Interacting selectively with a mitogen-activated protein kinase.

Interacting selectively with an apolipoprotein E receptor.

lysosphingolipid and lysophosphatidic acid receptor activity

Combining with lysosphingolipid or lysophosphatidic acid to initiate a change in cell activity.

The chemical reactions involving terpenes, any of a large group of hydrocarbons that are made up of isoprene (C5H8) units which may be cyclic, acyclic or multicyclic, saturated or unsaturated, and may contain various functional groups. A monoterpene is made up of two units, a sesquiterpene three units, and a diterpene is made up of four units. Terpenes are widely used as flavorings, deodorants, and medicines (as in the treatment of acne).

regulation of calcium-independent cell-cell adhesion

Any process that modulates the frequency, rate or extent of the attachment of one cell to another cell via adhesion molecules that do not require the presence of calcium for the interaction.

Any process that modulates the frequency, rate or extent of the phosphorylation of peptidyl-tyrosine.

positive regulation of calcium-independent cell-cell adhesion

Any process that activates or increases the rate of calcium-independent cell-cell adhesion.

positive regulation of peptidyl-tyrosine phosphorylation

Any process that activates or increases the rate of the phosphorylation of peptidyl-tyrosine.

The breakdown into simpler components of compounds derived from amino acids, organic acids containing one or more amino substituents.

negative regulation of peptidyl-tyrosine phosphorylation

Any process that stops, prevents or reduces the rate of the phosphorylation of peptidyl-tyrosine.

The stages of blood cell formation that take place within the embryo.

regulation of membrane protein ectodomain proteolysis

Any process that modulates the frequency, rate or extent of the proteolytic cleavage of transmembrane proteins and release of their ectodomain (extracellular domain).

Interacting selectively with an RS domain of a protein; RS domains are usually highly phosphorylated and characterized by the presence of arginine (R)/serine (S) dipeptides. The RS domain promotes protein-protein interactions and directs subcellular localization and, in certain situations, nucleocytoplasmic shuttling of individual SR proteins. They also play a role in splicing.