Profilin 1

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Protein PFN1 PDB 1awi.png
Available structures
PDB Ortholog search: PDBe RCSB
Aliases PFN1, ALS18, Profilin 1
External IDs MGI: 97549 HomoloGene: 3684 GeneCards: PFN1
RNA expression pattern
PBB GE PFN1 200634 at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 17: 4.95 – 4.95 Mb Chr 11: 70.65 – 70.65 Mb
PubMed search [1] [2]
View/Edit Human View/Edit Mouse

Profilin-1 is a protein that in humans is encoded by the PFN1 gene.[3][4]


The protein encoded by this gene is a ubiquitous actin monomer-binding protein belonging to the profilin family. It is thought to regulate actin polymerization in response to extracellular signals. Deletion of this gene is associated with Miller-Dieker syndrome.[5]


Profilin 1 has been shown to interact with:


  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ Kwiatkowski DJ, Bruns GA (May 1988). "Human profilin. Molecular cloning, sequence comparison, and chromosomal analysis". J Biol Chem. 263 (12): 5910–5. PMID 3356709. 
  4. ^ Kwiatkowski DJ, Aklog L, Ledbetter DH, Morton CC (April 1990). "Identification of the functional profilin gene, its localization to chromosome subband 17p13.3, and demonstration of its deletion in some patients with Miller-Dieker syndrome". Am J Hum Genet. 46 (3): 559–67. PMC 1683621Freely accessible. PMID 1968707. 
  5. ^ "Entrez Gene: PFN1 profilin 1". 
  6. ^ Yayoshi-Yamamoto S, Taniuchi I, Watanabe T (September 2000). "FRL, a novel formin-related protein, binds to Rac and regulates cell motility and survival of macrophages". Mol. Cell. Biol. 20 (18): 6872–81. PMC 86228Freely accessible. PMID 10958683. doi:10.1128/mcb.20.18.6872-6881.2000. 
  7. ^ Boettner B, Govek EE, Cross J, Van Aelst L (August 2000). "The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin". Proc. Natl. Acad. Sci. U.S.A. 97 (16): 9064–9. PMC 16822Freely accessible. PMID 10922060. doi:10.1073/pnas.97.16.9064. 
  8. ^ Harbeck B, Hüttelmaier S, Schluter K, Jockusch BM, Illenberger S (October 2000). "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. 275 (40): 30817–25. PMID 10882740. doi:10.1074/jbc.M005066200. 
  9. ^ Miki H, Suetsugu S, Takenawa T (December 1998). "WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac". EMBO J. 17 (23): 6932–41. PMC 1171041Freely accessible. PMID 9843499. doi:10.1093/emboj/17.23.6932. 
  10. ^ Mimuro H, Suzuki T, Suetsugu S, Miki H, Takenawa T, Sasakawa C (September 2000). "Profilin is required for sustaining efficient intra- and intercellular spreading of Shigella flexneri". J. Biol. Chem. 275 (37): 28893–901. PMID 10867004. doi:10.1074/jbc.M003882200. 
  11. ^ Suetsugu S, Miki H, Takenawa T (November 1998). "The essential role of profilin in the assembly of actin for microspike formation". EMBO J. 17 (22): 6516–26. PMC 1170999Freely accessible. PMID 9822597. doi:10.1093/emboj/17.22.6516. 

Further reading[edit]