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PROSITE documentation PDOC51925

SWIB/MDM2 domain profile





Description

The SWIB/MDM2 domain is largely common in Eukaryota and SWIB/MDM2 proteins have been localized to the mitochondria, nucleus, chloroplast, and cytoplasm within a variety of organisms. Two broad groups of SWIB/MDM2 domains have been identified. The first group is involved in p53 binding and identified in MDM2 oncoproteins. The second group is identified in a variety of eukaryotic proteins and participates in chromatin remodeling, transcriptional regulation and unknown functions, such as that found in the mammalian BAF60b protein of the SWIB complex, the Saccharomyces cerevisiae SNF12 protein, the eukaryotic initiation factor 2 (eIF2) and the Arabidopsis thaliana At1g31760 protein for example. SWIB/MDM2 domains participate in activities such as protein-protein and chromatin-related interactions, but their precise functional role(s) in the cell are poorly characterized [1,2,3].

SWIB/MDM2 domains exhibit ‘twisted cleft’ topologies constituted by four helices, creating a ‘barrel’, capped by one or more β sheets (see <PDB:1YCQ>) [1,2,3].

The profile we developed covers the entire SWIB/MDM2 domain.

Last update:

April 2020 / First entry.

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Technical section

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

SWIB_MDM2, PS51925; SWIB/MDM2 domain profile  (MATRIX)


References

1AuthorsBennett-Lovsey R. Hart S.E. Shirai H. Mizuguchi K.
TitleThe SWIB and the MDM2 domains are homologous and share a common fold.
SourceBioinformatics 18:626-630(2002).
PubMed ID12016060
DOI10.1093/bioinformatics/18.4.626

2AuthorsVieira W.A. Coetzer T.L.
TitleLocalization and interactions of Plasmodium falciparum SWIB/MDM2 homologues.
SourceMalar. J. 15:32-32(2016).
PubMed ID26791088
DOI10.1186/s12936-015-1065-9

3AuthorsVaidya A.T. Lomakin I.B. Joseph N.N. Dmitriev S.E. Steitz T.A.
TitleCrystal Structure of the C-terminal Domain of Human eIF2D and Its Implications on Eukaryotic Translation Initiation.
SourceJ. Mol. Biol. 429:2765-2771(2017).
PubMed ID28736176
DOI10.1016/j.jmb.2017.07.015



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