CATH Superfamily 2.30.29.30
Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
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:
"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
".
FunFam 20: Actin filament-associated protein 1-like 2 isoform...
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 10 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).
|
6 | Q5DTU0 (/IPI) Q8BZI0 (/IPI) Q8BZI0 (/IPI) Q8TED9 (/IPI) Q8VH46 (/IPI) Q90738 (/IPI) |
SH3 domain binding GO:0017124
Interacting selectively and non-covalently with a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins.
|
2 | Q8N4X5 (/IPI) Q8VH46 (/IPI) |
SH3 domain binding GO:0017124
Interacting selectively and non-covalently with a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins.
|
2 | Q5DTU0 (/ISO) Q80YS6 (/ISO) |
SH2 domain binding GO:0042169
Interacting selectively and non-covalently with a SH2 domain (Src homology 2) of a protein, a protein domain of about 100 amino-acid residues and belonging to the alpha + beta domain class.
|
2 | Q8N4X5 (/IPI) Q8VH46 (/IPI) |
SH2 domain binding GO:0042169
Interacting selectively and non-covalently with a SH2 domain (Src homology 2) of a protein, a protein domain of about 100 amino-acid residues and belonging to the alpha + beta domain class.
|
2 | Q5DTU0 (/ISO) Q80YS6 (/ISO) |
SH3 domain binding GO:0017124
Interacting selectively and non-covalently with a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins.
|
1 | Q90738 (/IDA) |
Protein tyrosine kinase activator activity GO:0030296
Increases the activity of a protein tyrosine kinase, an enzyme which phosphorylates a tyrosyl phenolic group on a protein.
|
1 | Q8N4X5 (/IDA) |
Protein tyrosine kinase activator activity GO:0030296
Increases the activity of a protein tyrosine kinase, an enzyme which phosphorylates a tyrosyl phenolic group on a protein.
|
1 | Q5DTU0 (/ISO) |
Phosphatidylinositol-3-phosphate binding GO:0032266
Interacting selectively and non-covalently with phosphatidylinositol-3-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' position.
|
1 | Q92349 (/IMP) |
SH2 domain binding GO:0042169
Interacting selectively and non-covalently with a SH2 domain (Src homology 2) of a protein, a protein domain of about 100 amino-acid residues and belonging to the alpha + beta domain class.
|
1 | Q90738 (/IDA) |
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 |
---|---|---|
Inflammatory response GO:0006954
The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages.
|
1 | Q8N4X5 (/IDA) |
Inflammatory response GO:0006954
The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages.
|
1 | Q5DTU0 (/ISO) |
Signal transduction GO:0007165
The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.
|
1 | Q8VH46 (/NAS) |
Regulation of mitotic cell cycle GO:0007346
Any process that modulates the rate or extent of progress through the mitotic cell cycle.
|
1 | Q8N4X5 (/IDA) |
Regulation of mitotic cell cycle GO:0007346
Any process that modulates the rate or extent of progress through the mitotic cell cycle.
|
1 | Q5DTU0 (/ISO) |
Regulation of signal transduction GO:0009966
Any process that modulates the frequency, rate or extent of signal transduction.
|
1 | Q8VH46 (/IDA) |
Regulation of signal transduction GO:0009966
Any process that modulates the frequency, rate or extent of signal transduction.
|
1 | Q80YS6 (/ISO) |
Peptidyl-tyrosine phosphorylation GO:0018108
The phosphorylation of peptidyl-tyrosine to form peptidyl-O4'-phospho-L-tyrosine.
|
1 | Q90738 (/IGI) |
Peptidyl-arginine phosphorylation GO:0018109
The phosphorylation of peptidyl-arginine to form omega-N-phospho-L-arginine.
|
1 | Q90738 (/IMP) |
Ascospore-type prospore-specific spindle pole body remodeling GO:0031322
A spindle pole body (SPB) organization process that takes place during the second meiotic division during ascospore formation and results in the structural reorganization of the SPB; includes the recruitment of sporulation-specific proteins to the outer plaque to form the meiotic outer plaque (MOP).
|
1 | Q92349 (/IMP) |
Ascospore-type prospore membrane assembly GO:0032120
The process in which the nascent membrane forms at the meiotic outer plaque and grows until closure occurs and forespores, or prospores, are formed.
|
1 | Q92349 (/IMP) |
Regulation of interleukin-6 production GO:0032675
Any process that modulates the frequency, rate, or extent of interleukin-6 production.
|
1 | Q8N4X5 (/IDA) |
Regulation of interleukin-6 production GO:0032675
Any process that modulates the frequency, rate, or extent of interleukin-6 production.
|
1 | Q5DTU0 (/ISO) |
Positive regulation of interleukin-8 production GO:0032757
Any process that activates or increases the frequency, rate, or extent of interleukin-8 production.
|
1 | Q8N4X5 (/IDA) |
Positive regulation of interleukin-8 production GO:0032757
Any process that activates or increases the frequency, rate, or extent of interleukin-8 production.
|
1 | Q5DTU0 (/ISO) |
Positive regulation of epidermal growth factor receptor signaling pathway GO:0045742
Any process that activates or increases the frequency, rate or extent of epidermal growth factor receptor signaling pathway activity.
|
1 | Q8N4X5 (/IDA) |
Positive regulation of epidermal growth factor receptor signaling pathway GO:0045742
Any process that activates or increases the frequency, rate or extent of epidermal growth factor receptor signaling pathway activity.
|
1 | Q5DTU0 (/ISO) |
Positive regulation of transcription, DNA-templated GO:0045893
Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription.
|
1 | Q8N4X5 (/IDA) |
Positive regulation of transcription, DNA-templated GO:0045893
Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription.
|
1 | Q5DTU0 (/ISO) |
Spore membrane bending pathway GO:0070583
The process in which a bending force is generated in the prospore membrane to form the characteristic curved shape of the prospore.
|
1 | Q92349 (/IMP) |
Cellular response to mechanical stimulus GO:0071260
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a mechanical stimulus.
|
1 | Q8VH46 (/IEP) |
There are 18 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 |
---|---|---|
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
2 | Q8N4X5 (/IDA) Q8N556 (/IDA) |
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
2 | Q5DTU0 (/ISO) Q80YS6 (/ISO) |
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
|
2 | Q8N4X5 (/IDA) Q90738 (/IDA) |
Nuclear envelope GO:0005635
The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space).
|
1 | Q92349 (/HDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | Q92349 (/HDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | Q8N4X5 (/IDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | Q5DTU0 (/ISO) |
Actin filament GO:0005884
A filamentous structure formed of a two-stranded helical polymer of the protein actin and associated proteins. Actin filaments are a major component of the contractile apparatus of skeletal muscle and the microfilaments of the cytoskeleton of eukaryotic cells. The filaments, comprising polymerized globular actin molecules, appear as flexible structures with a diameter of 5-9 nm. They are organized into a variety of linear bundles, two-dimensional networks, and three dimensional gels. In the cytoskeleton they are most highly concentrated in the cortex of the cell just beneath the plasma membrane.
|
1 | Q8VH46 (/IDA) |
Actin filament GO:0005884
A filamentous structure formed of a two-stranded helical polymer of the protein actin and associated proteins. Actin filaments are a major component of the contractile apparatus of skeletal muscle and the microfilaments of the cytoskeleton of eukaryotic cells. The filaments, comprising polymerized globular actin molecules, appear as flexible structures with a diameter of 5-9 nm. They are organized into a variety of linear bundles, two-dimensional networks, and three dimensional gels. In the cytoskeleton they are most highly concentrated in the cortex of the cell just beneath the plasma membrane.
|
1 | Q80YS6 (/ISO) |
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
|
1 | Q5DTU0 (/ISO) |
Focal adhesion GO:0005925
Small region on the surface of a cell that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments.
|
1 | Q8N556 (/HDA) |
Focal adhesion GO:0005925
Small region on the surface of a cell that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments.
|
1 | Q8N556 (/IDA) |
Focal adhesion GO:0005925
Small region on the surface of a cell that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments.
|
1 | Q80YS6 (/ISO) |
Actin cytoskeleton GO:0015629
The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes.
|
1 | Q8N556 (/IDA) |
Actin cytoskeleton GO:0015629
The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes.
|
1 | Q80YS6 (/ISO) |
Nuclear periphery GO:0034399
The portion of the nuclear lumen proximal to the inner nuclear membrane.
|
1 | Q92349 (/IDA) |
Meiotic spindle pole body GO:0035974
The microtubule organizing center that forms as part of the meiotic cell cycle; functionally homologous to the animal cell centrosome.
|
1 | Q92349 (/IDA) |
Mitotic spindle GO:0072686
A spindle that forms as part of mitosis. Mitotic and meiotic spindles contain distinctive complements of proteins associated with microtubules.
|
1 | Q92349 (/HDA) |