KEN domain (IPR010513)

Short name: KEN_dom

Overlapping homologous superfamilies

Domain relationships



The proteins listed below share a common architecture with a protein kinase homology domain (see PDOC00100) followed by an ~135-residue globular kinase-extension nuclease (KEN) domain made of eight helices [PMID: 18191223]:

  • Mammalian 2-5A-dependent RNase or RNase L (EC 3.1.26.-), an interferon-induced enzyme implicated in both the molecular mechanisms of interferon action and the fundamental control of RNA stability. 2-5A-dependent RNase is a unique enzyme in that it requires 2-5A, unusual oligoadenylates with 2',5'-phosphodiester linkages. RNase L is catalytically active only after binding to an unusual activator molecule containing a 5'-phosphorylated 2', 5'-linked oligoadenylate (2-5A), in the N-terminal half. RNase L consists of three domains, namely the N-terminal ankyrin repeat domain (see PDOC50088), the protein kinase homology domain, and the C-terminal KEN domain [PMID: 7680958, PMID: 15385955, PMID: 18426919].
  • Eukaryotic Ire1/Ern1, an ancient transmembrane sensor of endoplasmic reticulum (ER) stress with dual protein kinase and ribonuclease activities. In response to ER stress Ire1/Ern1 catalyzes the splicing of target mRNAs in a spliceosome-independent manner. Ire1/Ern1 is a type 1 transmembrane receptor consisting of an N-terminal ER luminal domain, a transmembrane segment and a cytoplasmic region. The cytoplasmic region encompasses a protein kinase domain followed by a C-terminal KEN domain [PMID: 18191223, PMID: 9637683].

The dimerisation of the kinase domain activates the ribonuclease function of the KEN domain [PMID: 18191223].

GO terms

Biological Process

GO:0006397 mRNA processing

Molecular Function

GO:0004540 ribonuclease activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles