CRKL_HUMAN
ID CRKL_HUMAN Reviewed; 303 AA.
AC P46109; A8KA44; D3DX35;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Crk-like protein;
GN Name=CRKL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RX PubMed=8361759;
RA ten Hoeve J., Morris C., Heisterkamp N., Groffen J.;
RT "Isolation and chromosomal localization of CRKL, a human crk-like gene.";
RL Oncogene 8:2469-2474(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH IRS4.
RX PubMed=9614078; DOI=10.1074/jbc.273.24.14780;
RA Koval A.P., Karas M., Zick Y., LeRoith D.;
RT "Interplay of the proto-oncogene proteins CrkL and CrkII in insulin-like
RT growth factor-I receptor-mediated signal transduction.";
RL J. Biol. Chem. 273:14780-14787(1998).
RN [7]
RP INTERACTION WITH CBLB.
RX PubMed=10022120; DOI=10.1038/sj.onc.1202411;
RA Elly C., Witte S., Zhang Z., Rosnet O., Lipkowitz S., Altman A., Liu Y.-C.;
RT "Tyrosine phosphorylation and complex formation of Cbl-b upon T cell
RT receptor stimulation.";
RL Oncogene 18:1147-1156(1999).
RN [8]
RP INTERACTION WITH DOCK2.
RX PubMed=12393632; DOI=10.1182/blood-2001-11-0032;
RA Nishihara H., Maeda M., Oda A., Tsuda M., Sawa H., Nagashima K., Tanaka S.;
RT "DOCK2 associates with CrkL and regulates Rac1 in human leukemia cell
RT lines.";
RL Blood 100:3968-3974(2002).
RN [9]
RP INTERACTION WITH EPOR AND INPP5D.
RX PubMed=11443118; DOI=10.1074/jbc.m102924200;
RA Arai A., Kanda E., Nosaka Y., Miyasaka N., Miura O.;
RT "CrkL is recruited through its SH2 domain to the erythropoietin receptor
RT and plays a role in Lyn-mediated receptor signaling.";
RL J. Biol. Chem. 276:33282-33290(2001).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-207, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP INTERACTION WITH DOCK5, AND MUTAGENESIS OF TRP-160.
RX PubMed=19004829; DOI=10.1074/jbc.m808010200;
RA Sanders M.A., Ampasala D., Basson M.D.;
RT "DOCK5 and DOCK1 regulate Caco-2 intestinal epithelial cell spreading and
RT migration on collagen IV.";
RL J. Biol. Chem. 284:27-35(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-127, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP STRUCTURE BY NMR OF 220-303.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structures of the SH3 domain of human CRK-like protein.";
RL Submitted (DEC-2006) to the PDB data bank.
CC -!- FUNCTION: May mediate the transduction of intracellular signals.
CC -!- SUBUNIT: Interacts with tyrosine-phosphorylated EPOR and INPP5D/SHIP1
CC (PubMed:11443118). Interacts with DOCK2 and DOCK5 via its first SH3
CC domain (PubMed:12393632, PubMed:19004829). Interacts with
CC phosphorylated CBLB and IRS4 (PubMed:10022120, PubMed:9614078).
CC {ECO:0000269|PubMed:10022120, ECO:0000269|PubMed:11443118,
CC ECO:0000269|PubMed:12393632, ECO:0000269|PubMed:19004829,
CC ECO:0000269|PubMed:9614078}.
CC -!- INTERACTION:
CC P46109; P00519: ABL1; NbExp=3; IntAct=EBI-910, EBI-375543;
CC P46109; P51451: BLK; NbExp=3; IntAct=EBI-910, EBI-2105445;
CC P46109; P22681: CBL; NbExp=3; IntAct=EBI-910, EBI-518228;
CC P46109; Q13191: CBLB; NbExp=4; IntAct=EBI-910, EBI-744027;
CC P46109; P46109: CRKL; NbExp=4; IntAct=EBI-910, EBI-910;
CC P46109; Q96PD2: DCBLD2; NbExp=3; IntAct=EBI-910, EBI-8536103;
CC P46109; P00533: EGFR; NbExp=4; IntAct=EBI-910, EBI-297353;
CC P46109; P04626: ERBB2; NbExp=2; IntAct=EBI-910, EBI-641062;
CC P46109; P21860: ERBB3; NbExp=3; IntAct=EBI-910, EBI-720706;
CC P46109; P17948: FLT1; NbExp=9; IntAct=EBI-910, EBI-1026718;
CC P46109; P36888: FLT3; NbExp=2; IntAct=EBI-910, EBI-3946257;
CC P46109; Q13480: GAB1; NbExp=5; IntAct=EBI-910, EBI-517684;
CC P46109; P05556: ITGB1; NbExp=2; IntAct=EBI-910, EBI-703066;
CC P46109; Q92918: MAP4K1; NbExp=5; IntAct=EBI-910, EBI-881;
CC P46109; P16234: PDGFRA; NbExp=3; IntAct=EBI-910, EBI-2861522;
CC P46109; P62333: PSMC6; NbExp=5; IntAct=EBI-910, EBI-357669;
CC P46109; A2A3K4: PTPDC1; NbExp=3; IntAct=EBI-910, EBI-11603375;
CC P46109; Q13905: RAPGEF1; NbExp=3; IntAct=EBI-910, EBI-976876;
CC P46109; Q70EK8: USP53; NbExp=5; IntAct=EBI-910, EBI-742050;
CC P46109; P07947: YES1; NbExp=3; IntAct=EBI-910, EBI-515331;
CC P46109; Q08460: Kcnma1; Xeno; NbExp=5; IntAct=EBI-910, EBI-1633915;
CC P46109; Q9EQG6: Kidins220; Xeno; NbExp=2; IntAct=EBI-910, EBI-976654;
CC -!- SIMILARITY: Belongs to the CRK family. {ECO:0000305}.
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DR EMBL; X59656; CAA42199.1; -; mRNA.
DR EMBL; CR456423; CAG30309.1; -; mRNA.
DR EMBL; AK292909; BAF85598.1; -; mRNA.
DR EMBL; CH471176; EAX02932.1; -; Genomic_DNA.
DR EMBL; CH471176; EAX02933.1; -; Genomic_DNA.
DR EMBL; CH471176; EAX02934.1; -; Genomic_DNA.
DR EMBL; BC043500; AAH43500.1; -; mRNA.
DR CCDS; CCDS13785.1; -.
DR PIR; S41754; S41754.
DR RefSeq; NP_005198.1; NM_005207.3.
DR PDB; 2BZX; X-ray; 2.80 A; A=237-303.
DR PDB; 2BZY; X-ray; 2.50 A; A/B=237-303.
DR PDB; 2DBK; NMR; -; A=229-303.
DR PDB; 2EO3; NMR; -; A=1-104.
DR PDB; 2LQN; NMR; -; A=1-303.
DR PDB; 2LQW; NMR; -; A=1-303.
DR PDBsum; 2BZX; -.
DR PDBsum; 2BZY; -.
DR PDBsum; 2DBK; -.
DR PDBsum; 2EO3; -.
DR PDBsum; 2LQN; -.
DR PDBsum; 2LQW; -.
DR AlphaFoldDB; P46109; -.
DR BMRB; P46109; -.
DR SMR; P46109; -.
DR BioGRID; 107789; 187.
DR CORUM; P46109; -.
DR DIP; DIP-29165N; -.
DR IntAct; P46109; 116.
DR MINT; P46109; -.
DR STRING; 9606.ENSP00000346300; -.
DR GlyGen; P46109; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P46109; -.
DR MetOSite; P46109; -.
DR PhosphoSitePlus; P46109; -.
DR BioMuta; CRKL; -.
DR DMDM; 1169094; -.
DR OGP; P46109; -.
DR EPD; P46109; -.
DR jPOST; P46109; -.
DR MassIVE; P46109; -.
DR MaxQB; P46109; -.
DR PaxDb; P46109; -.
DR PeptideAtlas; P46109; -.
DR PRIDE; P46109; -.
DR ProteomicsDB; 55734; -.
DR Antibodypedia; 255; 751 antibodies from 39 providers.
DR DNASU; 1399; -.
DR Ensembl; ENST00000354336.8; ENSP00000346300.3; ENSG00000099942.13.
DR Ensembl; ENST00000411769.1; ENSP00000396646.1; ENSG00000099942.13.
DR GeneID; 1399; -.
DR KEGG; hsa:1399; -.
DR MANE-Select; ENST00000354336.8; ENSP00000346300.3; NM_005207.4; NP_005198.1.
DR UCSC; uc002ztf.2; human.
DR CTD; 1399; -.
DR DisGeNET; 1399; -.
DR GeneCards; CRKL; -.
DR HGNC; HGNC:2363; CRKL.
DR HPA; ENSG00000099942; Low tissue specificity.
DR MalaCards; CRKL; -.
DR MIM; 602007; gene.
DR neXtProt; NX_P46109; -.
DR OpenTargets; ENSG00000099942; -.
DR Orphanet; 261330; Distal 22q11.2 microdeletion syndrome.
DR PharmGKB; PA26881; -.
DR VEuPathDB; HostDB:ENSG00000099942; -.
DR eggNOG; KOG4792; Eukaryota.
DR GeneTree; ENSGT00820000127055; -.
DR HOGENOM; CLU_060542_0_1_1; -.
DR InParanoid; P46109; -.
DR OMA; FTHVQLF; -.
DR OrthoDB; 1414461at2759; -.
DR PhylomeDB; P46109; -.
DR TreeFam; TF321436; -.
DR PathwayCommons; P46109; -.
DR Reactome; R-HSA-170968; Frs2-mediated activation.
DR Reactome; R-HSA-186763; Downstream signal transduction.
DR Reactome; R-HSA-8875555; MET activates RAP1 and RAC1.
DR Reactome; R-HSA-8875656; MET receptor recycling.
DR Reactome; R-HSA-9027284; Erythropoietin activates RAS.
DR Reactome; R-HSA-912631; Regulation of signaling by CBL.
DR SignaLink; P46109; -.
DR SIGNOR; P46109; -.
DR BioGRID-ORCS; 1399; 569 hits in 1083 CRISPR screens.
DR ChiTaRS; CRKL; human.
DR EvolutionaryTrace; P46109; -.
DR GeneWiki; CRKL; -.
DR GenomeRNAi; 1399; -.
DR Pharos; P46109; Tbio.
DR PRO; PR:P46109; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P46109; protein.
DR Bgee; ENSG00000099942; Expressed in secondary oocyte and 207 other tissues.
DR Genevisible; P46109; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0098890; C:extrinsic component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:MGI.
DR GO; GO:0035591; F:signaling adaptor activity; IBA:GO_Central.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0090630; P:activation of GTPase activity; IEA:Ensembl.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0001783; P:B cell apoptotic process; IEA:Ensembl.
DR GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
DR GO; GO:0060326; P:cell chemotaxis; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0098761; P:cellular response to interleukin-7; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IMP:ARUK-UCL.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0098749; P:cerebellar neuron development; IEA:Ensembl.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:1904888; P:cranial skeletal system development; IEA:Ensembl.
DR GO; GO:0016358; P:dendrite development; IEA:Ensembl.
DR GO; GO:0086100; P:endothelin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0030010; P:establishment of cell polarity; IEA:Ensembl.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0035685; P:helper T cell diapedesis; IEA:Ensembl.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
DR GO; GO:0007254; P:JNK cascade; TAS:ProtInc.
DR GO; GO:0006629; P:lipid metabolic process; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:ARUK-UCL.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl.
DR GO; GO:0060017; P:parathyroid gland development; IEA:Ensembl.
DR GO; GO:0060465; P:pharynx development; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:CACAO.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:ARUK-UCL.
DR GO; GO:1903977; P:positive regulation of glial cell migration; IMP:ARUK-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:ARUK-UCL.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; TAS:ProtInc.
DR GO; GO:0038026; P:reelin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
DR GO; GO:0050773; P:regulation of dendrite development; IEA:Ensembl.
DR GO; GO:1904393; P:regulation of skeletal muscle acetylcholine-gated channel clustering; IEA:Ensembl.
DR GO; GO:2000404; P:regulation of T cell migration; IEA:Ensembl.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007338; P:single fertilization; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0007416; P:synapse assembly; IEA:Ensembl.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR GO; GO:0001655; P:urogenital system development; IEA:Ensembl.
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; Phosphoprotein; Reference proteome; Repeat; SH2 domain;
KW SH3 domain.
FT CHAIN 1..303
FT /note="Crk-like protein"
FT /id="PRO_0000079347"
FT DOMAIN 14..102
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 123..183
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 184..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 127
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 207
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MUTAGEN 160
FT /note="W->L: Abolishes interaction with DOCK5."
FT /evidence="ECO:0000269|PubMed:19004829"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:2EO3"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:2EO3"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:2EO3"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:2LQW"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:2EO3"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:2EO3"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:2EO3"
FT STRAND 57..66
FT /evidence="ECO:0007829|PDB:2EO3"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:2EO3"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:2EO3"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2EO3"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:2EO3"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:2EO3"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:2LQW"
FT STRAND 119..132
FT /evidence="ECO:0007829|PDB:2LQN"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:2LQN"
FT STRAND 146..154
FT /evidence="ECO:0007829|PDB:2LQN"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:2LQN"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:2LQN"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:2LQN"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:2LQN"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:2LQW"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:2LQN"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:2BZY"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:2BZY"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:2DBK"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:2BZY"
FT STRAND 271..279
FT /evidence="ECO:0007829|PDB:2BZY"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:2BZY"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:2BZY"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:2BZY"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:2LQN"
SQ SEQUENCE 303 AA; 33777 MW; 294CF1EE2CD44B81 CRC64;
MSSARFDSSD RSAWYMGPVS RQEAQTRLQG QRHGMFLVRD SSTCPGDYVL SVSENSRVSH
YIINSLPNRR FKIGDQEFDH LPALLEFYKI HYLDTTTLIE PAPRYPSPPM GSVSAPNLPT
AEDNLEYVRT LYDFPGNDAE DLPFKKGEIL VIIEKPEEQW WSARNKDGRV GMIPVPYVEK
LVRSSPHGKH GNRNSNSYGI PEPAHAYAQP QTTTPLPAVS GSPGAAITPL PSTQNGPVFA
KAIQKRVPCA YDKTALALEV GDIVKVTRMN INGQWEGEVN GRKGLFPFTH VKIFDPQNPD
ENE
