The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:
"Bromodomain-like
".
FunFam 5: protein kinase C-binding protein 1 isoform X2
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 17 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 |
|---|---|---|
|
Transcription corepressor activity GO:0003714
A protein or a member of a complex that interacts specifically and non-covalently with a DNA-bound DNA-binding transcription factor to repress the transcription of specific genes. Corepressors 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 occludes DNA-binding transcription factor protein-protein interaction domains. A fourth class of corepressors prevents interactions of DNA bound DNA-binding transcription factor with coactivators.
|
13 |
A2A480 (/ISO)
A2A481 (/ISO)
A2A482 (/ISO)
A2A483 (/ISO)
A2A484 (/ISO)
A2A485 (/ISO)
E9Q8D1 (/ISO)
Q3U1M7 (/ISO)
Q3UH28 (/ISO)
Q3V1I9 (/ISO)
(3 more) |
|
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
|
13 |
A2A480 (/ISO)
A2A481 (/ISO)
A2A482 (/ISO)
A2A483 (/ISO)
A2A484 (/ISO)
A2A485 (/ISO)
E9Q8D1 (/ISO)
Q3U1M7 (/ISO)
Q3UH28 (/ISO)
Q3V1I9 (/ISO)
(3 more) |
|
Protein domain specific binding GO:0019904
Interacting selectively and non-covalently with a specific domain of a protein.
|
13 |
A2A480 (/ISO)
A2A481 (/ISO)
A2A482 (/ISO)
A2A483 (/ISO)
A2A484 (/ISO)
A2A485 (/ISO)
E9Q8D1 (/ISO)
Q3U1M7 (/ISO)
Q3UH28 (/ISO)
Q3V1I9 (/ISO)
(3 more) |
|
Methylated histone binding GO:0035064
Interacting selectively and non-covalently with a histone in which a residue has been modified by methylation. Histones are any of a group of water-soluble proteins found in association with the DNA of eukaroytic chromosomes.
|
13 |
A2A480 (/ISO)
A2A481 (/ISO)
A2A482 (/ISO)
A2A483 (/ISO)
A2A484 (/ISO)
A2A485 (/ISO)
E9Q8D1 (/ISO)
Q3U1M7 (/ISO)
Q3UH28 (/ISO)
Q3V1I9 (/ISO)
(3 more) |
|
Protein N-terminus binding GO:0047485
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.
|
13 |
A2A480 (/ISO)
A2A481 (/ISO)
A2A482 (/ISO)
A2A483 (/ISO)
A2A484 (/ISO)
A2A485 (/ISO)
E9Q8D1 (/ISO)
Q3U1M7 (/ISO)
Q3UH28 (/ISO)
Q3V1I9 (/ISO)
(3 more) |
|
Lysine-acetylated histone binding GO:0070577
Interacting selectively and non-covalently with a histone in which a lysine residue has been modified by acetylation.
|
13 |
A2A480 (/ISO)
A2A481 (/ISO)
A2A482 (/ISO)
A2A483 (/ISO)
A2A484 (/ISO)
A2A485 (/ISO)
E9Q8D1 (/ISO)
Q3U1M7 (/ISO)
Q3UH28 (/ISO)
Q3V1I9 (/ISO)
(3 more) |
|
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).
|
2 | A8C4G9 (/IPI) Q9ULU4 (/IPI) |
|
Protein N-terminus binding GO:0047485
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.
|
2 | A0A0G2K9F7 (/IPI) A8C4G9 (/IPI) |
|
Transcription corepressor activity GO:0003714
A protein or a member of a complex that interacts specifically and non-covalently with a DNA-bound DNA-binding transcription factor to repress the transcription of specific genes. Corepressors 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 occludes DNA-binding transcription factor protein-protein interaction domains. A fourth class of corepressors prevents interactions of DNA bound DNA-binding transcription factor with coactivators.
|
1 | D5LMF5 (/IDA) |
|
Transcription corepressor activity GO:0003714
A protein or a member of a complex that interacts specifically and non-covalently with a DNA-bound DNA-binding transcription factor to repress the transcription of specific genes. Corepressors 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 occludes DNA-binding transcription factor protein-protein interaction domains. A fourth class of corepressors prevents interactions of DNA bound DNA-binding transcription factor with coactivators.
|
1 | Q9ULU4 (/IMP) |
|
Transcription corepressor activity GO:0003714
A protein or a member of a complex that interacts specifically and non-covalently with a DNA-bound DNA-binding transcription factor to repress the transcription of specific genes. Corepressors 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 occludes DNA-binding transcription factor protein-protein interaction domains. A fourth class of corepressors prevents interactions of DNA bound DNA-binding transcription factor with coactivators.
|
1 | Q9ULU4 (/ISS) |
|
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
|
1 | Q9ULU4 (/IDA) |
|
Protein domain specific binding GO:0019904
Interacting selectively and non-covalently with a specific domain of a protein.
|
1 | Q9ULU4 (/IDA) |
|
Methylated histone binding GO:0035064
Interacting selectively and non-covalently with a histone in which a residue has been modified by methylation. Histones are any of a group of water-soluble proteins found in association with the DNA of eukaroytic chromosomes.
|
1 | Q9ULU4 (/IDA) |
|
Repressing transcription factor binding GO:0070491
Interacting selectively and non-covalently with a transcription repressor, any protein whose activity is required to prevent or downregulate transcription.
|
1 | D5LMF5 (/IPI) |
|
Repressing transcription factor binding GO:0070491
Interacting selectively and non-covalently with a transcription repressor, any protein whose activity is required to prevent or downregulate transcription.
|
1 | Q9ULU4 (/ISS) |
|
Lysine-acetylated histone binding GO:0070577
Interacting selectively and non-covalently with a histone in which a lysine residue has been modified by acetylation.
|
1 | Q9ULU4 (/IDA) |
There are 13 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 |
|---|---|---|
|
Negative regulation of cell migration GO:0030336
Any process that stops, prevents, or reduces the frequency, rate or extent of cell migration.
|
13 |
A2A480 (/ISO)
A2A481 (/ISO)
A2A482 (/ISO)
A2A483 (/ISO)
A2A484 (/ISO)
A2A485 (/ISO)
E9Q8D1 (/ISO)
Q3U1M7 (/ISO)
Q3UH28 (/ISO)
Q3V1I9 (/ISO)
(3 more) |
|
Positive regulation of filopodium assembly GO:0051491
Any process that activates or increases the frequency, rate or extent of the assembly of a filopodium, a thin, stiff protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal growth cone.
|
13 |
A2A480 (/ISO)
A2A481 (/ISO)
A2A482 (/ISO)
A2A483 (/ISO)
A2A484 (/ISO)
A2A485 (/ISO)
E9Q8D1 (/ISO)
Q3U1M7 (/ISO)
Q3UH28 (/ISO)
Q3V1I9 (/ISO)
(3 more) |
|
Positive regulation of dendritic spine development GO:0060999
Any process that increases the rate, frequency, or extent of dendritic spine development, the process whose specific outcome is the progression of the dendritic spine over time, from its formation to the mature structure.
|
13 |
A2A480 (/ISO)
A2A481 (/ISO)
A2A482 (/ISO)
A2A483 (/ISO)
A2A484 (/ISO)
A2A485 (/ISO)
E9Q8D1 (/ISO)
Q3U1M7 (/ISO)
Q3UH28 (/ISO)
Q3V1I9 (/ISO)
(3 more) |
|
Modulation of excitatory postsynaptic potential GO:0098815
Any process that modulates the frequency, rate or extent of excitatory postsynaptic potential (EPSP). EPSP is a process that leads to a temporary increase in postsynaptic potential due to the flow of positively charged ions into the postsynaptic cell. The flow of ions that causes an EPSP is an excitatory postsynaptic current (EPSC) and makes it easier for the neuron to fire an action potential.
|
13 |
A2A480 (/ISO)
A2A481 (/ISO)
A2A482 (/ISO)
A2A483 (/ISO)
A2A484 (/ISO)
A2A485 (/ISO)
E9Q8D1 (/ISO)
Q3U1M7 (/ISO)
Q3UH28 (/ISO)
Q3V1I9 (/ISO)
(3 more) |
|
Regulation of postsynaptic density protein 95 clustering GO:1902897
Any process that modulates the frequency, rate or extent of postsynaptic density protein 95 clustering.
|
13 |
A2A480 (/ISO)
A2A481 (/ISO)
A2A482 (/ISO)
A2A483 (/ISO)
A2A484 (/ISO)
A2A485 (/ISO)
E9Q8D1 (/ISO)
Q3U1M7 (/ISO)
Q3UH28 (/ISO)
Q3V1I9 (/ISO)
(3 more) |
|
Positive regulation of dendritic spine maintenance GO:1902952
Any process that activates or increases the frequency, rate or extent of dendritic spine maintenance.
|
13 |
A2A480 (/ISO)
A2A481 (/ISO)
A2A482 (/ISO)
A2A483 (/ISO)
A2A484 (/ISO)
A2A485 (/ISO)
E9Q8D1 (/ISO)
Q3U1M7 (/ISO)
Q3UH28 (/ISO)
Q3V1I9 (/ISO)
(3 more) |
|
Positive regulation of filopodium assembly GO:0051491
Any process that activates or increases the frequency, rate or extent of the assembly of a filopodium, a thin, stiff protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal growth cone.
|
2 | A0A0G2K9F7 (/IMP) A8C4G9 (/IMP) |
|
Positive regulation of dendritic spine development GO:0060999
Any process that increases the rate, frequency, or extent of dendritic spine development, the process whose specific outcome is the progression of the dendritic spine over time, from its formation to the mature structure.
|
2 | A0A0G2K9F7 (/IMP) A8C4G9 (/IMP) |
|
Modulation of excitatory postsynaptic potential GO:0098815
Any process that modulates the frequency, rate or extent of excitatory postsynaptic potential (EPSP). EPSP is a process that leads to a temporary increase in postsynaptic potential due to the flow of positively charged ions into the postsynaptic cell. The flow of ions that causes an EPSP is an excitatory postsynaptic current (EPSC) and makes it easier for the neuron to fire an action potential.
|
2 | A0A0G2K9F7 (/IMP) A8C4G9 (/IMP) |
|
Regulation of postsynaptic density protein 95 clustering GO:1902897
Any process that modulates the frequency, rate or extent of postsynaptic density protein 95 clustering.
|
2 | A0A0G2K9F7 (/IMP) A8C4G9 (/IMP) |
|
Positive regulation of dendritic spine maintenance GO:1902952
Any process that activates or increases the frequency, rate or extent of dendritic spine maintenance.
|
2 | A0A0G2K9F7 (/IMP) A8C4G9 (/IMP) |
|
Nervous system development GO:0007399
The process whose specific outcome is the progression of nervous tissue over time, from its formation to its mature state.
|
1 | D5LMF5 (/IMP) |
|
Negative regulation of cell migration GO:0030336
Any process that stops, prevents, or reduces the frequency, rate or extent of cell migration.
|
1 | Q9ULU4 (/IMP) |
There are 10 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.
|
13 |
A2A480 (/ISO)
A2A481 (/ISO)
A2A482 (/ISO)
A2A483 (/ISO)
A2A484 (/ISO)
A2A485 (/ISO)
E9Q8D1 (/ISO)
Q3U1M7 (/ISO)
Q3UH28 (/ISO)
Q3V1I9 (/ISO)
(3 more) |
|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
13 |
A2A480 (/ISO)
A2A481 (/ISO)
A2A482 (/ISO)
A2A483 (/ISO)
A2A484 (/ISO)
A2A485 (/ISO)
E9Q8D1 (/ISO)
Q3U1M7 (/ISO)
Q3UH28 (/ISO)
Q3V1I9 (/ISO)
(3 more) |
|
Dendritic spine GO:0043197
A small, membranous protrusion from a dendrite that forms a postsynaptic compartment - typically receiving input from a single presynapse. They function as partially isolated biochemical and an electrical compartments. Spine morphology is variable including \thin\, \stubby\, \mushroom\, and \branched\, with a continuum of intermediate morphologies. They typically terminate in a bulb shape, linked to the dendritic shaft by a restriction. Spine remodeling is though to be involved in synaptic plasticity.
|
13 |
A2A480 (/ISO)
A2A481 (/ISO)
A2A482 (/ISO)
A2A483 (/ISO)
A2A484 (/ISO)
A2A485 (/ISO)
E9Q8D1 (/ISO)
Q3U1M7 (/ISO)
Q3UH28 (/ISO)
Q3V1I9 (/ISO)
(3 more) |
|
Dendritic shaft GO:0043198
Cylindric portion of the dendrite, directly stemming from the perikaryon, and carrying the dendritic spines.
|
13 |
A2A480 (/ISO)
A2A481 (/ISO)
A2A482 (/ISO)
A2A483 (/ISO)
A2A484 (/ISO)
A2A485 (/ISO)
E9Q8D1 (/ISO)
Q3U1M7 (/ISO)
Q3UH28 (/ISO)
Q3V1I9 (/ISO)
(3 more) |
|
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.
|
4 | A0A0G2K9F7 (/IDA) A8C4G9 (/IDA) D5LMF5 (/IDA) Q9ULU4 (/IDA) |
|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
2 | A0A0G2K9F7 (/IDA) A8C4G9 (/IDA) |
|
Dendritic spine GO:0043197
A small, membranous protrusion from a dendrite that forms a postsynaptic compartment - typically receiving input from a single presynapse. They function as partially isolated biochemical and an electrical compartments. Spine morphology is variable including \thin\, \stubby\, \mushroom\, and \branched\, with a continuum of intermediate morphologies. They typically terminate in a bulb shape, linked to the dendritic shaft by a restriction. Spine remodeling is though to be involved in synaptic plasticity.
|
2 | A0A0G2K9F7 (/IDA) A8C4G9 (/IDA) |
|
Dendritic shaft GO:0043198
Cylindric portion of the dendrite, directly stemming from the perikaryon, and carrying the dendritic spines.
|
2 | A0A0G2K9F7 (/IDA) A8C4G9 (/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 | Q9ULU4 (/ISS) |
|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | Q9ULU4 (/IMP) |