PLEKHO1

Pleckstrin homology domain containing, family O member 1
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 3AA1​
Identifiers
Symbols	PLEKHO1 ; CKIP-1; CKIP1; JBP; OC120
External IDs	OMIM: 608335 MGI: 1914470 HomoloGene: 9448 GeneCards: PLEKHO1 Gene
Gene ontology Molecular function • protein binding Cellular component • nucleus • cytoplasm • plasma membrane Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	51177	67220
Ensembl	ENSG00000023902	ENSMUSG00000015745
UniProt	Q53GL0	Q9JIY0
RefSeq (mRNA)	NM_001304722	NM_023320
RefSeq (protein)	NP_001291651	NP_075809
Location (UCSC)	Chr 1: 150.15 – 150.16 Mb	Chr 3: 95.99 – 96 Mb
PubMed search

Pleckstrin homology domain-containing family O member 1 is a protein that in humans is encoded by the PLEKHO1 gene.^[1][2]

Interactions

PLEKHO1 has been shown to interact with Casein kinase 2, alpha 1^[1] and SMURF1.^[3]

References

1. Bosc DG, Graham KC, Saulnier RB, Zhang C, Prober D, Gietz RD, Litchfield DW (Jun 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. doi:10.1074/jbc.275.19.14295. PMID 10799509.
2. "Entrez Gene: PLEKHO1 pleckstrin homology domain containing, family O member 1".
3. Lu, Kefeng; Yin Xiushan; Weng Tujun; Xi Shenli; Li Li; Xing Guichun; Cheng Xuan; Yang Xiao; Zhang Lingqiang; He Fuchu (Aug 2008). "Targeting WW domains linker of HECT-type ubiquitin ligase Smurf1 for activation by CKIP-1". Nat. Cell Biol. (England) 10 (8): 994–1002. doi:10.1038/ncb1760. PMID 18641638.

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. doi:10.1016/0378-1119(94)90802-8. 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. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. 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. PMC 139241. 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. PMC 528930. 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. PMC 549613. 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. PMC 1084316. 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. PMC 1347501. 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. PMC 2583070. 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.