Interacting selectively with fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis.

Interacting selectively with iron (Fe) ions.

The alteration of a histone by the covalent addition or removal of a chemical group.

Interacting selectively with copper (Cu) ions.

The modification of histones by addition of methyl groups.

The modification of histones by addition of phosphoric groups.

Interacting selectively with calcium ions (Ca2+).

The modification of histones by addition of acetyl groups.

The modification of histones by addition of ubiquitin groups.

The modification of histones by removal of acetyl groups.

The modification of histones by removal of phosphoric groups.

The modification of histones by removal of methyl groups.

The modification of histones by removal of ubiquitin groups.

The removal of one or more ubiquitin moieties from a protein.

growth hormone-releasing hormone receptor activity

Combining with growth hormone-releasing hormone to initiate a change in cell activity.

Combining with alpha-latrotoxin, a potent presynaptic neurotoxin, to initiate a change in cell activity.

Any process that stops, prevents or reduces the rate, frequency or extent of angiogenesis.

G-protein coupled receptor activity, unknown ligand

A G-protein coupled receptor for which the ligand has not been determined.

The cytoplasm of a muscle fiber; includes the sarcoplasmic reticulum.

A fine reticular network of membrane-limited elements that pervades the sarcoplasm of a muscle fiber; continuous over large portions of the cell and with the nuclear envelope; an endoplasmic reticulum specialized for the sequestration of calcium ions.

Catalysis of the formation of endothelin 1 by cleavage of the Trp21-Val22 bond in the precursor.

A heterodimer with alpha- and beta-subunits that binds the core site 5'-PYGPYGGT-3' of several enhancers and promoters; the beta-subunit enhances the DNA binding of the alpha-subunit.

Any of a family of protein complexes that regulate transcription by remodeling chromatin. Swi/Snf complexes comprise nine or more proteins, including both conserved (core) and nonconserved components; the Swi2/Snf2 ATPase is one of the core components.