UHRF1 PHD domain (human recombinant)

Territorial Availability: Available through Bertin Technologies only in France

• Correlated keywords
  • histones chromatin PHD domains zinc fingers epigenetics methylation plants homeodomains binding binds tudors multidomain-containing multidomains containing multi-domains nuclear proteins DNA methylation H3 Hthree three H promyelocytic leukemia PML methyl readers genes regulations cancers nuclear Np95 Np 95 HuNp95 hNp95 ubiquitin-like-containing ubiquitin like containing RING one 1
• Product Overview:
  Recognition of epigenetic marks can be mediated by small modular protein units of ~50 amino acids called Plant Homeodomain (PHD) fingers. PHD fingers are zinc binding domains that have a Cys4-His-Cys3 motif and are found in more than 100 nuclear proteins that play a role in regulating chromatin.{23085} PHD domains often work with other protein regions, such as bromodomains and Tudor domains, to recognize post-translational modifications in many proteins.{23085} Ubiquitin-like with PHD and ring finger domains 1 (UHRF1) is a multidomain-containing nuclear protein known to bind chromatin and participate in the maintenance of DNA methylation.{23843,23841} The SET and RING associated domain of UHRF1, also called the YDG motif, binds methyl cytosines, while trimethylated histone H3 lysine 9 (H3K9me3) and unmethylated histone H3 Arginine 2 (H3R2me0) are recognized by the tandem Tudor-like domains and the PHD domain, respectively.{23842,23851,23847,23844,23846,23849} Some evidence suggests the tandem Tudor-like region and adjacent PHD domain may operate together to recognize H3K9me3.{23850} The combinatorial recognition of the histone tail region and hemi-methylated DNA functions to regulate gene silencing by directly interacting with DNA (cytosine-5)-methyltransferase 1.{23853,23843,23852} UHRF1 also posseses E3 ubiquitin ligase activity toward histone H3 and the tumor suppressor promyelocytic leukemia protein.{23844,23845} This protein product contains the PHD finger region of UHRF1.