PSCD4

PSCD4

Pleckstrin homology, Sec7 and coiled-coil domains 4, also known as PSCD4, is a human gene.cite web | title = Entrez Gene: PSCD4 pleckstrin homology, Sec7 and coiled-coil domains 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27128| accessdate = ]

PBB_Summary
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summary_text = Pleckstrin homology, Sec7 and coiled/coil domains 4 (PSCD4) is a member of the PSCD family. Members of this family have identical structural organization that consists of an N-terminal coiled-coil motif, a central Sec7 domain, and a C-terminal pleckstrin homology (PH) domain. The coiled-coil motif is involved in homodimerization, the Sec7 domain contains guanine-nucleotide exchange protein (GEP) activity, and the PH domain interacts with phospholipids and is responsible for association of PSCDs with membranes. Members of this family appear to mediate the regulation of protein sorting and membrane trafficking. The PSCD4 exhibits GEP activity in vitro with both ARF1 and ARF5 but is inactive with ARF6. The PSCD4 and PSCD1 gene structures are very similar.cite web | title = Entrez Gene: PSCD4 pleckstrin homology, Sec7 and coiled-coil domains 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27128| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Morishige M, Hashimoto S, Ogawa E, "et al." |title=GEP100 links epidermal growth factor receptor signalling to Arf6 activation to induce breast cancer invasion. |journal=Nat. Cell Biol. |volume=10 |issue= 1 |pages= 85–92 |year= 2008 |pmid= 18084281 |doi= 10.1038/ncb1672
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Collins JE, Wright CL, Edwards CA, "et al." |title=A genome annotation-driven approach to cloning the human ORFeome. |journal=Genome Biol. |volume=5 |issue= 10 |pages= R84 |year= 2005 |pmid= 15461802 |doi= 10.1186/gb-2004-5-10-r84
*cite journal | author=Beausoleil SA, Jedrychowski M, Schwartz D, "et al." |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130–5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Venkateswarlu K |title=Interaction protein for cytohesin exchange factors 1 (IPCEF1) binds cytohesin 2 and modifies its activity. |journal=J. Biol. Chem. |volume=278 |issue= 44 |pages= 43460–9 |year= 2003 |pmid= 12920129 |doi= 10.1074/jbc.M304078200
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Ogasawara M, Kim SC, Adamik R, "et al." |title=Similarities in function and gene structure of cytohesin-4 and cytohesin-1, guanine nucleotide-exchange proteins for ADP-ribosylation factors. |journal=J. Biol. Chem. |volume=275 |issue= 5 |pages= 3221–30 |year= 2000 |pmid= 10652308 |doi=
*cite journal | author=Dunham I, Shimizu N, Roe BA, "et al." |title=The DNA sequence of human chromosome 22. |journal=Nature |volume=402 |issue= 6761 |pages= 489–95 |year= 1999 |pmid= 10591208 |doi= 10.1038/990031
*cite journal | author=Trofatter JA, Long KR, Murrell JR, "et al." |title=An expression-independent catalog of genes from human chromosome 22. |journal=Genome Res. |volume=5 |issue= 3 |pages= 214–24 |year= 1996 |pmid= 8593609 |doi=

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  • Pleckstrin homology domain — Pfam box Symbol = PH Name = width =250 caption =PH domain of tyrosine protein kinase BTK Pfam= PF00169 InterPro= IPR001849 SMART= PH PROSITE=PDOC50003 SCOP = 1dyn TCDB = OPM family= 51 OPM protein= 1pls PDB=PDB3|1dynB:520 625 PDB3|2dynA:520 625… …   Wikipedia

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