AKT1S1

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AKT1 substrate 1 (proline-rich)
Identifiers
Symbol(s) AKT1S1; Lobe; MGC2865; PRAS40
External IDs OMIM: 610221 MGI: 1914855 HomoloGene: 12162
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 84335 67605
Ensembl ENSG00000204673 ENSMUSG00000011096
Uniprot Q96B36 Q9D1F4
Refseq NM_032375 (mRNA)
NP_115751 (protein)		 NM_026270 (mRNA)
NP_080546 (protein)
Location Chr 19: 55.06 - 55.07 Mb Chr 7: 44.72 - 44.72 Mb
Pubmed search [1] [2]

AKT1 substrate 1 (proline-rich), also known as AKT1S1, is a human gene.[1]


[edit] References

  1. ^ Entrez Gene: AKT1S1 AKT1 substrate 1 (proline-rich).

[edit] Further reading

  • 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. 
  • 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. 
  • 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:10.1073/pnas.242603899. PMID 12477932. 
  • Kovacina KS, Park GY, Bae SS, et al. (2003). "Identification of a proline-rich Akt substrate as a 14-3-3 binding partner.". J. Biol. Chem. 278 (12): 10189–94. doi:10.1074/jbc.M210837200. PMID 12524439. 
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
  • Saito A, Narasimhan P, Hayashi T, et al. (2004). "Neuroprotective role of a proline-rich Akt substrate in apoptotic neuronal cell death after stroke: relationships with nerve growth factor.". J. Neurosci. 24 (7): 1584–93. doi:10.1523/JNEUROSCI.5209-03.2004. PMID 14973226. 
  • Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins.". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMID 15302935. 
  • Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization.". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660. 
  • 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:10.1101/gr.2596504. PMID 15489334. 
  • Huang B, Porter G (2006). "Expression of proline-rich Akt-substrate PRAS40 in cell survival pathway and carcinogenesis.". Acta Pharmacol. Sin. 26 (10): 1253–8. PMID 16174443. 
  • Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMID 16344560. 
  • Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. 
  • Vander Haar E, Lee SI, Bandhakavi S, et al. (2007). "Insulin signalling to mTOR mediated by the Akt/PKB substrate PRAS40.". Nat. Cell Biol. 9 (3): 316–23. doi:10.1038/ncb1547. PMID 17277771. 
  • Sancak Y, Thoreen CC, Peterson TR, et al. (2007). "PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein kinase.". Mol. Cell 25 (6): 903–15. doi:10.1016/j.molcel.2007.03.003. PMID 17386266. 
  • Wang L, Harris TE, Roth RA, Lawrence JC (2007). "PRAS40 regulates mTORC1 kinase activity by functioning as a direct inhibitor of substrate binding.". J. Biol. Chem. 282 (27): 20036–44. doi:10.1074/jbc.M702376200. PMID 17510057. 
  • Fonseca BD, Smith EM, Lee VH, et al. (2007). "PRAS40 is a target for mammalian target of rapamycin complex 1 and is required for signaling downstream of this complex.". J. Biol. Chem. 282 (34): 24514–24. doi:10.1074/jbc.M704406200. PMID 17604271. 
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