CATH Superfamily 3.90.70.80
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: waiting to be named.
FunFam 5: OTU domain-containing protein 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 6 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).
|
2 | B1AZ99 (/IPI) Q5T2D3 (/IPI) |
Thiol-dependent ubiquitin-specific protease activity GO:0004843
Catalysis of the thiol-dependent hydrolysis of a peptide bond formed by the C-terminal glycine of ubiquitin and another protein.
|
1 | Q5T2D3 (/IDA) |
Thiol-dependent ubiquitin-specific protease activity GO:0004843
Catalysis of the thiol-dependent hydrolysis of a peptide bond formed by the C-terminal glycine of ubiquitin and another protein.
|
1 | Q5T2D3 (/IMP) |
Thiol-dependent ubiquitin-specific protease activity GO:0004843
Catalysis of the thiol-dependent hydrolysis of a peptide bond formed by the C-terminal glycine of ubiquitin and another protein.
|
1 | B1AZ99 (/ISO) |
Thiol-dependent ubiquitin-specific protease activity GO:0004843
Catalysis of the thiol-dependent hydrolysis of a peptide bond formed by the C-terminal glycine of ubiquitin and another protein.
|
1 | B1AZ99 (/ISS) |
Thiol-dependent ubiquitinyl hydrolase activity GO:0036459
Catalysis of the thiol-dependent hydrolysis of an ester, thioester, amide, peptide or isopeptide bond formed by the C-terminal glycine of ubiquitin.
|
1 | Q5T2D3 (/TAS) |
There are 17 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 |
---|---|---|
Protein deubiquitination GO:0016579
The removal of one or more ubiquitin groups from a protein.
|
1 | Q5T2D3 (/TAS) |
Protein K11-linked deubiquitination GO:0035871
A protein deubiquitination process in which a K11-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 11 of the ubiquitin monomers, is removed from a protein.
|
1 | Q5T2D3 (/IDA) |
Protein K11-linked deubiquitination GO:0035871
A protein deubiquitination process in which a K11-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 11 of the ubiquitin monomers, is removed from a protein.
|
1 | B1AZ99 (/ISO) |
Protein K11-linked deubiquitination GO:0035871
A protein deubiquitination process in which a K11-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 11 of the ubiquitin monomers, is removed from a protein.
|
1 | B1AZ99 (/ISS) |
Protein K6-linked deubiquitination GO:0044313
A protein deubiquitination process in which a K6-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 6 of the ubiquitin monomers, is removed from a protein.
|
1 | Q5T2D3 (/IDA) |
Protein K6-linked deubiquitination GO:0044313
A protein deubiquitination process in which a K6-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 6 of the ubiquitin monomers, is removed from a protein.
|
1 | B1AZ99 (/ISO) |
Protein K6-linked deubiquitination GO:0044313
A protein deubiquitination process in which a K6-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 6 of the ubiquitin monomers, is removed from a protein.
|
1 | B1AZ99 (/ISS) |
Protein stabilization GO:0050821
Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
|
1 | Q5T2D3 (/IDA) |
Protein stabilization GO:0050821
Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
|
1 | Q5T2D3 (/IMP) |
Protein stabilization GO:0050821
Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
|
1 | B1AZ99 (/ISO) |
Negative regulation of protein kinase B signaling GO:0051898
Any process that stops, prevents, or reduces the frequency, rate or extent of protein kinase B signaling, a series of reactions mediated by the intracellular serine/threonine kinase protein kinase B.
|
1 | Q5T2D3 (/IDA) |
Negative regulation of protein kinase B signaling GO:0051898
Any process that stops, prevents, or reduces the frequency, rate or extent of protein kinase B signaling, a series of reactions mediated by the intracellular serine/threonine kinase protein kinase B.
|
1 | Q5T2D3 (/IMP) |
Negative regulation of protein kinase B signaling GO:0051898
Any process that stops, prevents, or reduces the frequency, rate or extent of protein kinase B signaling, a series of reactions mediated by the intracellular serine/threonine kinase protein kinase B.
|
1 | B1AZ99 (/ISO) |
Protein K48-linked deubiquitination GO:0071108
A protein deubiquitination process in which a K48-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 48 of the ubiquitin monomers, is removed from a protein.
|
1 | Q5T2D3 (/IDA) |
Protein K48-linked deubiquitination GO:0071108
A protein deubiquitination process in which a K48-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 48 of the ubiquitin monomers, is removed from a protein.
|
1 | B1AZ99 (/ISO) |
Protein K27-linked deubiquitination GO:1990167
A protein deubiquitination process in which a K27-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 27 of the ubiquitin monomers, is removed from a protein.
|
1 | Q5T2D3 (/IDA) |
Protein K27-linked deubiquitination GO:1990167
A protein deubiquitination process in which a K27-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 27 of the ubiquitin monomers, is removed from a protein.
|
1 | B1AZ99 (/ISO) |
There are 3 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 |
---|---|---|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | Q5T2D3 (/IDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | B1AZ99 (/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 | Q5T2D3 (/TAS) |