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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Motifs
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Amino Acid Sequence
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Animals
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Binding Sites
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Carrier Proteins / chemistry
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Carrier Proteins / metabolism
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Chromatin / metabolism
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DNA / metabolism
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Evolution, Molecular
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Group IV Phospholipases A2
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Humans
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Intracellular Signaling Peptides and Proteins*
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Molecular Sequence Data
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Nerve Tissue Proteins / chemistry*
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Nerve Tissue Proteins / metabolism
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Phospholipases A / chemistry*
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Phospholipases A / metabolism
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Polycomb Repressive Complex 2
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Protein Structure, Tertiary
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Proteins / chemistry*
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Proteins / metabolism
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Retinoblastoma-Binding Protein 2
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Transcription Factors*
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Tumor Suppressor Proteins*
Substances
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Carrier Proteins
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Chromatin
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HR protein, human
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Intracellular Signaling Peptides and Proteins
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Jarid2 protein, mouse
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Nerve Tissue Proteins
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Proteins
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Transcription Factors
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Tumor Suppressor Proteins
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DNA
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KDM5A protein, human
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Retinoblastoma-Binding Protein 2
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Polycomb Repressive Complex 2
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Phospholipases A
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Group IV Phospholipases A2