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:
"Tetratricopeptide repeat domain
".
FunFam 55: Serine/threonine-protein phosphatase
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 28 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).
|
4 | P53041 (/IPI) P53041 (/IPI) P53042 (/IPI) Q60676 (/IPI) |
Phosphoprotein phosphatase activity GO:0004721
Catalysis of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cell proteins and thereby provide an important mechanism for regulating cellular activity.
|
2 | P53042 (/IMP) Q60676 (/IMP) |
Phosphoprotein phosphatase activity GO:0004721
Catalysis of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cell proteins and thereby provide an important mechanism for regulating cellular activity.
|
2 | P53041 (/ISS) P53041 (/ISS) |
Phosphoprotein phosphatase activity GO:0004721
Catalysis of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cell proteins and thereby provide an important mechanism for regulating cellular activity.
|
2 | P53041 (/TAS) P53041 (/TAS) |
Protein serine/threonine phosphatase activity GO:0004722
Catalysis of the reaction: protein serine phosphate + H2O = protein serine + phosphate, and protein threonine phosphate + H2O = protein threonine + phosphate.
|
2 | P53041 (/ISS) P53041 (/ISS) |
Protein serine/threonine phosphatase activity GO:0004722
Catalysis of the reaction: protein serine phosphate + H2O = protein serine + phosphate, and protein threonine phosphate + H2O = protein threonine + phosphate.
|
2 | P53041 (/TAS) P53041 (/TAS) |
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
|
2 | P53041 (/IDA) P53041 (/IDA) |
Phosphatase activity GO:0016791
Catalysis of the hydrolysis of phosphoric monoesters, releasing inorganic phosphate.
|
2 | P53041 (/IDA) P53041 (/IDA) |
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
2 | P53041 (/IPI) P53041 (/IPI) |
ADP binding GO:0043531
Interacting selectively and non-covalently with ADP, adenosine 5'-diphosphate.
|
2 | P53041 (/IDA) P53041 (/IDA) |
Tau protein binding GO:0048156
Interacting selectively and non-covalently with tau protein. tau is a microtubule-associated protein, implicated in Alzheimer's disease, Down Syndrome and ALS.
|
2 | P53041 (/NAS) P53041 (/NAS) |
Hsp90 protein binding GO:0051879
Interacting selectively and non-covalently with Hsp90 proteins, any of a group of heat shock proteins around 90kDa in size.
|
2 | P53041 (/IPI) P53041 (/IPI) |
G-protein alpha-subunit binding GO:0001965
Interacting selectively and non-covalently with a G-protein alpha subunit. The alpha subunit binds a guanine nucleotide.
|
1 | P53042 (/IDA) |
G-protein alpha-subunit binding GO:0001965
Interacting selectively and non-covalently with a G-protein alpha subunit. The alpha subunit binds a guanine nucleotide.
|
1 | Q60676 (/ISO) |
RNA binding GO:0003723
Interacting selectively and non-covalently with an RNA molecule or a portion thereof.
|
1 | Q60676 (/IDA) |
Phosphoprotein phosphatase activity GO:0004721
Catalysis of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cell proteins and thereby provide an important mechanism for regulating cellular activity.
|
1 | P53042 (/IDA) |
Phosphoprotein phosphatase activity GO:0004721
Catalysis of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cell proteins and thereby provide an important mechanism for regulating cellular activity.
|
1 | Q60676 (/ISO) |
Protein serine/threonine phosphatase activity GO:0004722
Catalysis of the reaction: protein serine phosphate + H2O = protein serine + phosphate, and protein threonine phosphate + H2O = protein threonine + phosphate.
|
1 | P53042 (/IDA) |
Protein serine/threonine phosphatase activity GO:0004722
Catalysis of the reaction: protein serine phosphate + H2O = protein serine + phosphate, and protein threonine phosphate + H2O = protein threonine + phosphate.
|
1 | Q60676 (/ISO) |
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
|
1 | Q60676 (/ISO) |
Microtubule binding GO:0008017
Interacting selectively and non-covalently with microtubules, filaments composed of tubulin monomers.
|
1 | P53042 (/IDA) |
Microtubule binding GO:0008017
Interacting selectively and non-covalently with microtubules, filaments composed of tubulin monomers.
|
1 | Q60676 (/ISO) |
Phosphatase activity GO:0016791
Catalysis of the hydrolysis of phosphoric monoesters, releasing inorganic phosphate.
|
1 | Q60676 (/ISO) |
Heat shock protein binding GO:0031072
Interacting selectively and non-covalently with a heat shock protein, any protein synthesized or activated in response to heat shock.
|
1 | P53042 (/IPI) |
Heat shock protein binding GO:0031072
Interacting selectively and non-covalently with a heat shock protein, any protein synthesized or activated in response to heat shock.
|
1 | Q60676 (/ISO) |
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
1 | Q60676 (/ISO) |
ADP binding GO:0043531
Interacting selectively and non-covalently with ADP, adenosine 5'-diphosphate.
|
1 | Q60676 (/ISO) |
Hsp90 protein binding GO:0051879
Interacting selectively and non-covalently with Hsp90 proteins, any of a group of heat shock proteins around 90kDa in size.
|
1 | Q60676 (/ISO) |
There are 34 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 |
---|---|---|
MAPK cascade GO:0000165
An intracellular protein kinase cascade containing at least a MAPK, a MAPKK and a MAP3K. The cascade can also contain an additional tiers: the upstream MAP4K. The kinases in each tier phosphorylate and activate the kinase in the downstream tier to transmit a signal within a cell.
|
2 | P53041 (/TAS) P53041 (/TAS) |
Mitotic cell cycle GO:0000278
Progression through the phases of the mitotic cell cycle, the most common eukaryotic cell cycle, which canonically comprises four successive phases called G1, S, G2, and M and includes replication of the genome and the subsequent segregation of chromosomes into daughter cells. In some variant cell cycles nuclear replication or nuclear division may not be followed by cell division, or G1 and G2 phases may be absent.
|
2 | P53041 (/TAS) P53041 (/TAS) |
Transcription, DNA-templated GO:0006351
The cellular synthesis of RNA on a template of DNA.
|
2 | P53041 (/TAS) P53041 (/TAS) |
Protein dephosphorylation GO:0006470
The process of removing one or more phosphoric residues from a protein.
|
2 | P53041 (/TAS) P53041 (/TAS) |
Response to lead ion GO:0010288
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lead ion stimulus.
|
2 | P53041 (/ISS) P53041 (/ISS) |
Peptidyl-threonine dephosphorylation GO:0035970
The removal of phosphoric residues from peptidyl-O-phospho-L-threonine to form peptidyl-threonine.
|
2 | P53041 (/TAS) P53041 (/TAS) |
Positive regulation of I-kappaB kinase/NF-kappaB signaling GO:0043123
Any process that activates or increases the frequency, rate or extent of I-kappaB kinase/NF-kappaB signaling.
|
2 | P53041 (/HMP) P53041 (/HMP) |
Peptidyl-serine dephosphorylation GO:0070262
The removal of phosphoric residues from peptidyl-O-phospho-L-serine to form peptidyl-serine.
|
2 | P53041 (/TAS) P53041 (/TAS) |
Response to arachidonic acid GO:1904550
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an arachidonic acid stimulus.
|
2 | P53041 (/ISS) P53041 (/ISS) |
Negative regulation of protein phosphorylation GO:0001933
Any process that stops, prevents or reduces the rate of addition of phosphate groups to amino acids within a protein.
|
1 | P53042 (/IMP) |
Negative regulation of protein phosphorylation GO:0001933
Any process that stops, prevents or reduces the rate of addition of phosphate groups to amino acids within a protein.
|
1 | Q60676 (/ISO) |
Protein dephosphorylation GO:0006470
The process of removing one or more phosphoric residues from a protein.
|
1 | P53042 (/IDA) |
Protein dephosphorylation GO:0006470
The process of removing one or more phosphoric residues from a protein.
|
1 | P53042 (/IMP) |
Protein dephosphorylation GO:0006470
The process of removing one or more phosphoric residues from a protein.
|
1 | Q60676 (/ISO) |
Response to lead ion GO:0010288
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lead ion stimulus.
|
1 | P53042 (/IDA) |
Response to lead ion GO:0010288
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lead ion stimulus.
|
1 | P53042 (/IEP) |
Response to lead ion GO:0010288
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lead ion stimulus.
|
1 | Q60676 (/ISO) |
Histone dephosphorylation GO:0016576
The modification of histones by removal of phosphate groups.
|
1 | P53042 (/IDA) |
Histone dephosphorylation GO:0016576
The modification of histones by removal of phosphate groups.
|
1 | Q60676 (/ISO) |
Response to morphine GO:0043278
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a morphine stimulus. Morphine is an opioid alkaloid, isolated from opium, with a complex ring structure.
|
1 | Q60676 (/IMP) |
Protein complex oligomerization GO:0051259
The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of component monomers; protein oligomers may be composed of different or identical monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
|
1 | P53042 (/IDA) |
Protein complex oligomerization GO:0051259
The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of component monomers; protein oligomers may be composed of different or identical monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
|
1 | Q60676 (/ISO) |
Protein heterooligomerization GO:0051291
The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of component monomers that are not all identical. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
|
1 | P53042 (/IPI) |
Protein heterooligomerization GO:0051291
The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of component monomers that are not all identical. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
|
1 | Q60676 (/ISO) |
Negative regulation of cell death GO:0060548
Any process that decreases the rate or frequency of cell death. Cell death is the specific activation or halting of processes within a cell so that its vital functions markedly cease, rather than simply deteriorating gradually over time, which culminates in cell death.
|
1 | P53042 (/IMP) |
Negative regulation of cell death GO:0060548
Any process that decreases the rate or frequency of cell death. Cell death is the specific activation or halting of processes within a cell so that its vital functions markedly cease, rather than simply deteriorating gradually over time, which culminates in cell death.
|
1 | Q60676 (/ISO) |
Cellular response to hydrogen peroxide GO:0070301
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 hydrogen peroxide (H2O2) stimulus.
|
1 | P53042 (/IEP) |
Cellular response to cadmium ion GO:0071276
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 cadmium (Cd) ion stimulus.
|
1 | P53042 (/IEP) |
Negative regulation of neuron death GO:1901215
Any process that stops, prevents or reduces the frequency, rate or extent of neuron death.
|
1 | P53042 (/IMP) |
Negative regulation of neuron death GO:1901215
Any process that stops, prevents or reduces the frequency, rate or extent of neuron death.
|
1 | Q60676 (/ISO) |
Response to arachidonic acid GO:1904550
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an arachidonic acid stimulus.
|
1 | P53042 (/IDA) |
Response to arachidonic acid GO:1904550
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an arachidonic acid stimulus.
|
1 | Q60676 (/ISO) |
Positive regulation of glucocorticoid receptor signaling pathway GO:2000324
Any process that activates or increases the frequency, rate or extent of glucocorticoid receptor signaling pathway.
|
1 | P53042 (/IMP) |
Positive regulation of glucocorticoid receptor signaling pathway GO:2000324
Any process that activates or increases the frequency, rate or extent of glucocorticoid receptor signaling pathway.
|
1 | Q60676 (/ISO) |
There are 25 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.
|
6 | A0A024R0Q7 (/IDA) A0A024R0Q7 (/IDA) P53041 (/IDA) P53041 (/IDA) P53042 (/IDA) Q60676 (/IDA) |
Intracellular membrane-bounded organelle GO:0043231
Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
|
4 | A0A024R0Q7 (/IDA) A0A024R0Q7 (/IDA) P53041 (/IDA) P53041 (/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.
|
2 | P53041 (/TAS) P53041 (/TAS) |
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
2 | P53041 (/TAS) P53041 (/TAS) |
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 | P53041 (/TAS) P53041 (/TAS) |
Protein-containing complex GO:0032991
A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
|
2 | P53041 (/IDA) P53041 (/IDA) |
Chaperone complex GO:0101031
A protein complex required for the non-covalent folding or unfolding, maturation, stabilization or assembly or disassembly of macromolecular structures. Usually active during or immediately after completion of translation. Many chaperone complexes contain heat shock proteins.
|
2 | P53041 (/IDA) P53041 (/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 | P53042 (/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 | Q60676 (/ISO) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | P53042 (/IDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | Q60676 (/ISO) |
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
1 | Q60676 (/ISO) |
Protein-containing complex GO:0032991
A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
|
1 | Q60676 (/ISO) |
Neuron projection GO:0043005
A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
|
1 | P53042 (/IDA) |
Neuron projection GO:0043005
A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
|
1 | Q60676 (/ISO) |
Neuronal cell body GO:0043025
The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
|
1 | P53042 (/IDA) |
Neuronal cell body GO:0043025
The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
|
1 | Q60676 (/ISO) |
Perikaryon GO:0043204
The portion of the cell soma (neuronal cell body) that excludes the nucleus.
|
1 | P53042 (/IDA) |
Perikaryon GO:0043204
The portion of the cell soma (neuronal cell body) that excludes the nucleus.
|
1 | Q60676 (/ISO) |
Intracellular membrane-bounded organelle GO:0043231
Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
|
1 | Q60676 (/ISO) |
Cell periphery GO:0071944
The part of a cell encompassing the cell cortex, the plasma membrane, and any external encapsulating structures.
|
1 | P53042 (/IDA) |
Cell periphery GO:0071944
The part of a cell encompassing the cell cortex, the plasma membrane, and any external encapsulating structures.
|
1 | Q60676 (/ISO) |
Chaperone complex GO:0101031
A protein complex required for the non-covalent folding or unfolding, maturation, stabilization or assembly or disassembly of macromolecular structures. Usually active during or immediately after completion of translation. Many chaperone complexes contain heat shock proteins.
|
1 | Q60676 (/ISO) |
Proximal dendrite GO:1990635
The dendrite of the dendritic tree that is closest to the neuronal cell body (the soma).
|
1 | P53042 (/IDA) |
Proximal dendrite GO:1990635
The dendrite of the dendritic tree that is closest to the neuronal cell body (the soma).
|
1 | Q60676 (/ISO) |