PLEKHA8

Pleckstrin homology domain containing A8 is a protein that in humans is encoded by the PLEKHA8 gene. [5]

PLEKHA8
Identifiers
Aliases	PLEKHA8, FAPP2, pleckstrin homology domain containing A8
External IDs	OMIM: 608639 MGI: 2681164 HomoloGene: 32284 GeneCards: PLEKHA8
Gene location (Human) Chr. Chromosome 7 (human)[1] Band 7p14.3 Start 30,027,404 bp[1] End 30,130,483 bp[1]
Gene location (Mouse) Chr. Chromosome 6 (mouse)[2] Band 6|6 B3 Start 54,595,111 bp[2] End 54,645,839 bp[2]
Gene ontology Molecular function • phosphatidylinositol-4-phosphate binding • ceramide binding • lipid binding • glycolipid transporter activity • glycolipid binding • intermembrane lipid transfer activity • ceramide 1-phosphate binding • ceramide 1-phosphate transporter 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: 54.6 – 54.65 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

References

1. GRCh38: Ensembl release 89: ENSG00000106086 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000005225 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: Pleckstrin homology domain containing A8". Retrieved 2017-06-09.

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.