The volume enclosed by the membranes of a particular organelle, e.g. endoplasmic reticulum lumen, or the space between the two lipid bilayers of a double membrane surrounding an organelle, e.g. nuclear membrane lumen.

Blood vessel formation when new vessels emerge from the proliferation of pre-existing blood vessels.

Any protein group composed of two or more subunits, which may or may not be identical, which undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.

Extracellular matrix components occurring independently or along with elastin. Thought to have force-bearing functions in tendon. In addition to fibrillins, microfibrils may contain other associated proteins.

Interacting selectively with laminins, glycoproteins that are major constituents of the basement membrane of cells.

modification of morphology or physiology of other organism during symbiotic interaction

The process by which an organism effects a change in the structure or function of a second organism, where the two organisms are in a symbiotic relationship.

Interacting selectively with laminin-1, a glycoprotein trimer with the subunit composition alpha1, beta1, gamma1.

disruption of cells of other organism during symbiotic interaction

A process by which an organism has a negative effect on the functioning of the second organism's cells, where the two organisms are in a symbiotic relationship.

Posttranscriptional addition of a methyl group to either a nucleotide or 2'-O ribose in an polyribonucleotide. Usually uses S-adenosylmethionine as a cofactor.

The process by which cell surface receptors are monoubiquitinated following ligand-induced activation, and subsequently taken up into endocytic vesicles and targeted to the lysosome or vacuole for degradation; serves as a mechanism to downregulate receptor signaling.

Interacting selectively with a ubiquitin protein ligase enzyme, any of the E3 proteins.

The incorporation of selenocysteine into a peptide; uses a special tRNA that recognizes the UGA codon as selenocysteine, rather than as a termination codon. Selenocysteine is synthesized from serine before its incorporation, it is not a posttranslational modification of peptidyl-cysteine.