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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.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

PROSITE documentation PDOC51048
SGS domain profile


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PURL: https://purl.expasy.org/prosite/documentation/PDOC51048

Description

The SGT1-specific (SGS) domain is a module of ~90 amino acids, which was initially identified in eukaryotic SGT1 proteins [1]. It was latter also found in calcyclin-binding proteins [2]. The SGS domain has been shown to bind to proteins of the S100 family, which are thought to function as sensors of calcium ion concentration in the cell [2].

Some proteins known to contain a SGS domain are listed below:

  • Yeast suppressor of the G2 allele of skp1 (SGT1). It is required for cell cycle progression at the G1/S-phase and G2/M-phase transitions. It associates with Skp1 and regulates its function in the Skp1/Cullin1/F-box complex ubiquitin ligase and in kinetochore complexes.
  • Arabidopsis thaliana SGT1a and SGT1b.
  • Mammalian SGT1.
  • Mammalian calcyclin-binding protein/Siah-1-interacting protein (CacyBP/SIP), a component of a novel pathway of β-catenin ubiquitination.

The profile we developed covers the entire SGS domain.

Last update:

December 2004 / First entry.

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Technical section

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

SGS, PS51048; SGS domain profile  (MATRIX)


References

1AuthorsAzevedo C. Sadanandom A. Kitagawa K. Freialdenhoven A. Shirasu K. Schulze-Lefert P.
TitleThe RAR1 interactor SGT1, an essential component of R gene-triggered disease resistance.
SourceScience 295:2073-2076(2002).
PubMed ID11847307
DOI10.1126/science.1067554;

2AuthorsNowotny M. Spiechowicz M. Jastrzebska B. Filipek A. Kitagawa K. Kuznicki J.
TitleCalcium-regulated interaction of Sgt1 with S100A6 (calcyclin) and other S100 proteins.
SourceJ. Biol. Chem. 278:26923-26928(2003).
PubMed ID12746458
DOI10.1074/jbc.M211518200;



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