PLEKHA8

PLEKHA8
Identifiers
Aliases	PLEKHA8, FAPP2, pleckstrin homology domain containing A8
External IDs	OMIM: 608639; MGI: 2681164; HomoloGene: 32284; GeneCards: PLEKHA8; OMA:PLEKHA8 - orthologs
Gene location (Human) Chr. Chromosome 7 (human) Band 7p14.3 Start 30,027,404 bp End 30,130,483 bp
Gene location (Mouse) Chr. Chromosome 6 (mouse) Band 6|6 B3 Start 54,572,096 bp End 54,622,824 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ventricular zone placenta ganglionic eminence mucosa of ileum bone marrow cells testicle visceral pleura gonad epithelium of colon parietal pleura Top expressed in hand secondary oocyte zygote primary oocyte superior cervical ganglion Gonadal ridge abdominal wall endocardial cushion spermatocyte vas deferens More reference expression data BioGPS n/a
Gene ontology Molecular function phosphatidylinositol-4-phosphate binding ceramide binding lipid binding glycolipid transfer activity glycolipid binding lipid transfer activity ceramide 1-phosphate binding ceramide 1-phosphate transfer activity Cellular component cytoplasm trans-Golgi network membrane Golgi membrane nucleoplasm Golgi apparatus cytosol Biological process protein transport ER to Golgi ceramide transport lipid transport glycolipid transport phosphatidylinositol biosynthetic process intermembrane lipid transfer ceramide transport ceramide 1-phosphate transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 84725 231999 Ensembl ENSG00000106086 ENSMUSG00000005225 UniProt Q96JA3 Q80W71 RefSeq (mRNA) NM_001197026 NM_001197027 NM_032639 NM_001350973 NM_001350974 NM_001350975 NM_001363473 NM_001363474 NM_001001335 NM_001164361 RefSeq (protein) NP_001183955 NP_001183956 NP_116028 NP_001337902 NP_001337903 NP_001337904 NP_001350402 NP_001350403 NP_001001335 NP_001157833 Location (UCSC) Chr 7: 30.03 – 30.13 Mb Chr 6: 54.57 – 54.62 Mb PubMed search
Wikidata
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Pleckstrin homology domain containing A8 is a protein that in humans is encoded by the PLEKHA8 gene.

Further reading

• Godi A, Di Campli A, Konstantakopoulos A, Di Tullio G, Alessi DR, Kular GS, Daniele T, Marra P, Lucocq JM, De Matteis MA (2004). "FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P". Nat. Cell Biol. 6 (5): 393–404. doi:10.1038/ncb1119. PMID 15107860.
• Vieira OV, Verkade P, Manninen A, Simons K (2005). "FAPP2 is involved in the transport of apical cargo in polarized MDCK cells". J. Cell Biol. 170 (4): 521–6. doi:10.1083/jcb.200503078. PMC 2171512. PMID 16103222.
• Vieira OV, Gaus K, Verkade P, Fullekrug J, Vaz WL, Simons K (2006). "FAPP2, cilium formation, and compartmentalization of the apical membrane in polarized Madin-Darby canine kidney (MDCK) cells". Proc. Natl. Acad. Sci. U.S.A. 103 (49): 18556–61. doi:10.1073/pnas.0608291103. PMC 1693701. PMID 17116893.
• D'Angelo G, Polishchuk E, Di Tullio G, Santoro M, Di Campli A, Godi A, West G, Bielawski J, Chuang CC, van der Spoel AC, Platt FM, Hannun YA, Polishchuk R, Mattjus P, De Matteis MA (2007). "Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide". Nature. 449 (7158): 62–7. doi:10.1038/nature06097. PMID 17687330.
• Tritz R, Hickey MJ, Lin AH, Hadwiger P, Sah DW, Neuwelt EA, Mueller BM, Kruse CA (2009). "FAPP2 gene downregulation increases tumor cell sensitivity to Fas-induced apoptosis". Biochem. Biophys. Res. Commun. 383 (2): 167–71. doi:10.1016/j.bbrc.2009.03.126. PMC 3998642. PMID 19341712.
• Cao X, Coskun U, Rössle M, Buschhorn SB, Grzybek M, Dafforn TR, Lenoir M, Overduin M, Simons K (2009). "Golgi protein FAPP2 tubulates membranes". Proc. Natl. Acad. Sci. U.S.A. 106 (50): 21121–5. doi:10.1073/pnas.0911789106. PMC 2795549. PMID 19940249.
• D'Angelo G, Rega LR, De Matteis MA (2012). "Connecting vesicular transport with lipid synthesis: FAPP2". Biochim. Biophys. Acta. 1821 (8): 1089–95. doi:10.1016/j.bbalip.2012.01.003. PMC 4331668. PMID 22266015.