Full text data of CRKL
CRKL
[Confidence: low (only semi-automatic identification from reviews)]
Crk-like protein
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Crk-like protein
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P46109
ID CRKL_HUMAN Reviewed; 303 AA.
AC P46109; A8KA44; D3DX35;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1995, sequence version 1.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=Crk-like protein;
GN Name=CRKL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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-
RT like 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.,
RA 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.,
RA 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.
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
RT receptor 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 MASS
RP SPECTROMETRY.
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
RT 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-127, AND MASS
RP SPECTROMETRY.
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 [13]
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.,
RA Buerckstuemmer T., 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 [14]
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 INPP5D/SHIP1. Interacts with DOCK2 and
CC EPOR. Interacts with phosphorylated CBLB and IRS4.
CC -!- INTERACTION:
CC P00519:ABL1; NbExp=2; IntAct=EBI-910, EBI-375543;
CC P22681:CBL; NbExp=2; IntAct=EBI-910, EBI-518228;
CC Q96PD2:DCBLD2; NbExp=3; IntAct=EBI-910, EBI-8536103;
CC P00533:EGFR; NbExp=2; IntAct=EBI-910, EBI-297353;
CC P04626:ERBB2; NbExp=2; IntAct=EBI-910, EBI-641062;
CC P21860:ERBB3; NbExp=3; IntAct=EBI-910, EBI-720706;
CC P17948:FLT1; NbExp=9; IntAct=EBI-910, EBI-1026718;
CC Q08460:Kcnma1 (xeno); NbExp=5; IntAct=EBI-910, EBI-1633915;
CC Q9EQG6:Kidins220 (xeno); NbExp=2; IntAct=EBI-910, EBI-976654;
CC Q92918:MAP4K1; NbExp=5; IntAct=EBI-910, EBI-881;
CC P27986:PIK3R1; NbExp=2; IntAct=EBI-910, EBI-79464;
CC Q05397:PTK2; NbExp=2; IntAct=EBI-910, EBI-702142;
CC Q13905:RAPGEF1; NbExp=2; IntAct=EBI-910, EBI-976876;
CC Q07889:SOS1; NbExp=2; IntAct=EBI-910, EBI-297487;
CC -!- SIMILARITY: Belongs to the CRK family.
CC -!- SIMILARITY: Contains 1 SH2 domain.
CC -!- SIMILARITY: Contains 2 SH3 domains.
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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 PIR; S41754; S41754.
DR RefSeq; NP_005198.1; NM_005207.3.
DR UniGene; Hs.5613; -.
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 ProteinModelPortal; P46109; -.
DR SMR; P46109; 1-303.
DR DIP; DIP-29165N; -.
DR IntAct; P46109; 55.
DR MINT; MINT-137265; -.
DR STRING; 9606.ENSP00000346300; -.
DR PhosphoSite; P46109; -.
DR DMDM; 1169094; -.
DR OGP; P46109; -.
DR PaxDb; P46109; -.
DR PeptideAtlas; P46109; -.
DR PRIDE; P46109; -.
DR DNASU; 1399; -.
DR Ensembl; ENST00000354336; ENSP00000346300; ENSG00000099942.
DR Ensembl; ENST00000411769; ENSP00000396646; ENSG00000099942.
DR GeneID; 1399; -.
DR KEGG; hsa:1399; -.
DR UCSC; uc002ztf.2; human.
DR CTD; 1399; -.
DR GeneCards; GC22P021272; -.
DR HGNC; HGNC:2363; CRKL.
DR HPA; HPA001100; -.
DR MIM; 602007; gene.
DR neXtProt; NX_P46109; -.
DR Orphanet; 261330; Distal 22q11.2 microdeletion syndrome.
DR PharmGKB; PA26881; -.
DR eggNOG; NOG292767; -.
DR HOGENOM; HOG000236288; -.
DR HOVERGEN; HBG105616; -.
DR InParanoid; P46109; -.
DR KO; K04438; -.
DR OMA; RTLYDFT; -.
DR OrthoDB; EOG7NW69P; -.
DR PhylomeDB; P46109; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P46109; -.
DR ChiTaRS; CRKL; human.
DR EvolutionaryTrace; P46109; -.
DR GeneWiki; CRKL; -.
DR GenomeRNAi; 1399; -.
DR NextBio; 5727; -.
DR PRO; PR:P46109; -.
DR Bgee; P46109; -.
DR CleanEx; HS_CRKL; -.
DR Genevestigator; P46109; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005768; C:endosome; TAS:Reactome.
DR GO; GO:0005070; F:SH3/SH2 adaptor activity; TAS:ProtInc.
DR GO; GO:0004871; F:signal transducer activity; TAS:ProtInc.
DR GO; GO:0000186; P:activation of MAPKK activity; TAS:Reactome.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0007254; P:JNK cascade; TAS:ProtInc.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR GO; GO:0009887; P:organ morphogenesis; IEA:Ensembl.
DR GO; GO:0060017; P:parathyroid gland development; IEA:Ensembl.
DR GO; GO:0007265; P:Ras protein signal transduction; TAS:ProtInc.
DR GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR011511; SH3_2.
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 PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Phosphoprotein; Reference proteome;
KW Repeat; SH2 domain; SH3 domain.
FT CHAIN 1 303 Crk-like protein.
FT /FTId=PRO_0000079347.
FT DOMAIN 14 102 SH2.
FT DOMAIN 123 183 SH3 1.
FT DOMAIN 235 296 SH3 2.
FT MOD_RES 127 127 Phosphotyrosine.
FT MOD_RES 207 207 Phosphotyrosine.
FT HELIX 11 14
FT STRAND 15 18
FT HELIX 21 28
FT STRAND 29 31
FT STRAND 36 40
FT STRAND 42 46
FT STRAND 48 54
FT STRAND 57 66
FT TURN 67 69
FT STRAND 70 73
FT STRAND 78 80
FT HELIX 81 88
FT STRAND 93 96
FT STRAND 105 107
FT STRAND 119 132
FT STRAND 138 141
FT STRAND 146 154
FT STRAND 157 164
FT STRAND 170 174
FT HELIX 175 177
FT STRAND 178 182
FT HELIX 190 192
FT HELIX 203 205
FT STRAND 238 242
FT STRAND 248 251
FT STRAND 253 255
FT STRAND 263 269
FT STRAND 271 279
FT STRAND 282 287
FT HELIX 288 290
FT STRAND 291 293
FT STRAND 296 299
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
//
ID CRKL_HUMAN Reviewed; 303 AA.
AC P46109; A8KA44; D3DX35;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1995, sequence version 1.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=Crk-like protein;
GN Name=CRKL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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-
RT like 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.,
RA 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.,
RA 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.
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
RT receptor 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 MASS
RP SPECTROMETRY.
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
RT 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-127, AND MASS
RP SPECTROMETRY.
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 [13]
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.,
RA Buerckstuemmer T., 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 [14]
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 INPP5D/SHIP1. Interacts with DOCK2 and
CC EPOR. Interacts with phosphorylated CBLB and IRS4.
CC -!- INTERACTION:
CC P00519:ABL1; NbExp=2; IntAct=EBI-910, EBI-375543;
CC P22681:CBL; NbExp=2; IntAct=EBI-910, EBI-518228;
CC Q96PD2:DCBLD2; NbExp=3; IntAct=EBI-910, EBI-8536103;
CC P00533:EGFR; NbExp=2; IntAct=EBI-910, EBI-297353;
CC P04626:ERBB2; NbExp=2; IntAct=EBI-910, EBI-641062;
CC P21860:ERBB3; NbExp=3; IntAct=EBI-910, EBI-720706;
CC P17948:FLT1; NbExp=9; IntAct=EBI-910, EBI-1026718;
CC Q08460:Kcnma1 (xeno); NbExp=5; IntAct=EBI-910, EBI-1633915;
CC Q9EQG6:Kidins220 (xeno); NbExp=2; IntAct=EBI-910, EBI-976654;
CC Q92918:MAP4K1; NbExp=5; IntAct=EBI-910, EBI-881;
CC P27986:PIK3R1; NbExp=2; IntAct=EBI-910, EBI-79464;
CC Q05397:PTK2; NbExp=2; IntAct=EBI-910, EBI-702142;
CC Q13905:RAPGEF1; NbExp=2; IntAct=EBI-910, EBI-976876;
CC Q07889:SOS1; NbExp=2; IntAct=EBI-910, EBI-297487;
CC -!- SIMILARITY: Belongs to the CRK family.
CC -!- SIMILARITY: Contains 1 SH2 domain.
CC -!- SIMILARITY: Contains 2 SH3 domains.
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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 PIR; S41754; S41754.
DR RefSeq; NP_005198.1; NM_005207.3.
DR UniGene; Hs.5613; -.
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 ProteinModelPortal; P46109; -.
DR SMR; P46109; 1-303.
DR DIP; DIP-29165N; -.
DR IntAct; P46109; 55.
DR MINT; MINT-137265; -.
DR STRING; 9606.ENSP00000346300; -.
DR PhosphoSite; P46109; -.
DR DMDM; 1169094; -.
DR OGP; P46109; -.
DR PaxDb; P46109; -.
DR PeptideAtlas; P46109; -.
DR PRIDE; P46109; -.
DR DNASU; 1399; -.
DR Ensembl; ENST00000354336; ENSP00000346300; ENSG00000099942.
DR Ensembl; ENST00000411769; ENSP00000396646; ENSG00000099942.
DR GeneID; 1399; -.
DR KEGG; hsa:1399; -.
DR UCSC; uc002ztf.2; human.
DR CTD; 1399; -.
DR GeneCards; GC22P021272; -.
DR HGNC; HGNC:2363; CRKL.
DR HPA; HPA001100; -.
DR MIM; 602007; gene.
DR neXtProt; NX_P46109; -.
DR Orphanet; 261330; Distal 22q11.2 microdeletion syndrome.
DR PharmGKB; PA26881; -.
DR eggNOG; NOG292767; -.
DR HOGENOM; HOG000236288; -.
DR HOVERGEN; HBG105616; -.
DR InParanoid; P46109; -.
DR KO; K04438; -.
DR OMA; RTLYDFT; -.
DR OrthoDB; EOG7NW69P; -.
DR PhylomeDB; P46109; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P46109; -.
DR ChiTaRS; CRKL; human.
DR EvolutionaryTrace; P46109; -.
DR GeneWiki; CRKL; -.
DR GenomeRNAi; 1399; -.
DR NextBio; 5727; -.
DR PRO; PR:P46109; -.
DR Bgee; P46109; -.
DR CleanEx; HS_CRKL; -.
DR Genevestigator; P46109; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005768; C:endosome; TAS:Reactome.
DR GO; GO:0005070; F:SH3/SH2 adaptor activity; TAS:ProtInc.
DR GO; GO:0004871; F:signal transducer activity; TAS:ProtInc.
DR GO; GO:0000186; P:activation of MAPKK activity; TAS:Reactome.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0007254; P:JNK cascade; TAS:ProtInc.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR GO; GO:0009887; P:organ morphogenesis; IEA:Ensembl.
DR GO; GO:0060017; P:parathyroid gland development; IEA:Ensembl.
DR GO; GO:0007265; P:Ras protein signal transduction; TAS:ProtInc.
DR GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR011511; SH3_2.
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 PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Phosphoprotein; Reference proteome;
KW Repeat; SH2 domain; SH3 domain.
FT CHAIN 1 303 Crk-like protein.
FT /FTId=PRO_0000079347.
FT DOMAIN 14 102 SH2.
FT DOMAIN 123 183 SH3 1.
FT DOMAIN 235 296 SH3 2.
FT MOD_RES 127 127 Phosphotyrosine.
FT MOD_RES 207 207 Phosphotyrosine.
FT HELIX 11 14
FT STRAND 15 18
FT HELIX 21 28
FT STRAND 29 31
FT STRAND 36 40
FT STRAND 42 46
FT STRAND 48 54
FT STRAND 57 66
FT TURN 67 69
FT STRAND 70 73
FT STRAND 78 80
FT HELIX 81 88
FT STRAND 93 96
FT STRAND 105 107
FT STRAND 119 132
FT STRAND 138 141
FT STRAND 146 154
FT STRAND 157 164
FT STRAND 170 174
FT HELIX 175 177
FT STRAND 178 182
FT HELIX 190 192
FT HELIX 203 205
FT STRAND 238 242
FT STRAND 248 251
FT STRAND 253 255
FT STRAND 263 269
FT STRAND 271 279
FT STRAND 282 287
FT HELIX 288 290
FT STRAND 291 293
FT STRAND 296 299
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
//
MIM
602007
*RECORD*
*FIELD* NO
602007
*FIELD* TI
*602007 V-CRK AVIAN SARCOMA VIRUS CT10 ONCOGENE HOMOLOG-LIKE; CRKL
;;ONCOGENE CRKL
read more*FIELD* TX
CLONING
CRK (164762) was originally identified as an oncogene transduced by the
avian sarcoma virus CT10. Ten Hoeve et al. (1993) identified and
characterized a gene, which they called CRKL for CRK-like, from a human
K562 lambda gt10 cDNA library. CRKL encodes a 303-amino acid polypeptide
with a predicted molecular mass of 36 kD. While CRKL is not the human
homolog of CRK, it is similar to protein-tyrosine kinases with SH2 and
SH3 (src homology) domains.
GENE FUNCTION
Senechal et al. (1996) showed that CRKL becomes phosphorylated when
overexpressed, activates Ras-dependent and JNK (601158) pathways, and
transforms fibroblasts. The authors also found CRKL to be a substrate
for the BCR-ABL tyrosine kinase (ABL; 189980), leading them to conclude
that CRKL is a tyrosine kinase and an oncogene.
Sasahara et al. (2002) showed that the adaptor protein CRKL binds
directly to WIP (602357) and that, following T-cell receptor ligation, a
CRKL-WIP-WASP (300392) complex is recruited by ZAP70 (176947) to lipid
rafts and immunologic synapses.
Since Fgf8 (600483) deletion in mice, like Crkl deletion, results in
many of the phenotypic features of DiGeorge syndrome (DGS;
188400)/velocardiofacial syndrome (VCFS; 192430), Moon et al. (2006)
investigated whether Crkl mediates Fgf8 signaling. In addition to
finding interactions between Crkl and Fgf8 during the development of
structures affected in DGS/VCFS, Moon et al. (2006) found that Fgf8
induced tyrosine phosphorylation of Fgfr1 (136350) and Fgfr2 (176943)
and their binding to Crkl. Crkl was required for normal cellular
responses to Fgf8, including survival and migration, Erk (see MAPK3;
601795) activation, and target gene expression.
Hallock et al. (2010) found that Crk and Crkl were recruited to mouse
skeletal muscle synapses and played redundant roles in synaptic
differentiation. Crk and Crkl bound the same tyrosine-phosphorylated
sequences in Dok7 (610285), a protein that functions downstream of agrin
(AGRN; 103320) and muscle-specific receptor kinase (MUSK; 601296) in
synapse formation.
MAPPING
By fluorescence in situ hybridization, ten Hoeve et al. (1993) localized
the CRKL gene to chromosome 22q11, centromeric of the chronic
myelogenous leukemia breakpoint region.
ANIMAL MODEL
Since the CRKL gene maps within the common deletion region for DGS/VCFS,
Guris et al. (2001) created mice homozygous for a targeted null mutation
at the Crkl locus (symbolized Crkol in mice) and found that they
exhibited defects in multiple cranial and cardiac neural crest
derivatives including the cranial ganglia, aortic arch arteries, cardiac
outflow tract, thymus, parathyroid glands, and craniofacial structures.
They showed that the migration and early expansion of neural crest cells
was unaffected in Crkol -/- embryos. These results therefore indicated
an essential stage- and tissue-specific role for Crkol in the function,
differentiation, and/or survival of neural crest cells during
development. The similarity between the Crkol -/- phenotype and the
clinical manifestations of DGS/VCFS implicated defects in CRKL-mediated
signaling pathways as part of the molecular mechanism underlying this
syndrome.
Guris et al. (2006) found that compound heterozygosity for null alleles
of the mouse Crkl and Tbx1 (602054) genes recapitulated thymic,
parathyroid, and cardiovascular defects characteristic of DGS at a
penetrance far greater than that generated by heterozygosity of Crkl or
Tbx1 alone.
Hallock et al. (2010) found that knockout of both Crk and Crkl in mouse
skeletal muscle, but not of either gene alone, caused perinatal
lethality. Lungs from Crk- and Crkl-deficient newborns failed to expand.
Embryonic day-18.5 muscle from Crk- and Crkl-deficient mice lacked
innervation and showed severe defects in presynaptic and postsynaptic
differentiation.
*FIELD* RF
1. Guris, D. L.; Duester, G.; Papaioannou, V. E.; Imamoto, A.: Dose-dependent
interaction of Tbx1 and Crkl and locally aberrant RA signaling in
a model of del22q11 syndrome. Dev. Cell 10: 81-92, 2006.
2. Guris, D. L.; Fantes, J.; Tara, D.; Druker, B. J.; Imamoto, A.
: Mice lacking the homologue of the human 22q11.2 gene CRKL phenocopy
neurocristopathies of DiGeorge syndrome. Nature Genet. 27: 293-298,
2001.
3. Hallock, P. T.; Xu, C.-F.; Park, T.-J.; Neubert, T. A.; Curran,
T.; Burden, S. J.: Dok-7 regulates neuromuscular synapse formation
by recruiting Crk and Crk-L. Genes Dev. 24: 2451-2461, 2010.
4. Moon, A. M.; Guris, D. L.; Seo, J.; Li, L.; Hammond, J.; Talbot,
A.; Imamoto, A.: Crkl deficiency disrupts Fgf8 signaling in a mouse
model of 22q11 deletion syndromes. Dev. Cell 10: 71-80, 2006.
5. Sasahara, Y.; Rachid, R.; Byrne, M. J.; de la Fuente, M. A.; Abraham,
R. T.; Ramesh, N.; Geha, R. S.: Mechanism of recruitment of WASP
to the immunological synapse and of its activation following TCR ligation. Molec.
Cell 10: 1269-1281, 2002.
6. Senechal, K.; Halpern, J.; Sawyers, C. L.: The CRKL adaptor protein
transforms fibroblasts and functions in transformation by the BCR-ABL
oncogene. J. Biol. Chem. 38: 23255-23261, 1996.
7. ten Hoeve, J.; Morris, C.; Heisterkamp, N.; Groffen, J.: Isolation
and chromosomal localization of CRKL, a human crk-like gene. Oncogene 8:
2469-2474, 1993.
*FIELD* CN
Patricia A. Hartz - updated: 9/24/2013
Patricia A. Hartz - updated: 2/8/2006
Stylianos E. Antonarakis - updated: 4/28/2003
Victor A. McKusick - updated: 2/22/2001
*FIELD* CD
Lori M. Kelman: 9/18/1997
*FIELD* ED
mgross: 11/08/2013
tpirozzi: 9/24/2013
wwang: 3/2/2006
wwang: 2/16/2006
terry: 2/8/2006
mgross: 4/28/2003
alopez: 2/22/2001
terry: 2/22/2001
dholmes: 10/6/1997
dholmes: 10/2/1997
dholmes: 10/1/1997
dholmes: 9/26/1997
dholmes: 9/19/1997
*RECORD*
*FIELD* NO
602007
*FIELD* TI
*602007 V-CRK AVIAN SARCOMA VIRUS CT10 ONCOGENE HOMOLOG-LIKE; CRKL
;;ONCOGENE CRKL
read more*FIELD* TX
CLONING
CRK (164762) was originally identified as an oncogene transduced by the
avian sarcoma virus CT10. Ten Hoeve et al. (1993) identified and
characterized a gene, which they called CRKL for CRK-like, from a human
K562 lambda gt10 cDNA library. CRKL encodes a 303-amino acid polypeptide
with a predicted molecular mass of 36 kD. While CRKL is not the human
homolog of CRK, it is similar to protein-tyrosine kinases with SH2 and
SH3 (src homology) domains.
GENE FUNCTION
Senechal et al. (1996) showed that CRKL becomes phosphorylated when
overexpressed, activates Ras-dependent and JNK (601158) pathways, and
transforms fibroblasts. The authors also found CRKL to be a substrate
for the BCR-ABL tyrosine kinase (ABL; 189980), leading them to conclude
that CRKL is a tyrosine kinase and an oncogene.
Sasahara et al. (2002) showed that the adaptor protein CRKL binds
directly to WIP (602357) and that, following T-cell receptor ligation, a
CRKL-WIP-WASP (300392) complex is recruited by ZAP70 (176947) to lipid
rafts and immunologic synapses.
Since Fgf8 (600483) deletion in mice, like Crkl deletion, results in
many of the phenotypic features of DiGeorge syndrome (DGS;
188400)/velocardiofacial syndrome (VCFS; 192430), Moon et al. (2006)
investigated whether Crkl mediates Fgf8 signaling. In addition to
finding interactions between Crkl and Fgf8 during the development of
structures affected in DGS/VCFS, Moon et al. (2006) found that Fgf8
induced tyrosine phosphorylation of Fgfr1 (136350) and Fgfr2 (176943)
and their binding to Crkl. Crkl was required for normal cellular
responses to Fgf8, including survival and migration, Erk (see MAPK3;
601795) activation, and target gene expression.
Hallock et al. (2010) found that Crk and Crkl were recruited to mouse
skeletal muscle synapses and played redundant roles in synaptic
differentiation. Crk and Crkl bound the same tyrosine-phosphorylated
sequences in Dok7 (610285), a protein that functions downstream of agrin
(AGRN; 103320) and muscle-specific receptor kinase (MUSK; 601296) in
synapse formation.
MAPPING
By fluorescence in situ hybridization, ten Hoeve et al. (1993) localized
the CRKL gene to chromosome 22q11, centromeric of the chronic
myelogenous leukemia breakpoint region.
ANIMAL MODEL
Since the CRKL gene maps within the common deletion region for DGS/VCFS,
Guris et al. (2001) created mice homozygous for a targeted null mutation
at the Crkl locus (symbolized Crkol in mice) and found that they
exhibited defects in multiple cranial and cardiac neural crest
derivatives including the cranial ganglia, aortic arch arteries, cardiac
outflow tract, thymus, parathyroid glands, and craniofacial structures.
They showed that the migration and early expansion of neural crest cells
was unaffected in Crkol -/- embryos. These results therefore indicated
an essential stage- and tissue-specific role for Crkol in the function,
differentiation, and/or survival of neural crest cells during
development. The similarity between the Crkol -/- phenotype and the
clinical manifestations of DGS/VCFS implicated defects in CRKL-mediated
signaling pathways as part of the molecular mechanism underlying this
syndrome.
Guris et al. (2006) found that compound heterozygosity for null alleles
of the mouse Crkl and Tbx1 (602054) genes recapitulated thymic,
parathyroid, and cardiovascular defects characteristic of DGS at a
penetrance far greater than that generated by heterozygosity of Crkl or
Tbx1 alone.
Hallock et al. (2010) found that knockout of both Crk and Crkl in mouse
skeletal muscle, but not of either gene alone, caused perinatal
lethality. Lungs from Crk- and Crkl-deficient newborns failed to expand.
Embryonic day-18.5 muscle from Crk- and Crkl-deficient mice lacked
innervation and showed severe defects in presynaptic and postsynaptic
differentiation.
*FIELD* RF
1. Guris, D. L.; Duester, G.; Papaioannou, V. E.; Imamoto, A.: Dose-dependent
interaction of Tbx1 and Crkl and locally aberrant RA signaling in
a model of del22q11 syndrome. Dev. Cell 10: 81-92, 2006.
2. Guris, D. L.; Fantes, J.; Tara, D.; Druker, B. J.; Imamoto, A.
: Mice lacking the homologue of the human 22q11.2 gene CRKL phenocopy
neurocristopathies of DiGeorge syndrome. Nature Genet. 27: 293-298,
2001.
3. Hallock, P. T.; Xu, C.-F.; Park, T.-J.; Neubert, T. A.; Curran,
T.; Burden, S. J.: Dok-7 regulates neuromuscular synapse formation
by recruiting Crk and Crk-L. Genes Dev. 24: 2451-2461, 2010.
4. Moon, A. M.; Guris, D. L.; Seo, J.; Li, L.; Hammond, J.; Talbot,
A.; Imamoto, A.: Crkl deficiency disrupts Fgf8 signaling in a mouse
model of 22q11 deletion syndromes. Dev. Cell 10: 71-80, 2006.
5. Sasahara, Y.; Rachid, R.; Byrne, M. J.; de la Fuente, M. A.; Abraham,
R. T.; Ramesh, N.; Geha, R. S.: Mechanism of recruitment of WASP
to the immunological synapse and of its activation following TCR ligation. Molec.
Cell 10: 1269-1281, 2002.
6. Senechal, K.; Halpern, J.; Sawyers, C. L.: The CRKL adaptor protein
transforms fibroblasts and functions in transformation by the BCR-ABL
oncogene. J. Biol. Chem. 38: 23255-23261, 1996.
7. ten Hoeve, J.; Morris, C.; Heisterkamp, N.; Groffen, J.: Isolation
and chromosomal localization of CRKL, a human crk-like gene. Oncogene 8:
2469-2474, 1993.
*FIELD* CN
Patricia A. Hartz - updated: 9/24/2013
Patricia A. Hartz - updated: 2/8/2006
Stylianos E. Antonarakis - updated: 4/28/2003
Victor A. McKusick - updated: 2/22/2001
*FIELD* CD
Lori M. Kelman: 9/18/1997
*FIELD* ED
mgross: 11/08/2013
tpirozzi: 9/24/2013
wwang: 3/2/2006
wwang: 2/16/2006
terry: 2/8/2006
mgross: 4/28/2003
alopez: 2/22/2001
terry: 2/22/2001
dholmes: 10/6/1997
dholmes: 10/2/1997
dholmes: 10/1/1997
dholmes: 9/26/1997
dholmes: 9/19/1997