SAM domain of Ph (polyhomeotic) proteins of Polycomb group
SAM (sterile alpha motif) domain of Ph (polyhomeotic) proteins of Polycomb group is a protein-protein interaction domain. Ph1,2,3 proteins are members of PRC1 complex. This complex is involved in transcriptional repression of Hox (Homeobox) cluster genes. It is recruited through methylated H3Lys27 and supports the repression state by mediating monoubiquitination of histone H2A. Proteins of the Ph1,2,3 subfamily contribute to anterior-posterior neural tissue specification during embryogenesis. Additionally, the P2 protein of zebrafish is known to be involved in epiboly and tailbud formation. SAM domains of Ph proteins may interact with each other, forming homooligomers, as well as with SAM domains of other proteins, in particular with the SAM domain of Scm (sex comb on midleg) proteins, forming heterooligomers. Homooligomers are similar to the ones formed by SAM Pointed domains of the TEL proteins. Such SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome.
Feature 1:oligomer interface ML [polypeptide binding site]
Evidence:
Structure:1PK1_A; Drosophila SAM_Ph/SAM_Scm complex, contacts at 4A.
Comment:The mid-loop (ML) surface of the SAM domain of Ph protein interacts with the end-helix (EH) surface of the SAM domain of Scm protein forming heterodimers.