Catalysis of the reaction: S-adenosyl-L-methionine + (protein)-arginine = S-adenosyl-L-homocysteine + (protein)-N-methyl-arginine.

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

Catalysis of the addition of a methyl group to either of the unmethylated terminal nitrogen atoms (also called omega nitrogen) in peptidyl-arginine to form an omega-N-G-monomethylated arginine residue. The reaction is S-adenosyl-L-methionine +

Catalysis of the addition of a second methyl group to methylated peptidyl-arginine. Methylation is on the same terminal nitrogen (omega nitrogen) residue that was previously methylated, resulting in asymmetrical peptidyl-N(omega),N(omega)-dimethylated arginine residues.

Interacting selectively and non-covalently with an identical protein or proteins.

Catalysis of the addition of a second methyl group to methylated peptidyl-arginine. Methylation is on the same terminal nitrogen (omega nitrogen) residue that was previously methylated, resulting in asymmetrical peptidyl-N(omega),N(omega)-dimethylated arginine residues.

Catalysis of the transfer of a methyl group to the nitrogen atom of an acceptor molecule.

Catalysis of the transfer of a methyl group (CH3-) to a protein.

Catalysis of the transfer of a methyl group (CH3-) to a protein.

Catalysis of the reaction: S-adenosyl-L-methionine + (histone)-arginine = S-adenosyl-L-homocysteine + (histone)-N-methyl-arginine.

Catalysis of the reaction: S-adenosyl-L-methionine + histone = S-adenosyl-L-homocysteine + methyl-histone. Histone methylation generally occurs on either an arginine or lysine residue.

Catalysis of the reaction: S-adenosyl-L-methionine + (histone H4)-arginine (position 3) = S-adenosyl-L-homocysteine + (histone H4)-N-methyl-arginine (position 3). This reaction is the addition of a methyl group to arginine at position 3 of histone H4.

Interacting selectively and non-covalently with S-adenosyl-L-methionine.

Catalysis of the transfer of a methyl group (CH3-) to a protein.

Interacting selectively and non-covalently with an identical protein or proteins.

Interacting selectively and non-covalently with an RNA molecule or a portion thereof.

Catalysis of the transfer of a methyl group to an acceptor molecule.

Catalysis of the transfer of a methyl group to the nitrogen atom of an acceptor molecule.

Catalysis of the transfer of a methyl group to the nitrogen atom of an acceptor molecule.

Interacting selectively and non-covalently with a methylated cytosine/guanine dinucleotide.

Catalysis of the reaction: S-adenosyl-L-methionine + (protein)-arginine = S-adenosyl-L-homocysteine + (protein)-N-methyl-arginine.

Catalysis of the reaction: S-adenosyl-L-methionine + (protein)-arginine = S-adenosyl-L-homocysteine + (protein)-N-methyl-arginine.

Interacting selectively and non-covalently with any enzyme.

Catalysis of the reaction: S-adenosyl-L-methionine + (histone H4)-arginine (position 3) = S-adenosyl-L-homocysteine + (histone H4)-N-methyl-arginine (position 3). This reaction is the addition of a methyl group to arginine at position 3 of histone H4.

Interacting selectively and non-covalently with mitogen-activated protein kinase p38, an enzyme that catalyzes the transfer of phosphate from ATP to hydroxyl side chains on proteins in response to mitogen activation.

Interacting selectively and non-covalently with S-adenosyl-L-methionine.

Catalysis of the addition of a methyl group to either of the unmethylated terminal nitrogen atoms (also called omega nitrogen) in peptidyl-arginine to form an omega-N-G-monomethylated arginine residue. The reaction is S-adenosyl-L-methionine +

Interacting selectively and non-covalently with an identical protein or proteins.

Catalysis of the addition of a methyl group to either of the unmethylated terminal nitrogen atoms (also called omega nitrogen) in peptidyl-arginine to form an omega-N-G-monomethylated arginine residue. The reaction is S-adenosyl-L-methionine +

Catalysis of the reaction: S-adenosyl-L-methionine + (histone H4)-arginine (position 3) = S-adenosyl-L-homocysteine + (histone H4)-N-methyl-arginine (position 3). This reaction is the addition of a methyl group to arginine at position 3 of histone H4.

Catalysis of the reaction: S-adenosyl-L-methionine + (histone)-arginine = S-adenosyl-L-homocysteine + (histone)-N-methyl-arginine.

Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to a substrate.

Enables the transfer of a methyl group from S-adenosyl-L-methionine to an amino group of an arginine residue.

Interacting selectively and non-covalently with a methylated cytosine/guanine dinucleotide.

Catalysis of the transfer of a methyl group to the nitrogen atom of an acceptor molecule.

Catalysis of the reaction: S-adenosyl-L-methionine + (histone)-arginine = S-adenosyl-L-homocysteine + (histone)-N-methyl-arginine.

Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to a substrate.

Catalysis of the reaction: S-adenosyl-L-methionine + (cytochrome c)-arginine = S-adenosyl-L-homocysteine + (cytochrome c)-N(omega)-methyl-arginine.

Interacting selectively and non-covalently with any part of a small nucleolar ribonucleoprotein particle.

Catalysis of the addition of a methyl group to either of the unmethylated terminal nitrogen atoms (also called omega nitrogen) in peptidyl-arginine to form an omega-N-G-monomethylated arginine residue. The reaction is S-adenosyl-L-methionine +

Catalysis of the addition of a second methyl group to methylated peptidyl-arginine. Methylation is on the same terminal nitrogen (omega nitrogen) residue that was previously methylated, resulting in asymmetrical peptidyl-N(omega),N(omega)-dimethylated arginine residues.

Catalysis of the addition of a second methyl group to methylated peptidyl-arginine. Methylation is on the same terminal nitrogen (omega nitrogen) residue that was previously methylated, resulting in asymmetrical peptidyl-N(omega),N(omega)-dimethylated arginine residues.

Catalysis of the reaction: S-adenosyl-L-methionine + histone = S-adenosyl-L-homocysteine + methyl-histone. Histone methylation generally occurs on either an arginine or lysine residue.

Interacting selectively and non-covalently with an identical protein or proteins.

Interacting selectively and non-covalently with S-adenosyl-L-methionine.

Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to a substrate.

Catalysis of the reaction: S-adenosyl-L-methionine + (protein)-arginine = S-adenosyl-L-homocysteine + (protein)-N-methyl-arginine.

Catalysis of the reaction: S-adenosyl-L-methionine + (protein)-arginine = S-adenosyl-L-homocysteine + (protein)-N-methyl-arginine.

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

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

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

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

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.

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.

Catalysis of the transfer of a methyl group to the nitrogen atom of an acceptor molecule.

Catalysis of the transfer of a methyl group (CH3-) to a protein.

Interacting selectively and non-covalently with a methylated cytosine/guanine dinucleotide.

Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to a substrate.

Enables the transfer of a methyl group from S-adenosyl-L-methionine to an amino group of an arginine residue.

Catalysis of the reaction: S-adenosyl-L-methionine + (protein)-arginine = S-adenosyl-L-homocysteine + (protein)-N-methyl-arginine.

Catalysis of the reaction: S-adenosyl-L-methionine + (protein)-arginine = S-adenosyl-L-homocysteine + (protein)-N-methyl-arginine.

Catalysis of the reaction: S-adenosyl-L-methionine + (cytochrome c)-arginine = S-adenosyl-L-homocysteine + (cytochrome c)-N(omega)-methyl-arginine.

Interacting selectively and non-covalently with any enzyme.

Interacting selectively and non-covalently with any part of a small nucleolar ribonucleoprotein particle.

Catalysis of the reaction: S-adenosyl-L-methionine + histone = S-adenosyl-L-homocysteine + methyl-histone. Histone methylation generally occurs on either an arginine or lysine residue.

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

Catalysis of the reaction: S-adenosyl-L-methionine + (histone H4)-arginine (position 3) = S-adenosyl-L-homocysteine + (histone H4)-N-methyl-arginine (position 3). This reaction is the addition of a methyl group to arginine at position 3 of histone H4.

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

Interacting selectively and non-covalently with mitogen-activated protein kinase p38, an enzyme that catalyzes the transfer of phosphate from ATP to hydroxyl side chains on proteins in response to mitogen activation.