Abstract
Enzymes that covalently modify histones control many cellular processes by affecting gene expression. A new class of these enzymes is the histone lysine methyltransferase family, whose catalytic activity lies within a conserved domain, the SET domain. This article surveys the evidence for a connection between SET-domain-containing proteins and cancer. It proposes that deregulation of SET-domain function has an important role in carcinogenesis.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Amino Acid Sequence
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Animals
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Carrier Proteins / genetics
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Carrier Proteins / metabolism
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism
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Histone Methyltransferases
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Histone-Lysine N-Methyltransferase / genetics
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Histone-Lysine N-Methyltransferase / metabolism*
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Humans
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Intracellular Signaling Peptides and Proteins*
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Methyltransferases / genetics
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Methyltransferases / metabolism
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Mice
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Molecular Sequence Data
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Neoplasms / metabolism
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Neoplasms / physiopathology*
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Nuclear Proteins / genetics
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Nuclear Proteins / metabolism
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Protein Structure, Tertiary
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Retinoblastoma Protein / metabolism
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism
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Transcription Factors / genetics
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Transcription Factors / metabolism
Substances
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Carrier Proteins
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DNA-Binding Proteins
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Intracellular Signaling Peptides and Proteins
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Nuclear Proteins
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Retinoblastoma Protein
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Saccharomyces cerevisiae Proteins
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Transcription Factors
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Histone Methyltransferases
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Methyltransferases
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SU(VAR)3-9
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Set2 protein, S cerevisiae
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Histone-Lysine N-Methyltransferase
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NSD1 protein, human
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Nsd1 protein, mouse
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PRDM2 protein, human
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SET1 protein, S cerevisiae