| Predicate | Object |
|---|---|
| rdf:type | |
| http://www.biopax.org/relea... |
cpath:CPATH-LOCAL-134852,
cpath:CPATH-LOCAL-134852,
cpath:CPATH-LOCAL-134852,
cpath:CPATH-LOCAL-134853,
cpath:CPATH-LOCAL-134853,
cpath:CPATH-LOCAL-134853,
cpath:CPATH-LOCAL-134854,
cpath:CPATH-LOCAL-134854,
cpath:CPATH-LOCAL-134854,
cpath:CPATH-LOCAL-134855,
cpath:CPATH-LOCAL-134855,
cpath:CPATH-LOCAL-134855,
cpath:CPATH-LOCAL-134856,
cpath:CPATH-LOCAL-134856,
cpath:CPATH-LOCAL-134856,
cpath:CPATH-LOCAL-134857,
cpath:CPATH-LOCAL-134857,
cpath:CPATH-LOCAL-134857,
cpath:CPATH-LOCAL-134858,
cpath:CPATH-LOCAL-134858,
cpath:CPATH-LOCAL-134858,
cpath:CPATH-LOCAL-134859,
cpath:CPATH-LOCAL-134859,
cpath:CPATH-LOCAL-134859,
cpath:CPATH-LOCAL-134860,
cpath:CPATH-LOCAL-134860,
cpath:CPATH-LOCAL-134860,
cpath:CPATH-LOCAL-134861,
cpath:CPATH-LOCAL-134861,
cpath:CPATH-LOCAL-134861,
cpath:CPATH-LOCAL-139327,
cpath:CPATH-LOCAL-139327,
cpath:CPATH-LOCAL-139327
|
| http://www.biopax.org/relea... |
Adapter molecule crk,
Adapter molecule crk,
Adapter molecule crk
|
| http://www.biopax.org/relea... |
CRK_HUMAN,
CRK_HUMAN,
CRK_HUMAN
|
| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
Proto-oncogene c-Crk,
Proto-oncogene c-Crk,
Proto-oncogene c-Crk,
p38,
p38,
p38
|
| http://www.biopax.org/relea... |
FUNCTION: The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk- II 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. SUBUNIT: Interacts with ABL1, C3G, SOS, MAP4K1, MAPK8 and DOCK3 via its first SH3 domain. Interacts with BCAR1, CBL, CBLB, PXN, IRS4 and GAB1 via its SH2 domain upon stimulus-induced tyrosine phosphorylation. Interacts with several tyrosine-phosphorylated growth factor receptors such as EGFR, PDGFR and INSR via its SH2 domain (By similarity). Interacts with DOCK1 and DOCK4. Interacts with SHB. Interacts with PEAK1. Interacts with FASLG. SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By similarity). Note=Translocated to the plasma membrane upon cell adhesion (By similarity). ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=Crk-II; IsoId=P46108-1; Sequence=Displayed; Name=Crk-I; IsoId=P46108-2; Sequence=VSP_041153, VSP_041154; DOMAIN: The C-terminal SH3 domain function as a negative modulator for transformation and the N-terminal SH3 domain appears to function as a positive regulator for transformation (By similarity). DOMAIN: The SH2 domain mediates interaction with SHB. PTM: Phosphorylation of Crk-II (40 kDa) gives rise to a 42 kDa form. PTM: 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. SIMILARITY: Belongs to the CRK family. SIMILARITY: Contains 1 SH2 domain. SIMILARITY: Contains 2 SH3 domains. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
FUNCTION: The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk- II 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. SUBUNIT: Interacts with ABL1, C3G, SOS, MAP4K1, MAPK8 and DOCK3 via its first SH3 domain. Interacts with BCAR1, CBL, CBLB, PXN, IRS4 and GAB1 via its SH2 domain upon stimulus-induced tyrosine phosphorylation. Interacts with several tyrosine-phosphorylated growth factor receptors such as EGFR, PDGFR and INSR via its SH2 domain (By similarity). Interacts with DOCK1 and DOCK4. Interacts with SHB. Interacts with PEAK1. Interacts with FASLG. SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By similarity). Note=Translocated to the plasma membrane upon cell adhesion (By similarity). ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=Crk-II; IsoId=P46108-1; Sequence=Displayed; Name=Crk-I; IsoId=P46108-2; Sequence=VSP_041153, VSP_041154; DOMAIN: The C-terminal SH3 domain function as a negative modulator for transformation and the N-terminal SH3 domain appears to function as a positive regulator for transformation (By similarity). DOMAIN: The SH2 domain mediates interaction with SHB. PTM: Phosphorylation of Crk-II (40 kDa) gives rise to a 42 kDa form. PTM: 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. SIMILARITY: Belongs to the CRK family. SIMILARITY: Contains 1 SH2 domain. SIMILARITY: Contains 2 SH3 domains. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
FUNCTION: The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk- II 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. SUBUNIT: Interacts with ABL1, C3G, SOS, MAP4K1, MAPK8 and DOCK3 via its first SH3 domain. Interacts with BCAR1, CBL, CBLB, PXN, IRS4 and GAB1 via its SH2 domain upon stimulus-induced tyrosine phosphorylation. Interacts with several tyrosine-phosphorylated growth factor receptors such as EGFR, PDGFR and INSR via its SH2 domain (By similarity). Interacts with DOCK1 and DOCK4. Interacts with SHB. Interacts with PEAK1. Interacts with FASLG. SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By similarity). Note=Translocated to the plasma membrane upon cell adhesion (By similarity). ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=Crk-II; IsoId=P46108-1; Sequence=Displayed; Name=Crk-I; IsoId=P46108-2; Sequence=VSP_041153, VSP_041154; DOMAIN: The C-terminal SH3 domain function as a negative modulator for transformation and the N-terminal SH3 domain appears to function as a positive regulator for transformation (By similarity). DOMAIN: The SH2 domain mediates interaction with SHB. PTM: Phosphorylation of Crk-II (40 kDa) gives rise to a 42 kDa form. PTM: 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. SIMILARITY: Belongs to the CRK family. SIMILARITY: Contains 1 SH2 domain. SIMILARITY: Contains 2 SH3 domains. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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| skos:exactMatch | |
| skos:closeMatch |