PROSITE documentation PDOC51518SGF29 C-terminal domain profile
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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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Kurabe N. Katagiri K. Komiya Y. Ito R. Sugiyama A. Kawasaki Y. Tashiro F. |
| Title | Deregulated 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. | |
| Source | Oncogene 26:5626-5634(2007). | |
| PubMed ID | 17334388 | |
| DOI | 10.1038/sj.onc.1210349 |
| 2 | Authors | Vermeulen 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. |
| Title | Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers. | |
| Source | Cell 142:967-980(2010). | |
| PubMed ID | 20850016 | |
| DOI | 10.1016/j.cell.2010.08.020 |
| 3 | Authors | Bian 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. |
| Title | Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation. | |
| Source | EMBO J. 30:2829-2842(2011). | |
| PubMed ID | 21685874 | |
| DOI | 10.1038/emboj.2011.193 |
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