PHENOMENA AND PROCESSES Chemical Phenomena [G02] Chemical Phenomena Biochemical Phenomena [G02.111] Biochemical Phenomena Molecular Structure [G02.111.570] Molecular Structure Molecular Conformation [G02.111.570.820] Molecular Conformation Protein Conformation [G02.111.570.820.709] Protein Conformation Protein Structural Elements [G02.111.570.820.709.275] Protein Structural Elements Amino Acid Motifs [G02.111.570.820.709.275.500] Amino Acid Motifs Zinc Fingers [G02.111.570.820.709.275.500.985] Zinc Fingers CYS2-HIS2 Zinc Fingers [G02.111.570.820.709.275.500.985.250] CYS2-HIS2 Zinc Fingers MYND Domains [G02.111.570.820.709.275.500.985.375] MYND Domains PHD Zinc Fingers [G02.111.570.820.709.275.500.985.438] PHD Zinc Fingers RING Finger Domains [G02.111.570.820.709.275.500.985.500] RING Finger Domains

PHD Zinc Fingers - Preferred

Concept UI	M000631685
Scope note	Zinc finger domains of approximately 50 to 80 amino acids in length that are characterized by a conserved Cysteine(3)-Histidine-Cysteine(4) amino acid motif which coordinates binding of two zinc ions. They are similar structurally to RING FINGER DOMAINS, with a globular fold topology of two BETA-SHEETS and an ALPHA-HELIX. PHD fingers occur in many proteins that function in chromatin-mediated gene expression and EPIGENETICS such as POLYCOMB-GROUP PROTEINS.
Preferred term	PHD Zinc Fingers
Entry term(s)	Domain, PHD Domain, PHD Finger Domains, PHD Domains, PHD Finger Finger Domain, PHD Finger Domains, PHD Finger, PHD Finger, PHD Zinc Fingers, PHD Fingers, PHD Zinc Motif, PHD Motifs, PHD PHD Domain PHD Domains PHD Finger PHD Finger Domain PHD Finger Domains PHD Fingers PHD Motif PHD Motifs PHD Zinc Finger Zinc Finger, PHD Zinc Fingers, PHD