Catalysis of the hydrolysis of proteins, including elastin.

The formation from simpler components of triacylglycerol, any triester of glycerol.

neurotensin receptor activity, G-protein coupled

neurotensin receptor activity, G protein coupled

G-protein coupled receptor for the tridecapeptide neurotensin. Associated with G-protein signaling, coupled to IP3 second messenger (phospholipase C activating).

The breakdown into simpler components of triacylglycerol, any triester of glycerol.

Combining with a C-C chemokine to initiate a change in cell activity. C-C chemokines do not have an amino acid between the first two cysteines of the characteristic four-cysteine motif.

Interacting selectively with a transcription factor, any protein required to initiate or regulate transcription.

Combining with a C-X-C chemokine to initiate a change in cell activity. A C-X-C chemokine has a single amino acid between the first two cysteines of the characteristic four cysteine motif.

translation factor activity, nucleic acid binding

Functions during translation by binding nucleic acids during polypeptide synthesis at the ribosome.

Any process that modulates the frequency, rate or extent of cell proliferation.

Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.

The formation from simpler components of aromatic compounds, any substance containing an aromatic carbon ring.

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

Any process that modulates the frequency, rate or extent of T cell proliferation.

Interacting selectively with a nuclear localization sequence, a specific peptide sequence that acts as a signal to localize the protein within the nucleus.

The breakdown into simpler components of aromatic compounds, any substance containing an aromatic carbon ring.

Combining with orexin to initiate a change in cell activity.

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.