Category: Proteins & Peptides

Active filters

Reference: CSB-EP020619HU_100

Calcium channel that mediates the release of Ca2+ from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules. Repeated very high-level exercise increases the open probability of the channel and leads to Ca2+ leaking into the cytoplasm. Can also mediate the release of Ca2+ from intracellular stores in neurons, and may thereby promote prolonged Ca2+ signaling in the brain. Required for normal bryonic development of muscle fibers and skeletal muscle. Required for normal heart morphogenesis, skin development and ossification during bryogenesis .

Reference: CSB-EP020619HU_20

Calcium channel that mediates the release of Ca2+ from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules. Repeated very high-level exercise increases the open probability of the channel and leads to Ca2+ leaking into the cytoplasm. Can also mediate the release of Ca2+ from intracellular stores in neurons, and may thereby promote prolonged Ca2+ signaling in the brain. Required for normal bryonic development of muscle fibers and skeletal muscle. Required for normal heart morphogenesis, skin development and ossification during bryogenesis .

Reference: CSB-EP020621HU_1

Calcium channel that mediates the release of Ca2+ from the sarcoplasmic reticulum into the cytoplasm in muscle and thereby plays a role in triggering muscle contraction. May regulate Ca2+ release by other calcium channels. Calcium channel that mediates Ca2+-induced Ca2+ release from the endoplasmic reticulum in non-muscle cells. Contributes to cellular calcium ion homeostasis . Plays a role in cellular calcium signaling.1 Publication

Reference: CSB-EP020621HU_100

Calcium channel that mediates the release of Ca2+ from the sarcoplasmic reticulum into the cytoplasm in muscle and thereby plays a role in triggering muscle contraction. May regulate Ca2+ release by other calcium channels. Calcium channel that mediates Ca2+-induced Ca2+ release from the endoplasmic reticulum in non-muscle cells. Contributes to cellular calcium ion homeostasis . Plays a role in cellular calcium signaling.1 Publication

Reference: CSB-EP020621HU_20

Calcium channel that mediates the release of Ca2+ from the sarcoplasmic reticulum into the cytoplasm in muscle and thereby plays a role in triggering muscle contraction. May regulate Ca2+ release by other calcium channels. Calcium channel that mediates Ca2+-induced Ca2+ release from the endoplasmic reticulum in non-muscle cells. Contributes to cellular calcium ion homeostasis . Plays a role in cellular calcium signaling.1 Publication

Reference: CSB-EP020622HU_1

Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity.

Reference: CSB-EP020622HU_100

Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity.

Reference: CSB-EP020622HU_20

Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity.

Reference: CSB-EP020623HU_1

Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase.

Reference: CSB-EP020623HU_100

Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase.

Reference: CSB-EP020623HU_20

Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase.