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:
"Zinc/RING finger domain, C3HC4 (zinc finger)
".
FunFam 1174: Ring finger protein 138
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 4 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 |
|---|---|---|
|
Single-stranded DNA binding GO:0003697
Interacting selectively and non-covalently with single-stranded DNA.
|
1 | Q1L721 (/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.
|
1 | Q1L721 (/IPI) |
|
Ubiquitin conjugating enzyme binding GO:0031624
Interacting selectively and non-covalently with a ubiquitin conjugating enzyme, any of the E2 proteins.
|
1 | Q1L721 (/IPI) |
|
Ubiquitin protein ligase activity GO:0061630
Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues.
|
1 | Q1L721 (/ISS) |
There are 4 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 |
|---|---|---|
|
Double-strand break repair via homologous recombination GO:0000724
The error-free repair of a double-strand break in DNA in which the broken DNA molecule is repaired using homologous sequences. A strand in the broken DNA searches for a homologous region in an intact chromosome to serve as the template for DNA synthesis. The restoration of two intact DNA molecules results in the exchange, reciprocal or nonreciprocal, of genetic material between the intact DNA molecule and the broken DNA molecule.
|
1 | Q1L721 (/ISS) |
|
Ubiquitin-dependent protein catabolic process GO:0006511
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
|
1 | Q1L721 (/IMP) |
|
DNA double-strand break processing involved in repair via single-strand annealing GO:0010792
The 5' to 3' exonucleolytic resection of the DNA at the site of the break to form a 3' single-strand DNA overhang that results in the repair of a double strand break via single-strand annealing.
|
1 | Q1L721 (/ISS) |
|
Protein autoubiquitination GO:0051865
The ubiquitination by a protein of one or more of its own amino acid residues, or residues on an identical protein. Ubiquitination occurs on the lysine residue by formation of an isopeptide crosslink.
|
1 | Q1L721 (/IDA) |
There are 1 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 |
|---|---|---|
|
Site of double-strand break GO:0035861
A region of a chromosome at which a DNA double-strand break has occurred. DNA damage signaling and repair proteins accumulate at the lesion to respond to the damage and repair the DNA to form a continuous DNA helix.
|
1 | Q1L721 (/ISS) |