Abstract
On the basis of significant sequence similarity, we have identified JmjC domains in more than 100 eukaryotic and bacterial sequences. These include human hairless, mutated in individuals with alopecia universalis, retinoblastoma-binding protein 2 and several putative chromatin-associated proteins. JmjC domains are predicted to be metalloenzymes that adopt the cupin fold, and are candidates for enzymes that regulate chromatin remodelling.
| Original language | English |
|---|---|
| Pages (from-to) | 7-9 |
| Number of pages | 3 |
| Journal | Trends in biochemical sciences |
| Volume | 26 |
| Issue number | 1 |
| Publication status | Published - Jan 2001 |
Keywords
- Amino Acid Motifs
- Amino Acid Sequence
- Animals
- Binding Sites
- Carrier Proteins
- Chromatin
- DNA
- Evolution, Molecular
- Group IV Phospholipases A2
- Humans
- Intracellular Signaling Peptides and Proteins
- Molecular Sequence Data
- Nerve Tissue Proteins
- Phospholipases A
- Polycomb Repressive Complex 2
- Protein Structure, Tertiary
- Proteins
- Retinoblastoma-Binding Protein 2
- Transcription Factors
- Tumor Suppressor Proteins