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Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules). Interacting selectively and non-covalently with the insulin-like growth factor receptor. Interacting selectively and non-covalently with the insulin receptor. Interacting selectively and non-covalently with the Notch (N) protein, a surface receptor. Interacting selectively and non-covalently with the peripheral benzodiazepine receptor (PBR). Interaction with the receptor tyrosine kinase-like orphan receptor (Ror). Interacting selectively and non-covalently with the Roundabout (ROBO) receptor, a transmembrane receptor. Interacting selectively and non-covalently with the patched (ptc) protein, a receptor for hedgehog proteins. The activity of binding to and activating specific cell surface receptors, thereby inducing behavioral, developmental, or physiological response(s) from a responding organism or cell. The substance may be released or retained on the cell surface. Pheromones may serve as a specific attractant, social communicator, or sexual stimulant. Interacting selectively and non-covalently with a T cell receptor, the antigen-recognizing receptor on the surface of T cells. Interacting selectively and non-covalently with a CD4, a receptor found on the surface of T cells, monocytes and macrophages. Interacting selectively and non-covalently with the RAGE receptor, the receptor for advanced glycation end-products. Naturally occurring peptide that is an opioid (any non-alkaloid having an opiate-like effect that can be reversed by naloxone or other recognized morphine antagonist). These include Leu- and Met-enkephalin, dynorphin and neoendorphin, alpha, beta, gamma and delta endorphins formed from beta-lipotropin, various pronase-resistant peptides such as beta casamorphin, and other peptides whose opiate-like action seems to be indirect. Interacts with receptors to reduce the action of another ligand, the agonist. Interacting selectively and non-covalently with the protein-tyrosine kinase receptor ErbB-3/HER3. Interacting selectively and non-covalently with the sulfonylurea receptor, a regulatory subunit of the ATP-sensitive potassium ion channel. Interacts with receptors such that the proportion of receptors in the active form is increased. Interacting selectively and non-covalently with one or more specific sites on an immunoglobulin receptor molecule. Interacting selectively and non-covalently, in a ligand dependent manner, with a nuclear receptor protein. Interacting selectively and non-covalently with a lectin-like natural killer cell receptor. Interacting selectively and non-covalently with receptors for intercellular adhesion molecule-3 (ICAM-3), such as DC-SIGN and LFA-1. Interacting selectively and non-covalently with the Toll protein, a transmembrane receptor. Interacting selectively and non-covalently with the torso (tor) protein, a receptor tyrosine kinase. Interacting selectively and non-covalently with scavenger receptors, a family of proteins that are expressed on myeloid cells and are involved in the uptake of effete cellular components and foreign particles. Functions to control the survival, growth, differentiation and effector function of tissues and cells. Interacting selectively with a cytokine receptor. Interacting selectively and non-covalently with a Toll-like protein, a pattern recognition receptor that binds pattern motifs from a variety of microbial sources to initiate an innate immune response. Interacting selectively and non-covalently with the sevenless (sev) protein, a receptor tyrosine kinase. Interacting selectively and non-covalently with the protein-tyrosine kinase receptor Neu/ErbB-2/HER2. Interacting selectively and non-covalently with wishful thinking (Wit), a type II bone morphogenic protein receptor. Interacting selectively and non-covalently with an integrin. Interacting selectively and non-covalently with the smoothened (smo) protein, which interacts with patched to transmit hedgehog signals. The action characteristic of a hormone, any substance formed in very small amounts in one specialized organ or group of cells and carried (sometimes in the bloodstream) to another organ or group of cells in the same organism, upon which it has a specific regulatory action. The term was originally applied to agents with a stimulatory physiological action in vertebrate animals (as opposed to a chalone, which has a depressant action). Usage is now extended to regulatory compounds in lower animals and plants, and to synthetic substances having comparable effects; all bind receptors and trigger some biological process. Interacting selectively and non-covalently with an ephrin receptor. Interacting selectively and non-covalently with a receptor on the host cell surface. Interacting selectively and non-covalently with an aryl hydrocarbon receptor. The function that stimulates a cell to grow or proliferate. Most growth factors have other actions besides the induction of cell growth or proliferation. Interacting selectively and non-covalently with major histocompatibility complex molecules; a set of molecules displayed on cell surfaces that are responsible for lymphocyte recognition and antigen presentation. Interacting selectively and non-covalently with a receptor for hormones. Interacting selectively and non-covalently with the gamma-aminobutyric acid (GABA, 4-aminobutyrate) receptor. Interacting selectively and non-covalently with a lipoprotein receptor. Interacting selectively and non-covalently with any of the peroxisome proliferator activated receptors, alpha, beta or gamma. Interacting selectively and non-covalently with a high molecular weight kininogen receptor. Interacting selectively with a growth factor receptor. Interacting selectively and non-covalently with an apolipoprotein receptor. Interacting selectively and non-covalently with a receptor that possesses protein serine/threonine kinase activity. Interacting selectively and non-covalently with a receptor that possesses protein tyrosine kinase activity. Interacting selectively and non-covalently with a G-protein-coupled receptor. Interacting selectively and non-covalently with a CD8, a receptor found on the surface of thymocytes and cytotoxic and suppressor T-lymphocytes. Interacting selectively and non-covalently with a CD70, a receptor found on the surface of most activated B cells and some activated T cells. Interacting selectively and non-covalently with one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function. Interacting selectively and non-covalently with an acetylcholine receptor. Interacting selectively and non-covalently with CD154, a receptor found on the surface of some activated lymphocytes. Interacting selectively and non-covalently with a toxin receptor, a receptor for substances that cause injury to living organisms. The selective, non-covalent, often stoichiometric, interaction of a molecule with one or more specific sites on another molecule. Interacting selectively and non-covalently with a glutamate receptor. Interacting selectively and non-covalently with semaphorin receptors.

View Gene Ontology (GO) Term

GO TERM SUMMARY

Name: receptor binding
Acc: GO:0005102
Aspect: Molecular Function
Desc: Interacting selectively and non-covalently with one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
Synonyms:
  • receptor ligand
  • receptor-associated protein activity
Proteins in PDR annotated with:
   This term: 463 [Search]
   Term or descendants: 2091 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0005102 - receptor binding (interactive image map)

YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle