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 27-MAR-2024, entry version 215. 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 NEDD9 AND BCAR1. RX PubMed=9020138; DOI=10.1074/jbc.272.7.4230; RA Manie S.N., Beck A.R.P., Astier A., Law S.F., Canty T., Hirai H., RA Druker B.J., Avraham H., Haghayeghi N., Sattler M., Salgia R., RA Griffin J.D., Golemis E.A., Freedman A.S.; RT "Involvement of p130(Cas) and p105(HEF1), a novel Cas-like docking protein, RT in a cytoskeleton-dependent signaling pathway initiated by ligation of RT integrin or antigen receptor on human B cells."; RL J. Biol. Chem. 272:4230-4236(1997). RN [8] 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 [9] 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 [10] 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 [11] 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 [12] 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 [13] 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 [14] 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 [15] 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 [16] 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 [17] 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 [18] 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 Interacts with BCAR1/CAS and NEDD9/HEF1 (PubMed:9020138). CC {ECO:0000269|PubMed:10022120, ECO:0000269|PubMed:11443118, CC ECO:0000269|PubMed:12393632, ECO:0000269|PubMed:19004829, CC ECO:0000269|PubMed:9020138, 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}. 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; 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; 211. DR CORUM; P46109; -. DR DIP; DIP-29165N; -. DR IntAct; P46109; 122. 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; 9606-ENSP00000346300; -. DR PeptideAtlas; P46109; -. DR ProteomicsDB; 55734; -. DR Pumba; P46109; -. DR Antibodypedia; 255; 807 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 AGR; HGNC:2363; -. 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; WYVGPLS; -. DR OrthoDB; 2900795at2759; -. 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; 588 hits in 1169 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 209 other cell types or tissues. 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: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:0160093; P:chordate pharynx 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: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:0035022; P:positive regulation of Rac protein signal transduction; IEA:Ensembl. DR GO; GO:1904395; P:positive regulation of skeletal muscle acetylcholine-gated channel clustering; IEA:Ensembl. DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB. DR GO; GO:0098698; P:postsynaptic specialization assembly; IEA:Ensembl. 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: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: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; cd09926; SH2_CRK_like; 1. DR CDD; cd11759; SH3_CRK_C; 1. DR CDD; cd11758; SH3_CRK_N; 1. DR Gene3D; 3.30.505.10; SH2 domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 2. 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 PANTHER; PTHR19969:SF20; CRK-LIKE PROTEIN; 1. DR PANTHER; PTHR19969; SH2-SH3 ADAPTOR PROTEIN-RELATED; 1. 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; SSF55550; SH2 domain; 1. DR SUPFAM; SSF50044; SH3-domain; 2. DR PROSITE; PS50001; SH2; 1. DR PROSITE; PS50002; SH3; 2. DR Genevisible; P46109; HS. 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 //