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Focal adhesion kinase 1 (FADK 1) (EC 2.7.10.2) (Focal adhesion kinase-related nonkinase) (FRNK) (Protein phosphatase 1 regulatory subunit 71) (PPP1R71) (Protein-tyrosine kinase 2) (p125FAK) (pp125FAK)

 FAK1_HUMAN              Reviewed;        1052 AA.
Q05397; B4E2N6; F5H4S4; J3QT16; Q14291; Q8IYN9; Q9UD85;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
07-APR-2021, entry version 244.
RecName: Full=Focal adhesion kinase 1 {ECO:0000305};
Short=FADK 1;
EC=2.7.10.2;
AltName: Full=Focal adhesion kinase-related nonkinase;
Short=FRNK;
AltName: Full=Protein phosphatase 1 regulatory subunit 71;
Short=PPP1R71;
AltName: Full=Protein-tyrosine kinase 2;
AltName: Full=p125FAK;
AltName: Full=pp125FAK;
Name=PTK2 {ECO:0000312|HGNC:HGNC:9611}; Synonyms=FAK, FAK1;
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 1), AND TISSUE SPECIFICITY.
TISSUE=T-cell;
PubMed=7692878; DOI=10.1089/dna.1993.12.823;
Whitney G.S., Chan P.Y., Blake J., Cosand W.L., Neubauer M.G., Aruffo A.,
Kanner S.B.;
"Human T and B lymphocytes express a structurally conserved focal adhesion
kinase, pp125FAK.";
DNA Cell Biol. 12:823-830(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=8422239; DOI=10.1006/bbrc.1993.1022;
Andre E., Becker-Andre M.;
"Expression of an N-terminally truncated form of human focal adhesion
kinase in brain.";
Biochem. Biophys. Res. Commun. 190:140-147(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Trachea;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
Platzer M., Shimizu N., Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
TISSUE=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).
[6]
PROTEIN SEQUENCE OF 2-19; 192-199; 222-236; 243-252; 350-364; 414-419;
468-476; 562-569; 674-690; 798-811; 832-838; 904-933; 963-981; 989-1000 AND
1003-1042, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Osteosarcoma;
Bienvenut W.V., Glen H., Brunton V.G., Frame M.C.;
Submitted (JUL-2007) to UniProtKB.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 552-602, AND TISSUE SPECIFICITY.
TISSUE=Melanocyte;
PubMed=8247543;
Lee S.-T., Strunk K.M., Spritz R.A.;
"A survey of protein tyrosine kinase mRNAs expressed in normal human
melanocytes.";
Oncogene 8:3403-3410(1993).
[8]
INTERACTION WITH TGFB1I1.
PubMed=9422762; DOI=10.1074/jbc.273.2.1003;
Matsuya M., Sasaki H., Aoto H., Mitaka T., Nagura K., Ohba T., Ishino M.,
Takahashi S., Suzuki R., Sasaki T.;
"Cell adhesion kinase beta forms a complex with a new member, Hic-5, of
proteins localized at focal adhesions.";
J. Biol. Chem. 273:1003-1014(1998).
[9]
INTERACTION WITH TGFB1I1, AND MUTAGENESIS OF VAL-928 AND LEU-1034.
PubMed=9756887; DOI=10.1074/jbc.273.41.26516;
Fujita H., Kamiguchi K., Cho D., Shibanuma M., Morimoto C., Tachibana K.;
"Interaction of Hic-5, A senescence-related protein, with focal adhesion
kinase.";
J. Biol. Chem. 273:26516-26521(1998).
[10]
FUNCTION IN PXN PHOSPHORYLATION; REGULATION OF CELL SHAPE AND MIGRATION,
INTERACTION WITH EPHA2, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, ACTIVITY
REGULATION, DEPHOSPHORYLATION BY PTPN11, AND SUBCELLULAR LOCATION.
PubMed=10655584; DOI=10.1038/35000008;
Miao H., Burnett E., Kinch M., Simon E., Wang B.;
"Activation of EphA2 kinase suppresses integrin function and causes focal-
adhesion-kinase dephosphorylation.";
Nat. Cell Biol. 2:62-69(2000).
[11]
FUNCTION IN CELL MIGRATION AND ACTIVATION OF BMX, CATALYTIC ACTIVITY,
AUTOPHOSPHORYLATION, MUTAGENESIS OF TYR-397, AND INTERACTION WITH BMX.
PubMed=11331870; DOI=10.1038/35074500;
Chen R., Kim O., Li M., Xiong X., Guan J.L., Kung H.J., Chen H.,
Shimizu Y., Qiu Y.;
"Regulation of the PH-domain-containing tyrosine kinase Etk by focal
adhesion kinase through the FERM domain.";
Nat. Cell Biol. 3:439-444(2001).
[12]
FUNCTION IN PHOSPHORYLATION OF SHC1, AUTOPHOSPHORYLATION, INTERACTION WITH
SHC1 AND SRC, AND ROLE IN DISEASE.
PubMed=11980671;
Hecker T.P., Grammer J.R., Gillespie G.Y., Stewart J. Jr., Gladson C.L.;
"Focal adhesion kinase enhances signaling through the Shc/extracellular
signal-regulated kinase pathway in anaplastic astrocytoma tumor biopsy
samples.";
Cancer Res. 62:2699-2707(2002).
[13]
INTERACTION WITH RB1CC1.
PubMed=12221124; DOI=10.1091/mbc.e02-05-0295;
Abbi S., Ueda H., Zheng C., Cooper L.A., Zhao J., Christopher R.,
Guan J.L.;
"Regulation of focal adhesion kinase by a novel protein inhibitor FIP200.";
Mol. Biol. Cell 13:3178-3191(2002).
[14]
PHOSPHORYLATION AT TYR-397; TYR-407; TYR-577; TYR-861 AND TYR-925, AND
INTERACTION WITH FGR.
PubMed=12387730; DOI=10.1042/bj20020410;
Relou I.A.M., Bax L.A.B., Van Rijn H.J.M., Akkerman J.-W.N.;
"Site-specific phosphorylation of platelet focal adhesion kinase by low-
density lipoprotein.";
Biochem. J. 369:407-416(2003).
[15]
FUNCTION IN INTEGRIN SIGNALING; REGULATION OF APOPTOSIS; REGULATION OF CELL
SHAPE AND ACTIVATION OF PHOSPHATIDYLINOSITOL KINASE AND AKT1 SIGNALING
PATHWAY.
PubMed=15166238; DOI=10.1074/jbc.m313265200;
Xia H., Nho R.S., Kahm J., Kleidon J., Henke C.A.;
"Focal adhesion kinase is upstream of phosphatidylinositol 3-kinase/Akt in
regulating fibroblast survival in response to contraction of type I
collagen matrices via a beta 1 integrin viability signaling pathway.";
J. Biol. Chem. 279:33024-33034(2004).
[16]
FUNCTION IN REGULATION OF CELL MIGRATION, AND PHOSPHORYLATION AT TYR-407;
TYR-397 AND TYR-576.
PubMed=15561106; DOI=10.1016/j.yexcr.2004.09.005;
Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L.,
Lowell C.A., Berton G.;
"The proto-oncogene Fgr regulates cell migration and this requires its
plasma membrane localization.";
Exp. Cell Res. 302:253-269(2005).
[17]
INTERACTION WITH P53/TP53, AND SUBCELLULAR LOCATION.
PubMed=15855171; DOI=10.1074/jbc.m414172200;
Golubovskaya V.M., Finch R., Cance W.G.;
"Direct interaction of the N-terminal domain of focal adhesion kinase with
the N-terminal transactivation domain of p53.";
J. Biol. Chem. 280:25008-25021(2005).
[18]
FUNCTION IN FOCAL ADHESION DISASSEMBLY.
PubMed=15895076; DOI=10.1038/ncb1262;
Ezratty E.J., Partridge M.A., Gundersen G.G.;
"Microtubule-induced focal adhesion disassembly is mediated by dynamin and
focal adhesion kinase.";
Nat. Cell Biol. 7:581-590(2005).
[19]
INTERACTION WITH FLT4.
PubMed=16452200; DOI=10.1158/0008-5472.can-05-1661;
Garces C.A., Kurenova E.V., Golubovskaya V.M., Cance W.G.;
"Vascular endothelial growth factor receptor-3 and focal adhesion kinase
bind and suppress apoptosis in breast cancer cells.";
Cancer Res. 66:1446-1454(2006).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling
networks.";
Cell 127:635-648(2006).
[21]
ALTERNATIVE PROMOTER USAGE, IDENTIFICATION OF ISOFORM 6, AND DEVELOPMENTAL
STAGE (ISOFORM 6).
PubMed=16998626; DOI=10.1007/s00795-006-0325-8;
Nagoshi Y., Yamamoto G., Irie T., Tachikawa T.;
"Expression of FAK-related non-kinase (FRNK) coincides with morphological
change in the early stage of cell adhesion.";
Med. Mol. Morphol. 39:154-160(2006).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation
analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[23]
ACTIVITY REGULATION, ROLE IN DISEASE, AND PHOSPHORYLATION AT TYR-397 AND
TYR-861.
PubMed=18006843; DOI=10.1158/0008-5472.can-07-2667;
Halder J., Lin Y.G., Merritt W.M., Spannuth W.A., Nick A.M., Honda T.,
Kamat A.A., Han L.Y., Kim T.J., Lu C., Tari A.M., Bornmann W.,
Fernandez A., Lopez-Berestein G., Sood A.K.;
"Therapeutic efficacy of a novel focal adhesion kinase inhibitor TAE226 in
ovarian carcinoma.";
Cancer Res. 67:10976-10983(2007).
[24]
FUNCTION, ACTIVITY REGULATION, ROLE IN DISEASE, AND PHOSPHORYLATION AT
TYR-397.
PubMed=17395594; DOI=10.1074/jbc.m606695200;
Slack-Davis J.K., Martin K.H., Tilghman R.W., Iwanicki M., Ung E.J.,
Autry C., Luzzio M.J., Cooper B., Kath J.C., Roberts W.G., Parsons J.T.;
"Cellular characterization of a novel focal adhesion kinase inhibitor.";
J. Biol. Chem. 282:14845-14852(2007).
[25]
FUNCTION IN OSTEOBLAST DIFFERENTIATION.
PubMed=16927379; DOI=10.1002/jcb.21074;
Salasznyk R.M., Klees R.F., Boskey A., Plopper G.E.;
"Activation of FAK is necessary for the osteogenic differentiation of human
mesenchymal stem cells on laminin-5.";
J. Cell. Biochem. 100:499-514(2007).
[26]
FUNCTION, ACTIVITY REGULATION, ROLE IN DISEASE, AND PHOSPHORYLATION AT
TYR-397.
PubMed=17431114; DOI=10.1158/1535-7163.mct-06-0476;
Liu T.J., LaFortune T., Honda T., Ohmori O., Hatakeyama S., Meyer T.,
Jackson D., de Groot J., Yung W.K.;
"Inhibition of both focal adhesion kinase and insulin-like growth factor-I
receptor kinase suppresses glioma proliferation in vitro and in vivo.";
Mol. Cancer Ther. 6:1357-1367(2007).
[27]
FUNCTION, AND INTERACTION WITH LPXN.
PubMed=18497331; DOI=10.1161/circresaha.107.170357;
Sundberg-Smith L.J., DiMichele L.A., Sayers R.L., Mack C.P., Taylor J.M.;
"The LIM protein leupaxin is enriched in smooth muscle and functions as an
serum response factor cofactor to induce smooth muscle cell gene
transcription.";
Circ. Res. 102:1502-1511(2008).
[28]
FUNCTION, AND INTERACTION WITH BMX.
PubMed=18292575; DOI=10.4049/jimmunol.180.5.3485;
Semaan N., Alsaleh G., Gottenberg J.E., Wachsmann D., Sibilia J.;
"Etk/BMX, a Btk family tyrosine kinase, and Mal contribute to the cross-
talk between MyD88 and FAK pathways.";
J. Immunol. 180:3485-3491(2008).
[29]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CASS4.
PubMed=18256281; DOI=10.1091/mbc.e07-09-0953;
Singh M.K., Dadke D., Nicolas E., Serebriiskii I.G., Apostolou S.,
Canutescu A., Egleston B.L., Golemis E.A.;
"A novel Cas family member, HEPL, regulates FAK and cell spreading.";
Mol. Biol. Cell 19:1627-1636(2008).
[30]
FUNCTION IN REGULATION OF P53/TP53 LEVELS; CELL PROLIFERATION AND CELL
SURVIVAL, AND SUBCELLULAR LOCATION.
PubMed=18206965; DOI=10.1016/j.molcel.2007.11.031;
Lim S.T., Chen X.L., Lim Y., Hanson D.A., Vo T.T., Howerton K.,
Larocque N., Fisher S.J., Schlaepfer D.D., Ilic D.;
"Nuclear FAK promotes cell proliferation and survival through FERM-enhanced
p53 degradation.";
Mol. Cell 29:9-22(2008).
[31]
INTERACTION WITH ESR1; PIK3R1 AND/OR PIK3R2 AND SRC.
PubMed=18657504; DOI=10.1016/j.molcel.2008.05.025;
Le Romancer M., Treilleux I., Leconte N., Robin-Lespinasse Y., Sentis S.,
Bouchekioua-Bouzaghou K., Goddard S., Gobert-Gosse S., Corbo L.;
"Regulation of estrogen rapid signaling through arginine methylation by
PRMT1.";
Mol. Cell 31:212-221(2008).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; SER-29; SER-887 AND
SER-910, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the
kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910, 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).
[34]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[35]
PHOSPHORYLATION AT TYR-397; TYR-576; TYR-577; SER-722; TYR-861 AND TYR-925,
AND IDENTIFICATION IN A COMPLEX WITH CTTN AND FER.
PubMed=19339212; DOI=10.1016/j.bbamcr.2009.01.015;
Oh M.A., Choi S., Lee M.J., Choi M.C., Lee S.A., Ko W., Cance W.G.,
Oh E.S., Buday L., Kim S.H., Lee J.W.;
"Specific tyrosine phosphorylation of focal adhesion kinase mediated by Fer
tyrosine kinase in suspended hepatocytes.";
Biochim. Biophys. Acta 1793:781-791(2009).
[36]
FUNCTION IN SRC-MEDIATED PHOSPHORYLATION OF PXN.
PubMed=19138410; DOI=10.1186/1471-2407-9-12;
Sachdev S., Bu Y., Gelman I.H.;
"Paxillin-Y118 phosphorylation contributes to the control of Src-induced
anchorage-independent growth by FAK and adhesion.";
BMC Cancer 9:12-12(2009).
[37]
INTERACTION WITH STEAP4.
PubMed=19787193; DOI=10.3892/ijmm_00000270;
Tamura T., Chiba J.;
"STEAP4 regulates focal adhesion kinase activation and CpG motifs within
STEAP4 promoter region are frequently methylated in DU145, human androgen-
independent prostate cancer cells.";
Int. J. Mol. Med. 24:599-604(2009).
[38]
INTERACTION WITH EMP2.
PubMed=19494199; DOI=10.1167/iovs.08-3315;
Morales S.A., Mareninov S., Coulam P., Wadehra M., Goodglick L., Braun J.,
Gordon L.K.;
"Functional consequences of interactions between FAK and epithelial
membrane protein 2 (EMP2).";
Invest. Ophthalmol. Vis. Sci. 50:4949-4956(2009).
[39]
FUNCTION IN SRC-MEDIATED PHOSPHORYLATION OF BCAR1, AND ROLE IN DISEASE.
PubMed=19147981; DOI=10.1172/jci37160;
Pylayeva Y., Gillen K.M., Gerald W., Beggs H.E., Reichardt L.F.,
Giancotti F.G.;
"Ras- and PI3K-dependent breast tumorigenesis in mice and humans requires
focal adhesion kinase signaling.";
J. Clin. Invest. 119:252-266(2009).
[40]
INTERACTION WITH EPHA1.
PubMed=19118217; DOI=10.1242/jcs.036467;
Yamazaki T., Masuda J., Omori T., Usui R., Akiyama H., Maru Y.;
"EphA1 interacts with integrin-linked kinase and regulates cell morphology
and motility.";
J. Cell Sci. 122:243-255(2009).
[41]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT TYR-5; THR-13; SER-29; TYR-397; TYR-570; SER-580 AND SER-910,
CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[42]
ROLE IN DISEASE, AND ACTIVITY REGULATION.
PubMed=20495381; DOI=10.4161/cbt.10.1.11993;
Sun H., Pisle S., Gardner E.R., Figg W.D.;
"Bioluminescent imaging study: FAK inhibitor, PF-562,271, preclinical study
in PC3M-luc-C6 local implant and metastasis xenograft models.";
Cancer Biol. Ther. 10:38-43(2010).
[43]
INTERACTION WITH LPXN.
PubMed=19917054; DOI=10.1111/j.1349-7006.2009.01398.x;
Tanaka T., Moriwaki K., Murata S., Miyasaka M.;
"LIM domain-containing adaptor, leupaxin, localizes in focal adhesion and
suppresses the integrin-induced tyrosine phosphorylation of paxillin.";
Cancer Sci. 101:363-368(2010).
[44]
FUNCTION (ISOFORM 6), AND TISSUE SPECIFICITY.
PubMed=20109444; DOI=10.1016/j.yexcr.2010.01.021;
Cai G.Q., Zheng A., Tang Q., White E.S., Chou C.F., Gladson C.L.,
Olman M.A., Ding Q.;
"Downregulation of FAK-related non-kinase mediates the migratory phenotype
of human fibrotic lung fibroblasts.";
Exp. Cell Res. 316:1600-1609(2010).
[45]
INTERACTION WITH ZFYVE21, AND DEPHOSPHORYLATION AT TYR-397.
PubMed=20439989; DOI=10.1074/jbc.m110.106443;
Nagano M., Hoshino D., Sakamoto T., Kawasaki N., Koshikawa N., Seiki M.;
"ZF21 protein regulates cell adhesion and motility.";
J. Biol. Chem. 285:21013-21022(2010).
[46]
INTERACTION WITH CD36.
PubMed=20037584; DOI=10.1038/ni.1836;
Stewart C.R., Stuart L.M., Wilkinson K., van Gils J.M., Deng J., Halle A.,
Rayner K.J., Boyer L., Zhong R., Frazier W.A., Lacy-Hulbert A.,
El Khoury J., Golenbock D.T., Moore K.J.;
"CD36 ligands promote sterile inflammation through assembly of a Toll-like
receptor 4 and 6 heterodimer.";
Nat. Immunol. 11:155-161(2010).
[47]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910 AND THR-914, 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).
[48]
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).
[49]
INTERACTION WITH RET, FUNCTION IN RET PHOSPHORYLATION, AND PHOSPHORYLATION
AT TYR-576 AND TYR-577.
PubMed=21454698; DOI=10.1074/jbc.m110.168500;
Plaza-Menacho I., Morandi A., Mologni L., Boender P.,
Gambacorti-Passerini C., Magee A.I., Hofstra R.M.W., Knowles P.,
McDonald N.Q., Isacke C.M.;
"Focal adhesion kinase (FAK) binds RET kinase via its FERM domain, priming
a direct and reciprocal RET-FAK transactivation mechanism.";
J. Biol. Chem. 286:17292-17302(2011).
[50]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; SER-29; SER-843 AND
SER-910, 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).
[51]
INTERACTION WITH CIB1 ISOFORM 2.
TISSUE=Brain;
PubMed=23503467; DOI=10.1038/onc.2013.43;
Armacki M., Joodi G., Nimmagadda S.C., de Kimpe L., Pusapati G.V.,
Vandoninck S., Van Lint J., Illing A., Seufferlein T.;
"A novel splice variant of calcium and integrin-binding protein 1 mediates
protein kinase D2-stimulated tumour growth by regulating angiogenesis.";
Oncogene 33:1167-1180(2014).
[52]
REVIEW ON SIGNALING AND ON DIRECT PTK2/FAK1 SUBSTRATES.
PubMed=10354709; DOI=10.1016/s0079-6107(98)00052-2;
Schlaepfer D.D., Hauck C.R., Sieg D.J.;
"Signaling through focal adhesion kinase.";
Prog. Biophys. Mol. Biol. 71:435-478(1999).
[53]
REVIEW ON FUNCTION IN NETRIN SIGNALING.
PubMed=15725728;
Nikolopoulos S.N., Giancotti F.G.;
"Netrin-integrin signaling in epithelial morphogenesis, axon guidance and
vascular patterning.";
Cell Cycle 4:E131-E135(2005).
[54]
REVIEW ON FUNCTION IN CELL MIGRATION; FOCAL ADHESION TURNOVER AND
ACTIVATION OF SIGNALING PATHWAYS, AND ROLE IN DISEASE.
PubMed=16919435; DOI=10.1016/j.ceb.2006.08.011;
Mitra S.K., Schlaepfer D.D.;
"Integrin-regulated FAK-Src signaling in normal and cancer cells.";
Curr. Opin. Cell Biol. 18:516-523(2006).
[55]
FUNCTION.
PubMed=17968709; DOI=10.1080/15216540701694245;
Vadali K., Cai X., Schaller M.D.;
"Focal adhesion kinase: an essential kinase in the regulation of
cardiovascular functions.";
IUBMB Life 59:709-716(2007).
[56]
REVIEW ON ROLE IN INTEGRIN SIGNALING AND IN REGULATION OF P53/TP53
ACTIVITIES, ROLE IN DISEASE, AND ACTIVITY REGULATION.
PubMed=18677107; DOI=10.4161/cc.6367;
Lim S.T., Mikolon D., Stupack D.G., Schlaepfer D.D.;
"FERM control of FAK function: implications for cancer therapy.";
Cell Cycle 7:2306-2314(2008).
[57]
REVIEW ON FUNCTION IN REGULATION OF RHO FAMILY GTPASE ACTIVITY.
PubMed=19525103; DOI=10.1016/j.ceb.2009.05.006;
Tomar A., Schlaepfer D.D.;
"Focal adhesion kinase: switching between GAPs and GEFs in the regulation
of cell motility.";
Curr. Opin. Cell Biol. 21:676-683(2009).
[58]
REVIEW ON EXPRESSION IN CANCER, AND ROLE IN DISEASE.
PubMed=19224453; DOI=10.14670/hh-24.503;
Golubovskaya V.M., Kweh F.A., Cance W.G.;
"Focal adhesion kinase and cancer.";
Histol. Histopathol. 24:503-510(2009).
[59]
REVIEW ON FUNCTION IN REGULATION OF P53/TP53.
PubMed=20515733; DOI=10.2741/3653;
Golubovskaya V.M., Cance W.;
"Focal adhesion kinase and p53 signal transduction pathways in cancer.";
Front. Biosci. 15:901-912(2010).
[60]
REVIEW ON ROLE IN DEVELOPMENT.
PubMed=20552554; DOI=10.14670/hh-25.1039;
Chatzizacharias N.A., Kouraklis G.P., Theocharis S.E.;
"The role of focal adhesion kinase in early development.";
Histol. Histopathol. 25:1039-1055(2010).
[61]
REVIEW ON FUNCTION IN INTEGRIN SIGNALING AND ACTIVATION OF DOWNSTREAM
SIGNALING PATHWAYS.
PubMed=20101634; DOI=10.1002/iub.303;
Guan J.L.;
"Integrin signaling through FAK in the regulation of mammary stem cells and
breast cancer.";
IUBMB Life 62:268-276(2010).
[62]
FUNCTION, AND SIGNALING.
PubMed=20332118; DOI=10.1242/jcs.045112;
Schaller M.D.;
"Cellular functions of FAK kinases: insight into molecular mechanisms and
novel functions.";
J. Cell Sci. 123:1007-1013(2010).
[63]
REVIEW ON FUNCTION; SUBUNIT; PHOSPHORYLATION; ACTIVITY REGULATION AND ROLE
IN DISEASE.
PubMed=21482413; DOI=10.1016/b978-0-12-386041-5.00005-4;
Hall J.E., Fu W., Schaller M.D.;
"Focal adhesion kinase: exploring Fak structure to gain insight into
function.";
Int. Rev. Cell Mol. Biol. 288:185-225(2011).
[64]
INTERACTION WITH MISP.
PubMed=23509069; DOI=10.1083/jcb.201207050;
Zhu M., Settele F., Kotak S., Sanchez-Pulido L., Ehret L., Ponting C.P.,
Goenczy P., Hoffmann I.;
"MISP is a novel Plk1 substrate required for proper spindle orientation and
mitotic progression.";
J. Cell Biol. 200:773-787(2013).
[65]
SUBUNIT.
PubMed=29069646; DOI=10.1159/000484298;
Rui Y.N., Xu Z., Fang X., Menezes M.R., Balzeau J., Niu A., Hagan J.P.,
Kim D.H.;
"The Intracranial Aneurysm Gene THSD1 Connects Endosome Dynamics to Nascent
Focal Adhesion Assembly.";
Cell. Physiol. Biochem. 43:2200-2211(2017).
[66]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=31630787; DOI=10.1016/j.ajhg.2019.09.022;
Wallmeier J., Frank D., Shoemark A., Noethe-Menchen T., Cindric S.,
Olbrich H., Loges N.T., Aprea I., Dougherty G.W., Pennekamp P., Kaiser T.,
Mitchison H.M., Hogg C., Carr S.B., Zariwala M.A., Ferkol T., Leigh M.W.,
Davis S.D., Atkinson J., Dutcher S.K., Knowles M.R., Thiele H.,
Altmueller J., Krenz H., Woeste M., Brentrup A., Ahrens F., Vogelberg C.,
Morris-Rosendahl D.J., Omran H.;
"De Novo Mutations in FOXJ1 Result in a Motile Ciliopathy with
Hydrocephalus and Randomization of Left/Right Body Asymmetry.";
Am. J. Hum. Genet. 105:1030-1039(2019).
[67]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 891-1052, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=12005431; DOI=10.1016/s0969-2126(02)00717-7;
Arold S.T., Hoellerer M.K., Noble M.E.;
"The structural basis of localization and signaling by the focal adhesion
targeting domain.";
Structure 10:319-327(2002).
[68]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 411-686 IN COMPLEX WITH ATP.
PubMed=12467573; DOI=10.1016/s0969-2126(02)00907-3;
Nowakowski J., Cronin C.N., McRee D.E., Knuth M.W., Nelson C.G.,
Pavletich N.P., Rogers J., Sang B.C., Scheibe D.N., Swanson R.V.,
Thompson D.A.;
"Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases
from nanovolume crystallography.";
Structure 10:1659-1667(2002).
[69]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 892-1052 IN COMPLEX WITH PXN, AND
INTERACTION WITH PXN.
PubMed=14527389; DOI=10.1016/j.str.2003.08.010;
Hoellerer M.K., Noble M.E., Labesse G., Campbell I.D., Werner J.M.,
Arold S.T.;
"Molecular recognition of paxillin LD motifs by the focal adhesion
targeting domain.";
Structure 11:1207-1217(2003).
[70]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 414-689 IN COMPLEX WITH
INHIBITOR, CATALYTIC ACTIVITY, AND AUTOPHOSPHORYLATION.
PubMed=18339875; DOI=10.1158/0008-5472.can-07-5155;
Roberts W.G., Ung E., Whalen P., Cooper B., Hulford C., Autry C.,
Richter D., Emerson E., Lin J., Kath J., Coleman K., Yao L.,
Martinez-Alsina L., Lorenzen M., Berliner M., Luzzio M., Patel N.,
Schmitt E., LaGreca S., Jani J., Wessel M., Marr E., Griffor M., Vajdos F.;
"Antitumor activity and pharmacology of a selective focal adhesion kinase
inhibitor, PF-562,271.";
Cancer Res. 68:1935-1944(2008).
[71]
X-RAY CRYSTALLOGRAPHY (2.82 ANGSTROMS) OF 891-1052 IN COMPLEX WITH CD4,
SUBCELLULAR LOCATION, AND INTERACTION WITH CD4.
PubMed=18078954; DOI=10.1016/j.jmb.2007.11.040;
Garron M.L., Arthos J., Guichou J.F., McNally J., Cicala C., Arold S.T.;
"Structural basis for the interaction between focal adhesion kinase and
CD4.";
J. Mol. Biol. 375:1320-1328(2008).
[72]
VARIANTS [LARGE SCALE ANALYSIS] PRO-292; GLN-292; ALA-793; GLU-1030 AND
GLU-1044.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Non-receptor protein-tyrosine kinase that plays an essential
role in regulating cell migration, adhesion, spreading, reorganization
of the actin cytoskeleton, formation and disassembly of focal adhesions
and cell protrusions, cell cycle progression, cell proliferation and
apoptosis. Required for early embryonic development and placenta
development. Required for embryonic angiogenesis, normal cardiomyocyte
migration and proliferation, and normal heart development. Regulates
axon growth and neuronal cell migration, axon branching and synapse
formation; required for normal development of the nervous system. Plays
a role in osteogenesis and differentiation of osteoblasts. Functions in
integrin signal transduction, but also in signaling downstream of
numerous growth factor receptors, G-protein coupled receptors (GPCR),
EPHA2, netrin receptors and LDL receptors. Forms multisubunit signaling
complexes with SRC and SRC family members upon activation; this leads
to the phosphorylation of additional tyrosine residues, creating
binding sites for scaffold proteins, effectors and substrates.
Regulates numerous signaling pathways. Promotes activation of
phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes
activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling
cascade. Promotes localized and transient activation of guanine
nucleotide exchange factors (GEFs) and GTPase-activating proteins
(GAPs), and thereby modulates the activity of Rho family GTPases.
Signaling via CAS family members mediates activation of RAC1. Recruits
the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby
regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal
degradation. Phosphorylates SRC; this increases SRC kinase activity.
Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes
phosphorylation of PXN and STAT1; most likely PXN and STAT1 are
phosphorylated by a SRC family kinase that is recruited to
autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes
phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and
PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. Isoform 6 (FRNK)
does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation
and signaling. Its enhanced expression can attenuate the nuclear
accumulation of LPXN and limit its ability to enhance serum response
factor (SRF)-dependent gene transcription.
{ECO:0000269|PubMed:10655584, ECO:0000269|PubMed:11331870,
ECO:0000269|PubMed:11980671, ECO:0000269|PubMed:15166238,
ECO:0000269|PubMed:15561106, ECO:0000269|PubMed:15895076,
ECO:0000269|PubMed:16919435, ECO:0000269|PubMed:16927379,
ECO:0000269|PubMed:17395594, ECO:0000269|PubMed:17431114,
ECO:0000269|PubMed:17968709, ECO:0000269|PubMed:18006843,
ECO:0000269|PubMed:18206965, ECO:0000269|PubMed:18256281,
ECO:0000269|PubMed:18292575, ECO:0000269|PubMed:18497331,
ECO:0000269|PubMed:18677107, ECO:0000269|PubMed:19138410,
ECO:0000269|PubMed:19147981, ECO:0000269|PubMed:19224453,
ECO:0000269|PubMed:20332118, ECO:0000269|PubMed:20495381,
ECO:0000269|PubMed:21454698}.
-!- FUNCTION: [Isoform 6]: Isoform 6 (FRNK) does not contain a kinase
domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its
enhanced expression can attenuate the nuclear accumulation of LPXN and
limit its ability to enhance serum response factor (SRF)-dependent gene
transcription. {ECO:0000269|PubMed:20109444}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
Evidence={ECO:0000255|PROSITE-ProRule:PRU10028,
ECO:0000269|PubMed:10655584, ECO:0000269|PubMed:11331870,
ECO:0000269|PubMed:18339875};
-!- ACTIVITY REGULATION: Subject to autoinhibition, mediated by
interactions between the FERM domain and the kinase domain. Activated
by autophosphorylation at Tyr-397. This promotes interaction with SRC
and phosphorylation at Tyr-576 and Tyr-577 in the kinase activation
loop. Phosphorylation at Tyr-576 and Tyr-577 is required for maximal
kinase activity. Inhibited by TAC544, TAE226, PF-573,228 and PF-
562,271. {ECO:0000269|PubMed:10655584, ECO:0000269|PubMed:17395594,
ECO:0000269|PubMed:17431114, ECO:0000269|PubMed:18006843,
ECO:0000269|PubMed:18677107, ECO:0000269|PubMed:20495381}.
-!- SUBUNIT: Interacts (via first Pro-rich region) with CAS family members
(via SH3 domain), including BCAR1, BCAR3, CASS4 and NEDD9. Interacts
with GIT1. Interacts with SORBS1. Interacts with ARHGEF28. Interacts
with SHB. Part of a complex composed of THSD1, PTK2/FAK1, TLN1 and VCL
(PubMed:29069646). Interacts with PXN and TLN1. Interacts with STAT1.
Interacts with DCC. Interacts with WASL. Interacts with ARHGEF7.
Interacts with GRB2 and GRB7 (By similarity). Component of a complex
that contains at least FER, CTTN and PTK2/FAK1. Interacts with BMX.
Interacts with TGFB1I1. Interacts with STEAP4. Interacts with ZFYVE21.
Interacts with ESR1. Interacts with PIK3R1 or PIK3R2. Interacts with
SRC, FGR, FLT4 and RET. Interacts with EPHA2 in resting cells;
activation of EPHA2 recruits PTPN11, leading to dephosphorylation of
PTK2/FAK1 and dissociation of the complex. Interacts with EPHA1 (kinase
activity-dependent). Interacts with CD4; this interaction requires the
presence of HIV-1 gp120. Interacts with PIAS1. Interacts with ARHGAP26
and SHC1. Interacts with RB1CC1; this inhibits PTK2/FAK1 activity and
activation of downstream signaling pathways. Interacts with P53/TP53
and MDM2. Interacts with LPXN (via LD motif 3). Interacts with MISP.
Interacts with CIB1 isoform 2. Interacts with CD36. Interacts with
EMP2; regulates PTK2 activation and localization (PubMed:19494199).
Interacts with DSCAM (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P34152, ECO:0000269|PubMed:10655584,
ECO:0000269|PubMed:11331870, ECO:0000269|PubMed:11980671,
ECO:0000269|PubMed:12221124, ECO:0000269|PubMed:12387730,
ECO:0000269|PubMed:12467573, ECO:0000269|PubMed:14527389,
ECO:0000269|PubMed:15855171, ECO:0000269|PubMed:16452200,
ECO:0000269|PubMed:18078954, ECO:0000269|PubMed:18256281,
ECO:0000269|PubMed:18292575, ECO:0000269|PubMed:18339875,
ECO:0000269|PubMed:18497331, ECO:0000269|PubMed:18657504,
ECO:0000269|PubMed:19118217, ECO:0000269|PubMed:19339212,
ECO:0000269|PubMed:19494199, ECO:0000269|PubMed:19787193,
ECO:0000269|PubMed:19917054, ECO:0000269|PubMed:20037584,
ECO:0000269|PubMed:20439989, ECO:0000269|PubMed:21454698,
ECO:0000269|PubMed:23503467, ECO:0000269|PubMed:23509069,
ECO:0000269|PubMed:29069646, ECO:0000269|PubMed:9422762,
ECO:0000269|PubMed:9756887}.
-!- INTERACTION:
Q05397; P56945: BCAR1; NbExp=2; IntAct=EBI-702142, EBI-702093;
Q05397; P46108: CRK; NbExp=3; IntAct=EBI-702142, EBI-886;
Q05397; P00533: EGFR; NbExp=7; IntAct=EBI-702142, EBI-297353;
Q05397; P29317: EPHA2; NbExp=3; IntAct=EBI-702142, EBI-702104;
Q05397; P62993: GRB2; NbExp=4; IntAct=EBI-702142, EBI-401755;
Q05397; Q14451: GRB7; NbExp=3; IntAct=EBI-702142, EBI-970191;
Q05397; P08631-2: HCK; NbExp=2; IntAct=EBI-702142, EBI-9834454;
Q05397; P16144: ITGB4; NbExp=7; IntAct=EBI-702142, EBI-948678;
Q05397; Q92569: PIK3R3; NbExp=3; IntAct=EBI-702142, EBI-79893;
Q05397; Q9H3S7: PTPN23; NbExp=4; IntAct=EBI-702142, EBI-724478;
Q05397; P29350-3: PTPN6; NbExp=3; IntAct=EBI-702142, EBI-7399369;
Q05397; Q9Y3E5: PTRH2; NbExp=2; IntAct=EBI-702142, EBI-1056751;
Q05397; P49023: PXN; NbExp=17; IntAct=EBI-702142, EBI-702209;
Q05397; Q9NP31: SH2D2A; NbExp=3; IntAct=EBI-702142, EBI-490630;
Q05397; P12931: SRC; NbExp=9; IntAct=EBI-702142, EBI-621482;
Q05397; O43294: TGFB1I1; NbExp=2; IntAct=EBI-702142, EBI-1051449;
Q05397; Q68CZ2: TNS3; NbExp=3; IntAct=EBI-702142, EBI-1220488;
Q05397; P04637: TP53; NbExp=13; IntAct=EBI-702142, EBI-366083;
Q05397; Q824H6: CCA_00170; Xeno; NbExp=3; IntAct=EBI-702142, EBI-26494126;
Q05397; P05480: Src; Xeno; NbExp=5; IntAct=EBI-702142, EBI-298680;
Q05397; Q62219: Tgfb1i1; Xeno; NbExp=3; IntAct=EBI-702142, EBI-642844;
-!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell membrane;
Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cell cortex.
Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000250}. Nucleus. Cytoplasm,
cytoskeleton, cilium basal body {ECO:0000269|PubMed:31630787}.
Note=Constituent of focal adhesions. Detected at microtubules.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=7;
Name=1;
IsoId=Q05397-1; Sequence=Displayed;
Name=2;
IsoId=Q05397-2; Sequence=VSP_004967, VSP_004968, VSP_004969,
VSP_004970;
Name=3;
IsoId=Q05397-3; Sequence=VSP_004967, VSP_004968, VSP_004969,
VSP_004973, VSP_004974;
Name=4;
IsoId=Q05397-4; Sequence=VSP_004967, VSP_004968, VSP_004969,
VSP_004971, VSP_004972;
Name=5;
IsoId=Q05397-5; Sequence=VSP_042169, VSP_042170;
Name=6; Synonyms=FRNK;
IsoId=Q05397-6; Sequence=VSP_042168;
Name=7;
IsoId=Q05397-7; Sequence=VSP_057268;
-!- TISSUE SPECIFICITY: Detected in B and T-lymphocytes. Isoform 1 and
isoform 6 are detected in lung fibroblasts (at protein level).
Ubiquitous. Expressed in epithelial cells (at protein level)
(PubMed:31630787). {ECO:0000269|PubMed:20109444,
ECO:0000269|PubMed:31630787, ECO:0000269|PubMed:7692878,
ECO:0000269|PubMed:8247543, ECO:0000269|PubMed:8422239}.
-!- DEVELOPMENTAL STAGE: [Isoform 6]: Detected in cultured cells,
immediately after seeding and before formation of focal adhesions (at
protein level). {ECO:0000269|PubMed:20109444}.
-!- DOMAIN: The Pro-rich regions interact with the SH3 domain of CAS family
members, such as BCAR1 and NEDD9, and with the GTPase activating
protein ARHGAP26.
-!- DOMAIN: The carboxy-terminal region is the site of focal adhesion
targeting (FAT) sequence which mediates the localization of FAK1 to
focal adhesions.
-!- PTM: Phosphorylated on tyrosine residues upon activation, e.g. upon
integrin signaling. Tyr-397 is the major autophosphorylation site, but
other kinases can also phosphorylate this residue. Phosphorylation at
Tyr-397 promotes interaction with SRC and SRC family members, leading
to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine
residues. FGR promotes phosphorylation at Tyr-397 and Tyr-576. FER
promotes phosphorylation at Tyr-577, Tyr-861 and Tyr-925, even when
cells are not adherent. Tyr-397, Tyr-576 and Ser-722 are phosphorylated
only when cells are adherent. Phosphorylation at Tyr-397 is important
for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-925
is important for interaction with GRB2. Dephosphorylated by PTPN11;
PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated).
Microtubule-induced dephosphorylation at Tyr-397 is crucial for the
induction of focal adhesion disassembly; this dephosphorylation could
be catalyzed by PTPN11 and regulated by ZFYVE21. Phosphorylation on
tyrosine residues is enhanced by NTN1 (By similarity).
{ECO:0000250|UniProtKB:P34152, ECO:0000269|PubMed:12387730,
ECO:0000269|PubMed:15561106, ECO:0000269|PubMed:17395594,
ECO:0000269|PubMed:17431114, ECO:0000269|PubMed:18006843,
ECO:0000269|PubMed:19339212, ECO:0000269|PubMed:21454698}.
-!- PTM: Sumoylated; this enhances autophosphorylation. {ECO:0000250}.
-!- DISEASE: Note=Aberrant PTK2/FAK1 expression may play a role in cancer
cell proliferation, migration and invasion, in tumor formation and
metastasis. PTK2/FAK1 overexpression is seen in many types of cancer.
-!- MISCELLANEOUS: [Isoform 6]: Produced by alternative promoter usage.
{ECO:0000305}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. FAK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PTK2ID41898ch8q24.html";
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EMBL; L13616; AAA58469.1; -; mRNA.
EMBL; L05186; AAA35819.1; -; mRNA.
EMBL; AK304356; BAG65198.1; -; mRNA.
EMBL; AC067931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC100860; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC105009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC105235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF458878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF458882; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC035404; AAH35404.1; -; mRNA.
CCDS; CCDS56557.1; -. [Q05397-5]
CCDS; CCDS6381.1; -. [Q05397-1]
PIR; I53012; I53012.
PIR; PC1225; PC1225.
RefSeq; NP_001186578.1; NM_001199649.1. [Q05397-5]
RefSeq; NP_722560.1; NM_153831.3. [Q05397-1]
RefSeq; XP_016869162.1; XM_017013673.1.
PDB; 1K04; X-ray; 1.95 A; A=891-1052.
PDB; 1K05; X-ray; 2.90 A; A/B/C=891-1052.
PDB; 1MP8; X-ray; 1.60 A; A=411-686.
PDB; 1OW6; X-ray; 2.35 A; A/B/C=892-1052.
PDB; 1OW7; X-ray; 2.60 A; A/B/C=892-1052.
PDB; 1OW8; X-ray; 2.85 A; A/B/C=892-1052.
PDB; 2ETM; X-ray; 2.30 A; A/B=411-689.
PDB; 2IJM; X-ray; 2.19 A; A/B=411-689.
PDB; 3B71; X-ray; 2.82 A; A/B/C=891-1052.
PDB; 3BZ3; X-ray; 2.20 A; A=414-689.
PDB; 3PXK; X-ray; 1.79 A; A/B=411-689.
PDB; 3S9O; X-ray; 2.60 A; A/B/C=891-1052.
PDB; 4EBV; X-ray; 1.67 A; A=411-686.
PDB; 4EBW; X-ray; 2.65 A; A=411-686.
PDB; 4GU6; X-ray; 1.95 A; A/B=411-689.
PDB; 4GU9; X-ray; 2.40 A; A/B=410-686.
PDB; 4I4E; X-ray; 1.55 A; A=411-686.
PDB; 4I4F; X-ray; 1.75 A; A=411-686.
PDB; 4K8A; X-ray; 2.91 A; A/B=410-686.
PDB; 4K9Y; X-ray; 2.00 A; A=410-686.
PDB; 4KAB; X-ray; 2.71 A; A/B=410-686.
PDB; 4KAO; X-ray; 2.39 A; A/B=410-689.
PDB; 4NY0; X-ray; 2.80 A; A/B/C/D=31-405.
PDB; 4Q9S; X-ray; 2.07 A; A=411-686.
PDB; 6I8Z; X-ray; 1.99 A; A=411-689.
PDB; 6LES; X-ray; 2.00 A; A/B/X/Y=805-832.
PDB; 6PW8; X-ray; 1.95 A; A=922-1047.
PDBsum; 1K04; -.
PDBsum; 1K05; -.
PDBsum; 1MP8; -.
PDBsum; 1OW6; -.
PDBsum; 1OW7; -.
PDBsum; 1OW8; -.
PDBsum; 2ETM; -.
PDBsum; 2IJM; -.
PDBsum; 3B71; -.
PDBsum; 3BZ3; -.
PDBsum; 3PXK; -.
PDBsum; 3S9O; -.
PDBsum; 4EBV; -.
PDBsum; 4EBW; -.
PDBsum; 4GU6; -.
PDBsum; 4GU9; -.
PDBsum; 4I4E; -.
PDBsum; 4I4F; -.
PDBsum; 4K8A; -.
PDBsum; 4K9Y; -.
PDBsum; 4KAB; -.
PDBsum; 4KAO; -.
PDBsum; 4NY0; -.
PDBsum; 4Q9S; -.
PDBsum; 6I8Z; -.
PDBsum; 6LES; -.
PDBsum; 6PW8; -.
SMR; Q05397; -.
BioGRID; 111719; 146.
CORUM; Q05397; -.
ELM; Q05397; -.
IntAct; Q05397; 90.
MINT; Q05397; -.
STRING; 9606.ENSP00000341189; -.
BindingDB; Q05397; -.
ChEMBL; CHEMBL2695; -.
DrugBank; DB07460; 2-({5-CHLORO-2-[(2-METHOXY-4-MORPHOLIN-4-YLPHENYL)AMINO]PYRIMIDIN-4-YL}AMINO)-N-METHYLBENZAMIDE.
DrugBank; DB07248; 7-PYRIDIN-2-YL-N-(3,4,5-TRIMETHOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-2-AMINE.
DrugBank; DB06423; Endostatin.
DrugBank; DB12010; Fostamatinib.
DrugCentral; Q05397; -.
GuidetoPHARMACOLOGY; 2180; -.
CarbonylDB; Q05397; -.
iPTMnet; Q05397; -.
PhosphoSitePlus; Q05397; -.
BioMuta; PTK2; -.
DMDM; 3183518; -.
CPTAC; CPTAC-1785; -.
EPD; Q05397; -.
jPOST; Q05397; -.
MassIVE; Q05397; -.
MaxQB; Q05397; -.
PaxDb; Q05397; -.
PeptideAtlas; Q05397; -.
PRIDE; Q05397; -.
ProteomicsDB; 58320; -. [Q05397-1]
ProteomicsDB; 58321; -. [Q05397-2]
ProteomicsDB; 58322; -. [Q05397-3]
ProteomicsDB; 58323; -. [Q05397-4]
ProteomicsDB; 58324; -. [Q05397-5]
ProteomicsDB; 58325; -. [Q05397-6]
ProteomicsDB; 71210; -.
Antibodypedia; 725; 2822 antibodies.
DNASU; 5747; -.
Ensembl; ENST00000340930; ENSP00000341189; ENSG00000169398. [Q05397-5]
Ensembl; ENST00000395218; ENSP00000378644; ENSG00000169398. [Q05397-7]
Ensembl; ENST00000521059; ENSP00000429474; ENSG00000169398. [Q05397-1]
Ensembl; ENST00000522684; ENSP00000429911; ENSG00000169398. [Q05397-1]
GeneID; 5747; -.
KEGG; hsa:5747; -.
UCSC; uc003yvu.4; human. [Q05397-1]
CTD; 5747; -.
DisGeNET; 5747; -.
GeneCards; PTK2; -.
HGNC; HGNC:9611; PTK2.
HPA; ENSG00000169398; Low tissue specificity.
MIM; 600758; gene.
neXtProt; NX_Q05397; -.
OpenTargets; ENSG00000169398; -.
PharmGKB; PA33955; -.
VEuPathDB; HostDB:ENSG00000169398.19; -.
eggNOG; KOG4257; Eukaryota.
GeneTree; ENSGT00940000155113; -.
HOGENOM; CLU_002646_0_0_1; -.
InParanoid; Q05397; -.
OrthoDB; 43729at2759; -.
PhylomeDB; Q05397; -.
TreeFam; TF316643; -.
BRENDA; 2.7.10.2; 2681.
PathwayCommons; Q05397; -.
Reactome; R-HSA-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-354192; Integrin signaling.
Reactome; R-HSA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-HSA-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-HSA-375165; NCAM signaling for neurite out-growth.
Reactome; R-HSA-391160; Signal regulatory protein family interactions.
Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
Reactome; R-HSA-418885; DCC mediated attractive signaling.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-8874081; MET activates PTK2 signaling.
Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
Reactome; R-HSA-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
SignaLink; Q05397; -.
SIGNOR; Q05397; -.
BioGRID-ORCS; 5747; 385 hits in 1036 CRISPR screens.
ChiTaRS; PTK2; human.
EvolutionaryTrace; Q05397; -.
GeneWiki; PTK2; -.
GenomeRNAi; 5747; -.
Pharos; Q05397; Tchem.
PRO; PR:Q05397; -.
Proteomes; UP000005640; Chromosome 8.
RNAct; Q05397; protein.
Bgee; ENSG00000169398; Expressed in corpus callosum and 241 other tissues.
ExpressionAtlas; Q05397; baseline and differential.
Genevisible; Q05397; HS.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
GO; GO:0003779; F:actin binding; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005178; F:integrin binding; IPI:ARUK-UCL.
GO; GO:0008432; F:JUN kinase binding; IDA:BHF-UCL.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0019903; F:protein phosphatase binding; IPI:BHF-UCL.
GO; GO:0004713; F:protein tyrosine kinase activity; EXP:Reactome.
GO; GO:0042169; F:SH2 domain binding; IPI:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:RHEA.
GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
GO; GO:0007411; P:axon guidance; TAS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0048870; P:cell motility; TAS:UniProtKB.
GO; GO:0035995; P:detection of muscle stretch; TAS:BHF-UCL.
GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IBA:GO_Central.
GO; GO:0030010; P:establishment of cell polarity; TAS:UniProtKB.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0060396; P:growth hormone receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0003007; P:heart morphogenesis; TAS:UniProtKB.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0022408; P:negative regulation of cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0038007; P:netrin-activated signaling pathway; TAS:UniProtKB.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0001890; P:placenta development; TAS:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
GO; GO:0010763; P:positive regulation of fibroblast migration; IDA:ARUK-UCL.
GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IGI:ARUK-UCL.
GO; GO:0120041; P:positive regulation of macrophage proliferation; IGI:ARUK-UCL.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; TAS:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:UniProtKB.
GO; GO:0045860; P:positive regulation of protein kinase activity; IMP:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0090303; P:positive regulation of wound healing; IDA:ARUK-UCL.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; IBA:GO_Central.
GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IDA:UniProtKB.
GO; GO:0042127; P:regulation of cell population proliferation; IMP:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
GO; GO:0051493; P:regulation of cytoskeleton organization; TAS:UniProtKB.
GO; GO:0010594; P:regulation of endothelial cell migration; TAS:UniProtKB.
GO; GO:0010632; P:regulation of epithelial cell migration; IGI:UniProtKB.
GO; GO:0051893; P:regulation of focal adhesion assembly; IGI:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; TAS:UniProtKB.
GO; GO:0045667; P:regulation of osteoblast differentiation; IMP:UniProtKB.
GO; GO:0001932; P:regulation of protein phosphorylation; IGI:UniProtKB.
GO; GO:1900024; P:regulation of substrate adhesion-dependent cell spreading; IGI:UniProtKB.
GO; GO:0007172; P:signal complex assembly; IEA:InterPro.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
CDD; cd14473; FERM_B-lobe; 1.
CDD; cd13190; FERM_C_FAK1; 1.
Gene3D; 1.20.80.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR019749; Band_41_domain.
InterPro; IPR041390; FADK_N.
InterPro; IPR041784; FAK1/PYK2_FERM_C.
InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
InterPro; IPR035963; FERM_2.
InterPro; IPR019748; FERM_central.
InterPro; IPR000299; FERM_domain.
InterPro; IPR036137; Focal_adhe_kin_target_dom_sf.
InterPro; IPR005189; Focal_adhesion_kin_target_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR029071; Ubiquitin-like_domsf.
Pfam; PF00373; FERM_M; 1.
Pfam; PF18038; FERM_N_2; 1.
Pfam; PF03623; Focal_AT; 1.
Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00295; B41; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF47031; SSF47031; 1.
SUPFAM; SSF54236; SSF54236; 1.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF68993; SSF68993; 1.
PROSITE; PS00661; FERM_2; 1.
PROSITE; PS50057; FERM_3; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative promoter usage;
Alternative splicing; Angiogenesis; ATP-binding; Cell junction;
Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
Developmental protein; Direct protein sequencing; Isopeptide bond; Kinase;
Membrane; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Transferase; Tyrosine-protein kinase; Ubl conjugation.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19369195,
ECO:0007744|PubMed:19413330"
CHAIN 2..1052
/note="Focal adhesion kinase 1"
/id="PRO_0000088077"
DOMAIN 35..355
/note="FERM"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
DOMAIN 422..680
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 428..434
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000269|PubMed:12467573"
NP_BIND 500..502
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000269|PubMed:12467573"
REGION 707..1052
/note="Interaction with TGFB1I1"
REGION 912..1052
/note="Interaction with ARHGEF28"
/evidence="ECO:0000250"
COMPBIAS 712..733
/note="Pro-rich"
COMPBIAS 863..913
/note="Pro-rich"
ACT_SITE 546
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10028"
BINDING 454
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000269|PubMed:12467573"
MOD_RES 2
/note="N-acetylalanine"
/evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19369195,
ECO:0007744|PubMed:19413330"
MOD_RES 5
/note="Phosphotyrosine"
/evidence="ECO:0007744|PubMed:19369195"
MOD_RES 13
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:18691976,
ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163"
MOD_RES 29
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18691976,
ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163"
MOD_RES 54
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P34152"
MOD_RES 397
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:12387730,
ECO:0000269|PubMed:15561106, ECO:0000269|PubMed:17395594,
ECO:0000269|PubMed:17431114, ECO:0000269|PubMed:18006843,
ECO:0000269|PubMed:19339212, ECO:0007744|PubMed:19369195"
MOD_RES 407
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:12387730,
ECO:0000269|PubMed:15561106"
MOD_RES 570
/note="Phosphotyrosine"
/evidence="ECO:0007744|PubMed:19369195"
MOD_RES 576
/note="Phosphotyrosine; by RET and SRC"
/evidence="ECO:0000269|PubMed:15561106,
ECO:0000269|PubMed:19339212, ECO:0000269|PubMed:21454698"
MOD_RES 577
/note="Phosphotyrosine; by RET and SRC"
/evidence="ECO:0000269|PubMed:12387730,
ECO:0000269|PubMed:19339212, ECO:0000269|PubMed:21454698"
MOD_RES 580
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:19369195"
MOD_RES 722
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:19339212"
MOD_RES 732
/note="Phosphoserine; by CDK5"
/evidence="ECO:0000250|UniProtKB:P34152"
MOD_RES 843
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 861
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:12387730,
ECO:0000269|PubMed:18006843, ECO:0000269|PubMed:19339212"
MOD_RES 887
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18691976"
MOD_RES 910
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
MOD_RES 914
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:20068231"
MOD_RES 925
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:12387730,
ECO:0000269|PubMed:19339212"
CROSSLNK 152
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO)"
/evidence="ECO:0000250"
VAR_SEQ 1..692
/note="Missing (in isoform 6)"
/evidence="ECO:0000305"
/id="VSP_042168"
VAR_SEQ 1..181
/note="Missing (in isoform 2, isoform 3 and isoform 4)"
/evidence="ECO:0000303|PubMed:8422239"
/id="VSP_004967"
VAR_SEQ 182..189
/note="EMRGNALE -> MSDYWVVG (in isoform 2, isoform 3 and
isoform 4)"
/evidence="ECO:0000303|PubMed:8422239"
/id="VSP_004968"
VAR_SEQ 472
/note="A -> ACHYTSLHWNWCRYISDPNVDACPDPRNAE (in isoform 2,
isoform 3 and isoform 4)"
/evidence="ECO:0000303|PubMed:8422239"
/id="VSP_004969"
VAR_SEQ 579..583
/note="ASKGK -> GKKSG (in isoform 4)"
/evidence="ECO:0000303|PubMed:8422239"
/id="VSP_004971"
VAR_SEQ 584..1052
/note="Missing (in isoform 4)"
/evidence="ECO:0000303|PubMed:8422239"
/id="VSP_004972"
VAR_SEQ 677..706
/note="STILEEEKAQQEERMRMESRRQATVSWDSG -> FQNPAQMLPASGRLPNQP
CPERENYSFATF (in isoform 3)"
/evidence="ECO:0000303|PubMed:8422239"
/id="VSP_004973"
VAR_SEQ 707..1052
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:8422239"
/id="VSP_004974"
VAR_SEQ 744..789
/note="Missing (in isoform 7)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_057268"
VAR_SEQ 834..854
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:8422239"
/id="VSP_004970"
VAR_SEQ 868
/note="D -> GKEEKNWAERN (in isoform 5)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_042169"
VAR_SEQ 903
/note="K -> KPWR (in isoform 5)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_042170"
VARIANT 292
/note="H -> P"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041682"
VARIANT 292
/note="H -> Q"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041683"
VARIANT 793
/note="V -> A (in a glioblastoma multiforme sample; somatic
mutation)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041684"
VARIANT 1030
/note="D -> E"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041685"
VARIANT 1044
/note="K -> E (in a metastatic melanoma sample; somatic
mutation)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041686"
MUTAGEN 397
/note="Y->F: Abolishes autophosphorylation. Abolishes
interaction with SRC and activation of BMX."
/evidence="ECO:0000269|PubMed:11331870"
MUTAGEN 928
/note="V->G: Loss of interaction with TGFB1I1."
/evidence="ECO:0000269|PubMed:9756887"
MUTAGEN 1034
/note="L->S: Loss of interaction with TGFB1I1."
/evidence="ECO:0000269|PubMed:9756887"
CONFLICT 184
/note="R -> L (in Ref. 3; BAG65198)"
/evidence="ECO:0000305"
CONFLICT 211
/note="L -> I (in Ref. 3; BAG65198)"
/evidence="ECO:0000305"
CONFLICT 778
/note="P -> S (in Ref. 2; AAA35819)"
/evidence="ECO:0000305"
STRAND 35..40
/evidence="ECO:0007744|PDB:4NY0"
HELIX 49..51
/evidence="ECO:0007744|PDB:4NY0"
STRAND 53..58
/evidence="ECO:0007744|PDB:4NY0"
HELIX 64..73
/evidence="ECO:0007744|PDB:4NY0"
TURN 74..76
/evidence="ECO:0007744|PDB:4NY0"
HELIX 80..82
/evidence="ECO:0007744|PDB:4NY0"
STRAND 83..89
/evidence="ECO:0007744|PDB:4NY0"
STRAND 95..98
/evidence="ECO:0007744|PDB:4NY0"
HELIX 104..114
/evidence="ECO:0007744|PDB:4NY0"
HELIX 117..119
/evidence="ECO:0007744|PDB:4NY0"
STRAND 120..126
/evidence="ECO:0007744|PDB:4NY0"
HELIX 133..137
/evidence="ECO:0007744|PDB:4NY0"
HELIX 141..158
/evidence="ECO:0007744|PDB:4NY0"
HELIX 165..179
/evidence="ECO:0007744|PDB:4NY0"
HELIX 185..187
/evidence="ECO:0007744|PDB:4NY0"
STRAND 188..190
/evidence="ECO:0007744|PDB:4NY0"
HELIX 191..194
/evidence="ECO:0007744|PDB:4NY0"
HELIX 197..201
/evidence="ECO:0007744|PDB:4NY0"
TURN 204..206
/evidence="ECO:0007744|PDB:4NY0"
HELIX 209..214
/evidence="ECO:0007744|PDB:4NY0"
TURN 217..219
/evidence="ECO:0007744|PDB:4NY0"
HELIX 220..228
/evidence="ECO:0007744|PDB:4NY0"
HELIX 229..231
/evidence="ECO:0007744|PDB:4NY0"
HELIX 236..247
/evidence="ECO:0007744|PDB:4NY0"
HELIX 248..250
/evidence="ECO:0007744|PDB:4NY0"
STRAND 256..262
/evidence="ECO:0007744|PDB:4NY0"
STRAND 264..266
/evidence="ECO:0007744|PDB:4NY0"
STRAND 268..275
/evidence="ECO:0007744|PDB:4NY0"
TURN 276..278
/evidence="ECO:0007744|PDB:4NY0"
STRAND 279..283
/evidence="ECO:0007744|PDB:4NY0"
STRAND 290..294
/evidence="ECO:0007744|PDB:4NY0"
HELIX 296..298
/evidence="ECO:0007744|PDB:4NY0"
STRAND 299..306
/evidence="ECO:0007744|PDB:4NY0"
STRAND 308..311
/evidence="ECO:0007744|PDB:4NY0"
STRAND 314..320
/evidence="ECO:0007744|PDB:4NY0"
STRAND 327..333
/evidence="ECO:0007744|PDB:4NY0"
HELIX 334..351
/evidence="ECO:0007744|PDB:4NY0"
HELIX 413..415
/evidence="ECO:0007744|PDB:4EBV"
HELIX 419..421
/evidence="ECO:0007744|PDB:4I4E"
STRAND 422..430
/evidence="ECO:0007744|PDB:4I4E"
STRAND 432..441
/evidence="ECO:0007744|PDB:4I4E"
STRAND 444..446
/evidence="ECO:0007744|PDB:6I8Z"
STRAND 448..455
/evidence="ECO:0007744|PDB:4I4E"
TURN 457..460
/evidence="ECO:0007744|PDB:4I4E"
HELIX 462..468
/evidence="ECO:0007744|PDB:4I4E"
HELIX 470..476
/evidence="ECO:0007744|PDB:4I4E"
STRAND 486..490
/evidence="ECO:0007744|PDB:4I4E"
STRAND 492..494
/evidence="ECO:0007744|PDB:4I4E"
STRAND 496..500
/evidence="ECO:0007744|PDB:4I4E"
HELIX 507..513
/evidence="ECO:0007744|PDB:4I4E"
TURN 514..517
/evidence="ECO:0007744|PDB:4I4E"
HELIX 520..539
/evidence="ECO:0007744|PDB:4I4E"
HELIX 549..551
/evidence="ECO:0007744|PDB:4I4E"
STRAND 552..556
/evidence="ECO:0007744|PDB:4I4E"
STRAND 559..562
/evidence="ECO:0007744|PDB:4I4E"
HELIX 565..568
/evidence="ECO:0007744|PDB:4GU6"
HELIX 570..573
/evidence="ECO:0007744|PDB:4GU6"
HELIX 574..576
/evidence="ECO:0007744|PDB:4GU6"
HELIX 586..588
/evidence="ECO:0007744|PDB:4I4E"
HELIX 591..596
/evidence="ECO:0007744|PDB:4I4E"
HELIX 601..616
/evidence="ECO:0007744|PDB:4I4E"
TURN 617..619
/evidence="ECO:0007744|PDB:4EBV"
TURN 622..625
/evidence="ECO:0007744|PDB:4I4E"
HELIX 628..630
/evidence="ECO:0007744|PDB:4I4E"
HELIX 631..636
/evidence="ECO:0007744|PDB:4I4E"
HELIX 649..658
/evidence="ECO:0007744|PDB:4I4E"
HELIX 663..665
/evidence="ECO:0007744|PDB:4I4E"
HELIX 669..684
/evidence="ECO:0007744|PDB:4I4E"
HELIX 685..687
/evidence="ECO:0007744|PDB:2IJM"
STRAND 915..917
/evidence="ECO:0007744|PDB:1K04"
HELIX 923..942
/evidence="ECO:0007744|PDB:1K04"
HELIX 947..949
/evidence="ECO:0007744|PDB:1K04"
HELIX 950..971
/evidence="ECO:0007744|PDB:1K04"
HELIX 972..974
/evidence="ECO:0007744|PDB:1K04"
HELIX 977..979
/evidence="ECO:0007744|PDB:1K04"
HELIX 980..1006
/evidence="ECO:0007744|PDB:1K04"
TURN 1007..1009
/evidence="ECO:0007744|PDB:1K04"
STRAND 1010..1012
/evidence="ECO:0007744|PDB:1K04"
HELIX 1013..1045
/evidence="ECO:0007744|PDB:1K04"
SEQUENCE 1052 AA; 119233 MW; D8A4C15138AB0243 CRC64;
MAAAYLDPNL NHTPNSSTKT HLGTGMERSP GAMERVLKVF HYFESNSEPT TWASIIRHGD
ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW
KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMLEIA DQVDQEIALK LGCLEIRRSY
WEMRGNALEK KSNYEVLEKD VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI
LKFFEILSPV YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFTQVQ
TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL VNGTSQSFII
RPQKEGERAL PSIPKLANSE KQGMRTHAVS VSETDDYAEI IDEEDTYTMP STRDYEIQRE
RIELGRCIGE GQFGDVHQGI YMSPENPALA VAIKTCKNCT SDSVREKFLQ EALTMRQFDH
PHIVKLIGVI TENPVWIIME LCTLGELRSF LQVRKYSLDL ASLILYAYQL STALAYLESK
RFVHRDIAAR NVLVSSNDCV KLGDFGLSRY MEDSTYYKAS KGKLPIKWMA PESINFRRFT
SASDVWMFGV CMWEILMHGV KPFQGVKNND VIGRIENGER LPMPPNCPPT LYSLMTKCWA
YDPSRRPRFT ELKAQLSTIL EEEKAQQEER MRMESRRQAT VSWDSGGSDE APPKPSRPGY
PSPRSSEGFY PSPQHMVQTN HYQVSGYPGS HGITAMAGSI YPGQASLLDQ TDSWNHRPQE
IAMWQPNVED STVLDLRGIG QVLPTHLMEE RLIRQQQEME EDQRWLEKEE RFLKPDVRLS
RGSIDREDGS LQGPIGNQHI YQPVGKPDPA APPKKPPRPG APGHLGSLAS LSSPADSYNE
GVKLQPQEIS PPPTANLDRS NDKVYENVTG LVKAVIEMSS KIQPAPPEEY VPMVKEVGLA
LRTLLATVDE TIPLLPASTH REIEMAQKLL NSDLGELINK MKLAQQYVMT SLQQEYKKQM
LTAAHALAVD AKNLLDVIDQ ARLKMLGQTR PH


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WP1493: Carbon assimilation C4 pathway
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WP2340: Thiamine (vitamin B1) biosynthesis and salvage
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WP1663: Homologous recombination
WP1694: Pyrimidine metabolism
WP2292: Chemokine signaling pathway
WP1701: Starch and sucrose metabolism
WP1672: Mismatch repair
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WP2199: Seed Development
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Related Genes :
[PTK2 FAK FAK1] Focal adhesion kinase 1 (FADK 1) (EC 2.7.10.2) (Focal adhesion kinase-related nonkinase) (FRNK) (Protein phosphatase 1 regulatory subunit 71) (PPP1R71) (Protein-tyrosine kinase 2) (p125FAK) (pp125FAK)
[PTK2 FAK FAK1] Focal adhesion kinase 1 (FADK 1) (EC 2.7.10.2) (Focal adhesion kinase-related nonkinase) (FRNK) (p41/p43FRNK) (Protein-tyrosine kinase 2) (p125FAK) (pp125FAK)
[Ptk2 Fak Fak1] Focal adhesion kinase 1 (FADK 1) (EC 2.7.10.2) (Focal adhesion kinase-related nonkinase) (FRNK) (Protein-tyrosine kinase 2) (p125FAK) (pp125FAK)
[Ptk2 Fadk Fak Fak1 Kiaa4203] Focal adhesion kinase 1 (FADK 1) (EC 2.7.10.2) (Focal adhesion kinase-related nonkinase) (FRNK) (Protein-tyrosine kinase 2) (p125FAK) (pp125FAK)
[ptk2 fak1] Focal adhesion kinase 1 (FADK 1) (EC 2.7.10.2) (Protein-tyrosine kinase 2) (pp125FAK)
[Ptk2b Fak2 Pyk2 Raftk] Protein-tyrosine kinase 2-beta (EC 2.7.10.2) (Calcium-dependent tyrosine kinase) (CADTK) (Calcium-regulated non-receptor proline-rich tyrosine kinase) (Cell adhesion kinase beta) (CAK-beta) (CAKB) (Focal adhesion kinase 2) (FADK 2) (Proline-rich tyrosine kinase 2) (Related adhesion focal tyrosine kinase) (RAFTK)
[PTK2B FAK2 PYK2 RAFTK] Protein-tyrosine kinase 2-beta (EC 2.7.10.2) (Calcium-dependent tyrosine kinase) (CADTK) (Calcium-regulated non-receptor proline-rich tyrosine kinase) (Cell adhesion kinase beta) (CAK-beta) (CAKB) (Focal adhesion kinase 2) (FADK 2) (Proline-rich tyrosine kinase 2) (Related adhesion focal tyrosine kinase) (RAFTK)
[Ptk2b Fak2 Pyk2] Protein-tyrosine kinase 2-beta (EC 2.7.10.2) (Calcium-dependent tyrosine kinase) (CADTK) (Calcium-regulated non-receptor proline-rich tyrosine kinase) (Cell adhesion kinase beta) (CAK-beta) (CAKB) (Focal adhesion kinase 2) (FADK 2) (Proline-rich tyrosine kinase 2)
[DDR1 CAK EDDR1 NEP NTRK4 PTK3A RTK6 TRKE] Epithelial discoidin domain-containing receptor 1 (Epithelial discoidin domain receptor 1) (EC 2.7.10.1) (CD167 antigen-like family member A) (Cell adhesion kinase) (Discoidin receptor tyrosine kinase) (HGK2) (Mammary carcinoma kinase 10) (MCK-10) (Protein-tyrosine kinase 3A) (Protein-tyrosine kinase RTK-6) (TRK E) (Tyrosine kinase DDR) (Tyrosine-protein kinase CAK) (CD antigen CD167a)
[Axl Ark Ufo] Tyrosine-protein kinase receptor UFO (EC 2.7.10.1) (Adhesion-related kinase)
[Tek Hyk Tie-2 Tie2] Angiopoietin-1 receptor (EC 2.7.10.1) (Endothelial tyrosine kinase) (HYK) (STK1) (Tunica interna endothelial cell kinase) (Tyrosine kinase with Ig and EGF homology domains-2) (Tyrosine-protein kinase receptor TEK) (Tyrosine-protein kinase receptor TIE-2) (mTIE2) (p140 TEK) (CD antigen CD202b)
[EPHA2 ECK] Ephrin type-A receptor 2 (EC 2.7.10.1) (Epithelial cell kinase) (Tyrosine-protein kinase receptor ECK)
[FLT1 FLT FRT VEGFR1] Vascular endothelial growth factor receptor 1 (VEGFR-1) (EC 2.7.10.1) (Fms-like tyrosine kinase 1) (FLT-1) (Tyrosine-protein kinase FRT) (Tyrosine-protein kinase receptor FLT) (FLT) (Vascular permeability factor receptor)
[KDR FLK1 VEGFR2] Vascular endothelial growth factor receptor 2 (VEGFR-2) (EC 2.7.10.1) (Fetal liver kinase 1) (FLK-1) (Kinase insert domain receptor) (KDR) (Protein-tyrosine kinase receptor flk-1) (CD antigen CD309)
[ABL1 ABL JTK7] Tyrosine-protein kinase ABL1 (EC 2.7.10.2) (Abelson murine leukemia viral oncogene homolog 1) (Abelson tyrosine-protein kinase 1) (Proto-oncogene c-Abl) (p150)
[TEK TIE2 VMCM VMCM1] Angiopoietin-1 receptor (EC 2.7.10.1) (Endothelial tyrosine kinase) (Tunica interna endothelial cell kinase) (Tyrosine kinase with Ig and EGF homology domains-2) (Tyrosine-protein kinase receptor TEK) (Tyrosine-protein kinase receptor TIE-2) (hTIE2) (p140 TEK) (CD antigen CD202b)
[Epha2 Eck Myk2 Sek2] Ephrin type-A receptor 2 (EC 2.7.10.1) (Epithelial cell kinase) (Tyrosine-protein kinase receptor ECK) (Tyrosine-protein kinase receptor MPK-5) (Tyrosine-protein kinase receptor SEK-2)
[FLT4 VEGFR3] Vascular endothelial growth factor receptor 3 (VEGFR-3) (EC 2.7.10.1) (Fms-like tyrosine kinase 4) (FLT-4) (Tyrosine-protein kinase receptor FLT4)
[EGFR ERBB ERBB1 HER1] Epidermal growth factor receptor (EC 2.7.10.1) (Proto-oncogene c-ErbB-1) (Receptor tyrosine-protein kinase erbB-1)
[SRC SRC1] Proto-oncogene tyrosine-protein kinase Src (EC 2.7.10.2) (Proto-oncogene c-Src) (pp60c-src) (p60-Src)
[Abl1 Abl] Tyrosine-protein kinase ABL1 (EC 2.7.10.2) (Abelson murine leukemia viral oncogene homolog 1) (Abelson tyrosine-protein kinase 1) (Proto-oncogene c-Abl) (p150)
[Csk] Tyrosine-protein kinase CSK (EC 2.7.10.2) (C-Src kinase) (Protein-tyrosine kinase MPK-2) (p50CSK)
[Lyn] Tyrosine-protein kinase Lyn (EC 2.7.10.2) (V-yes-1 Yamaguchi sarcoma viral related oncogene homolog) (p53Lyn) (p56Lyn)
[Mapk1 Erk2 Mapk Prkm1] Mitogen-activated protein kinase 1 (MAP kinase 1) (MAPK 1) (EC 2.7.11.24) (ERT1) (Extracellular signal-regulated kinase 2) (ERK-2) (MAP kinase isoform p42) (p42-MAPK) (Mitogen-activated protein kinase 2) (MAP kinase 2) (MAPK 2)
[RET CDHF12 CDHR16 PTC RET51] Proto-oncogene tyrosine-protein kinase receptor Ret (EC 2.7.10.1) (Cadherin family member 12) (Proto-oncogene c-Ret) [Cleaved into: Soluble RET kinase fragment; Extracellular cell-membrane anchored RET cadherin 120 kDa fragment]
[EPHB1 ELK EPHT2 HEK6 NET] Ephrin type-B receptor 1 (EC 2.7.10.1) (ELK) (EPH tyrosine kinase 2) (EPH-like kinase 6) (EK6) (hEK6) (Neuronally-expressed EPH-related tyrosine kinase) (NET) (Tyrosine-protein kinase receptor EPH-2)
[TEK TIE-2 TIE2] Angiopoietin-1 receptor (EC 2.7.10.1) (Endothelial tyrosine kinase) (Tyrosine kinase with Ig and EGF homology domains-2) (Tyrosine-protein kinase receptor TIE-2) (CD antigen CD202b)
[FER TYK3] Tyrosine-protein kinase Fer (EC 2.7.10.2) (Feline encephalitis virus-related kinase FER) (Fujinami poultry sarcoma/Feline sarcoma-related protein Fer) (Proto-oncogene c-Fer) (Tyrosine kinase 3) (p94-Fer)
[AHK4 CRE1 RAW1 WOL At2g01830 T23K3.2] Histidine kinase 4 (EC 2.7.13.3) (Arabidopsis histidine kinase 4) (AtHK4) (Cytokinin receptor CYTOKININ RESPONSE 1) (AtCRE1) (Cytokinin receptor CRE1) (Phosphoprotein phosphatase AHK4) (EC 3.1.3.16) (Protein AUTHENTIC HIS-KINASE 4) (Protein ROOT AS IN WOL 1) (Protein WOODEN LEG)
[SRC] Proto-oncogene tyrosine-protein kinase Src (EC 2.7.10.2) (Proto-oncogene c-Src) (pp60c-src) (p60-Src)

Bibliography :
No related Items