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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 PDOC51518
SGF29 C-terminal domain profile


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PURL: https://purl.expasy.org/prosite/documentation/PDOC51518

Description

Eukaryotic SGF29 is a component of histone acetyltransferase (HAT) complexes TATA-binding protein-free TAF-containing (TFTC) and SPT3-TAF9-GCN5-acetyltransferase (STAGA) or SPT-ADA-GCN5-acetyltransferase (SAGA) [1]. The SGF29 C-terminal domain contains a double Tudor-like motif that selectively binds the H3K4me2/3 lysine methylation site on the N terminus of histone H3 [2,3].

Each Tudor domain consists of five twisted anti-parallel β strands forming a typical barrel-like fold (see <PDB:3MEA>). The tandem Tudor domains tightly pack against each other face-to-face with each Tudor domain harboring a negatively charged pocket accommodating the first residue alanine and methylated K4 residue of histone H3, respectively [3].

The profile we developed covers the entire SGF29 C-terminal domain.

Last update:

December 2011 / Profile and text revised.

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Technical section

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

SGF29_C, PS51518; SGF29 C-terminal domain profile  (MATRIX)


References

1AuthorsKurabe N. Katagiri K. Komiya Y. Ito R. Sugiyama A. Kawasaki Y. Tashiro F.
TitleDeregulated expression of a novel component of TFTC/STAGA histone acetyltransferase complexes, rat SGF29, in hepatocellular carcinoma: possible implication for the oncogenic potential of c-Myc.
SourceOncogene 26:5626-5634(2007).
PubMed ID17334388
DOI10.1038/sj.onc.1210349

2AuthorsVermeulen M. Eberl H.C. Matarese F. Marks H. Denissov S. Butter F. Lee K.K. Olsen J.V. Hyman A.A. Stunnenberg H.G. Mann M.
TitleQuantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers.
SourceCell 142:967-980(2010).
PubMed ID20850016
DOI10.1016/j.cell.2010.08.020

3AuthorsBian C. Xu C. Ruan J. Lee K.K. Burke T.L. Tempel W. Barsyte D. Li J. Wu M. Zhou B.O. Fleharty B.E. Paulson A. Allali-Hassani A. Zhou J.-Q. Mer G. Grant P.A. Workman J.L. Zang J. Min J.
TitleSgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation.
SourceEMBO J. 30:2829-2842(2011).
PubMed ID21685874
DOI10.1038/emboj.2011.193



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