CRK_MOUSE
ID CRK_MOUSE Reviewed; 304 AA.
AC Q64010;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Adapter molecule crk;
DE AltName: Full=Proto-oncogene c-Crk;
DE AltName: Full=p38;
GN Name=Crk; Synonyms=Crko;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CRK-I AND CRK-II).
RC TISSUE=Liver;
RX PubMed=8183562;
RA Ogawa S., Toyoshima H., Kozutsumi H., Hagiwara K., Sakai R., Tanaka T.,
RA Hirano N., Mano H., Yazaki Y., Hirai H.;
RT "The C-terminal SH3 domain of the mouse c-Crk protein negatively regulates
RT tyrosine-phosphorylation of Crk associated p130 in rat 3Y1 cells.";
RL Oncogene 9:1669-1678(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CRK-II).
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PHOSPHORYLATION AT TYR-221, AND INTERACTION WITH ABL1.
RX PubMed=8194526; DOI=10.1002/j.1460-2075.1994.tb06518.x;
RA Feller S.M., Knudsen B., Hanafusa H.;
RT "c-Abl kinase regulates the protein binding activity of c-Crk.";
RL EMBO J. 13:2341-2351(1994).
RN [4]
RP INTERACTION WITH REPS1.
RC TISSUE=Muscle;
RX PubMed=9395447; DOI=10.1074/jbc.272.50.31230;
RA Yamaguchi A., Urano T., Goi T., Feig L.A.;
RT "An eps homology (EH) domain protein that binds to the ral-GTPase target,
RT RalBP1.";
RL J. Biol. Chem. 272:31230-31234(1997).
RN [5]
RP INTERACTION WITH FLT1.
RX PubMed=9722576; DOI=10.1074/jbc.273.36.23410;
RA Ito N., Wernstedt C., Engstrom U., Claesson-Welsh L.;
RT "Identification of vascular endothelial growth factor receptor-1 tyrosine
RT phosphorylation sites and binding of SH2 domain-containing molecules.";
RL J. Biol. Chem. 273:23410-23418(1998).
RN [6]
RP INTERACTION WITH DDEF1/ASAP1.
RX PubMed=9819391; DOI=10.1128/mcb.18.12.7038;
RA Brown M.T., Andrade J., Radhakrishna H., Donaldson J.G., Cooper J.A.,
RA Randazzo P.A.;
RT "ASAP1, a phospholipid-dependent arf GTPase-activating protein that
RT associates with and is phosphorylated by Src.";
RL Mol. Cell. Biol. 18:7038-7051(1998).
RN [7]
RP INTERACTION WITH DOCK3.
RC TISSUE=Brain;
RX PubMed=10854253; DOI=10.1046/j.1471-4159.2000.0750109.x;
RA Kashiwa A., Yoshida H., Lee S., Paladino T., Liu Y., Chen Q., Dargusch R.,
RA Schubert D., Kimura H.;
RT "Isolation and characterization of novel presenilin binding protein.";
RL J. Neurochem. 75:109-116(2000).
RN [8]
RP FUNCTION, AND INTERACTION WITH EPHA3.
RX PubMed=11870224; DOI=10.1242/jcs.115.5.1059;
RA Lawrenson I.D., Wimmer-Kleikamp S.H., Lock P., Schoenwaelder S.M., Down M.,
RA Boyd A.W., Alewood P.F., Lackmann M.;
RT "Ephrin-A5 induces rounding, blebbing and de-adhesion of EphA3-expressing
RT 293T and melanoma cells by CrkII and Rho-mediated signalling.";
RL J. Cell Sci. 115:1059-1072(2002).
RN [9]
RP INTERACTION WITH KIT, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP PHOSPHORYLATION.
RX PubMed=12878163; DOI=10.1016/s0014-4827(03)00206-4;
RA Lennartsson J., Wernstedt C., Engstrom U., Hellman U., Ronnstrand L.;
RT "Identification of Tyr900 in the kinase domain of c-Kit as a Src-dependent
RT phosphorylation site mediating interaction with c-Crk.";
RL Exp. Cell Res. 288:110-118(2003).
RN [10]
RP INTERACTION WITH CBLB.
RX PubMed=12842890; DOI=10.1074/jbc.m300664200;
RA Liu J., DeYoung S.M., Hwang J.B., O'Leary E.E., Saltiel A.R.;
RT "The roles of Cbl-b and c-Cbl in insulin-stimulated glucose transport.";
RL J. Biol. Chem. 278:36754-36762(2003).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 134-190.
RX PubMed=7735837; DOI=10.1016/s0969-2126(01)00151-4;
RA Wu X., Knudsen B., Feller S.M., Zheng J., Sali A., Cowburn D., Hanafusa H.,
RA Kuriyan J.;
RT "Structural basis for the specific interaction of lysine-containing
RT proline-rich peptides with the N-terminal SH3 domain of c-Crk.";
RL Structure 3:215-226(1995).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 133-191.
RX PubMed=9851931; DOI=10.1126/science.282.5396.2088;
RA Nguyen J.T., Turck C.W., Cohen F.E., Zuckermann R.N., Lim W.A.;
RT "Exploiting the basis of proline recognition by SH3 and WW domains: design
RT of N-substituted inhibitors.";
RL Science 282:2088-2092(1998).
CC -!- FUNCTION: Involved in cell branching and adhesion mediated by BCAR1-
CC CRK-RAPGEF1 signaling and activation of RAP1.
CC {ECO:0000250|UniProtKB:P46108}.
CC -!- FUNCTION: Isoform CRK-II: Regulates cell adhesion, spreading and
CC migration. Mediates attachment-induced MAPK8 activation, membrane
CC ruffling and cell motility in a Rac-dependent manner. Involved in
CC phagocytosis of apoptotic cells and cell motility via its interaction
CC with DOCK1 and DOCK4 (By similarity). May regulate the EFNA5-EPHA3
CC signaling (PubMed:11870224). {ECO:0000250|UniProtKB:P46108,
CC ECO:0000269|PubMed:11870224}.
CC -!- SUBUNIT: Component of a complex comprised of SH2D3C, BCAR1/CAS, and CRK
CC (By similarity). Within the complex, interacts with SH2D3C (via C-
CC terminus), and BCAR1/CAS (By similarity). Found in a complex with ABL1,
CC ABL2, CRK and UNC119; leading to the inhibition of CRK phosphorylation
CC by ABL kinases (By similarity). Interacts with ABL1, C3G, DOCK3, DOCK5,
CC MAP4K1, MAPK8 and SOS via its first SH3 domain. Interacts (via SH2
CC domain) with BCAR1, CBL, CBLB, PXN, IRS4 and GAB1 upon stimulus-induced
CC tyrosine phosphorylation. Interacts (via SH2 domain) with several
CC tyrosine-phosphorylated growth factor receptors such as EGFR and INSR.
CC Interacts with FLT1 (tyrosine-phosphorylated). Interacts with DOCK1 and
CC DOCK4. Interacts with SHB. Interacts with PEAK1. Interacts with FASLG.
CC Interacts with FLT4 (tyrosine-phosphorylated). Part of a collagen
CC stimulated complex involved in cell migration composed of CDC42, CRK,
CC TNK2 and p130cas/BCAR1. Interacts (via SH2 domain) with the 'Tyr-9'
CC phosphorylated form of PDPK1. Interacts with CBLC (By similarity).
CC {ECO:0000250|UniProtKB:P46108}.
CC -!- SUBUNIT: [Isoform Crk-II]: Interacts (via SH2 domain) with PDGFRA
CC (tyrosine phosphorylated) and PDGFRB (tyrosine phosphorylated) (By
CC similarity). Interacts with EPHA3 (phosphorylated); upon activation of
CC EPHA3 by the ligand EFNA5 and EPHA3 tyrosine kinase activity-dependent
CC and mediates EFNA5-EPHA3 signaling through RHOA GTPase activation
CC (PubMed:11870224). Interacts with KIT (PubMed:12878163). Interacts with
CC PEAK3; the interaction requires PEAK3 homodimerization (By similarity).
CC {ECO:0000250|UniProtKB:P46108, ECO:0000269|PubMed:11870224,
CC ECO:0000269|PubMed:12878163}.
CC -!- INTERACTION:
CC Q64010; P08069: IGF1R; Xeno; NbExp=3; IntAct=EBI-2906540, EBI-475981;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Note=Translocated to the plasma membrane upon cell
CC adhesion. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Crk-II;
CC IsoId=Q64010-1; Sequence=Displayed;
CC Name=Crk-I;
CC IsoId=Q64010-2; Sequence=VSP_004174;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The C-terminal SH3 domain function as a negative modulator for
CC transformation and the N-terminal SH3 domain appears to function as a
CC positive regulator for transformation. {ECO:0000250}.
CC -!- DOMAIN: The SH2 domain mediates interaction with tyrosine
CC phosphorylated proteins. Mediates interaction with SHB.
CC -!- PTM: Phosphorylated on Tyr-221 upon cell adhesion. Results in the
CC negative regulation of the association with SH2- and SH3-binding
CC partners, possibly by the formation of an intramolecular interaction of
CC phosphorylated Tyr-221 with the SH2 domain. This leads finally to the
CC down-regulation of the Crk signaling pathway (PubMed:8194526,
CC PubMed:12878163). Isoform Crk-II: Phosphorylated by KIT (By
CC similarity). {ECO:0000250|UniProtKB:P46108,
CC ECO:0000269|PubMed:12878163, ECO:0000269|PubMed:8194526}.
CC -!- PTM: Proline isomerization at Pro-237 by PPIA acts as a switch between
CC two conformations: an autoinhibitory conformation in the cis form,
CC where the tandem SH3 domains interact intramolecularly, and an
CC activated conformation in the trans form. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CRK family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S72408; AAB30755.1; -; mRNA.
DR EMBL; AK028488; BAC25976.1; -; mRNA.
DR CCDS; CCDS25055.1; -. [Q64010-1]
DR RefSeq; NP_598417.2; NM_133656.5. [Q64010-1]
DR PDB; 1B07; X-ray; 2.50 A; A=134-190.
DR PDB; 1CKA; X-ray; 1.50 A; A=134-190.
DR PDB; 1CKB; X-ray; 1.90 A; A=134-190.
DR PDB; 1JU5; NMR; -; B=217-228.
DR PDB; 1M30; NMR; -; A=134-191.
DR PDB; 1M3A; NMR; -; A=135-191.
DR PDB; 1M3B; NMR; -; A=134-191.
DR PDB; 1M3C; NMR; -; A=132-191.
DR PDB; 2GGR; NMR; -; A=230-304.
DR PDB; 5IH2; X-ray; 1.80 A; A/B=134-191.
DR PDB; 5JN0; X-ray; 1.68 A; A=6-121.
DR PDB; 5L23; X-ray; 1.77 A; A=134-191.
DR PDBsum; 1B07; -.
DR PDBsum; 1CKA; -.
DR PDBsum; 1CKB; -.
DR PDBsum; 1JU5; -.
DR PDBsum; 1M30; -.
DR PDBsum; 1M3A; -.
DR PDBsum; 1M3B; -.
DR PDBsum; 1M3C; -.
DR PDBsum; 2GGR; -.
DR PDBsum; 5IH2; -.
DR PDBsum; 5JN0; -.
DR PDBsum; 5L23; -.
DR AlphaFoldDB; Q64010; -.
DR BMRB; Q64010; -.
DR SMR; Q64010; -.
DR BioGRID; 198887; 28.
DR CORUM; Q64010; -.
DR DIP; DIP-57059N; -.
DR IntAct; Q64010; 25.
DR MINT; Q64010; -.
DR STRING; 10090.ENSMUSP00000017920; -.
DR iPTMnet; Q64010; -.
DR PhosphoSitePlus; Q64010; -.
DR EPD; Q64010; -.
DR jPOST; Q64010; -.
DR MaxQB; Q64010; -.
DR PaxDb; Q64010; -.
DR PeptideAtlas; Q64010; -.
DR PRIDE; Q64010; -.
DR ProteomicsDB; 284173; -. [Q64010-1]
DR ProteomicsDB; 284174; -. [Q64010-2]
DR Antibodypedia; 4185; 628 antibodies from 38 providers.
DR DNASU; 12928; -.
DR Ensembl; ENSMUST00000017920; ENSMUSP00000017920; ENSMUSG00000017776. [Q64010-1]
DR GeneID; 12928; -.
DR KEGG; mmu:12928; -.
DR UCSC; uc007keq.2; mouse. [Q64010-1]
DR CTD; 1398; -.
DR MGI; MGI:88508; Crk.
DR VEuPathDB; HostDB:ENSMUSG00000017776; -.
DR eggNOG; KOG4792; Eukaryota.
DR GeneTree; ENSGT00820000127055; -.
DR HOGENOM; CLU_060542_0_1_1; -.
DR InParanoid; Q64010; -.
DR PhylomeDB; Q64010; -.
DR TreeFam; TF321436; -.
DR Reactome; R-MMU-170984; ARMS-mediated activation.
DR Reactome; R-MMU-186763; Downstream signal transduction.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-372708; p130Cas linkage to MAPK signaling for integrins.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-MMU-8875555; MET activates RAP1 and RAC1.
DR Reactome; R-MMU-8875656; MET receptor recycling.
DR Reactome; R-MMU-912631; Regulation of signaling by CBL.
DR BioGRID-ORCS; 12928; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Crk; mouse.
DR EvolutionaryTrace; Q64010; -.
DR PRO; PR:Q64010; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q64010; protein.
DR Bgee; ENSMUSG00000017776; Expressed in atrioventricular valve and 258 other tissues.
DR ExpressionAtlas; Q64010; baseline and differential.
DR Genevisible; Q64010; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IMP:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0045309; F:protein phosphorylated amino acid binding; IDA:MGI.
DR GO; GO:0043621; F:protein self-association; ISO:MGI.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IBA:GO_Central.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0042169; F:SH2 domain binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0035591; F:signaling adaptor activity; ISO:MGI.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IPI:BHF-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IGI:MGI.
DR GO; GO:0060326; P:cell chemotaxis; IGI:MGI.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IGI:MGI.
DR GO; GO:1990859; P:cellular response to endothelin; ISO:MGI.
DR GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; ISO:MGI.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISO:MGI.
DR GO; GO:0071732; P:cellular response to nitric oxide; ISO:MGI.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:MGI.
DR GO; GO:0098749; P:cerebellar neuron development; IGI:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IGI:MGI.
DR GO; GO:0016358; P:dendrite development; IGI:MGI.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030010; P:establishment of cell polarity; IGI:MGI.
DR GO; GO:0035685; P:helper T cell diapedesis; IGI:MGI.
DR GO; GO:0021766; P:hippocampus development; IGI:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IGI:MGI.
DR GO; GO:2000146; P:negative regulation of cell motility; ISO:MGI.
DR GO; GO:0045953; P:negative regulation of natural killer cell mediated cytotoxicity; ISO:MGI.
DR GO; GO:0061045; P:negative regulation of wound healing; ISO:MGI.
DR GO; GO:0001764; P:neuron migration; IGI:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0072657; P:protein localization to membrane; ISO:MGI.
DR GO; GO:0038026; P:reelin-mediated signaling pathway; IGI:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IGI:MGI.
DR GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IGI:MGI.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0050773; P:regulation of dendrite development; IGI:MGI.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:1902531; P:regulation of intracellular signal transduction; ISO:MGI.
DR GO; GO:0002685; P:regulation of leukocyte migration; IGI:MGI.
DR GO; GO:0043393; P:regulation of protein binding; ISO:MGI.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; ISO:MGI.
DR GO; GO:0009966; P:regulation of signal transduction; ISO:MGI.
DR GO; GO:2000404; P:regulation of T cell migration; IGI:MGI.
DR GO; GO:0061847; P:response to cholecystokinin; ISO:MGI.
DR GO; GO:0035728; P:response to hepatocyte growth factor; ISO:MGI.
DR GO; GO:0042542; P:response to hydrogen peroxide; ISO:MGI.
DR GO; GO:1901652; P:response to peptide; ISO:MGI.
DR GO; GO:0001878; P:response to yeast; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd11759; SH3_CRK_C; 1.
DR CDD; cd11758; SH3_CRK_N; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR035458; CRK_SH3_C.
DR InterPro; IPR035457; CRK_SH3_N.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF50044; SSF50044; 2.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane; Cytoplasm;
KW Membrane; Phosphoprotein; Proto-oncogene; Reference proteome; Repeat;
KW SH2 domain; SH3 domain.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P46108"
FT CHAIN 2..304
FT /note="Adapter molecule crk"
FT /id="PRO_0000079352"
FT DOMAIN 13..118
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 132..192
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 235..296
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 60..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..82
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 237
FT /note="Proline switch"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P46108"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46108"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46108"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46108"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46108"
FT MOD_RES 108
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P46108"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46108"
FT MOD_RES 221
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000269|PubMed:8194526"
FT MOD_RES 239
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P46108"
FT VAR_SEQ 205..304
FT /note="Missing (in isoform Crk-I)"
FT /evidence="ECO:0000303|PubMed:8183562"
FT /id="VSP_004174"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:5JN0"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:5JN0"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:5JN0"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:5JN0"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:5JN0"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:5JN0"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:5JN0"
FT HELIX 97..106
FT /evidence="ECO:0007829|PDB:5JN0"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:5JN0"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:1CKA"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:1M30"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:1CKA"
FT STRAND 165..173
FT /evidence="ECO:0007829|PDB:1CKA"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:1CKA"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:1CKA"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:5L23"
FT STRAND 238..244
FT /evidence="ECO:0007829|PDB:2GGR"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:2GGR"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:2GGR"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:2GGR"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:2GGR"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:2GGR"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:2GGR"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:2GGR"
SQ SEQUENCE 304 AA; 33815 MW; 5491896FC7A89065 CRC64;
MAGNFDSEER SSWYWGRLSR QEAVALLQGQ RHGVFLVRDS STSPGDYVLS VSENSRVSHY
IINSSGPRPP VPPSPAQPPP GVSPSRLRIG DQEFDSLPAL LEFYKIHYLD TTTLIEPVAR
SRQGSGVILR QEEAEYVRAL FDFNGNDEED LPFKKGDILR IRDKPEEQWW NAEDSEGKRG
MIPVPYVEKY RPASASVSAL IGGNQEGSHP QPLGGPEPGP YAQPSVNTPL PNLQNGPIYA
RVIQKRVPNA YDKTALALEV GELVKVTKIN VSGQWEGECN GKRGHFPFTH VRLLDQQNPD
EDFS
