PLEKHO1

From Wikipedia, the free encyclopedia


Pleckstrin homology domain containing, family O member 1
Identifiers
Symbol(s) PLEKHO1; CKIP-1; OC120; RP11-458I7.3
External IDs OMIM: 608335 MGI1914470 HomoloGene9448
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 51177 67220
Ensembl ENSG00000023902 ENSMUSG00000015745
Uniprot Q53GL0 n/a
Refseq NM_016274 (mRNA)
NP_057358 (protein)
NM_023320 (mRNA)
NP_075809 (protein)
Location Chr 1: 148.39 - 148.4 Mb Chr 3: 96.07 - 96.08 Mb
Pubmed search [1] [2]

Pleckstrin homology domain containing, family O member 1, also known as PLEKHO1, is a human gene.[1]


[edit] References

[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. 
  • Bosc DG, Graham KC, Saulnier RB, et al. (2000). "Identification and characterization of CKIP-1, a novel pleckstrin homology domain-containing protein that interacts with protein kinase CK2.". J. Biol. Chem. 275 (19): 14295–306. PMID 10799509. 
  • Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788–95. PMID 11076863. 
  • 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. 
  • 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. 
  • Olsten ME, Canton DA, Zhang C, et al. (2004). "The Pleckstrin homology domain of CK2 interacting protein-1 is required for interactions and recruitment of protein kinase CK2 to the plasma membrane.". J. Biol. Chem. 279 (40): 42114–27. doi:10.1074/jbc.M407628200. PMID 15254037. 
  • Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to biology: a functional genomics pipeline.". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMID 15489336. 
  • Zhang L, Xing G, Tie Y, et al. (2005). "Role for the pleckstrin homology domain-containing protein CKIP-1 in AP-1 regulation and apoptosis.". EMBO J. 24 (4): 766–78. doi:10.1038/sj.emboj.7600532. PMID 15706351. 
  • Barrios-Rodiles M, Brown KR, Ozdamar B, et al. (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells.". Science 307 (5715): 1621–5. doi:10.1126/science.1105776. PMID 15761153. 
  • Canton DA, Olsten ME, Kim K, et al. (2005). "The pleckstrin homology domain-containing protein CKIP-1 is involved in regulation of cell morphology and the actin cytoskeleton and interaction with actin capping protein.". Mol. Cell. Biol. 25 (9): 3519–34. doi:10.1128/MCB.25.9.3519-3534.2005. PMID 15831458. 
  • Zhang L, Tie Y, Tian C, et al. (2007). "CKIP-1 recruits nuclear ATM partially to the plasma membrane through interaction with ATM.". Cell. Signal. 18 (9): 1386–95. doi:10.1016/j.cellsig.2005.10.017. PMID 16325375. 
  • Mehrle A, Rosenfelder H, Schupp I, et al. (2006). "The LIFEdb database in 2006.". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMID 16381901. 
  • Lim J, Hao T, Shaw C, et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration.". Cell 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569. 
  • Canton DA, Olsten ME, Niederstrasser H, et al. (2007). "The role of CKIP-1 in cell morphology depends on its interaction with actin-capping protein.". J. Biol. Chem. 281 (47): 36347–59. doi:10.1074/jbc.M607595200. PMID 16987810. 
  • Zhang L, Tang Y, Tie Y, et al. (2007). "The PH domain containing protein CKIP-1 binds to IFP35 and Nmi and is involved in cytokine signaling.". Cell. Signal. 19 (5): 932–44. doi:10.1016/j.cellsig.2006.11.002. PMID 17197158. 
  • Tokuda E, Fujita N, Oh-hara T, et al. (2007). "Casein kinase 2-interacting protein-1, a novel Akt pleckstrin homology domain-interacting protein, down-regulates PI3K/Akt signaling and suppresses tumor growth in vivo.". Cancer Res. 67 (20): 9666–76. doi:10.1158/0008-5472.CAN-07-1050. PMID 17942896.