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Cytohesin 1
Protein PSCD1 PDB 1bc9.png
PDB rendering based on 1bc9.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols CYTH1 ; B2-1; CYTOHESIN-1; D17S811E; PSCD1; SEC7
External IDs OMIM182115 MGI1334257 HomoloGene31262 GeneCards: CYTH1 Gene
RNA expression pattern
PBB GE PSCD1 202880 s at tn.png
PBB GE PSCD1 202879 s at tn.png
More reference expression data
Species Human Mouse
Entrez 9267 19157
Ensembl ENSG00000108669 ENSMUSG00000017132
UniProt Q15438 Q9QX11
RefSeq (mRNA) NM_001292018 NM_001112699
RefSeq (protein) NP_001278947 NP_001106169
Location (UCSC) Chr 17:
76.67 – 76.78 Mb
Chr 11:
118.13 – 118.25 Mb
PubMed search [1] [2]

Cytohesin-1 formerly known as Pleckstrin homology, Sec7 and coiled/coil domains 1 (PSCD1) is a protein that in humans is encoded by the CYTH1 gene.[1][2][3]


Cytohesin-1 (CYTH1) is a member of the cytohesin 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 CYTHs with membranes. Members of this family appear to mediate the regulation of protein sorting and membrane trafficking. The CYTH1 is highly expressed in natural killer and peripheral T cells, and regulates the adhesiveness of integrins at the plasma membrane of lymphocytes. CYTH1 protein is 83% homologous to CYTH2.[3]


CYTH1 has been shown to interact with:


  1. ^ Liu L, Pohajdak B (September 1992). "Cloning and sequencing of a human cDNA from cytolytic NK/T cells with homology to yeast SEC7". Biochim Biophys Acta 1132 (1): 75–8. doi:10.1016/0167-4781(92)90055-5. PMID 1511013. 
  2. ^ Dixon B, Mansour M, Pohajdak B (April 1993). "Assignment of human B2-1 gene (D17S811E) to chromosome 17qter by PCR analysis of somatic cell hybrids and fluorescence in situ hybridization". Cytogenet Cell Genet 63 (1): 42–4. doi:10.1159/000133498. PMID 8449036. 
  3. ^ a b "Entrez Gene: PSCD1 pleckstrin homology, Sec7 and coiled-coil domains 1(cytohesin 1)". 
  4. ^ Schürmann, A; Schmidt M, Asmus M, Bayer S, Fliegert F, Koling S, Massmann S, Schilf C, Subauste M C, Voss M, Jakobs K H, Joost H G (April 1999). "The ADP-ribosylation factor (ARF)-related GTPase ARF-related protein binds to the ARF-specific guanine nucleotide exchange factor cytohesin and inhibits the ARF-dependent activation of phospholipase D". J. Biol. Chem. (UNITED STATES) 274 (14): 9744–51. doi:10.1074/jbc.274.14.9744. ISSN 0021-9258. PMID 10092663. 
  5. ^ Rietzler M, Bittner M, Kolanus W, Schuster A, Holzmann B (October 1998). "The human WD repeat protein WAIT-1 specifically interacts with the cytoplasmic tails of beta7-integrins". J. Biol. Chem. 273 (42): 27459–66. doi:10.1074/jbc.273.42.27459. PMID 9765275. 
  6. ^ Geiger C, Nagel W, Boehm T, van Kooyk Y, Figdor CG, Kremmer E, Hogg N, Zeitlmann L, Dierks H, Weber KS, Kolanus W (June 2000). "Cytohesin-1 regulates beta-2 integrin-mediated adhesion through both ARF-GEF function and interaction with LFA-1". EMBO J. 19 (11): 2525–36. doi:10.1093/emboj/19.11.2525. PMC 212768. PMID 10835351. 
  7. ^ Vitale N, Pacheco-Rodriguez G, Ferrans VJ, Riemenschneider W, Moss J, Vaughan M (July 2000). "Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1)". J. Biol. Chem. 275 (28): 21331–9. doi:10.1074/jbc.M909642199. PMID 10748148. 

Further reading[edit]