CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.505 | SHC Adaptor Protein |
|
3.30.505.10 | SH2 domain |
Domain Context
CATH Clusters
| Superfamily | SH2 domain |
| Functional Family | E3 ubiquitin-protein ligase CBL |
Enzyme Information
| 2.3.2.27 |
RING-type E3 ubiquitin transferase.
based on mapping to UniProt Q9ULV8
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine.
-!- RING E3 ubiquitin transferases serve as mediators bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) and an acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon-amino group of an L-lysine residue of the acceptor protein. -!- Unlike EC 2.3.2.26 the RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin. -!- Many members of the RING-type E3 ubiquitin transferase family are not able to bind a substrate directly, and form a complex with a cullin scaffold protein and a substrate recognition module (the complexes are named CRL for Cullin-RING-Ligase). -!- In these complexes, the RING-type E3 ubiquitin transferase provides an additional function, mediating the transfer of a NEDD8 protein from a dedicated E2 carrier to the cullin protein (see EC 2.3.2.32). -!- Cf. EC 2.3.2.31.
|
UniProtKB Entries (1)
| P12931 |
SRC_HUMAN
Homo sapiens
Proto-oncogene tyrosine-protein kinase Src
|
PDB Structure
| PDB | 3VRO |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural flexibility regulates phosphopeptide-binding activity of the tyrosine kinase binding domain of Cbl-c.
J.Biochem.
|
