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Literature summary for 2.3.1.23 extracted from

  • Zou, C.; Ellis, B.M.; Smith, R.M.; Chen, B.B.; Zhao, Y.; Mallampalli, R.K.
    Acyl-CoA:lysophosphatidylcholine acyltransferase I (Lpcat1) catalyzes histone protein O-palmitoylation to regulate mRNA synthesis (2011), J. Biol. Chem., 286, 28019-28025.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus histone H4 protein is subject to palmitoylation catalyzed by Lpcat1 in a calcium-regulated manner. Cytosolic Lpcat1 shifts into the nucleus in lung epithelia in response to exogenous Ca2+. Nuclear Lpcat1 colocalizes with and binds to histone H4, where it catalyzes histone H4 palmitoylation. Residue Ser47 within histone H4 serves as a putative acceptor site, indicative of Lpcat1-mediated O-palmitoylation. Lpcat1 knock-down or expression of a histone H4 Ser47A mutant protein in cells decreases cellular mRNA synthesis ?
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?

Organism

Organism UniProt Comment Textmining
Mus musculus
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-
-

Source Tissue

Source Tissue Comment Organism Textmining
lung
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Mus musculus
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MLE-12 cell
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Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information histone H4 protein is subject to palmitoylation catalyzed by Lpcat1 in a calcium-regulated manner. Cytosolic Lpcat1 shifts into the nucleus in lung epithelia in response to exogenous Ca2+. Nuclear Lpcat1 colocalizes with and binds to histone H4, where it catalyzes histone H4 palmitoylation. Residue Ser47 within histone H4 serves as a putative acceptor site, indicative of Lpcat1-mediated O-palmitoylation. Lpcat1 knock-down or expression of a histone H4 Ser47A mutant protein in cells decreases cellular mRNA synthesis Mus musculus ?
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?

Synonyms

Synonyms Comment Organism
LPCAT1
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Mus musculus

General Information

General Information Comment Organism
physiological function histone H4 protein is subject to palmitoylation catalyzed by Lpcat1 in a calcium-regulated manner. Cytosolic Lpcat1 shifts into the nucleus in lung epithelia in response to exogenous Ca2+. Nuclear Lpcat1 colocalizes with and binds to histone H4, where it catalyzes histone H4 palmitoylation. Residue Ser47 within histone H4 serves as a putative acceptor site, indicative of Lpcat1-mediated O-palmitoylation. Lpcat1 knock-down or expression of a histone H4 Ser47A mutant protein in cells decrease cellular mRNA synthesis Mus musculus