Annotation inferences using phylogenetic trees
Combined Automated Annotation using Multiple IEA Methods.
A reference map of the human binary protein interactome.
Deep research on CSN1S1 function
Falcon deep research on CSN1S1 function
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Human CSN1S1 encodes αS1-casein, a secreted milk phosphoprotein that participates in casein micelle architecture and supports nutrient/mineral delivery; in humans αS1-casein is a minor casein component (~3% of casein) relative to β- and κ-casein, with mean human casein micelle diameter 64–80 nm.
"Primary function:** Human CSN1S1 encodes αS1-casein, a secreted milk phosphoprotein that participates in **casein micelle** architecture and thereby supports nutrient/mineral delivery; in humans it is a **minor casein component** relative to β- and κ-casein"
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αS1-casein is a documented precursor for Casoxin D (αS1-casein f158–164; YVPFPPF), classified in reviews as an opioid antagonist peptide.
"αS1-casein is a documented precursor for **Casoxin D** (αS1-casein f158–164; **YVPFPPF**), classified in reviews as an **opioid antagonist** peptide"
Caseins: Versatility of Their Micellar Organization in Relation to the Functional and Nutritional Properties of Milk
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αS1-, αS2-, and β-caseins are calcium-binding phosphoproteins located mainly in the casein micelle interior, associating with colloidal calcium phosphate; κ-casein forms the stabilizing surface layer.
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In human milk, αS1-casein is a minor casein fraction (~3% of casein), with total casein concentration 2.4–4.2 g/L and mean micelle diameter 64–80 nm.
Human casein alpha s1 (CSN1S1) skews in vitro differentiation of monocytes towards macrophages.
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Recombinant human CSN1S1 skews primary monocytes towards a macrophage-like phenotype and inhibits early GM-CSF-driven dendritic-cell differentiation in vitro.
"CSN1S1 skews in vitro differentiation of monocytes towards a macrophage-like phenotype."
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Inhibition of early GM-CSF-induced dendritic-cell differentiation.
"Early GM-CSF, but not GM-CSF/IL-4 induced differentiation of monocytes towards dendritic cells (DC) was inhibited by addition of CSN1S1."
Human casein alpha s1 induces proinflammatory cytokine expression in monocytic cells by TLR4 signaling.
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Recombinant CSN1S1 induces IL-1beta, IL-8 and IL-6 in monocytic cells through TLR4, and CK2 phosphorylation abolishes this effect and TLR4 binding.
"Phosphorylation of CSN1S1 by casein-kinase 2 completely abolished proinflammatory cytokine induction and binding to TLR4."
Human α(S1)-casein induces IL-8 secretion by binding to the ecto-domain of the TLR4/MD2 receptor complex.
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Human alpha-S1-casein binds the TLR4 ecto-domain.
"In this study, αS1-casein was identified as binder of theTLR4 ecto domain."
Structural Analysis of Breast-Milk α(S1)-Casein: An α-Helical Conformation Is Required for TLR4-Stimulation.
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Phosphorylation reduces the alpha-helical content of human alpha-S1-casein and abolishes its TLR4-agonist activity.
"Our results indicate that αS1-casein appears in two distinct conformations, an α-helical TLR4-agonistic and a less α-helical TLR4 non-agonistic conformation induced by phosphorylation."
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Alpha-S1-casein is less than 1% of human milk protein.
"A reason for this could be the low content of breast-milk αS1-casein with less than 1% (3 mg/L to 537 mg/L) of total milk protein content"
Alpha(S1)-casein is required for the efficient transport of beta- and kappa-casein from the endoplasmic reticulum to the Golgi apparatus of mammary epithelial cells.
Milk lacking α-casein leads to permanent reduction in body size in mice.
AlphaS1-casein, which is essential for efficient ER-to-Golgi casein transport, is also present in a tightly membrane-associated form.