The posttranslational modification of histone proteins via methylation has important functions in gene activation, transcriptional silencing, establishment of chromatin states, and likely many aspects of DNA metabolism. The identification of numerous effector protein domains with the capability of binding methylated histones has significantly advanced our understanding of how such histone modifications may exert their biological effects. Here, we summarize aspects of the generation of arginine and lysine methylation marks on core histones, the characterization of the protein modules that interact with them, and how histone methylation cross-talks with other modifications.