KH

K homology RNA-binding domain
KH
SMART accession number:SM00322
Description:
Interpro abstract (IPR004087):

The K homology (KH) domain was first identified in the human heterogeneous nuclear ribonucleoprotein (hnRNP) K. An evolutionarily conserved sequence of around 70 amino acids, the KH domain is present in a wide variety of nucleic acid-binding proteins. The KH domain binds RNA, and can function in RNA recognition (PUBMED:17437720). It is found in multiple copies in several proteins, where they can function cooperatively or independently. For example, in the AU-rich element RNA-binding protein KSRP, which has 4 KH domains, KH domains 3 and 4 behave as independent binding modules to interact with different regions of the AU-rich RNA targets (PUBMED:17437720). The solution structure of the first KH domain of FMR1 (PUBMED:9302998) and of the C-terminal KH domain of hnRNP K (PUBMED:10369774) determined by nuclear magnetic resonance (NMR) revealed a beta-alpha-alpha-beta-beta-alpha structure. Proteins containing KH domains include:

  • Bacterial and organelle PNPases (PUBMED:17337072).
  • Archaeal and eukaryotic exosome subunits (PUBMED:17159918).
  • Eukaryotic and prokaryotic RS3 ribosomal proteins (PUBMED:1160884).
  • Vertebrate fragile X mental retardation protein 1 (FMR1) (PUBMED:15805463).
  • Vigilin, which has 14 KH domains (PUBMED:14618268).
  • AU-rich element RNA-binding protein KSRP.
  • hnRNP K, which contains 3 KH domains.
  • Human onconeural ventral antigen-1 (NOVA-1) (PUBMED:10368286).

More information about these proteins can be found at Protein of the Month: RNA Exosomes.

GO function:RNA binding (GO:0003723)
Family alignment:
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There are 8776 KH domains in 5116 proteins in SMART's nrdb database.

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