793(03)00770-1. PMID 12914926.
- ^ "Entrez Gene: TP53RK TP53 regulating kinase".
- ^ Kisseleva-Romanova E, Lopreiato R, Baudin-Baillieu A, Rousselle JC, Ilan L, Hofmann K, Namane A, Mann C, Libri D (Aug 2006). "Yeast homolog of a cancer-testis antigen defines a new transcription complex". The EMBO Journal. 25 (15): 3576–85. doi:10.1038/sj.emboj.7601235. PMID 16874308.
- ^ Downey M, Houlsworth R, Maringele L, Rollie A, Brehme M, Galicia S, Guillard S, Partington M, Zubko MK, Krogan NJ, Emili A, Greenblatt JF, Harrington L, Lydall D, Durocher D (Mar 2006). "A genome-wide screen identifies the evolutionarily conserved KEOPS complex as a telomere regulator". Cell. 124 (6): 1155–68. doi:10.1016/j.cell.2005.12.044. PMID 16564010.
- ^ Srinivasan M, Mehta P, Yu Y, Prugar E, Koonin EV, Karzai AW, Sternglanz R (Mar 2011). "The highly conserved KEOPS/EKC complex is essential for a universal tRNA modification, t6A". The EMBO Journal. 30 (5): 873–81. doi:10.1038/emboj.2010.343. PMID 21183954.
- ^ Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
- ^ a b "International Mouse Phenotyping Consortium".
- ^ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
- ^ Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
- ^ Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
- ^ White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (Jul 2013). "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes". Cell. 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131.
- ^ a b "Infection and Immunity Immunophenotyping (3i) Consortium".
Further reading
- Bonaldo MF, Lennon G, Soares MB (Sep 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
- Miyoshi A, Kito K, Aramoto T, Abe Y, Kobayashi N, Ueda N (Apr 2003). "Identification of CGI-121, a novel PRPK (p53-related protein kinase)-binding protein". Biochemical and Biophysical Research Communications. 303 (2): 399–405. doi:10.1016/S0006-291X(03)00333-4. PMID 12659830.
- Wang SC, Lien HC, Xia W, Chen IF, Lo HW, Wang Z, Ali-Seyed M, Lee DF, Bartholomeusz G, Ou-Yang F, Giri DK, Hung MC (Sep 2004). "Binding at and transactivation of the COX-2 promoter by nuclear tyrosine kinase receptor ErbB-2". Cancer Cell. 6 (3): 251–61. doi:10.1016/j.ccr.2004.07.012. PMID 15380516.
- Abe Y, Takeuchi T, Imai Y, Murase R, Kamei Y, Fujibuchi T, Matsumoto S, Ueda N, Ogasawara M, Shigemoto K, Kito K (May 2006). "A Small Ras-like protein Ray/Rab1c modulates the p53-regulating activity of PRPK". Biochemical and Biophysical Research Communications. 344 (1): 377–85. doi:10.1016/j.bbrc.2006.03.071. PMID 16600182.
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