{PDOC51518} {PS51518; SGF29_C} {BEGIN} *********************************** * SGF29 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 beta strands forming a typical barrel-like fold (see ). 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. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: December 2011 / Profile and text revised. [ 1] Kurabe N., Katagiri K., Komiya Y., Ito R., Sugiyama A., Kawasaki Y., Tashiro F. "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." Oncogene 26:5626-5634(2007). PubMed=17334388; DOI=10.1038/sj.onc.1210349 [ 2] 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. "Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers." Cell 142:967-980(2010). PubMed=20850016; DOI=10.1016/j.cell.2010.08.020 [ 3] 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. "Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation." EMBO J. 30:2829-2842(2011). PubMed=21685874; DOI=10.1038/emboj.2011.193 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}