CRKL_MOUSE
ID CRKL_MOUSE Reviewed; 303 AA.
AC P47941; Q3TQ18; Q8BGC5;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Crk-like protein;
GN Name=Crkl; Synonyms=Crkol;
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].
RC STRAIN=C57BL X CBA; TISSUE=Placenta;
RX PubMed=7478571;
RA de Jong R.L., Haataja L., Voncken J.W., Heisterkamp N., Groffen J.;
RT "Tyrosine phosphorylation of murine Crkl.";
RL Oncogene 11:1469-1474(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic head, and Embryonic heart;
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 INTERACTION WITH INPP5D.
RX PubMed=11031258; DOI=10.1074/jbc.m006250200;
RA Sattler M., Verma S., Pride Y.B., Salgia R., Rohrschneider L.R.,
RA Griffin J.D.;
RT "SHIP1, an SH2 domain containing polyinositol-5-phosphatase, regulates
RT migration through two critical tyrosine residues and forms a novel
RT signaling complex with DOK1 and CRKL.";
RL J. Biol. Chem. 276:2451-2458(2001).
RN [4]
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 [5]
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 [6]
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).
CC -!- FUNCTION: May mediate the transduction of intracellular signals.
CC -!- SUBUNIT: Interacts with DOCK2 and EPOR. Interacts with phosphorylated
CC CBLB and IRS4 (By similarity). Interacts with INPP5D/SHIP1.
CC {ECO:0000250, ECO:0000269|PubMed:11031258}.
CC -!- PTM: Phosphorylated on tyrosine. Phosphorylation is prominent during
CC early development, but decreases at later embryonic stages and in
CC newborn mice.
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; X90648; CAA62220.1; -; mRNA.
DR EMBL; AK048641; BAC33406.1; -; mRNA.
DR EMBL; AK052315; BAC34933.1; -; mRNA.
DR EMBL; AK163981; BAE37567.1; -; mRNA.
DR CCDS; CCDS28002.1; -.
DR PIR; S58352; S58352.
DR RefSeq; NP_001264160.1; NM_001277231.1.
DR RefSeq; NP_031790.2; NM_007764.5.
DR AlphaFoldDB; P47941; -.
DR BMRB; P47941; -.
DR SMR; P47941; -.
DR BioGRID; 198888; 27.
DR CORUM; P47941; -.
DR IntAct; P47941; 9.
DR MINT; P47941; -.
DR STRING; 10090.ENSMUSP00000006293; -.
DR iPTMnet; P47941; -.
DR PhosphoSitePlus; P47941; -.
DR REPRODUCTION-2DPAGE; IPI00113362; -.
DR EPD; P47941; -.
DR jPOST; P47941; -.
DR MaxQB; P47941; -.
DR PaxDb; P47941; -.
DR PRIDE; P47941; -.
DR ProteomicsDB; 278035; -.
DR Antibodypedia; 255; 751 antibodies from 39 providers.
DR DNASU; 12929; -.
DR Ensembl; ENSMUST00000006293; ENSMUSP00000006293; ENSMUSG00000006134.
DR GeneID; 12929; -.
DR KEGG; mmu:12929; -.
DR UCSC; uc007ykv.2; mouse.
DR CTD; 1399; -.
DR MGI; MGI:104686; Crkl.
DR VEuPathDB; HostDB:ENSMUSG00000006134; -.
DR eggNOG; KOG4792; Eukaryota.
DR GeneTree; ENSGT00820000127055; -.
DR HOGENOM; CLU_060542_0_1_1; -.
DR InParanoid; P47941; -.
DR OMA; FTHVQLF; -.
DR OrthoDB; 1414461at2759; -.
DR PhylomeDB; P47941; -.
DR TreeFam; TF321436; -.
DR Reactome; R-MMU-170968; Frs2-mediated activation.
DR Reactome; R-MMU-186763; Downstream signal transduction.
DR Reactome; R-MMU-8875555; MET activates RAP1 and RAC1.
DR Reactome; R-MMU-8875656; MET receptor recycling.
DR Reactome; R-MMU-9027284; Erythropoietin activates RAS.
DR Reactome; R-MMU-912631; Regulation of signaling by CBL.
DR BioGRID-ORCS; 12929; 8 hits in 74 CRISPR screens.
DR ChiTaRS; Crkl; mouse.
DR PRO; PR:P47941; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P47941; protein.
DR Bgee; ENSMUSG00000006134; Expressed in rostral migratory stream and 270 other tissues.
DR ExpressionAtlas; P47941; baseline and differential.
DR Genevisible; P47941; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0098890; C:extrinsic component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0035591; F:signaling adaptor activity; IBA:GO_Central.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; IGI:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; IGI:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IGI:MGI.
DR GO; GO:0001783; P:B cell apoptotic process; IMP:MGI.
DR GO; GO:0001568; P:blood vessel development; IGI:MGI.
DR GO; GO:0060326; P:cell chemotaxis; IGI:MGI.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0098761; P:cellular response to interleukin-7; IDA:MGI.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:MGI.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:MGI.
DR GO; GO:0098749; P:cerebellar neuron development; IGI:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IGI:MGI.
DR GO; GO:1904888; P:cranial skeletal system development; IMP:MGI.
DR GO; GO:0016358; P:dendrite development; IGI:MGI.
DR GO; GO:0086100; P:endothelin receptor signaling pathway; IMP:MGI.
DR GO; GO:0030010; P:establishment of cell polarity; IGI:MGI.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0007507; P:heart development; 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:0008584; P:male gonad development; IMP:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:MGI.
DR GO; GO:0060017; P:parathyroid gland development; IGI:MGI.
DR GO; GO:0007389; P:pattern specification process; IGI:MGI.
DR GO; GO:0060465; P:pharynx development; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:MGI.
DR GO; GO:1903977; P:positive regulation of glial cell migration; ISO:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:0038026; P:reelin-mediated signaling pathway; IMP:MGI.
DR GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IGI:MGI.
DR GO; GO:0001558; P:regulation of cell growth; IDA:MGI.
DR GO; GO:0050773; P:regulation of dendrite development; IGI:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0002685; P:regulation of leukocyte migration; IGI:MGI.
DR GO; GO:1904393; P:regulation of skeletal muscle acetylcholine-gated channel clustering; IGI:MGI.
DR GO; GO:2000404; P:regulation of T cell migration; IGI:MGI.
DR GO; GO:0071774; P:response to fibroblast growth factor; IMP:MGI.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007338; P:single fertilization; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0007416; P:synapse assembly; IDA:SynGO.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IDA:MGI.
DR GO; GO:0048538; P:thymus development; IGI:MGI.
DR GO; GO:0001655; P:urogenital system development; IMP:MGI.
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 Phosphoprotein; Reference proteome; Repeat; SH2 domain; SH3 domain.
FT CHAIN 1..303
FT /note="Crk-like protein"
FT /id="PRO_0000079348"
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..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 127
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P46109"
FT MOD_RES 207
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P46109"
FT CONFLICT 165
FT /note="N -> T (in Ref. 1; CAA62220)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 303 AA; 33830 MW; A8C801F78EF73573 CRC64;
MSSARFDSSD RSAWYMGPVT RQEAQTRLQG QRHGMFLVRD SSTCPGDYVL SVSENSRVSH
YIINSLPNRR FKIGDQEFDH LPALLEFYKI HYLDTTTLIE PAPRYPSPPV GSVSAPNLPT
AEENLEYVRT LYDFPGNDAE DLPFKKGELL VIIEKPEEQW WSARNKDGRV GMIPVPYVEK
LVRSSPHGKH GNRNSNSYGI PEPAHAYAQP QTTTPLPTVA STPGAAINPL PSTQNGPVFA
KAIQKRVPCA YDKTALALEV GDIVKVTRMN INGQWEGEVN GRKGLFPFTH VKIFDPQNPD
DNE
