PLEKHO1

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

PLEKHO1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3AA1
Identifiers
Aliases	PLEKHO1, CKIP-1, OC120, CKIP1, JBP, pleckstrin homology domain containing O1
External IDs	OMIM: 608335; MGI: 1914470; HomoloGene: 9448; GeneCards: PLEKHO1; OMA:PLEKHO1 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1q21.2 Start 150,149,183 bp End 150,164,720 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3|3 F2.1 Start 95,895,741 bp End 95,903,313 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte gastric mucosa granulocyte muscle layer of sigmoid colon left testis right testis popliteal artery tibial arteries right coronary artery ganglionic eminence Top expressed in genital tubercle tail of embryo ventricular zone decidua gastrula ganglionic eminence superior frontal gyrus primary visual cortex cerebellar cortex internal carotid artery More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding Cellular component cytoplasm ruffle membrane plasma membrane muscle cell projection membrane membrane nucleus Biological process myoblast migration myoblast fusion lamellipodium morphogenesis regulation of cell shape Sources:Amigo / QuickGO
Orthologs Species Human Mouse 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 Mb Chr 3: 95.9 – 95.9 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Interactions

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

Further reading

• Maruyama K, Sugano S (January 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, Suyama A, Sugano S (October 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 (November 2000). "DNA cloning using in vitro site-specific recombination". Genome Research. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
• Olsten ME, Canton DA, Zhang C, Walton PA, Litchfield DW (October 2004). "The Pleckstrin homology domain of CK2 interacting protein-1 is required for interactions and recruitment of protein kinase CK2 to the plasma membrane". The Journal of Biological Chemistry. 279 (40): 42114–27. doi:10.1074/jbc.M407628200. PMID 15254037.
• Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, Bechtel S, Sauermann M, Korf U, Pepperkok R, Sültmann H, Poustka A (October 2004). "From ORFeome to biology: a functional genomics pipeline". Genome Research. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
• Zhang L, Xing G, Tie Y, Tang Y, Tian C, Li L, Sun L, Wei H, Zhu Y, He F (February 2005). "Role for the pleckstrin homology domain-containing protein CKIP-1 in AP-1 regulation and apoptosis". The EMBO Journal. 24 (4): 766–78. doi:10.1038/sj.emboj.7600532. PMC 549613. PMID 15706351.
• Barrios-Rodiles M, Brown KR, Ozdamar B, Bose R, Liu Z, Donovan RS, Shinjo F, Liu Y, Dembowy J, Taylor IW, Luga V, Przulj N, Robinson M, Suzuki H, Hayashizaki Y, Jurisica I, Wrana JL (March 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. S2CID 39457788.
• Canton DA, Olsten ME, Kim K, Doherty-Kirby A, Lajoie G, Cooper JA, Litchfield DW (May 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". Molecular and Cellular Biology. 25 (9): 3519–34. doi:10.1128/MCB.25.9.3519-3534.2005. PMC 1084316. PMID 15831458.
• Zhang L, Tie Y, Tian C, Xing G, Song Y, Zhu Y, Sun Z, He F (September 2006). "CKIP-1 recruits nuclear ATM partially to the plasma membrane through interaction with ATM". Cellular Signalling. 18 (9): 1386–95. doi:10.1016/j.cellsig.2005.10.017. PMID 16325375.
• Mehrle A, Rosenfelder H, Schupp I, del Val C, Arlt D, Hahne F, Bechtel S, Simpson J, Hofmann O, Hide W, Glatting KH, Huber W, Pepperkok R, Poustka A, Wiemann S (January 2006). "The LIFEdb database in 2006". Nucleic Acids Research. 34 (Database issue): D415-8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.
• Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M, Zoghbi HY (May 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. S2CID 13709685.
• Canton DA, Olsten ME, Niederstrasser H, Cooper JA, Litchfield DW (November 2006). "The role of CKIP-1 in cell morphology depends on its interaction with actin-capping protein". The Journal of Biological Chemistry. 281 (47): 36347–59. doi:10.1074/jbc.M607595200. PMC 2583070. PMID 16987810.
• Zhang L, Tang Y, Tie Y, Tian C, Wang J, Dong Y, Sun Z, He F (May 2007). "The PH domain containing protein CKIP-1 binds to IFP35 and Nmi and is involved in cytokine signaling". Cellular Signalling. 19 (5): 932–44. doi:10.1016/j.cellsig.2006.11.002. PMID 17197158.
• Tokuda E, Fujita N, Oh-hara T, Sato S, Kurata A, Katayama R, Itoh T, Takenawa T, Miyazono K, Tsuruo T (October 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 Research. 67 (20): 9666–76. doi:10.1158/0008-5472.CAN-07-1050. PMID 17942896.