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FYVE zinc finger
Early endosome antigen 1 (EEA1) dimer with lipids
Symbol FYVE
Pfam PF01363
InterPro IPR000306
SCOP 1vfy
OPM family 62
OPM protein 1vfy

FYVE zinc finger domain is named after four cysteine-rich proteins that it has been found in: Fab 1 (yeast orthologue of PIKfyve), YOTB, Vac 1 (vesicle transport protein), and EEA1.

The FYVE finger binds two zinc ions. The FYVE finger has eight potential zinc coordinating cysteine positions and is characterized by having basic amino acids around the cysteines. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue.

FYVE domains bind Phosphatidylinositol 3-phosphate, in a way dependent on its metal ion coordination and basic amino acids. It has been speculated these bindings cause conformational changes or regulate protein-protein or lipid-protein interactions[1].

The FYVE finger is structurally similar to the RING domain and the PHD finger.

The FYVE domain has been connected to vacuolar protein sorting and endosome function.[1]



The following is a list of human proteins containing this domain:

Further reading

  • Endosomal localization of the autoantigen EEA1 is mediated by a zinc-binding FYVE finger. Stenmark H, Aasland R, Toh BH, D'Arrigo A; J Biol Chem 1996;271:24048-24054. PubMed
  • FYVE fingers bind PtdIns(3)P. Gaullier JM, Simonsen A, D'Arrigo A, Bremnes B, Stenmark H, Aasland R; Nature 1998;394:432-433. PubMed
  • FYVE-finger proteins - effectors of an inositol lipid. Stenmark H, Aasland R; J Cell Sci 1999;112:4175-4183. PubMed


  1. ^ a b Leevers SJ, Vanhaesebroeck B, Waterfield MD (April 1999). "Signalling through phosphoinositide 3-kinases: the lipids take centre stage". Current Opinion in Cell Biology 11 (2): 219–25. doi:10.1016/S0955-0674(99)80029-5. PMID 10209156.  

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