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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

KLHL12  -  kelch-like family member 12

Homo sapiens

Synonyms: C3IP1, CUL3-interacting protein 1, DKIR, DKIR homolog, Kelch-like protein 12, ...
 
 
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Disease relevance of KLHL12

  • Finally, domain analysis revealed that both the N-terminal POZ (poxviruses and zinc fingers) and intervening region (IVR) domains of hDKIR are essential for ring-like structure activity, suggesting that the development of the ring-like structure is independent of the ability to bind actin [1].
 

High impact information on KLHL12

  • The KLHL12-Cullin-3 ubiquitin ligase negatively regulates the Wnt-beta-catenin pathway by targeting Dishevelled for degradation [2].
  • This study warranted clinical evaluations of autoantibodies against IFI16, KLHL12 and KLHL7 in combination with anti-SS-B/La autoantibodies [3].
 

Associations of KLHL12 with chemical compounds

 

Analytical, diagnostic and therapeutic context of KLHL12

  • Here we report the molecular cloning and characterization of one of these genes, which encodes a novel human kelch protein containing 568 amino acid residues, termed hDKIR [1].

References

  1. hDKIR, a human homologue of the Drosophila kelch protein, involved in a ring-like structure. Mai, A., Jung, S.K., Yonehara, S. Exp. Cell Res. (2004) [Pubmed]
  2. The KLHL12-Cullin-3 ubiquitin ligase negatively regulates the Wnt-beta-catenin pathway by targeting Dishevelled for degradation. Angers, S., Thorpe, C.J., Biechele, T.L., Goldenberg, S.J., Zheng, N., MacCoss, M.J., Moon, R.T. Nat. Cell Biol. (2006) [Pubmed]
  3. Identification of specific autoantigens in Sjögren's syndrome by SEREX. Uchida, K., Akita, Y., Matsuo, K., Fujiwara, S., Nakagawa, A., Kazaoka, Y., Hachiya, H., Naganawa, Y., Oh-Iwa, I., Ohura, K., Saga, S., Kawai, T., Matsumoto, Y., Shimozato, K., Kozaki, K. Immunology (2005) [Pubmed]
  4. BTB Protein KLHL12 targets the dopamine D4 receptor for ubiquitination by a Cul3-based E3 ligase. Rondou, P., Haegeman, G., Vanhoenacker, P., Van Craenenbroeck, K. J. Biol. Chem. (2008) [Pubmed]
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