PLEKHA8

PLEKHA8
Identifiers
AliasesPLEKHA8, FAPP2, pleckstrin homology domain containing A8
External IDsMGI: 2681164 HomoloGene: 32284 GeneCards: PLEKHA8
Gene location (Human)
Chr.Chromosome 7 (human)[1]
Band7p14.3Start30,027,404 bp[1]
End30,130,483 bp[1]
Orthologs
SpeciesHumanMouse
Entrez

84725

231999

Ensembl

ENSG00000106086

ENSMUSG00000005225

UniProt

Q96JA3

Q80W71

RefSeq (mRNA)

NM_001001335
NM_001164361

RefSeq (protein)

NP_001001335
NP_001157833

Location (UCSC)Chr 7: 30.03 – 30.13 MbChr 6: 54.6 – 54.65 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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


References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000106086 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000005225 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  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.


This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.