Interacting selectively and non-covalently with an RNA polymerase II transcription factor, any protein required to initiate or regulate transcription by RNA polymerase II.

A protein or a member of a complex that interacts specifically and non-covalently with a DNA-bound DNA-binding transcription factor to activate the transcription of specific genes. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second ATP-dependent class modifies the conformation of chromatin. Another type of coregulator activity is the bridging of a DNA-binding transcription factor to the basal transcription machinery. The Mediator complex, which bridges transcription factors and RNA polymerase, is also a transcription coactivator.

Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).

A protein or a member of a complex that interacts specifically and non-covalently with a DNA-bound DNA-binding transcription factor to activate the transcription of specific genes. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second ATP-dependent class modifies the conformation of chromatin. Another type of coregulator activity is the bridging of a DNA-binding transcription factor to the basal transcription machinery. The Mediator complex, which bridges transcription factors and RNA polymerase, is also a transcription coactivator.

Interacting selectively and non-covalently with the alpha subunit of the catenin complex.

Interacting selectively and non-covalently with cadherin, a type I membrane protein involved in cell adhesion.

Interacting selectively and non-covalently with any protein phosphatase.

Interacting selectively and non-covalently with cadherin, a type I membrane protein involved in cell adhesion.

Interacting selectively and non-covalently with an RNA polymerase II transcription factor, any protein required to initiate or regulate transcription by RNA polymerase II.

A protein or a member of a complex that interacts specifically and non-covalently with a DNA-bound DNA-binding transcription factor to activate the transcription of specific genes. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second ATP-dependent class modifies the conformation of chromatin. Another type of coregulator activity is the bridging of a DNA-binding transcription factor to the basal transcription machinery. The Mediator complex, which bridges transcription factors and RNA polymerase, is also a transcription coactivator.

Interacting selectively and non-covalently with a transcription factor, a protein required to initiate or regulate transcription.

Interacting selectively and non-covalently with any enzyme.

Interacting selectively and non-covalently with a nuclear hormone receptor, a ligand-dependent receptor found in the nucleus of the cell.

Interacting selectively and non-covalently with a kinase, any enzyme that catalyzes the transfer of a phosphate group.

Interacting selectively and non-covalently with a protein C-terminus, the end of any peptide chain at which the 1-carboxyl function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.

Interacting selectively and non-covalently with an RNA polymerase II transcription factor, any protein required to initiate or regulate transcription by RNA polymerase II.

Interacting selectively and non-covalently with an RNA polymerase II transcription activating factor, a protein involved in positive regulation of transcription.

Interacting selectively and non-covalently with chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase.

Interacting selectively and non-covalently with a transcription factor, a protein required to initiate or regulate transcription.

Interacting selectively and non-covalently with an estrogen receptor.

Interacting selectively and non-covalently with a nuclear hormone receptor, a ligand-dependent receptor found in the nucleus of the cell.

Interacting selectively and non-covalently with one or more specific sites on an ion channel, a protein complex that spans a membrane and forms a water-filled channel across the phospholipid bilayer allowing selective ion transport down its electrochemical gradient.

Interacting selectively and non-covalently with a SMAD signaling protein.

Interacting selectively and non-covalently with an androgen receptor.

Interacting selectively and non-covalently with an inhibitory SMAD signaling protein.

A protein or a member of a complex that interacts specifically and non-covalently with a DNA-bound DNA-binding transcription factor to activate the transcription of specific genes. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second ATP-dependent class modifies the conformation of chromatin. Another type of coregulator activity is the bridging of a DNA-binding transcription factor to the basal transcription machinery. The Mediator complex, which bridges transcription factors and RNA polymerase, is also a transcription coactivator.

The action of a molecule that contributes to the structural integrity of a complex or its assembly within or outside a cell.

The action of a molecule that contributes to the structural integrity of a cell wall.

Interacting selectively and non-covalently with a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.

Interacting selectively and non-covalently with any protein phosphatase.

Interacting selectively and non-covalently with an identical protein to form a homodimer.

Interacting selectively and non-covalently with the alpha subunit of the catenin complex.

Interacting selectively and non-covalently with cadherin, a type I membrane protein involved in cell adhesion.

Interacting selectively and non-covalently with a cell adhesion molecule.

Interacting selectively and non-covalently with any protein or protein complex that results in the connection of a bundle of His cell with a Purkinje myocyte and contributes to the communication between the two cells.

Interacting selectively and non-covalently with an RNA polymerase II transcription factor, any protein required to initiate or regulate transcription by RNA polymerase II.

Interacting selectively and non-covalently with an RNA polymerase II transcription activating factor, a protein involved in positive regulation of transcription.

Interacting selectively and non-covalently with chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase.

Interacting selectively and non-covalently with chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase.

A protein or a member of a complex that interacts selectively and non-covalently with a specific DNA sequence (sometimes referred to as a motif) within the regulatory region of a gene to modulate transcription. Regulatory regions include promoters (proximal and distal) and enhancers. Genes are transcriptional units, and include bacterial operons.

Interacting selectively and non-covalently with a protein C-terminus, the end of any peptide chain at which the 1-carboxyl function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.

Interacting selectively and non-covalently with a transcription factor, a protein required to initiate or regulate transcription.

Interacting selectively and non-covalently with any enzyme.

Interacting selectively and non-covalently with a kinase, any enzyme that catalyzes the transfer of a phosphate group.

Interacting selectively and non-covalently with an estrogen receptor.

Interacting selectively and non-covalently with an ionotropic glutamate receptor. Ionotropic glutamate receptors bind glutamate and exert an effect through the regulation of ion channels.

Interacting selectively and non-covalently with a nuclear hormone receptor, a ligand-dependent receptor found in the nucleus of the cell.

Interacting selectively and non-covalently with one or more specific sites on an ion channel, a protein complex that spans a membrane and forms a water-filled channel across the phospholipid bilayer allowing selective ion transport down its electrochemical gradient.

Interacting selectively and non-covalently with a macromolecular complex.

Interacting selectively and non-covalently with the alpha subunit of the catenin complex.

Interacting selectively and non-covalently with a SMAD signaling protein.

Interacting selectively and non-covalently with a nonidentical protein to form a heterodimer.

Interacting selectively and non-covalently with the enzyme nitric-oxide synthase.

Interacting selectively and non-covalently with an inhibitory SMAD signaling 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 a disordered domain of a protein.

Interacting selectively and non-covalently with a histone methyltransferase enzyme.

A protein or a member of a complex that interacts specifically and non-covalently with a DNA-bound DNA-binding transcription factor to activate the transcription of specific genes. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second ATP-dependent class modifies the conformation of chromatin. Another type of coregulator activity is the bridging of a DNA-binding transcription factor to the basal transcription machinery. The Mediator complex, which bridges transcription factors and RNA polymerase, is also a transcription coactivator.

Interacting selectively and non-covalently with a transcription factor, a protein required to initiate or regulate transcription.

Interacting selectively and non-covalently with cadherin, a type I membrane protein involved in cell adhesion.

A protein or a member of a complex that interacts specifically and non-covalently with a DNA-bound DNA-binding transcription factor to either activate or repress the transcription of specific genes. Coregulators often act by altering chromatin structure and modifications. For example, one class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second ATP-dependent class modifies the conformation of chromatin. A third class modulates interactions of DNA-binding transcription factor with other transcription coregulators.

Interacting selectively and non-covalently with a transcription factor, a protein required to initiate or regulate transcription.

The function of a transcription cofactor that activates transcription in conjuction with a ligand-dependent nuclear receptor from a RNA polymerase II promoter; does not bind DNA itself.

Interacting selectively and non-covalently with DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding.

Interacting selectively and non-covalently with a DNA region that regulates the transcription of a region of DNA, which may be a gene, cistron, or operon. Binding may occur as a sequence specific interaction or as an interaction observed only once a factor has been recruited to the DNA by other factors.

Interacting selectively and non-covalently with cadherin, a type I membrane protein involved in cell adhesion.

Interacting selectively and non-covalently with cadherin, a type I membrane protein involved in cell adhesion.

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 a component of the extracellular matrix.

The action of a molecule that contributes to the structural integrity of a complex or its assembly within or outside a cell.

The action of a molecule that contributes to the structural integrity of a complex or its assembly within or outside a cell.

Interacting selectively and non-covalently with a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.

Interacting selectively and non-covalently with an ionotropic glutamate receptor. Ionotropic glutamate receptors bind glutamate and exert an effect through the regulation of ion channels.

Interacting selectively and non-covalently with an identical protein to form a homodimer.

Interacting selectively and non-covalently with a macromolecular complex.

Interacting selectively and non-covalently with a cell adhesion molecule.

Interacting selectively and non-covalently with the enzyme nitric-oxide synthase.