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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
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Amos Bairoch

PROSITE documentation PDOC51229
DCUN1 domain profile


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PURL: https://purl.expasy.org/prosite/documentation/PDOC51229

Description

The DCUN1 domain is an ~190-residue module found in the eukaryotic defective in cullin neddylation (DCN) protein family, which includes:

  • Yeast DCN1.
  • Vertebrate DCN1-like protein 1.
  • Vertebrate DCN1-like protein 2.
  • Vertebrate DCN1-like protein 4.

Proteins of the DCN family may contribute to neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes, which are multi-protein complexes required for polyubiquitination and subsequent degradation of target proteins by the 26S proteasome [1]. Although the DCUN1 domain function is unknown, it has been suggested that it has features of a basic helix-loop-helix leucine zipper (bHLH-ZIP) domain [2].

The DCUN1 domain can be found in association with an UBA-like domain [1].

The profile we developed covers the entire DCUN1 domain.

Last update:

July 2006 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

DCUN1, PS51229; DCUN1 domain profile  (MATRIX)


References

1AuthorsKurz T. Oezlu N. Rudolf F. O'Rourke S.M. Luke B. Hofmann K. Hyman A.A. Bowerman B. Peter M.
TitleThe conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S. cerevisiae.
SourceNature 435:1257-1261(2005).
PubMed ID15988528
DOI10.1038/nature03662

2AuthorsPourcel C. Jaubert J. Hadchouel M. Wu X. Schweizer J.
TitleA new family of genes and pseudogenes potentially expressing testis- and brain-specific leucine zipper proteins in man and mouse.
SourceGene 249:105-113(2000).
PubMed ID10831844



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