PLEKHO1

PLEKHO1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPLEKHO1, CKIP-1, OC120, CKIP1, JBP, pleckstrin homology domain containing O1
External IDsMGI: 1914470 HomoloGene: 9448 GeneCards: PLEKHO1
Gene location (Human)
Chr.Chromosome 1 (human)[1]
Band1q21.2Start150,149,183 bp[1]
End150,164,720 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

51177

67220

Ensembl

ENSG00000023902

ENSMUSG00000015745

UniProt

Q53GL0

Q9JIY0

RefSeq (mRNA)

NM_016274
NM_001304722
NM_001304723
NM_001304724

NM_023320

RefSeq (protein)

NP_001291651
NP_001291652
NP_001291653
NP_057358

NP_075809

Location (UCSC)Chr 1: 150.15 – 150.16 MbChr 3: 95.99 – 96 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Pleckstrin homology domain-containing family O member 1 is a protein that in humans is encoded by the PLEKHO1 gene.[5][6]

Interactions

PLEKHO1 has been shown to interact with Casein kinase 2, alpha 1[5] and SMURF1.[7]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000023902 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000015745 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. 1 2 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.
  6. ↑ "Entrez Gene: PLEKHO1 pleckstrin homology domain containing, family O member 1".
  7. ↑ 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2005Sci...307.1621B. 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.


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