| 释义 |
- Interactions
- References
- Further reading
{{Infobox_gene}}Pleckstrin homology domain-containing family O member 1 is a protein that in humans is encoded by the PLEKHO1 gene.[1][2]{{PBB_Summary
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}}InteractionsPLEKHO1 has been shown to interact with Casein kinase 2, alpha 1[1] and SMURF1.[3] References1. ^1 {{cite journal |vauthors=Bosc DG, Graham KC, Saulnier RB, Zhang C, Prober D, Gietz RD, Litchfield DW | title = Identification and characterization of CKIP-1, a novel pleckstrin homology domain-containing protein that interacts with protein kinase CK2 | journal = J Biol Chem | volume = 275 | issue = 19 | pages = 14295–306 |date=Jun 2000 | pmid = 10799509 | pmc = | doi =10.1074/jbc.275.19.14295 }}
2. ^{{cite web | title = Entrez Gene: PLEKHO1 pleckstrin homology domain containing, family O member 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51177| accessdate = }}
3. ^{{cite journal |last=Lu |first=Kefeng |authorlink= |author2=Yin Xiushan |author3=Weng Tujun |author4=Xi Shenli |author5=Li Li |author6=Xing Guichun |author7=Cheng Xuan |author8=Yang Xiao |author9=Zhang Lingqiang |author10=He Fuchu |date=Aug 2008 |title=Targeting WW domains linker of HECT-type ubiquitin ligase Smurf1 for activation by CKIP-1 |journal=Nat. Cell Biol. |volume=10 |issue=8 |pages=994–1002 |publisher= |location = England| issn = | pmid = 18641638 |doi = 10.1038/ncb1760 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}
Further reading{{refbegin | 2}}- {{cite journal |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
- {{cite journal |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 }}
- {{cite journal |vauthors=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=10.1101/gr.143000 | pmc=310948 }}
- {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |bibcode=2002PNAS...9916899M }}
- {{cite journal |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
- {{cite journal |vauthors=Olsten ME, Canton DA, Zhang C, etal |title=The Pleckstrin homology domain of CK2 interacting protein-1 is required for interactions and recruitment of protein kinase CK2 to the plasma membrane |journal=J. Biol. Chem. |volume=279 |issue= 40 |pages= 42114–27 |year= 2004 |pmid= 15254037 |doi= 10.1074/jbc.M407628200 }}
- {{cite journal |vauthors=Wiemann S, Arlt D, Huber W, etal |title=From ORFeome to biology: a functional genomics pipeline |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136–44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 | pmc=528930 }}
- {{cite journal |vauthors=Zhang L, Xing G, Tie Y, etal |title=Role for the pleckstrin homology domain-containing protein CKIP-1 in AP-1 regulation and apoptosis |journal=EMBO J. |volume=24 |issue= 4 |pages= 766–78 |year= 2005 |pmid= 15706351 |doi= 10.1038/sj.emboj.7600532 | pmc=549613 }}
- {{cite journal |vauthors=Barrios-Rodiles M, Brown KR, Ozdamar B, etal |title=High-throughput mapping of a dynamic signaling network in mammalian cells |journal=Science |volume=307 |issue= 5715 |pages= 1621–5 |year= 2005 |pmid= 15761153 |doi= 10.1126/science.1105776 |bibcode=2005Sci...307.1621B }}
- {{cite journal |vauthors=Canton DA, Olsten ME, Kim K, etal |title=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 |journal=Mol. Cell. Biol. |volume=25 |issue= 9 |pages= 3519–34 |year= 2005 |pmid= 15831458 |doi= 10.1128/MCB.25.9.3519-3534.2005 | pmc=1084316 |url=http://digitalcommons.wustl.edu/cgi/viewcontent.cgi?article=3252&context=open_access_pubs }}
- {{cite journal |vauthors=Zhang L, Tie Y, Tian C, etal |title=CKIP-1 recruits nuclear ATM partially to the plasma membrane through interaction with ATM |journal=Cell. Signal. |volume=18 |issue= 9 |pages= 1386–95 |year= 2007 |pmid= 16325375 |doi= 10.1016/j.cellsig.2005.10.017 }}
- {{cite journal |vauthors=Mehrle A, Rosenfelder H, Schupp I, etal |title=The LIFEdb database in 2006 |journal=Nucleic Acids Res. |volume=34 |issue= Database issue |pages= D415–8 |year= 2006 |pmid= 16381901 |doi= 10.1093/nar/gkj139 | pmc=1347501 }}
- {{cite journal |vauthors=Lim J, Hao T, Shaw C, etal |title=A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration |journal=Cell |volume=125 |issue= 4 |pages= 801–14 |year= 2006 |pmid= 16713569 |doi= 10.1016/j.cell.2006.03.032 }}
- {{cite journal |vauthors=Canton DA, Olsten ME, Niederstrasser H, etal |title=The role of CKIP-1 in cell morphology depends on its interaction with actin-capping protein |journal=J. Biol. Chem. |volume=281 |issue= 47 |pages= 36347–59 |year= 2007 |pmid= 16987810 |doi= 10.1074/jbc.M607595200 | pmc=2583070 }}
- {{cite journal |vauthors=Zhang L, Tang Y, Tie Y, etal |title=The PH domain containing protein CKIP-1 binds to IFP35 and Nmi and is involved in cytokine signaling |journal=Cell. Signal. |volume=19 |issue= 5 |pages= 932–44 |year= 2007 |pmid= 17197158 |doi= 10.1016/j.cellsig.2006.11.002 }}
- {{cite journal |vauthors=Tokuda E, Fujita N, Oh-hara T, etal |title=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 |journal=Cancer Res. |volume=67 |issue= 20 |pages= 9666–76 |year= 2007 |pmid= 17942896 |doi= 10.1158/0008-5472.CAN-07-1050 }}
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