Table I.

Tandem Domains, With Their Modifications Detected, Unique Properties and PDB IDs

Protein	Tandem domain	Modification detected	Properties	PDB ID
TAF1	Bromo-Bromo	H4K5/8/12/16ac	Simultaneous detection of two to four acetylated residues, located 25 Angstroms apart.	1EQF, 3AAD
DPF3b	PHD-PHD	H3(1-9), H3K14ac, H4Nac	PHD1 binds H3K14ac while PHD2 binds the unmodified N-terminus of H3. PHD2 can also recognize an acetylated H4 N-terminus.	2KWJ, 2KWN
CHD1	CHD-CHD	H3K4me3	Both chromodomains fuse to make a joint binding surface.	2B2W
TRIM24	PHD-Bromo	H3K4me0, H3K23ac	Simultaneous detection of H3K4me0 and H3K23ac.	3O34, 3O34
BPTF	PHD-Bromo	H3K4me3, H4Kac	Simultaneous intranucleosomal reading of H3K4me3 and H4Kac.	2F6J
KAP1	PHD-Bromo	None recognized	PHD functions as an intramolecular SUMO E3 ligase	2RO1
MLL1	PHD-Bromo	H3K4me3	Interacting domains acts as molecular switch to bind H3K4me3 and Cyp33 RRM simultaneously for gene repression.	3LQJ, 2KU7
UHRF1	TTD-PHD	H3K9me3 and H3K4me0	PBR of UHRF1 can block H3K9me3 binding. Binding of PI5P to PBR can relieve this block.	4GY5, 3ASK, 3ASL
CBP/p300	Bromo-RING-PHD-HAT	H3/4ac	RING and PHD domains can regulate HAT activity of adjacent HAT domain	4N4F, 4BHW
ZMYND11	Bromo-ZnF-PWWP	H3.3K36me3	Shows preference for the histone variant H3.3. Binding interface extends across multiple domains.	4N4I. 4NS5

Note: PDB, Protein Data Bank; SUMO, small ubiquitin-like modifier; PHD, plant homeodomain; TTD, tandem tudor domain; PBR, poly-basic region; PI5P, phosphatidylinositol-5-phosphate; HAT, histone acetyltransferase; RING, really interesting new gene; ZnF, zinc-finger; ac, acetylated; me0, unmethylated; me3, trimethylated.