Q9XYM0
Gene name |
Crk (CG1587) |
Protein name |
Adapter molecule Crk |
Names |
|
Species |
Drosophila melanogaster (Fruit fly) |
KEGG Pathway |
dme:Dmel_CG1587 |
EC number |
|
Protein Class |
|

Descriptions
Autoinhibitory domains (AIDs)
Target domain |
109-163 (N-terminal Src Homology 3 domain of Ct10 Regulator of Kinase adaptor proteins) |
Relief mechanism |
PTM |
Assay |
|
Accessory elements
No accessory elements
References
- Kobashigawa Y et al. (2007) "Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK", Nature structural & molecular biology, 14, 503-10
- Ogawa S et al. (1994) "The C-terminal SH3 domain of the mouse c-Crk protein negatively regulates tyrosine-phosphorylation of Crk associated p130 in rat 3Y1 cells", Oncogene, 9, 1669-78
- Sriram G et al. (2012) "Commentary: The carboxyl-terminal Crk SH3 domain: Regulatory strategies and new perspectives", FEBS letters, 586, 2615-8
Autoinhibited structure

Activated structure

1 structures for Q9XYM0
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
AF-Q9XYM0-F1 | Predicted | AlphaFoldDB |
No variants for Q9XYM0
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for Q9XYM0 |
No associated diseases with Q9XYM0
5 regional properties for Q9XYM0
Type | Name | Position | InterPro Accession |
---|---|---|---|
domain | SH2 domain | 10 - 104 | IPR000980 |
domain | SH3 domain | 106 - 166 | IPR001452-1 |
domain | SH3 domain | 199 - 260 | IPR001452-2 |
domain | CRK, N-terminal SH3 domain | 109 - 163 | IPR035457 |
domain | CRK, C-terminal SH3 domain | 201 - 257 | IPR035458 |
No GO annotations of cellular component
Name | Definition |
---|---|
No GO annotations for cellular component |
2 GO annotations of molecular function
Name | Definition |
---|---|
receptor tyrosine kinase binding | Binding to a receptor that possesses protein tyrosine kinase activity. |
signaling adaptor activity | The binding activity of a molecule that brings together two or more molecules in a signaling pathway, permitting those molecules to function in a coordinated way. Adaptor molecules themselves do not have catalytic activity. |
11 GO annotations of biological process
Name | Definition |
---|---|
border follicle cell migration | The directed movement of a border cell through the nurse cells to reach the oocyte. An example of this is found in Drosophila melanogaster. |
cell migration | The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues. |
ephrin receptor signaling pathway | The series of molecular signals initiated by ephrin binding to its receptor, and ending with the regulation of a downstream cellular process, e.g. transcription. |
imaginal disc fusion, thorax closure | The joining of the parts of the wing imaginal discs, giving rise to the adult thorax. |
myoblast fusion | A process in which non-proliferating myoblasts fuse to existing fibers or to myotubes to form new fibers. A myoblast is a mononucleate cell type that, by fusion with other myoblasts, gives rise to the myotubes that eventually develop into skeletal muscle fibers. |
phagocytosis, engulfment | The internalization of bacteria, immune complexes and other particulate matter or of an apoptotic cell by phagocytosis, including the membrane and cytoskeletal processes required, which involves one of three mechanisms |
positive regulation of JNK cascade | Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the JNK cascade. |
regulation of actin cytoskeleton organization | Any process that modulates the frequency, rate or extent of the formation, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins. |
regulation of GTPase activity | Any process that modulates the rate of GTP hydrolysis by a GTPase. |
signal transduction | The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell. |
vascular endothelial growth factor receptor signaling pathway | The series of molecular signals initiated by a ligand binding to a vascular endothelial growth factor receptor (VEGFR) on the surface of the target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. |
8 homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
Q04929 | CRK | Adapter molecule crk | Gallus gallus (Chicken) | SS |
P46109 | CRKL | Crk-like protein | Homo sapiens (Human) | SS |
P46108 | CRK | Adapter molecule crk | Homo sapiens (Human) | EV |
P47941 | Crkl | Crk-like protein | Mus musculus (Mouse) | SS |
Q64010 | Crk | Adapter molecule crk | Mus musculus (Mouse) | EV SS |
Q5U2U2 | Crkl | Crk-like protein | Rattus norvegicus (Rat) | SS |
Q63768 | Crk | Adapter molecule crk | Rattus norvegicus (Rat) | SS |
Q9NHC3 | ced-2 | Cell death abnormality protein 2 | Caenorhabditis elegans | SS |
10 | 20 | 30 | 40 | 50 | 60 |
MDTFDVSDRN | SWYFGPMSRQ | DATEVLMNER | ERGVFLVRDS | NSIAGDYVLC | VREDTKVSNY |
70 | 80 | 90 | 100 | 110 | 120 |
IINKVQQQDQ | IVYRIGDQSF | DNLPKLLTFY | TLHYLDTTPL | KRPACRRVEK | VIGKFDFVGS |
130 | 140 | 150 | 160 | 170 | 180 |
DQDDLPFQRG | EVLTIVRKDE | DQWWTARNSS | GKIGQIPVPY | IQQYDDYMDE | DAIDKNEPSI |
190 | 200 | 210 | 220 | 230 | 240 |
SGSSNVFEST | LKRTDLNRKL | PAYARVKQSR | VPNAYDKTAL | KLEIGDIIKV | TKTNINGQWE |
250 | 260 | 270 | |||
GELNGKNGHF | PFTHVEFVDD | CDLSKNSTEI | C |