CRK

CRK (CRK Proto-Oncogene, Adaptor Protein) is a Protein Coding gene. Diseases associated with CRK include Sarcoma and Chromosome 17P13.3, Centromeric, Duplication Syndrome. Among its related pathways are RET signaling and NFAT and Cardiac Hypertrophy. Gene Ontology (GO) annotations related to this gene include protein domain specific binding and SH3/SH2 adaptor activity. An important paralog of this gene is CRKL.

CRK Proto-Oncogene, Adaptor Protein

Involved in cell branching and adhesion mediated by BCAR1-CRK-RAPGEF1 signaling and activation of RAP1.

Isoform Crk-II:
Regulates cell adhesion, spreading and migration (PubMed:31311869).

Mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4 (PubMed:19004829).

May regulate the EFNA5-EPHA3 signaling (By similarity).

Actin cytoskeleton organization Source: UniProtKB
Activation of GTPase activity Source: Ensembl
Activation of MAPKK activity Source: Reactome
Cell chemotaxis Source: Ensembl
Cellular response to endothelin Source: Ensembl
Cellular response to insulin-like growth factor stimulus Source: Ensembl
Cellular response to nerve growth factor stimulus Source: Ensembl
Cellular response to nitric oxide Source: Ensembl
Cellular response to transforming growth factor beta stimulus Source: Ensembl
Cerebellar neuron development Source: Ensembl
Cerebral cortex development Source: Ensembl
Cytokine-mediated signaling pathway Source: Reactome
Dendrite development Source: Ensembl
Ephrin receptor signaling pathway Source: UniProtKB
Establishment of cell polarity Source: Ensembl
Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
Helper T cell diapedesis Source: Ensembl
Hippocampus development Source: Ensembl
Lipid metabolic process Source: Ensembl
Negative regulation of cell motility Source: CAFA
Negative regulation of natural killer cell mediated cytotoxicity Source: Ensembl
Negative regulation of wound healing Source: CAFA
Neuron migration Source: Ensembl
Positive regulation of cell growth Source: CAFA
Positive regulation of smooth muscle cell migration Source: Ensembl
Positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
Reelin-mediated signaling pathway Source: Ensembl
Regulation of actin cytoskeleton organization Source: UniProtKB
Regulation of cell adhesion mediated by integrin Source: Ensembl
Regulation of cell shape Source: UniProtKB
Regulation of dendrite development Source: Ensembl
Regulation of GTPase activity Source: UniProtKB
Regulation of intracellular signal transduction Source: UniProtKB
Regulation of protein binding Source: CAFA
Regulation of Rac protein signal transduction Source: Ensembl
Regulation of signal transduction Source: CAFA
Regulation of T cell migration Source: Ensembl
Regulation of transcription by RNA polymerase II Source: ProtInc
Response to cholecystokinin Source: Ensembl
Response to hepatocyte growth factor Source: Ensembl
Response to hydrogen peroxide Source: Ensembl
Response to yeast Source: Ensembl
Vascular endothelial growth factor receptor signaling pathway Source: Reactome

Cell membrane; Cytoplasm. Translocated to the plasma membrane upon cell adhesion.

Phosphorylated on Tyr-221 upon cell adhesion. Results in the negative regulation of the association with SH2- and SH3-binding partners, possibly by the formation of an intramolecular interaction of phosphorylated Tyr-221 with the SH2 domain. This leads finally to the down-regulation of the Crk signaling pathway (PubMed:17515907). Isoform Crk-II: Phosphorylated by KIT (By similarity).
Proline isomerization at Pro-237 by PPIA acts as a switch between two conformations: an autoinhibitory conformation in the cis form, where the tandem SH3 domains interact intramolecularly, and an activated conformation in the trans form.