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Adapter molecule crk (Proto-oncogene c-Crk) (p38)

 CRK_HUMAN               Reviewed;         304 AA.
P46108; A8MWE8; B0LPE8; D3DTH6; Q96GA9; Q96HJ0;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
24-JUL-2007, sequence version 2.
30-AUG-2017, entry version 187.
RecName: Full=Adapter molecule crk;
AltName: Full=Proto-oncogene c-Crk;
AltName: Full=p38;
Name=CRK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CRK-II), FUNCTION (ISOFORM
CRK-II), AND ALTERNATIVE SPLICING.
TISSUE=Embryonic lung, and Placenta;
PubMed=1630456; DOI=10.1128/MCB.12.8.3482;
Matsuda M., Tanaka S., Nagata S., Kojima A., Kurata T., Shibuya M.;
"Two species of human CRK cDNA encode proteins with distinct
biological activities.";
Mol. Cell. Biol. 12:3482-3489(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8378094;
Fioretos T., Heisterkamp N., Groffen J., Benjes S., Morris C.;
"CRK proto-oncogene maps to human chromosome band 17p13.";
Oncogene 8:2853-2855(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CRK-II).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CRK-I).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS CRK-I AND CRK-II).
TISSUE=Eye, Lung, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
INTERACTION WITH DOCK1.
PubMed=8657152; DOI=10.1128/MCB.16.4.1770;
Hasegawa H., Kiyokawa E., Tanaka S., Nagashima K., Gotoh N.,
Shibuya M., Kurata T., Matsuda M.;
"DOCK180, a major CRK-binding protein, alters cell morphology upon
translocation to the cell membrane.";
Mol. Cell. Biol. 16:1770-1776(1996).
[10]
INTERACTION WITH DOCK1; C3G AND EPS15, AND MUTAGENESIS OF ASP-150.
PubMed=8662907; DOI=10.1074/jbc.271.24.14468;
Matsuda M., Ota S., Tanimura R., Nakamura H., Matuoka K., Takenawa T.,
Nagashima K., Kurata T.;
"Interaction between the amino-terminal SH3 domain of CRK and its
natural target proteins.";
J. Biol. Chem. 271:14468-14472(1996).
[11]
INTERACTION WITH IRS4.
PubMed=9614078; DOI=10.1074/jbc.273.24.14780;
Koval A.P., Karas M., Zick Y., LeRoith D.;
"Interplay of the proto-oncogene proteins CrkL and CrkII in insulin-
like growth factor-I receptor-mediated signal transduction.";
J. Biol. Chem. 273:14780-14787(1998).
[12]
INTERACTION WITH CBLC.
PubMed=10362357; DOI=10.1038/sj.onc.1202753;
Keane M.M., Ettenberg S.A., Nau M.M., Banerjee P., Cuello M.,
Penninger J., Lipkowitz S.;
"cbl-3: a new mammalian cbl family protein.";
Oncogene 18:3365-3375(1999).
[13]
INTERACTION WITH PDGFRA AND PDGFRB.
PubMed=10733900; DOI=10.1006/bbrc.2000.2374;
Matsumoto T., Yokote K., Take A., Takemoto M., Asaumi S.,
Hashimoto Y., Matsuda M., Saito Y., Mori S.;
"Differential interaction of CrkII adaptor protein with platelet-
derived growth factor alpha- and beta-receptors is determined by its
internal tyrosine phosphorylation.";
Biochem. Biophys. Res. Commun. 270:28-33(2000).
[14]
INTERACTION WITH SHB.
PubMed=10964504; DOI=10.1006/excr.2000.4984;
Lu L., Anneren C., Reedquist K.A., Bos J.L., Welsh M.;
"NGF-dependent neurite outgrowth in PC12 cells overexpressing the Src
homology 2-domain protein shb requires activation of the Rap1
pathway.";
Exp. Cell Res. 259:370-377(2000).
[15]
FUNCTION (ISOFORM CRK-II), AND INTERACTION WITH EPHA3.
PubMed=11870224;
Lawrenson I.D., Wimmer-Kleikamp S.H., Lock P., Schoenwaelder S.M.,
Down M., Boyd A.W., Alewood P.F., Lackmann M.;
"Ephrin-A5 induces rounding, blebbing and de-adhesion of EphA3-
expressing 293T and melanoma cells by CrkII and Rho-mediated
signalling.";
J. Cell Sci. 115:1059-1072(2002).
[16]
INTERACTION WITH DOCK4.
PubMed=12628187; DOI=10.1016/S0092-8674(03)00155-7;
Yajnik V., Paulding C., Sordella R., McClatchey A.I., Saito M.,
Wahrer D.C.R., Reynolds P., Bell D.W., Lake R., van den Heuvel S.,
Settleman J., Haber D.A.;
"DOCK4, a GTPase activator, is disrupted during tumorigenesis.";
Cell 112:673-684(2003).
[17]
INTERACTION WITH KIT, IDENTIFICATION BY MASS SPECTROMETRY, AND
PHOSPHORYLATION.
PubMed=12878163; DOI=10.1016/S0014-4827(03)00206-4;
Lennartsson J., Wernstedt C., Engstrom U., Hellman U., Ronnstrand L.;
"Identification of Tyr900 in the kinase domain of c-Kit as a Src-
dependent phosphorylation site mediating interaction with c-Crk.";
Exp. Cell Res. 288:110-118(2003).
[18]
INTERACTION WITH FLT4.
PubMed=16076871; DOI=10.1182/blood-2005-04-1388;
Salameh A., Galvagni F., Bardelli M., Bussolino F., Oliviero S.;
"Direct recruitment of CRK and GRB2 to VEGFR-3 induces proliferation,
migration, and survival of endothelial cells through the activation of
ERK, AKT, and JNK pathways.";
Blood 106:3423-3431(2005).
[19]
REVIEW ON ROLE IN KIT SIGNALING.
PubMed=16129412; DOI=10.1016/j.bbrc.2005.08.055;
Roskoski R. Jr.;
"Signaling by Kit protein-tyrosine kinase--the stem cell factor
receptor.";
Biochem. Biophys. Res. Commun. 337:1-13(2005).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-239, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[21]
INTERACTION WITH BCAR1; CDC42 AND TNK2.
PubMed=17038317; DOI=10.1074/jbc.M604342200;
Modzelewska K., Newman L.P., Desai R., Keely P.J.;
"Ack1 mediates Cdc42-dependent cell migration and signaling to
p130Cas.";
J. Biol. Chem. 281:37527-37535(2006).
[22]
INTERACTION WITH PDPK1.
PubMed=18024423; DOI=10.1074/jbc.M706361200;
Yang K.J., Shin S., Piao L., Shin E., Li Y., Park K.A., Byun H.S.,
Won M., Hong J., Kweon G.R., Hur G.M., Seok J.H., Chun T.,
Brazil D.P., Hemmings B.A., Park J.;
"Regulation of 3-phosphoinositide-dependent protein kinase-1 (PDK1) by
Src involves tyrosine phosphorylation of PDK1 and Src homology 2
domain binding.";
J. Biol. Chem. 283:1480-1491(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74 AND SER-83, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[24]
INTERACTION WITH FASLG.
PubMed=19807924; DOI=10.1186/1471-2172-10-53;
Voss M., Lettau M., Janssen O.;
"Identification of SH3 domain interaction partners of human FasL
(CD178) by phage display screening.";
BMC Immunol. 10:53-53(2009).
[25]
FUNCTION (ISOFORM CRK-II), INTERACTION WITH DOCK5, AND MUTAGENESIS OF
TRP-169.
PubMed=19004829; DOI=10.1074/jbc.M808010200;
Sanders M.A., Ampasala D., Basson M.D.;
"DOCK5 and DOCK1 regulate Caco-2 intestinal epithelial cell spreading
and migration on collagen IV.";
J. Biol. Chem. 284:27-35(2009).
[26]
IDENTIFICATION IN A COMPLEX WITH ABL1; ABL2 AND UNC119.
PubMed=19381274; DOI=10.1371/journal.pone.0005211;
Vepachedu R., Karim Z., Patel O., Goplen N., Alam R.;
"Unc119 protects from Shigella infection by inhibiting the Abl family
kinases.";
PLoS ONE 4:E5211-E5211(2009).
[27]
INTERACTION WITH PEAK1.
PubMed=20534451; DOI=10.1073/pnas.0914776107;
Wang Y., Kelber J.A., Tran Cao H.S., Cantin G.T., Lin R., Wang W.,
Kaushal S., Bristow J.M., Edgington T.S., Hoffman R.M., Bouvet M.,
Yates J.R. III, Klemke R.L.;
"Pseudopodium-enriched atypical kinase 1 regulates the cytoskeleton
and cancer progression.";
Proc. Natl. Acad. Sci. U.S.A. 107:10920-10925(2010).
[28]
ERRATUM.
Wang Y., Kelber J.A., Tran Cao H.S., Cantin G.T., Lin R., Wang W.,
Kaushal S., Bristow J.M., Edgington T.S., Hoffman R.M., Bouvet M.,
Yates J.R. III, Klemke R.L.;
Proc. Natl. Acad. Sci. U.S.A. 107:13556-13556(2010).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-74,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 (ISOFORM CRK-I), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[32]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[33]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; SER-41; TYR-108 AND
SER-125, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[36]
STRUCTURE BY NMR OF 12-120 IN COMPLEX WITH ABL1, AND INTERACTION OF
THE CRK SH2 DOMAIN WITH PHOSPHORYLATED TYR-221.
PubMed=12384576; DOI=10.1073/pnas.212518799;
Donaldson L.W., Gish G., Pawson T., Kay L.E., Forman-Kay J.D.;
"Structure of a regulatory complex involving the Abl SH3 domain, the
Crk SH2 domain, and a Crk-derived phosphopeptide.";
Proc. Natl. Acad. Sci. U.S.A. 99:14053-14058(2002).
[37]
STRUCTURE BY NMR (ISOFORMS CRK-I AND CRK-II), FUNCTION (ISOFORM
CRK-II), AND PHOSPHORYLATION AT TYR-221.
PubMed=17515907; DOI=10.1038/nsmb1241;
Kobashigawa Y., Sakai M., Naito M., Yokochi M., Kumeta H., Makino Y.,
Ogura K., Tanaka S., Inagaki F.;
"Structural basis for the transforming activity of human cancer-
related signaling adaptor protein CRK.";
Nat. Struct. Mol. Biol. 14:503-510(2007).
-!- FUNCTION: Isoform Crk-II: Regulates cell adhesion, spreading and
migration. Mediates attachment-induced MAPK8 activation, membrane
ruffling and cell motility in a Rac-dependent manner. Involved in
phagocytosis of apoptotic cells and cell motility via its
interaction with DOCK1 and DOCK4. May regulate the EFNA5-EPHA3
signaling. {ECO:0000269|PubMed:11870224,
ECO:0000269|PubMed:1630456, ECO:0000269|PubMed:17515907,
ECO:0000269|PubMed:19004829}.
-!- SUBUNIT: Interacts with ABL1, C3G, DOCK3, DOCK5, MAP4K1, MAPK8 and
SOS via its first SH3 domain. Interacts (via SH2 domain) with
BCAR1, CBL, CBLB, PXN, IRS4 and GAB1 upon stimulus-induced
tyrosine phosphorylation. Interacts (via SH2 domain) with several
tyrosine-phosphorylated growth factor receptors such as EGFR and
INSR. Interacts with FLT1 (tyrosine-phosphorylated). Interacts
with DOCK1 and DOCK4. Interacts with SHB. Interacts with PEAK1.
Interacts with FASLG. Isoform Crk-II interacts with KIT. Interacts
with EPHA3; upon activation of EPHA3 by the ligand EFNA5 and EPHA3
tyrosine kinase activity-dependent. Interacts with EPHA3
(phosphorylated); mediates EFNA5-EPHA3 signaling through RHOA
GTPase activation. Interacts with FLT4 (tyrosine-phosphorylated).
Isoform Crk-II (via SH2 domain) interacts with PDGFRA (tyrosine
phosphorylated) and PDGFRB (tyrosine phosphorylated). Part of a
collagen stimulated complex involved in cell migration composed of
CDC42, CRK, TNK2 and p130cas/BCAR1. Interacts (via SH2 domain)
with the 'Tyr-9' phosphorylated form of PDPK1. Interacts with
CBLC. Found in a complex with ABL1, ABL2, CRK and UNC119; leading
to the inhibition of CRK phosphorylation by ABL kinases.
{ECO:0000269|PubMed:10362357, ECO:0000269|PubMed:10733900,
ECO:0000269|PubMed:10964504, ECO:0000269|PubMed:11870224,
ECO:0000269|PubMed:12384576, ECO:0000269|PubMed:12628187,
ECO:0000269|PubMed:12878163, ECO:0000269|PubMed:16076871,
ECO:0000269|PubMed:17038317, ECO:0000269|PubMed:18024423,
ECO:0000269|PubMed:19381274, ECO:0000269|PubMed:19807924,
ECO:0000269|PubMed:20534451, ECO:0000269|PubMed:8657152,
ECO:0000269|PubMed:8662907, ECO:0000269|PubMed:9614078}.
-!- INTERACTION:
P00519:ABL1; NbExp=2; IntAct=EBI-886, EBI-375543;
P42684:ABL2; NbExp=5; IntAct=EBI-886, EBI-1102694;
O15085:ARHGEF11; NbExp=2; IntAct=EBI-886, EBI-311099;
Q9ULH1:ASAP1; NbExp=2; IntAct=EBI-886, EBI-346622;
Q96DX5:ASB9; NbExp=2; IntAct=EBI-886, EBI-745641;
P54253:ATXN1; NbExp=3; IntAct=EBI-886, EBI-930964;
P56945:BCAR1; NbExp=5; IntAct=EBI-886, EBI-702093;
P22681:CBL; NbExp=8; IntAct=EBI-886, EBI-518228;
Q13191:CBLB; NbExp=4; IntAct=EBI-886, EBI-744027;
P00533:EGFR; NbExp=3; IntAct=EBI-886, EBI-297353;
P21860:ERBB3; NbExp=2; IntAct=EBI-886, EBI-720706;
P11362:FGFR1; NbExp=2; IntAct=EBI-886, EBI-1028277;
P21333:FLNA; NbExp=3; IntAct=EBI-886, EBI-350432;
Q14315:FLNC; NbExp=2; IntAct=EBI-886, EBI-489954;
Q13480:GAB1; NbExp=2; IntAct=EBI-886, EBI-517684;
O14654:IRS4; NbExp=8; IntAct=EBI-886, EBI-356594;
P35968:KDR; NbExp=2; IntAct=EBI-886, EBI-1005487;
P10721:KIT; NbExp=4; IntAct=EBI-886, EBI-1379503;
Q92918:MAP4K1; NbExp=3; IntAct=EBI-886, EBI-881;
Q9Y4K4:MAP4K5; NbExp=5; IntAct=EBI-886, EBI-1279;
P45983:MAPK8; NbExp=2; IntAct=EBI-886, EBI-286483;
P20774:OGN; NbExp=2; IntAct=EBI-886, EBI-1753690;
O40931:ORF39 (xeno); NbExp=2; IntAct=EBI-886, EBI-2608673;
P16234:PDGFRA; NbExp=4; IntAct=EBI-886, EBI-2861522;
P27986:PIK3R1; NbExp=2; IntAct=EBI-886, EBI-79464;
Q92569:PIK3R3; NbExp=3; IntAct=EBI-886, EBI-79893;
P62333:PSMC6; NbExp=3; IntAct=EBI-886, EBI-357669;
Q05397:PTK2; NbExp=3; IntAct=EBI-886, EBI-702142;
P29074:PTPN4; NbExp=3; IntAct=EBI-886, EBI-710431;
Q13905:RAPGEF1; NbExp=3; IntAct=EBI-886, EBI-976876;
Q8TB24:RIN3; NbExp=2; IntAct=EBI-886, EBI-1570523;
Q8IYX7:SAXO1; NbExp=3; IntAct=EBI-886, EBI-3957636;
Q9UPX8:SHANK2; NbExp=2; IntAct=EBI-886, EBI-1570571;
P29353:SHC1; NbExp=3; IntAct=EBI-886, EBI-78835;
O60493:SNX3; NbExp=2; IntAct=EBI-886, EBI-727209;
Q07889:SOS1; NbExp=3; IntAct=EBI-886, EBI-297487;
Q07890:SOS2; NbExp=2; IntAct=EBI-886, EBI-298181;
Q9NYB0:TERF2IP; NbExp=2; IntAct=EBI-886, EBI-750109;
Q70EK8:USP53; NbExp=4; IntAct=EBI-886, EBI-742050;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
{ECO:0000250}. Note=Translocated to the plasma membrane upon cell
adhesion. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Crk-II;
IsoId=P46108-1; Sequence=Displayed;
Name=Crk-I;
IsoId=P46108-2; Sequence=VSP_041153, VSP_041154;
Note=Contains a phosphoserine at position 194.
{ECO:0000244|PubMed:20068231};
-!- DOMAIN: The C-terminal SH3 domain function as a negative modulator
for transformation and the N-terminal SH3 domain appears to
function as a positive regulator for transformation.
{ECO:0000250}.
-!- DOMAIN: The SH2 domain mediates interaction with tyrosine
phosphorylated proteins. Mediates interaction with SHB.
-!- PTM: Phosphorylation of Crk-II (40 kDa) gives rise to a 42 kDa
form. Isoform Crk-II is phosphorylated by KIT.
-!- PTM: Phosphorylated on Tyr-221 upon cell adhesion. Results in the
negative regulation of the association with SH2- and SH3-binding
partners, possibly by the formation of an intramolecular
interaction of phosphorylated Tyr-221 with the SH2 domain. This
leads finally to the down-regulation of the Crk signaling pathway.
{ECO:0000269|PubMed:17515907}.
-!- PTM: Proline isomerization at Pro-237 by PPIA acts as a switch
between two conformations: an autoinhibitory conformation in the
cis form, where the tandem SH3 domains interact intramolecularly,
and an activated conformation in the trans form. {ECO:0000250}.
-!- SIMILARITY: Belongs to the CRK family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CRKID40149ch17p13.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D10656; BAA01505.1; -; mRNA.
EMBL; S65701; AAB28213.1; -; Genomic_DNA.
EMBL; BT007277; AAP35941.1; -; mRNA.
EMBL; EU332838; ABY87527.1; -; Genomic_DNA.
EMBL; AK291060; BAF83749.1; -; mRNA.
EMBL; AC032044; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC100748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471108; EAW90621.1; -; Genomic_DNA.
EMBL; CH471108; EAW90624.1; -; Genomic_DNA.
EMBL; CH471108; EAW90625.1; -; Genomic_DNA.
EMBL; BC001718; AAH01718.1; -; mRNA.
EMBL; BC008506; AAH08506.1; -; mRNA.
EMBL; BC009837; AAH09837.1; -; mRNA.
CCDS; CCDS11002.1; -. [P46108-1]
CCDS; CCDS45561.1; -. [P46108-2]
PIR; A45022; A45022.
RefSeq; NP_005197.3; NM_005206.4. [P46108-2]
RefSeq; NP_058431.2; NM_016823.3. [P46108-1]
UniGene; Hs.461896; -.
PDB; 1JU5; NMR; -; A=12-120.
PDB; 2DVJ; NMR; -; A=1-228.
PDB; 2EYV; NMR; -; A=6-124.
PDB; 2EYW; NMR; -; A=125-198.
PDB; 2EYX; NMR; -; A=232-298.
PDB; 2EYY; NMR; -; A=1-204.
PDB; 2EYZ; NMR; -; A=1-304.
PDB; 2MS4; NMR; -; B=216-224.
PDBsum; 1JU5; -.
PDBsum; 2DVJ; -.
PDBsum; 2EYV; -.
PDBsum; 2EYW; -.
PDBsum; 2EYX; -.
PDBsum; 2EYY; -.
PDBsum; 2EYZ; -.
PDBsum; 2MS4; -.
DisProt; DP00748; -.
DisProt; DP00973; -.
ProteinModelPortal; P46108; -.
SMR; P46108; -.
BioGrid; 107788; 254.
DIP; DIP-199N; -.
IntAct; P46108; 274.
MINT; MINT-1208745; -.
STRING; 9606.ENSP00000300574; -.
ChEMBL; CHEMBL5005; -.
iPTMnet; P46108; -.
PhosphoSitePlus; P46108; -.
BioMuta; CRK; -.
DMDM; 158939322; -.
REPRODUCTION-2DPAGE; IPI00399054; -.
SWISS-2DPAGE; P46108; -.
EPD; P46108; -.
MaxQB; P46108; -.
PaxDb; P46108; -.
PeptideAtlas; P46108; -.
PRIDE; P46108; -.
TopDownProteomics; P46108-1; -. [P46108-1]
TopDownProteomics; P46108-2; -. [P46108-2]
DNASU; 1398; -.
Ensembl; ENST00000300574; ENSP00000300574; ENSG00000167193. [P46108-1]
Ensembl; ENST00000398970; ENSP00000381942; ENSG00000167193. [P46108-2]
GeneID; 1398; -.
KEGG; hsa:1398; -.
UCSC; uc002fsl.4; human. [P46108-1]
CTD; 1398; -.
DisGeNET; 1398; -.
GeneCards; CRK; -.
HGNC; HGNC:2362; CRK.
HPA; CAB010485; -.
HPA; HPA068087; -.
MIM; 164762; gene.
neXtProt; NX_P46108; -.
OpenTargets; ENSG00000167193; -.
PharmGKB; PA26880; -.
eggNOG; KOG4792; Eukaryota.
eggNOG; ENOG4110574; LUCA.
GeneTree; ENSGT00820000127055; -.
HOGENOM; HOG000236288; -.
HOVERGEN; HBG105616; -.
InParanoid; P46108; -.
KO; K04438; -.
OMA; GSWYWGR; -.
OrthoDB; EOG091G0JPQ; -.
PhylomeDB; P46108; -.
TreeFam; TF321436; -.
Reactome; R-HSA-170984; ARMS-mediated activation.
Reactome; R-HSA-186763; Downstream signal transduction.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
Reactome; R-HSA-8875555; MET activates RAP1 and RAC1.
Reactome; R-HSA-8875656; MET receptor recycling.
Reactome; R-HSA-912631; Regulation of signaling by CBL.
SignaLink; P46108; -.
SIGNOR; P46108; -.
ChiTaRS; CRK; human.
EvolutionaryTrace; P46108; -.
GeneWiki; CRK_(gene); -.
GenomeRNAi; 1398; -.
PRO; PR:P46108; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000167193; -.
CleanEx; HS_CRK; -.
ExpressionAtlas; P46108; baseline and differential.
Genevisible; P46108; HS.
GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IC:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0043234; C:protein complex; IPI:CAFA.
GO; GO:0008092; F:cytoskeletal protein binding; IEA:Ensembl.
GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB.
GO; GO:0005159; F:insulin-like growth factor receptor binding; IEA:Ensembl.
GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
GO; GO:0045309; F:protein phosphorylated amino acid binding; IDA:CAFA.
GO; GO:0043621; F:protein self-association; IDA:CAFA.
GO; GO:1990782; F:protein tyrosine kinase binding; IPI:CAFA.
GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
GO; GO:0042169; F:SH2 domain binding; IPI:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IPI:CAFA.
GO; GO:0005070; F:SH3/SH2 adaptor activity; IDA:CAFA.
GO; GO:0000186; P:activation of MAPKK activity; TAS:Reactome.
GO; GO:1990859; P:cellular response to endothelin; IEA:Ensembl.
GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IEA:Ensembl.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
GO; GO:0071732; P:cellular response to nitric oxide; IEA:Ensembl.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:UniProtKB.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:2000146; P:negative regulation of cell motility; IDA:CAFA.
GO; GO:0045953; P:negative regulation of natural killer cell mediated cytotoxicity; IEA:Ensembl.
GO; GO:0061045; P:negative regulation of wound healing; IDA:CAFA.
GO; GO:0030307; P:positive regulation of cell growth; IDA:CAFA.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IEA:Ensembl.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IDA:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IMP:CAFA.
GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
GO; GO:0043393; P:regulation of protein binding; IMP:CAFA.
GO; GO:0035020; P:regulation of Rac protein signal transduction; IEA:Ensembl.
GO; GO:0009966; P:regulation of signal transduction; IDA:CAFA.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0061847; P:response to cholecystokinin; IEA:Ensembl.
GO; GO:0035728; P:response to hepatocyte growth factor; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0001878; P:response to yeast; IEA:Ensembl.
GO; GO:0071538; P:SH2 domain-mediated complex assembly; IDA:CAFA.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
CDD; cd11759; SH3_CRK_C; 1.
CDD; cd11758; SH3_CRK_N; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR035458; CRK_SH3_C.
InterPro; IPR035457; CRK_SH3_N.
InterPro; IPR000980; SH2.
InterPro; IPR011511; SH3_2.
InterPro; IPR001452; SH3_domain.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
Pfam; PF07653; SH3_2; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 2.
SUPFAM; SSF50044; SSF50044; 3.
SUPFAM; SSF55550; SSF55550; 2.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell membrane;
Complete proteome; Cytoplasm; Membrane; Phosphoprotein;
Proto-oncogene; Reference proteome; Repeat; SH2 domain; SH3 domain.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 304 Adapter molecule crk.
/FTId=PRO_0000079351.
DOMAIN 13 118 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 132 192 SH3 1. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 237 296 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
SITE 237 237 Proline switch. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 40 40 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 41 41 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 74 74 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 83 83 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 108 108 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 125 125 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 221 221 Phosphotyrosine; by ABL1.
{ECO:0000269|PubMed:17515907}.
MOD_RES 239 239 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
VAR_SEQ 204 204 N -> R (in isoform Crk-I).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_041153.
VAR_SEQ 205 304 Missing (in isoform Crk-I).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_041154.
MUTAGEN 150 150 D->K: Abolishes interaction with DOCK1.
{ECO:0000269|PubMed:8662907}.
MUTAGEN 169 169 W->L: Abolishes interaction with DOCK5.
{ECO:0000269|PubMed:19004829}.
CONFLICT 109 109 L -> W (in Ref. 1; BAA01505 and 2;
AAB28213). {ECO:0000305}.
CONFLICT 215 215 G -> P (in Ref. 1; BAA01505 and 2;
AAB28213). {ECO:0000305}.
CONFLICT 278 278 E -> G (in Ref. 1; BAA01505 and 2;
AAB28213). {ECO:0000305}.
STRAND 7 13 {ECO:0000244|PDB:2DVJ}.
STRAND 14 16 {ECO:0000244|PDB:2EYY}.
HELIX 20 27 {ECO:0000244|PDB:1JU5}.
STRAND 30 33 {ECO:0000244|PDB:2DVJ}.
STRAND 34 39 {ECO:0000244|PDB:1JU5}.
STRAND 41 43 {ECO:0000244|PDB:1JU5}.
STRAND 46 52 {ECO:0000244|PDB:1JU5}.
STRAND 54 56 {ECO:0000244|PDB:2DVJ}.
STRAND 57 63 {ECO:0000244|PDB:1JU5}.
STRAND 66 69 {ECO:0000244|PDB:1JU5}.
STRAND 70 77 {ECO:0000244|PDB:2DVJ}.
TURN 78 80 {ECO:0000244|PDB:2DVJ}.
STRAND 87 89 {ECO:0000244|PDB:1JU5}.
STRAND 92 96 {ECO:0000244|PDB:1JU5}.
HELIX 97 106 {ECO:0000244|PDB:1JU5}.
STRAND 109 112 {ECO:0000244|PDB:1JU5}.
STRAND 116 118 {ECO:0000244|PDB:1JU5}.
STRAND 120 123 {ECO:0000244|PDB:2EYV}.
HELIX 126 128 {ECO:0000244|PDB:2EYY}.
STRAND 135 138 {ECO:0000244|PDB:2EYY}.
STRAND 146 150 {ECO:0000244|PDB:2DVJ}.
STRAND 158 166 {ECO:0000244|PDB:2EYY}.
STRAND 167 173 {ECO:0000244|PDB:2DVJ}.
STRAND 179 183 {ECO:0000244|PDB:2DVJ}.
HELIX 184 186 {ECO:0000244|PDB:2DVJ}.
STRAND 187 189 {ECO:0000244|PDB:2EYW}.
STRAND 208 210 {ECO:0000244|PDB:2DVJ}.
STRAND 224 227 {ECO:0000244|PDB:2EYZ}.
STRAND 229 231 {ECO:0000244|PDB:2EYZ}.
STRAND 239 242 {ECO:0000244|PDB:2EYX}.
STRAND 253 255 {ECO:0000244|PDB:2EYX}.
STRAND 260 269 {ECO:0000244|PDB:2EYX}.
STRAND 273 279 {ECO:0000244|PDB:2EYX}.
STRAND 282 287 {ECO:0000244|PDB:2EYX}.
HELIX 288 290 {ECO:0000244|PDB:2EYX}.
SEQUENCE 304 AA; 33831 MW; 4CFBFB65BFC2E265 CRC64;
MAGNFDSEER SSWYWGRLSR QEAVALLQGQ RHGVFLVRDS STSPGDYVLS VSENSRVSHY
IINSSGPRPP VPPSPAQPPP GVSPSRLRIG DQEFDSLPAL LEFYKIHYLD TTTLIEPVSR
SRQGSGVILR QEEAEYVRAL FDFNGNDEED LPFKKGDILR IRDKPEEQWW NAEDSEGKRG
MIPVPYVEKY RPASASVSAL IGGNQEGSHP QPLGGPEPGP YAQPSVNTPL PNLQNGPIYA
RVIQKRVPNA YDKTALALEV GELVKVTKIN VSGQWEGECN GKRGHFPFTH VRLLDQQNPD
EDFS


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