PLEKHA8

Protein-coding gene in the species Homo sapiens
PLEKHA8
Identifiers
AliasesPLEKHA8, FAPP2, pleckstrin homology domain containing A8
External IDsOMIM: 608639; MGI: 2681164; HomoloGene: 32284; GeneCards: PLEKHA8; OMA:PLEKHA8 - orthologs
Gene location (Human)
Chromosome 7 (human)
Chr.Chromosome 7 (human)[1]
Chromosome 7 (human)
Genomic location for PLEKHA8
Genomic location for PLEKHA8
Band7p14.3Start30,027,404 bp[1]
End30,130,483 bp[1]
Gene location (Mouse)
Chromosome 6 (mouse)
Chr.Chromosome 6 (mouse)[2]
Chromosome 6 (mouse)
Genomic location for PLEKHA8
Genomic location for PLEKHA8
Band6|6 B3Start54,572,096 bp[2]
End54,622,824 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 6: 54.57 – 54.62 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. ^ a b c GRCh38: Ensembl release 89: ENSG00000106086 – Ensembl, May 2017
  2. ^ a b c 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. S2CID 25874412.
  • 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. Bibcode:2007Natur.449...62D. doi:10.1038/nature06097. PMID 17687330. S2CID 4387982.
  • 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. Bibcode:2009PNAS..10621121C. 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.


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