4 GO Annotations
| GO Term | Gene Name |
|---|---|
| GO:0004674 | IPR015123 |
| GO:0005096 | IPR015123 |
| GO:0006468 | IPR015123 |
| GO:0007165 | IPR015123 |
4 Ontology Annotations
| GO Term | Gene Name |
|---|---|
| GO:0004674 | IPR015123 |
| GO:0005096 | IPR015123 |
| GO:0006468 | IPR015123 |
| GO:0007165 | IPR015123 |
| Type: | Domain | Name: | Bcr-Abl oncoprotein oligomerisation |
| Description: | This entry represents the oligomerisation domain of the breakpoint cluster region oncoprotein Bcr, and the Bcr/Abl (Abelson-leukemia-virus) fusion protein created by a reciprocal (9;22) fusion []. Brc displays serine/threonine protein kinase activity (), acting as a GTPase-activating protein for RAC1 and CDC42. Brc promotes the exchange of RAC or CDC42-bound GDP by GTP, thereby activating them []. The Bcr/Abl fusion protein loses some of the regulatory function of Bcr with regards to small Rho-like GTPases with negative consequences on cell motility, in particular on the capacity to adhere to endothelial cells [].The Bcr, Bcr/Abl oncoprotein oligomerisation domain consists of a short N-terminal helix (alpha-1), a flexible loop and a long C-terminal helix (alpha-2). Together these form an N-shaped structure, with the loop allowing the two helices to assume a parallel orientation. The monomeric domains associate into a dimer through the formation of an antiparallel coiled coil between the alpha-2 helices and domain swapping of two alpha-1 helices, where one alpha-1 helix swings back and packs against the alpha-2 helix from the second monomer. Two dimers then associate into a tetramer. The oligomerisation domain is essential for the oncogenicity of the Bcr-Abl protein []. | Short Name: | Bcr-Abl_oncoprot_oligo |
| GO Term | Gene Name |
|---|---|
| GO:0004674 | IPR015123 |
| GO:0005096 | IPR015123 |
| GO:0006468 | IPR015123 |
| GO:0007165 | IPR015123 |
| GO Term | Gene Name |
|---|---|
| GO:0004674 | IPR015123 |
| GO:0005096 | IPR015123 |
| GO:0006468 | IPR015123 |
| GO:0007165 | IPR015123 |
