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Interacting selectively and non-covalently with a phosphorylated protein. 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 calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states. Interacting selectively and non-covalently with collagen, a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals. Collagen is highly enriched in glycine (some regions are 33% glycine) and proline, occurring predominantly as 3-hydroxyproline (about 20%). Interacting selectively and non-covalently with a SMAD signaling protein. Catalysis of the transfer of a protein from one side of a membrane to the other. Interacting selectively and non-covalently with a hexon, the major protein component of the icosahedral capsid of an adenovirus. Interacting selectively and non-covalently with a domain within the same polypeptide. Interacting selectively and non-covalently with a polyglutamine tract, i.e. a series of consecutive glutamine residues, in a protein. Interacting selectvely with a heat shock protein, any protein synthesized or activated in response to heat shock. Interacting selectively and non-covalently with an antisigma factor, a factor which inhibits the ability of the sigma factor to function as a transcriptional initiator. The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits. Interacting selectively and non-covalently with any subunit of protein kinase A. Interacting selectively and non-covalently with two or more protein molecules, or a protein and another macromolecule or complex, simultaneously, thereby physically linking the bound proteins or complexes to each other. Interacting selectively and non-covalently with profilin, an actin-binding protein that forms a complex with G-actin and prevents it from polymerizing to form F-actin. Interacting selectively and non-covalently with a cell adhesion molecule. Interacting selectively and non-covalently with a proline-rich region, i.e. a region that contains a high proportion of proline residues, in a protein. Interacting selectively and non-covalently with a connexin, any of a group of related proteins that assemble to form gap junctions. Interacting selectively and non-covalently with lamin; any of a group of intermediate-filament proteins that form the fibrous matrix on the inner surface of the nuclear envelope. Interacting selectively and non-covalently with a haptoglobin, any alpha2 globulin of blood plasma that can combine with free oxyhemoglobin to form a stable complex. Interacting selectively and non-covalently with beta-2-microglobulin. Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules), in the presence of copper. Interacting selectively and non-covalently with tapasin, a member of the MHC class I loading complex which bridges the TAP peptide transporter to class I molecules. Interacting selectively and non-covalently with a G-protein gamma subunit. Interacting selectively and non-covalently with a cytokine, any of a group of proteins that function to control the survival, growth and differentiation of tissues and cells, and which have autocrine and paracrine activity. Interacting selectively and non-covalently with syndecan, an integral membrane proteoglycan (250-300 kDa) associated largely with epithelial cells. Interacting selectively and non-covalently with a transcription factor, any protein required to initiate or regulate transcription. Interacting selectively and non-covalently with TAP protein, transporter associated with antigen processing protein. TAP protein is a heterodimeric peptide transporter consisting of the subunits TAP1 and TAP2. Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules), in the presence of calcium. Interacting selectively and non-covalently with a kininogen, any of a group of plasma proteins that are kinin precursors. Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules) using energy from the hydrolysis of ATP. Interacting selectively and non-covalently with denatured proteins. Interacting selectively and non-covalently with a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport. Interacting selectively and non-covalently with a G-protein alpha subunit. The alpha subunit binds a guanine nucleotide. Interacting selectively and non-covalently with a histone, any of a group of water-soluble proteins found in association with the DNA of plant and animal chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in nonspecific suppression of gene activity. Interacting selectively and non-covalently with Ku70, a protein involved in non-homologous DNA end joining. Interacting selectively and non-covalently with phytochrome. Interacting selectively and non-covalently with a fibronectin, a group of related adhesive glycoproteins of high molecular weight found on the surface of animal cells, connective tissue matrices, and in extracellular fluids. Interacting selectively and non-covalently with X11-like protein, a neuron-specific adaptor protein. Interacting selectively and non-covalently and non-covalently with a small conjugating protein such as ubiquitin or a ubiquitin-like protein. 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 the Cystic Fibrosis Transmembrane conductance Regulator (CFTR) protein. Interacting selectively and non-covalently with S100 beta protein. S100 is a small calcium and zinc binding protein produced in astrocytes that is implicated in Alzheimer's disease, Down Syndrome and ALS. Interacting selectively and non-covalently with S100 alpha protein. S100 is a small calcium and zinc binding protein produced in astrocytes that is implicated in Alzheimer's disease, Down Syndrome and ALS. Functions to provide a physical support for the assembly of a multiprotein complex. Interacting selectively and non-covalently with a GDP-dissociation inhibitor protein. Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules) in the presence of sterols. Interacting selectively and non-covalently with a translation initiation factor, any polypeptide factor involved in the initiation of ribosome-mediated translation. Interacting selectively and non-covalently with an apolipoprotein, the protein component of a lipoprotein complex. Interacting selectively and non-covalently with any protein component of any cytoskeleton (actin, microtubule, or intermediate filament cytoskeleton). Interacting selectively and non-covalently with Wnt-protein, a secreted growth factor involved in signaling. Interacting selectively and non-covalently with the beta subunit of the catenin complex. Interacting selectively and non-covalently with any of the insulin receptor substrate (IRS) proteins, adaptor proteins that bind to the transphosphorylated insulin and insulin-like growth factor receptors, are themselves phosphorylated and in turn recruit SH2 domain-containing signaling molecules to form a productive signaling complex. Interacting selectively and non-covalently with any protein complex (a complex of two or more proteins that may include other nonprotein molecules). Interacting selectively and non-covalently with an identical protein or proteins. Interacting selectively and non-covalently with a preprotein, the unprocessed form of a protein destined to undergo co- or post-translational processing. Interacting selectively and non-covalently with a misfolded protein. Interacting selectively and non-covalently with any protein from the structural maintenance of chromosomes (SMC) family, a group of chromosomal ATPases with a role in mitotic chromosome organization. Interacting selectively and non-covalently with a glycoprotein, a protein that contains covalently bound glycose (monosaccharide) residues. These also include proteoglycans. Combining with a nuclear export signal to initiate a change in cell activity. Interacting selectively and non-covalently with a G-protein beta subunit. Interacting selectively and non-covalently with any component or product of the complement cascade. Interacting selectively and non-covalently with the gamma subunit of the catenin complex. Interacting selectively and non-covalently with the delta subunit of the catenin complex. Interacting selectively and non-covalently with the alpha subunit of the catenin complex. Interacting selectively and non-covalently with cyclins, proteins whose levels in a cell varies markedly during the cell cycle, rising steadily until mitosis, then falling abruptly to zero. As cyclins reach a threshold level, they are thought to drive cells into G2 phase and thus to mitosis. Interacting selectively and non-covalently with a specific domain of a protein. Interacting selectively and non-covalently with an opsonin, such as a complement component or antibody, deposited on the surface of a bacteria, virus, immune complex, or other particulate material. Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules) using energy from the hydrolysis of GTP. Interacting selectively and non-covalently with dynein, the multisubunit protein complex that is associated with microtubules. Interacting selectively and non-covalently with angiostatin, a proteolytic product of plasminogen or plasmin containing at least one intact kringle domain, and which is an inhibitor of angiogenesis. Interacting selectively and non-covalently with laminins, glycoproteins that are major constituents of the basement membrane of cells. Interacting selectively and non-covalently with TATA-binding protein (TBP), a component of various transcription factors. Interacting selectively and non-covalently with an unfolded protein. Interacting selectively and non-covalently with any enzyme. Interacting selectively and non-covalently with both a protein or protein complex and a membrane, in order to maintain the localization of the protein at a specific location on the membrane. Interacting selectively and non-covalently with proteins with similar structure/function to receptor protein tyrosine phosphatases. Interacting selectively and non-covalently with an opsin, any of a group of hydrophobic, integral membrane glycoproteins located primarily in the disc membrane of rods or cones, involved in photoreception. Interacting selectively and non-covalently with any conjugated, water-soluble protein in which the nonprotein moiety consists of a lipid or lipids. Elemental activities, such as catalysis or binding, describing the actions of a gene product at the molecular level. A given gene product may exhibit one or more molecular functions. Interacting selectively and non-covalently with one of the p53 family of proteins. Interacting selectively and non-covalently with hemoglobin, an oxygen carrying, conjugated protein containing four heme groups and globin. Interacting selectively and non-covalently with beta-amyloid peptide/protein and/or its precursor. Interacting selectively and non-covalently with any growth factor, proteins or polypeptides that stimulate a cell or organism to grow or proliferate. Interacting selectively and non-covalently with a clathrin heavy or light chain, the main components of the coat of coated vesicles and coated pits, and which also occurs in synaptic vesicles. Interacting selectively and non-covalently with a SNARE (soluble N-ethylmaleimide-sensitive factor attached protein receptor) protein. Interacting selectively and non-covalently with a transcription repressor, any protein whose activity is required to prevent or downregulate transcription. Interacting selectively and non-covalently with the peptide hormone follistatin. Interacting selectively and non-covalently with a transcription activator, any protein whose activity is required to initiate or upregulate transcription. Interacting selectively and non-covalently with TRAIL (TNF-related apoptosis inducing ligand), a member of the tumor necrosis factor ligand family that rapidly induces apoptosis in a variety of transformed cell lines. Interacting selectively and non-covalently with a protein C-terminus, the end of any peptide chain at which the 1-carboxy function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue. Interacting selectively and non-covalently with neurexins, synaptic cell surface proteins related to latrotoxin receptor, laminin and agrin. Neurexins act as cell recognition molecules at nerve terminals. Interacting selectively and non-covalently with a farnesylated protein. Interacting selectively and non-covalently with both N-ethylmaleimide-sensitive fusion protein (NSF) and a cis-SNARE complex (i.e. a SNARE complex in which all proteins are associated with the same membrane) and increasing the ATPase activity of NSF, thereby allowing ATP hydrolysis by NSF to disassemble the cis-SNARE complex. Interacting selectively and non-covalently with a GTPase activating protein. Acting as a marker to identify a membrane and interacting selectively with one or more SNAREs on another membrane to mediate membrane fusion. Interacting selectively and non-covalently with any isoform of the MDM2 protein, a negative regulator of p53. Interacting selectively and non-covalently with a protein N-terminus, the end of any peptide chain at which the 2-amino (or 2-imino) function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue. Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules) that contributes to the process of protein folding. Interacting selectively and non-covalently with any isoform of the MDM4 protein, a negative regulator of p53. 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 an inhibin monomer, any of the polypeptides that combine to form activin and inhibin dimers. The binding activity of a molecule that brings together an anion exchanger and one or more other molecules, permitting them to function in a coordinated way.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: protein binding
Acc: GO:0005515
Aspect: Molecular Function
Desc: Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
Synonyms:
  • protein amino acid binding
  • protein degradation tagging activity
  • GO:0045308
  • protein folding chaperone
  • protein tagging activity
  • alpha-2 macroglobulin receptor-associated protein activity
Proteins in PDR annotated with:
   This term: 18804 [Refine Search]
   Term or descendants: 25489 [Refine Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0005515 - protein binding (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle