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 122: DnaJ (Hsp40) homolog, subfamily C, member 3
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 kinase inhibitor activity GO:0004860
Stops, prevents or reduces the activity of a protein kinase, an enzyme which phosphorylates a protein.
|
7 | Q13217 (/ISS) Q13217 (/ISS) Q27968 (/ISS) Q5ZI13 (/ISS) Q91YW3 (/ISS) Q91YW3 (/ISS) Q9R0T3 (/ISS) |
Protein kinase binding GO:0019901
Interacting selectively and non-covalently with a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.
|
5 | Q13217 (/ISS) Q13217 (/ISS) Q27968 (/ISS) Q5ZI13 (/ISS) Q9R0T3 (/ISS) |
Protein kinase inhibitor activity GO:0004860
Stops, prevents or reduces the activity of a protein kinase, an enzyme which phosphorylates a protein.
|
3 | Q27968 (/IDA) Q91YW3 (/IDA) Q91YW3 (/IDA) |
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).
|
3 | Q27968 (/IPI) Q91YW3 (/IPI) Q91YW3 (/IPI) |
Protein kinase inhibitor activity GO:0004860
Stops, prevents or reduces the activity of a protein kinase, an enzyme which phosphorylates a protein.
|
2 | Q13217 (/TAS) Q13217 (/TAS) |
Protein kinase binding GO:0019901
Interacting selectively and non-covalently with a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.
|
2 | Q91YW3 (/IDA) Q91YW3 (/IDA) |
Protein kinase binding GO:0019901
Interacting selectively and non-covalently with a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.
|
2 | Q91YW3 (/IPI) Q91YW3 (/IPI) |
Chaperone binding GO:0051087
Interacting selectively and non-covalently with a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.
|
2 | Q91YW3 (/IDA) Q91YW3 (/IDA) |
Chaperone binding GO:0051087
Interacting selectively and non-covalently with a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.
|
2 | Q91YW3 (/IPI) Q91YW3 (/IPI) |
Misfolded protein binding GO:0051787
Interacting selectively and non-covalently with a misfolded protein.
|
2 | Q91YW3 (/IDA) Q91YW3 (/IDA) |
There are 19 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 |
---|---|---|
Positive regulation of translation initiation in response to endoplasmic reticulum stress GO:0036494
Any process that activates, or increases the frequency, rate or extent of translation initiation as a result of endoplasmic reticulum stress.
|
5 | Q13217 (/ISS) Q13217 (/ISS) Q27968 (/ISS) Q5ZI13 (/ISS) Q9R0T3 (/ISS) |
Cellular response to cold GO:0070417
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 cold stimulus, a temperature stimulus below the optimal temperature for that organism.
|
5 | Q13217 (/ISS) Q13217 (/ISS) Q27968 (/ISS) Q5ZI13 (/ISS) Q9R0T3 (/ISS) |
Negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation GO:1903912
Any process that stops, prevents or reduces the frequency, rate or extent of endoplasmic reticulum stress-induced eiF2alpha phosphorylation.
|
5 | Q13217 (/ISS) Q13217 (/ISS) Q27968 (/ISS) Q5ZI13 (/ISS) Q9R0T3 (/ISS) |
Negative regulation of protein kinase activity GO:0006469
Any process that stops, prevents, or reduces the frequency, rate or extent of protein kinase activity.
|
2 | Q91YW3 (/ISS) Q91YW3 (/ISS) |
Endoplasmic reticulum unfolded protein response GO:0030968
The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation.
|
2 | Q91YW3 (/IC) Q91YW3 (/IC) |
Response to endoplasmic reticulum stress GO:0034976
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 stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
|
2 | Q91YW3 (/IMP) Q91YW3 (/IMP) |
Positive regulation of translation initiation in response to endoplasmic reticulum stress GO:0036494
Any process that activates, or increases the frequency, rate or extent of translation initiation as a result of endoplasmic reticulum stress.
|
2 | Q91YW3 (/IDA) Q91YW3 (/IDA) |
IRE1-mediated unfolded protein response GO:0036498
A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB.
|
2 | Q13217 (/TAS) Q13217 (/TAS) |
Negative regulation of apoptotic process GO:0043066
Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
|
2 | Q13217 (/IMP) Q13217 (/IMP) |
Negative regulation of apoptotic process GO:0043066
Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
|
2 | Q91YW3 (/ISO) Q91YW3 (/ISO) |
Neutrophil degranulation GO:0043312
The regulated exocytosis of secretory granules containing preformed mediators such as proteases, lipases, and inflammatory mediators by a neutrophil.
|
2 | Q13217 (/TAS) Q13217 (/TAS) |
Post-translational protein modification GO:0043687
The process of covalently altering one or more amino acids in a protein after the protein has been completely translated and released from the ribosome.
|
2 | Q13217 (/TAS) Q13217 (/TAS) |
Cellular protein metabolic process GO:0044267
The chemical reactions and pathways involving a specific protein, rather than of proteins in general, occurring at the level of an individual cell. Includes cellular protein modification.
|
2 | Q13217 (/TAS) Q13217 (/TAS) |
Proteolysis involved in cellular protein catabolic process GO:0051603
The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells.
|
2 | Q91YW3 (/IDA) Q91YW3 (/IDA) |
Cellular response to cold GO:0070417
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 cold stimulus, a temperature stimulus below the optimal temperature for that organism.
|
2 | Q91YW3 (/IDA) Q91YW3 (/IDA) |
Negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation GO:1903912
Any process that stops, prevents or reduces the frequency, rate or extent of endoplasmic reticulum stress-induced eiF2alpha phosphorylation.
|
2 | Q91YW3 (/IDA) Q91YW3 (/IDA) |
Negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation GO:1903912
Any process that stops, prevents or reduces the frequency, rate or extent of endoplasmic reticulum stress-induced eiF2alpha phosphorylation.
|
2 | Q13217 (/IMP) Q13217 (/IMP) |
Negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation GO:1903912
Any process that stops, prevents or reduces the frequency, rate or extent of endoplasmic reticulum stress-induced eiF2alpha phosphorylation.
|
2 | Q91YW3 (/ISO) Q91YW3 (/ISO) |
Negative regulation of protein kinase activity GO:0006469
Any process that stops, prevents, or reduces the frequency, rate or extent of protein kinase activity.
|
1 | Q27968 (/IDA) |
There are 16 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.
|
5 | Q13217 (/ISS) Q13217 (/ISS) Q27968 (/ISS) Q5ZI13 (/ISS) Q9R0T3 (/ISS) |
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
|
4 | Q13217 (/ISS) Q13217 (/ISS) Q27968 (/ISS) Q5ZI13 (/ISS) |
Extracellular region GO:0005576
The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
|
2 | Q13217 (/TAS) Q13217 (/TAS) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
2 | Q91YW3 (/IDA) Q91YW3 (/IDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
2 | Q13217 (/TAS) Q13217 (/TAS) |
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
|
2 | Q91YW3 (/IDA) Q91YW3 (/IDA) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
2 | Q91YW3 (/IDA) Q91YW3 (/IDA) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
2 | Q13217 (/TAS) Q13217 (/TAS) |
Smooth endoplasmic reticulum GO:0005790
The smooth endoplasmic reticulum (smooth ER or SER) has no ribosomes attached to it. The smooth ER is the recipient of the proteins synthesized in the rough ER. Those proteins to be exported are passed to the Golgi complex, the resident proteins are returned to the rough ER and the lysosomal proteins after phosphorylation of their mannose residues are passed to the lysosomes. Glycosylation of the glycoproteins also continues. The smooth ER is the site of synthesis of lipids, including the phospholipids. The membranes of the smooth ER also contain enzymes that catalyze a series of reactions to detoxify both lipid-soluble drugs and harmful products of metabolism. Large quantities of certain compounds such as phenobarbital cause an increase in the amount of the smooth ER.
|
2 | Q91YW3 (/ISO) Q91YW3 (/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.
|
2 | Q91YW3 (/IDA) Q91YW3 (/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 | Q91YW3 (/TAS) Q91YW3 (/TAS) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
2 | Q13217 (/HDA) Q13217 (/HDA) |
Azurophil granule lumen GO:0035578
The volume enclosed by the membrane of an azurophil granule, a primary lysosomal granule found in neutrophil granulocytes that contains a wide range of hydrolytic enzymes and is released into the extracellular fluid.
|
2 | Q13217 (/TAS) Q13217 (/TAS) |
Extracellular exosome GO:0070062
A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.
|
2 | Q13217 (/HDA) Q13217 (/HDA) |
Extracellular vesicle GO:1903561
Any vesicle that is part of the extracellular region.
|
2 | Q13217 (/HDA) Q13217 (/HDA) |
Smooth endoplasmic reticulum GO:0005790
The smooth endoplasmic reticulum (smooth ER or SER) has no ribosomes attached to it. The smooth ER is the recipient of the proteins synthesized in the rough ER. Those proteins to be exported are passed to the Golgi complex, the resident proteins are returned to the rough ER and the lysosomal proteins after phosphorylation of their mannose residues are passed to the lysosomes. Glycosylation of the glycoproteins also continues. The smooth ER is the site of synthesis of lipids, including the phospholipids. The membranes of the smooth ER also contain enzymes that catalyze a series of reactions to detoxify both lipid-soluble drugs and harmful products of metabolism. Large quantities of certain compounds such as phenobarbital cause an increase in the amount of the smooth ER.
|
1 | Q9R0T3 (/IDA) |