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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.
27-SEP-2017, entry version 213.
RecName: Full=Focal adhesion kinase 1;
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; 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, ENZYME 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]
ENZYME 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, ENZYME 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, ENZYME 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 ENZYME 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 ENZYME 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; ENZYME 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]
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).
[66]
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).
[67]
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).
[68]
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).
[69]
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).
[70]
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}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:10655584,
ECO:0000269|PubMed:11331870, ECO:0000269|PubMed:18339875}.
-!- ENZYME 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. 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). {ECO:0000250,
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:9422762,
ECO:0000269|PubMed:9756887}.
-!- INTERACTION:
P56945:BCAR1; NbExp=2; IntAct=EBI-702142, EBI-702093;
P78396:CCNA1; NbExp=2; IntAct=EBI-702142, EBI-375065;
P46108:CRK; NbExp=3; IntAct=EBI-702142, EBI-886;
P46109:CRKL; NbExp=2; IntAct=EBI-702142, EBI-910;
P00533:EGFR; NbExp=3; IntAct=EBI-702142, EBI-297353;
P29317:EPHA2; NbExp=3; IntAct=EBI-702142, EBI-702104;
P04626:ERBB2; NbExp=2; IntAct=EBI-702142, EBI-641062;
P17948:FLT1; NbExp=2; IntAct=EBI-702142, EBI-1026718;
Q14451:GRB7; NbExp=3; IntAct=EBI-702142, EBI-970191;
P08631-2:HCK; NbExp=2; IntAct=EBI-702142, EBI-9834454;
P16144:ITGB4; NbExp=7; IntAct=EBI-702142, EBI-948678;
P07948:LYN; NbExp=2; IntAct=EBI-702142, EBI-79452;
Q92569:PIK3R3; NbExp=3; IntAct=EBI-702142, EBI-79893;
Q9H3S7:PTPN23; NbExp=4; IntAct=EBI-702142, EBI-724478;
P29350-3:PTPN6; NbExp=3; IntAct=EBI-702142, EBI-7399369;
Q9Y3E5:PTRH2; NbExp=2; IntAct=EBI-702142, EBI-1056751;
P49023:PXN; NbExp=15; IntAct=EBI-702142, EBI-702209;
Q9NP31:SH2D2A; NbExp=3; IntAct=EBI-702142, EBI-490630;
P12931:SRC; NbExp=8; IntAct=EBI-702142, EBI-621482;
P05480:Src (xeno); NbExp=5; IntAct=EBI-702142, EBI-298680;
O43294:TGFB1I1; NbExp=2; IntAct=EBI-702142, EBI-1051449;
Q62219:Tgfb1i1 (xeno); NbExp=3; IntAct=EBI-702142, EBI-642844;
Q68CZ2:TNS3; NbExp=3; IntAct=EBI-702142, EBI-1220488;
P04637:TP53; NbExp=13; IntAct=EBI-702142, EBI-366083;
-!- 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. 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;
Note=Produced by alternative promoter usage.;
Name=7;
IsoId=Q05397-7; Sequence=VSP_057268;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in B and T-lymphocytes. Isoform 1 and
isoform 6 are detected in lung fibroblasts (at protein level).
Ubiquitous. {ECO:0000269|PubMed:20109444,
ECO:0000269|PubMed:7692878, ECO:0000269|PubMed:8247543,
ECO:0000269|PubMed:8422239}.
-!- DEVELOPMENTAL STAGE: Isoform 6 is detected in cultured cells,
immediately after seeding and before formation of focal adhesions
(at protein level).
-!- 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. {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.
-!- 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. [Q05397-1]
UniGene; Hs.395482; -.
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.
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; -.
ProteinModelPortal; Q05397; -.
SMR; Q05397; -.
BioGrid; 111719; 123.
CORUM; Q05397; -.
ELM; Q05397; -.
IntAct; Q05397; 70.
MINT; MINT-92695; -.
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.
GuidetoPHARMACOLOGY; 2180; -.
iPTMnet; Q05397; -.
PhosphoSitePlus; Q05397; -.
BioMuta; PTK2; -.
DMDM; 3183518; -.
EPD; Q05397; -.
MaxQB; Q05397; -.
PaxDb; Q05397; -.
PeptideAtlas; Q05397; -.
PRIDE; Q05397; -.
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; -.
EuPathDB; HostDB:ENSG00000169398.19; -.
GeneCards; PTK2; -.
HGNC; HGNC:9611; PTK2.
HPA; CAB004036; -.
HPA; HPA001842; -.
HPA; HPA029671; -.
MIM; 600758; gene.
neXtProt; NX_Q05397; -.
OpenTargets; ENSG00000169398; -.
PharmGKB; PA33955; -.
eggNOG; KOG4257; Eukaryota.
eggNOG; ENOG410ZH9Y; LUCA.
GeneTree; ENSGT00760000118799; -.
HOGENOM; HOG000069938; -.
HOVERGEN; HBG004018; -.
InParanoid; Q05397; -.
KO; K05725; -.
PhylomeDB; Q05397; -.
TreeFam; TF316643; -.
BRENDA; 2.7.10.2; 2681.
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 alphaIIb beta3 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-3928663; EPHA-mediated growth cone collapse.
Reactome; R-HSA-418885; DCC mediated attractive signaling.
Reactome; R-HSA-418886; Netrin mediated repulsion signals.
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.
SignaLink; Q05397; -.
SIGNOR; Q05397; -.
ChiTaRS; PTK2; human.
EvolutionaryTrace; Q05397; -.
GeneWiki; PTK2; -.
GenomeRNAi; 5747; -.
PMAP-CutDB; Q05397; -.
PRO; PR:Q05397; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000169398; -.
CleanEx; HS_PTK2; -.
ExpressionAtlas; Q05397; baseline and differential.
Genevisible; Q05397; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
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:0030027; C:lamellipodium; IEA:Ensembl.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
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:0008432; F:JUN kinase binding; IDA:BHF-UCL.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0004672; F:protein kinase activity; TAS:Reactome.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; EXP:Reactome.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0005102; F:receptor binding; IBA:GO_Central.
GO; GO:0042169; F:SH2 domain binding; IPI:UniProtKB.
GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
GO; GO:0001525; P:angiogenesis; TAS:UniProtKB.
GO; GO:0007411; P:axon guidance; TAS:UniProtKB.
GO; GO:0048870; P:cell motility; TAS:UniProtKB.
GO; GO:0021955; P:central nervous system neuron axonogenesis; IEA:Ensembl.
GO; GO:0009790; P:embryo development; TAS:UniProtKB.
GO; GO:0043542; P:endothelial cell migration; IEA:Ensembl.
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:0040023; P:establishment of nucleus localization; IEA:Ensembl.
GO; GO:0097194; P:execution phase of apoptosis; TAS:Reactome.
GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
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:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
GO; GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0050771; P:negative regulation of axonogenesis; IEA:Ensembl.
GO; GO:0022408; P:negative regulation of cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0046621; P:negative regulation of organ growth; IEA:Ensembl.
GO; GO:0051964; P:negative regulation of synapse assembly; IEA:Ensembl.
GO; GO:0038007; P:netrin-activated signaling pathway; TAS:UniProtKB.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
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 proliferation; ISS:UniProtKB.
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 protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IDA:UniProtKB.
GO; GO:0042127; P:regulation of cell 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:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
CDD; cd14473; FERM_B-lobe; 1.
Gene3D; 1.20.80.10; -; 1.
InterPro; IPR019749; Band_41_domain.
InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
InterPro; IPR019748; FERM_central.
InterPro; IPR000299; FERM_domain.
InterPro; IPR005189; Focal_adhesion_kin_target_dom.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR011993; PH_dom-like.
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-rel_dom.
Pfam; PF00373; FERM_M; 1.
Pfam; PF03623; Focal_AT; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PRINTS; PR00109; TYRKINASE.
ProDom; PD006413; Focal_adhesion_target_reg; 1.
SMART; SM00295; B41; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF47031; SSF47031; 1.
SUPFAM; SSF50729; SSF50729; 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; Complete proteome; Cytoplasm; Cytoskeleton;
Developmental protein; Direct protein sequencing; Isopeptide bond;
Kinase; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Transferase;
Tyrosine-protein kinase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19413330,
ECO:0000269|Ref.6}.
CHAIN 2 1052 Focal adhesion kinase 1.
/FTId=PRO_0000088077.
DOMAIN 35 355 FERM. {ECO:0000255|PROSITE-
ProRule:PRU00084}.
DOMAIN 422 680 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 428 434 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:12467573}.
NP_BIND 500 502 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:12467573}.
REGION 707 1052 Interaction with TGFB1I1.
REGION 912 1052 Interaction with ARHGEF28. {ECO:0000250}.
COMPBIAS 712 733 Pro-rich.
COMPBIAS 863 913 Pro-rich.
ACT_SITE 546 546 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 454 454 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:12467573}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19413330,
ECO:0000269|Ref.6}.
MOD_RES 5 5 Phosphotyrosine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 13 13 Phosphothreonine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163}.
MOD_RES 54 54 Phosphoserine.
{ECO:0000250|UniProtKB:P34152}.
MOD_RES 397 397 Phosphotyrosine; by autocatalysis.
{ECO:0000244|PubMed:19369195,
ECO:0000269|PubMed:12387730,
ECO:0000269|PubMed:15561106,
ECO:0000269|PubMed:17395594,
ECO:0000269|PubMed:17431114,
ECO:0000269|PubMed:18006843,
ECO:0000269|PubMed:19339212}.
MOD_RES 407 407 Phosphotyrosine.
{ECO:0000269|PubMed:12387730,
ECO:0000269|PubMed:15561106}.
MOD_RES 570 570 Phosphotyrosine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 576 576 Phosphotyrosine; by RET and SRC.
{ECO:0000269|PubMed:15561106,
ECO:0000269|PubMed:19339212,
ECO:0000269|PubMed:21454698}.
MOD_RES 577 577 Phosphotyrosine; by RET and SRC.
{ECO:0000269|PubMed:12387730,
ECO:0000269|PubMed:19339212,
ECO:0000269|PubMed:21454698}.
MOD_RES 580 580 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 722 722 Phosphoserine.
{ECO:0000269|PubMed:19339212}.
MOD_RES 732 732 Phosphoserine; by CDK5.
{ECO:0000250|UniProtKB:P34152}.
MOD_RES 843 843 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 861 861 Phosphotyrosine.
{ECO:0000269|PubMed:12387730,
ECO:0000269|PubMed:18006843,
ECO:0000269|PubMed:19339212}.
MOD_RES 887 887 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 910 910 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 914 914 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 925 925 Phosphotyrosine.
{ECO:0000269|PubMed:12387730,
ECO:0000269|PubMed:19339212}.
CROSSLNK 152 152 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
VAR_SEQ 1 692 Missing (in isoform 6). {ECO:0000305}.
/FTId=VSP_042168.
VAR_SEQ 1 181 Missing (in isoform 2, isoform 3 and
isoform 4). {ECO:0000303|PubMed:8422239}.
/FTId=VSP_004967.
VAR_SEQ 182 189 EMRGNALE -> MSDYWVVG (in isoform 2,
isoform 3 and isoform 4).
{ECO:0000303|PubMed:8422239}.
/FTId=VSP_004968.
VAR_SEQ 472 472 A -> ACHYTSLHWNWCRYISDPNVDACPDPRNAE (in
isoform 2, isoform 3 and isoform 4).
{ECO:0000303|PubMed:8422239}.
/FTId=VSP_004969.
VAR_SEQ 579 583 ASKGK -> GKKSG (in isoform 4).
{ECO:0000303|PubMed:8422239}.
/FTId=VSP_004971.
VAR_SEQ 584 1052 Missing (in isoform 4).
{ECO:0000303|PubMed:8422239}.
/FTId=VSP_004972.
VAR_SEQ 677 706 STILEEEKAQQEERMRMESRRQATVSWDSG -> FQNPAQM
LPASGRLPNQPCPERENYSFATF (in isoform 3).
{ECO:0000303|PubMed:8422239}.
/FTId=VSP_004973.
VAR_SEQ 707 1052 Missing (in isoform 3).
{ECO:0000303|PubMed:8422239}.
/FTId=VSP_004974.
VAR_SEQ 744 789 Missing (in isoform 7).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_057268.
VAR_SEQ 834 854 Missing (in isoform 2).
{ECO:0000303|PubMed:8422239}.
/FTId=VSP_004970.
VAR_SEQ 868 868 D -> GKEEKNWAERN (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042169.
VAR_SEQ 903 903 K -> KPWR (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042170.
VARIANT 292 292 H -> P. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041682.
VARIANT 292 292 H -> Q. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041683.
VARIANT 793 793 V -> A (in a glioblastoma multiforme
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041684.
VARIANT 1030 1030 D -> E. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041685.
VARIANT 1044 1044 K -> E (in a metastatic melanoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041686.
MUTAGEN 397 397 Y->F: Abolishes autophosphorylation.
Abolishes interaction with SRC and
activation of BMX.
{ECO:0000269|PubMed:11331870}.
MUTAGEN 928 928 V->G: Loss of interaction with TGFB1I1.
{ECO:0000269|PubMed:9756887}.
MUTAGEN 1034 1034 L->S: Loss of interaction with TGFB1I1.
{ECO:0000269|PubMed:9756887}.
CONFLICT 184 184 R -> L (in Ref. 3; BAG65198).
{ECO:0000305}.
CONFLICT 211 211 L -> I (in Ref. 3; BAG65198).
{ECO:0000305}.
CONFLICT 778 778 P -> S (in Ref. 2; AAA35819).
{ECO:0000305}.
STRAND 35 40 {ECO:0000244|PDB:4NY0}.
HELIX 49 51 {ECO:0000244|PDB:4NY0}.
STRAND 53 58 {ECO:0000244|PDB:4NY0}.
HELIX 64 73 {ECO:0000244|PDB:4NY0}.
TURN 74 76 {ECO:0000244|PDB:4NY0}.
HELIX 80 82 {ECO:0000244|PDB:4NY0}.
STRAND 83 89 {ECO:0000244|PDB:4NY0}.
STRAND 95 98 {ECO:0000244|PDB:4NY0}.
HELIX 104 114 {ECO:0000244|PDB:4NY0}.
HELIX 117 119 {ECO:0000244|PDB:4NY0}.
STRAND 120 126 {ECO:0000244|PDB:4NY0}.
HELIX 133 137 {ECO:0000244|PDB:4NY0}.
HELIX 141 158 {ECO:0000244|PDB:4NY0}.
HELIX 165 179 {ECO:0000244|PDB:4NY0}.
HELIX 185 187 {ECO:0000244|PDB:4NY0}.
STRAND 188 190 {ECO:0000244|PDB:4NY0}.
HELIX 191 194 {ECO:0000244|PDB:4NY0}.
HELIX 197 201 {ECO:0000244|PDB:4NY0}.
TURN 204 206 {ECO:0000244|PDB:4NY0}.
HELIX 209 214 {ECO:0000244|PDB:4NY0}.
TURN 217 219 {ECO:0000244|PDB:4NY0}.
HELIX 220 228 {ECO:0000244|PDB:4NY0}.
HELIX 229 231 {ECO:0000244|PDB:4NY0}.
HELIX 236 247 {ECO:0000244|PDB:4NY0}.
HELIX 248 250 {ECO:0000244|PDB:4NY0}.
STRAND 256 262 {ECO:0000244|PDB:4NY0}.
STRAND 264 266 {ECO:0000244|PDB:4NY0}.
STRAND 268 275 {ECO:0000244|PDB:4NY0}.
TURN 276 278 {ECO:0000244|PDB:4NY0}.
STRAND 279 283 {ECO:0000244|PDB:4NY0}.
STRAND 290 294 {ECO:0000244|PDB:4NY0}.
HELIX 296 298 {ECO:0000244|PDB:4NY0}.
STRAND 299 306 {ECO:0000244|PDB:4NY0}.
STRAND 308 311 {ECO:0000244|PDB:4NY0}.
STRAND 314 320 {ECO:0000244|PDB:4NY0}.
STRAND 327 333 {ECO:0000244|PDB:4NY0}.
HELIX 334 351 {ECO:0000244|PDB:4NY0}.
HELIX 413 415 {ECO:0000244|PDB:4EBV}.
HELIX 419 421 {ECO:0000244|PDB:4I4E}.
STRAND 422 430 {ECO:0000244|PDB:4I4E}.
STRAND 432 441 {ECO:0000244|PDB:4I4E}.
STRAND 444 446 {ECO:0000244|PDB:4K9Y}.
STRAND 448 455 {ECO:0000244|PDB:4I4E}.
TURN 457 460 {ECO:0000244|PDB:4I4E}.
HELIX 462 468 {ECO:0000244|PDB:4I4E}.
HELIX 470 476 {ECO:0000244|PDB:4I4E}.
STRAND 486 490 {ECO:0000244|PDB:4I4E}.
STRAND 492 494 {ECO:0000244|PDB:4I4E}.
STRAND 496 500 {ECO:0000244|PDB:4I4E}.
HELIX 507 513 {ECO:0000244|PDB:4I4E}.
TURN 514 517 {ECO:0000244|PDB:4I4E}.
HELIX 520 539 {ECO:0000244|PDB:4I4E}.
HELIX 549 551 {ECO:0000244|PDB:4I4E}.
STRAND 552 556 {ECO:0000244|PDB:4I4E}.
STRAND 559 562 {ECO:0000244|PDB:4I4E}.
HELIX 565 568 {ECO:0000244|PDB:4GU6}.
HELIX 570 573 {ECO:0000244|PDB:4GU6}.
HELIX 574 576 {ECO:0000244|PDB:4GU6}.
HELIX 586 588 {ECO:0000244|PDB:4I4E}.
HELIX 591 596 {ECO:0000244|PDB:4I4E}.
HELIX 601 616 {ECO:0000244|PDB:4I4E}.
TURN 617 619 {ECO:0000244|PDB:4EBV}.
TURN 622 625 {ECO:0000244|PDB:4I4E}.
HELIX 628 630 {ECO:0000244|PDB:4I4E}.
HELIX 631 636 {ECO:0000244|PDB:4I4E}.
HELIX 649 658 {ECO:0000244|PDB:4I4E}.
HELIX 663 665 {ECO:0000244|PDB:4I4E}.
HELIX 669 684 {ECO:0000244|PDB:4I4E}.
HELIX 685 687 {ECO:0000244|PDB:2IJM}.
STRAND 915 917 {ECO:0000244|PDB:1K04}.
HELIX 923 942 {ECO:0000244|PDB:1K04}.
HELIX 947 949 {ECO:0000244|PDB:1K04}.
HELIX 950 971 {ECO:0000244|PDB:1K04}.
HELIX 972 974 {ECO:0000244|PDB:1K04}.
HELIX 977 979 {ECO:0000244|PDB:1K04}.
HELIX 980 1006 {ECO:0000244|PDB:1K04}.
TURN 1007 1009 {ECO:0000244|PDB:1K04}.
STRAND 1010 1012 {ECO:0000244|PDB:1K04}.
HELIX 1013 1045 {ECO:0000244|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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