The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was named:
"Hnrnp arginine n-methyltransferase1
".
FunFam 9: protein arginine N-methyltransferase 6
Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.
There are 31 GO terms relating to "molecular function"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
GO Term | Annotations | Evidence |
---|---|---|
Protein binding GO:0005515
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
|
7 | Q6NZB1 (/IPI) Q96LA8 (/IPI) Q96LA8 (/IPI) Q96LA8 (/IPI) Q96LA8 (/IPI) Q96LA8 (/IPI) Q96LA8 (/IPI) |
Histone-arginine N-methyltransferase activity GO:0008469
Catalysis of the reaction: S-adenosyl-L-methionine + (histone)-arginine = S-adenosyl-L-homocysteine + (histone)-N-methyl-arginine.
|
7 | Q6NZB1 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) |
Protein-arginine omega-N monomethyltransferase activity GO:0035241
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 +
|
7 | B0JYW5 (/ISS) Q5E9L5 (/ISS) Q5E9L5 (/ISS) Q68EZ3 (/ISS) Q68EZ3 (/ISS) Q6NWG4 (/ISS) Q6NZB1 (/ISS) |
Protein-arginine omega-N asymmetric methyltransferase activity GO:0035242
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.
|
7 | B0JYW5 (/ISS) Q5E9L5 (/ISS) Q5E9L5 (/ISS) Q68EZ3 (/ISS) Q68EZ3 (/ISS) Q6NWG4 (/ISS) Q6NZB1 (/ISS) |
Histone methyltransferase activity GO:0042054
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.
|
7 | B0JYW5 (/ISS) Q5E9L5 (/ISS) Q5E9L5 (/ISS) Q68EZ3 (/ISS) Q68EZ3 (/ISS) Q6NWG4 (/ISS) Q6NZB1 (/ISS) |
Histone binding GO:0042393
Interacting selectively and non-covalently with a histone, any of a group of water-soluble proteins found in association with the DNA of eukaroytic 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.
|
7 | B0JYW5 (/ISS) Q5E9L5 (/ISS) Q5E9L5 (/ISS) Q68EZ3 (/ISS) Q68EZ3 (/ISS) Q6NWG4 (/ISS) Q6NZB1 (/ISS) |
Histone methyltransferase activity (H4-R3 specific) GO:0044020
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.
|
7 | B0JYW5 (/ISS) Q5E9L5 (/ISS) Q5E9L5 (/ISS) Q68EZ3 (/ISS) Q68EZ3 (/ISS) Q6NWG4 (/ISS) Q6NZB1 (/ISS) |
Histone methyltransferase activity (H3-R2 specific) GO:0070611
Catalysis of the reaction: S-adenosyl-L-methionine + (histone H3)-arginine (position 2) = S-adenosyl-L-homocysteine + (histone H3)-N-methyl-arginine (position 2). This reaction is the addition of a methyl group to arginine at position 2 of histone H3.
|
7 | B0JYW5 (/ISS) Q5E9L5 (/ISS) Q5E9L5 (/ISS) Q68EZ3 (/ISS) Q68EZ3 (/ISS) Q6NWG4 (/ISS) Q6NZB1 (/ISS) |
Histone methyltransferase activity (H2A-R3 specific) GO:0070612
Catalysis of the reaction: S-adenosyl-L-methionine + (histone H2A)-arginine (position 3) = S-adenosyl-L-homocysteine + (histone H2A)-N-methyl-arginine (position 3). This reaction is the addition of a methyl group to arginine at position 3 of histone H2A.
|
7 | B0JYW5 (/ISS) Q5E9L5 (/ISS) Q5E9L5 (/ISS) Q68EZ3 (/ISS) Q68EZ3 (/ISS) Q6NWG4 (/ISS) Q6NZB1 (/ISS) |
Histone-arginine N-methyltransferase activity GO:0008469
Catalysis of the reaction: S-adenosyl-L-methionine + (histone)-arginine = S-adenosyl-L-homocysteine + (histone)-N-methyl-arginine.
|
6 | Q96LA8 (/EXP) Q96LA8 (/EXP) Q96LA8 (/EXP) Q96LA8 (/EXP) Q96LA8 (/EXP) Q96LA8 (/EXP) |
Histone-arginine N-methyltransferase activity GO:0008469
Catalysis of the reaction: S-adenosyl-L-methionine + (histone)-arginine = S-adenosyl-L-homocysteine + (histone)-N-methyl-arginine.
|
6 | B0JYW5 (/ISS) Q5E9L5 (/ISS) Q5E9L5 (/ISS) Q68EZ3 (/ISS) Q68EZ3 (/ISS) Q6NWG4 (/ISS) |
Histone-arginine N-methyltransferase activity GO:0008469
Catalysis of the reaction: S-adenosyl-L-methionine + (histone)-arginine = S-adenosyl-L-homocysteine + (histone)-N-methyl-arginine.
|
6 | Q96LA8 (/TAS) Q96LA8 (/TAS) Q96LA8 (/TAS) Q96LA8 (/TAS) Q96LA8 (/TAS) Q96LA8 (/TAS) |
Protein-arginine N-methyltransferase activity GO:0016274
Catalysis of the reaction: S-adenosyl-L-methionine + (protein)-arginine = S-adenosyl-L-homocysteine + (protein)-N-methyl-arginine.
|
6 | Q96LA8 (/TAS) Q96LA8 (/TAS) Q96LA8 (/TAS) Q96LA8 (/TAS) Q96LA8 (/TAS) Q96LA8 (/TAS) |
Protein-arginine omega-N monomethyltransferase activity GO:0035241
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 +
|
6 | Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) |
Protein-arginine omega-N asymmetric methyltransferase activity GO:0035242
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.
|
6 | Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) |
Histone methyltransferase activity GO:0042054
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.
|
6 | Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) |
Histone binding GO:0042393
Interacting selectively and non-covalently with a histone, any of a group of water-soluble proteins found in association with the DNA of eukaroytic 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.
|
6 | Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) |
Histone methyltransferase activity (H4-R3 specific) GO:0044020
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.
|
6 | Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) |
Histone methyltransferase activity (H3-R2 specific) GO:0070611
Catalysis of the reaction: S-adenosyl-L-methionine + (histone H3)-arginine (position 2) = S-adenosyl-L-homocysteine + (histone H3)-N-methyl-arginine (position 2). This reaction is the addition of a methyl group to arginine at position 2 of histone H3.
|
6 | Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) |
Histone methyltransferase activity (H2A-R3 specific) GO:0070612
Catalysis of the reaction: S-adenosyl-L-methionine + (histone H2A)-arginine (position 3) = S-adenosyl-L-homocysteine + (histone H2A)-N-methyl-arginine (position 3). This reaction is the addition of a methyl group to arginine at position 3 of histone H2A.
|
6 | Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) |
Chromatin binding GO:0003682
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.
|
1 | Q6NZB1 (/IDA) |
Histone-arginine N-methyltransferase activity GO:0008469
Catalysis of the reaction: S-adenosyl-L-methionine + (histone)-arginine = S-adenosyl-L-homocysteine + (histone)-N-methyl-arginine.
|
1 | Q6NZB1 (/ISO) |
S-adenosylmethionine-dependent methyltransferase activity GO:0008757
Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to a substrate.
|
1 | Q6NWG4 (/ISS) |
Protein-arginine N-methyltransferase activity GO:0016274
Catalysis of the reaction: S-adenosyl-L-methionine + (protein)-arginine = S-adenosyl-L-homocysteine + (protein)-N-methyl-arginine.
|
1 | Q6NZB1 (/IDA) |
Protein-arginine omega-N monomethyltransferase activity GO:0035241
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 +
|
1 | Q6NZB1 (/ISO) |
Protein-arginine omega-N asymmetric methyltransferase activity GO:0035242
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.
|
1 | Q6NZB1 (/ISO) |
Histone methyltransferase activity GO:0042054
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.
|
1 | Q6NZB1 (/ISO) |
Histone binding GO:0042393
Interacting selectively and non-covalently with a histone, any of a group of water-soluble proteins found in association with the DNA of eukaroytic 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.
|
1 | Q6NZB1 (/ISO) |
Histone methyltransferase activity (H4-R3 specific) GO:0044020
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.
|
1 | Q6NZB1 (/ISO) |
Histone methyltransferase activity (H3-R2 specific) GO:0070611
Catalysis of the reaction: S-adenosyl-L-methionine + (histone H3)-arginine (position 2) = S-adenosyl-L-homocysteine + (histone H3)-N-methyl-arginine (position 2). This reaction is the addition of a methyl group to arginine at position 2 of histone H3.
|
1 | Q6NZB1 (/ISO) |
Histone methyltransferase activity (H2A-R3 specific) GO:0070612
Catalysis of the reaction: S-adenosyl-L-methionine + (histone H2A)-arginine (position 3) = S-adenosyl-L-homocysteine + (histone H2A)-N-methyl-arginine (position 3). This reaction is the addition of a methyl group to arginine at position 3 of histone H2A.
|
1 | Q6NZB1 (/ISO) |
There are 21 GO terms relating to "biological process"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
GO Term | Annotations | Evidence |
---|---|---|
Peptidyl-arginine methylation, to asymmetrical-dimethyl arginine GO:0019919
The process of methylation of peptidyl-arginine to form peptidyl-N(omega),N(omega)-dimethyl-L-arginine.
|
7 | B0JYW5 (/ISS) Q5E9L5 (/ISS) Q5E9L5 (/ISS) Q68EZ3 (/ISS) Q68EZ3 (/ISS) Q6NWG4 (/ISS) Q6NZB1 (/ISS) |
Histone H3-R2 methylation GO:0034970
The modification of histone H3 by addition of a methyl group to arginine at position 2 of the histone.
|
7 | B0JYW5 (/ISS) Q5E9L5 (/ISS) Q5E9L5 (/ISS) Q68EZ3 (/ISS) Q68EZ3 (/ISS) Q6NWG4 (/ISS) Q6NZB1 (/ISS) |
Negative regulation of transcription, DNA-templated GO:0045892
Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription.
|
7 | B0JYW5 (/ISS) Q5E9L5 (/ISS) Q5E9L5 (/ISS) Q68EZ3 (/ISS) Q68EZ3 (/ISS) Q6NWG4 (/ISS) Q6NZB1 (/ISS) |
Base-excision repair GO:0006284
In base excision repair, an altered base is removed by a DNA glycosylase enzyme, followed by excision of the resulting sugar phosphate. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase.
|
6 | Q96LA8 (/TAS) Q96LA8 (/TAS) Q96LA8 (/TAS) Q96LA8 (/TAS) Q96LA8 (/TAS) Q96LA8 (/TAS) |
Histone methylation GO:0016571
The modification of histones by addition of methyl groups.
|
6 | Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) |
Peptidyl-arginine methylation, to asymmetrical-dimethyl arginine GO:0019919
The process of methylation of peptidyl-arginine to form peptidyl-N(omega),N(omega)-dimethyl-L-arginine.
|
6 | Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) |
Histone H3-R2 methylation GO:0034970
The modification of histone H3 by addition of a methyl group to arginine at position 2 of the histone.
|
6 | Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) |
Peptidyl-arginine N-methylation GO:0035246
The addition of a methyl group onto a nitrogen atom of an arginine residue in a protein.
|
6 | B0JYW5 (/ISS) Q5E9L5 (/ISS) Q5E9L5 (/ISS) Q68EZ3 (/ISS) Q68EZ3 (/ISS) Q6NWG4 (/ISS) |
Regulation of megakaryocyte differentiation GO:0045652
Any process that modulates the frequency, rate or extent of megakaryocyte differentiation.
|
6 | Q96LA8 (/TAS) Q96LA8 (/TAS) Q96LA8 (/TAS) Q96LA8 (/TAS) Q96LA8 (/TAS) Q96LA8 (/TAS) |
Negative regulation of transcription, DNA-templated GO:0045892
Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription.
|
6 | Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) |
Histone H3-R2 methylation GO:0034970
The modification of histone H3 by addition of a methyl group to arginine at position 2 of the histone.
|
2 | Q6NWG4 (/IMP) Q6NZB1 (/IMP) |
Negative regulation of histone H3-K4 methylation GO:0051572
Any process that stops, prevents, or reduces the frequency, rate or extent of the covalent addition of a methyl group to the lysine at position 4 of histone H3.
|
2 | Q6NWG4 (/IMP) Q6NZB1 (/IMP) |
Negative regulation of transcription by RNA polymerase II GO:0000122
Any process that stops, prevents, or reduces the frequency, rate or extent of transcription mediated by RNA polymerase II.
|
1 | Q6NZB1 (/IMP) |
Negative regulation of gene expression GO:0010629
Any process that decreases the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA or circRNA (for protein-coding genes) and the translation of that mRNA or circRNA into protein. Protein maturation is included when required to form an active form of a product from an inactive precursor form.
|
1 | Q6NWG4 (/IMP) |
Histone methylation GO:0016571
The modification of histones by addition of methyl groups.
|
1 | Q6NZB1 (/ISO) |
Peptidyl-arginine methylation, to asymmetrical-dimethyl arginine GO:0019919
The process of methylation of peptidyl-arginine to form peptidyl-N(omega),N(omega)-dimethyl-L-arginine.
|
1 | Q6NZB1 (/ISO) |
Histone H3-R2 methylation GO:0034970
The modification of histone H3 by addition of a methyl group to arginine at position 2 of the histone.
|
1 | Q6NZB1 (/ISO) |
Peptidyl-arginine N-methylation GO:0035246
The addition of a methyl group onto a nitrogen atom of an arginine residue in a protein.
|
1 | Q6NZB1 (/IDA) |
Negative regulation of transcription, DNA-templated GO:0045892
Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription.
|
1 | Q6NZB1 (/ISO) |
Cellular senescence GO:0090398
A cell aging process stimulated in response to cellular stress, whereby normal cells lose the ability to divide through irreversible cell cycle arrest.
|
1 | Q6NZB1 (/IMP) |
Regulation of signal transduction by p53 class mediator GO:1901796
Any process that modulates the frequency, rate or extent of signal transduction by p53 class mediator.
|
1 | Q6NZB1 (/IMP) |
There are 7 GO terms relating to "cellular component"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
GO Term | Annotations | Evidence |
---|---|---|
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
|
7 | B0JYW5 (/ISS) Q5E9L5 (/ISS) Q5E9L5 (/ISS) Q68EZ3 (/ISS) Q68EZ3 (/ISS) Q6NWG4 (/ISS) Q6NZB1 (/ISS) |
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
|
6 | Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) |
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
6 | Q96LA8 (/TAS) Q96LA8 (/TAS) Q96LA8 (/TAS) Q96LA8 (/TAS) Q96LA8 (/TAS) Q96LA8 (/TAS) |
Nucleolus GO:0005730
A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
|
6 | Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) Q96LA8 (/IDA) |
Chromatin GO:0000785
The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome.
|
1 | Q6NWG4 (/IDA) |
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
|
1 | Q6NZB1 (/ISO) |
Nucleolus GO:0005730
A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
|
1 | Q6NZB1 (/ISO) |