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Focal adhesion kinase 1 (FADK 1) (EC 2.7.10.2) (Focal adhesion kinase-related nonkinase) (FRNK) (Protein-tyrosine kinase 2) (p125FAK) (pp125FAK)

 FAK1_MOUSE              Reviewed;        1090 AA.
P34152; O08578; Q5DTH7; Q8C513; Q8CFH7; Q8CHM2; Q8K2S0; Q9DAW3;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
20-MAY-2008, sequence version 3.
27-SEP-2017, entry version 201.
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-tyrosine kinase 2;
AltName: Full=p125FAK;
AltName: Full=pp125FAK;
Name=Ptk2; Synonyms=Fadk, Fak, Fak1, Kiaa4203;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), CATALYTIC ACTIVITY,
SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
STRAIN=BALB/cJ; TISSUE=Embryo;
PubMed=1528852; DOI=10.1073/pnas.89.18.8487;
Hanks S.K., Calalb M.B., Harper M.C., Patel S.K.;
"Focal adhesion protein-tyrosine kinase phosphorylated in response to
cell attachment to fibronectin.";
Proc. Natl. Acad. Sci. U.S.A. 89:8487-8491(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 7).
STRAIN=BALB/cJ; TISSUE=Brain, and Embryo;
Yamakawa N.;
"Focal adhesion kinase.";
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 8).
STRAIN=C57BL/6J; TISSUE=Placenta, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Fetal brain;
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene.
The complete nucleotide sequences of mouse KIAA-homologous cDNAs
identified by screening of terminal sequences of cDNA clones randomly
sampled from size-fractionated libraries.";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
STRAIN=Czech II; TISSUE=Mammary tumor;
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; 39-57; 77-86; 92-121; 132-177; 179-204;
210-218; 222-259; 313-319; 350-381; 465-492; 504-546; 589-616;
622-635; 666-703; 707-728; 735-762; 836-876; 885-971; 942-971;
980-993; 1001-1019 AND 1027-1082, PROTEIN SEQUENCE OF 386-451 (ISOFORM
3), CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2,
PHOSPHORYLATION AT SER-948, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryonic fibroblast;
Bienvenut W.V., Sandilands E., Serrels B., Brunton V.G., Sumpton D.P.,
Frame M.C.;
Submitted (MAR-2008) to UniProtKB.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 391-460 (ISOFORMS 1 AND 2).
STRAIN=ICR X Swiss Webster;
PubMed=9353341; DOI=10.1074/jbc.272.45.28720;
Burgaya F., Toutant M., Studler J.-M., Costa A., Le Bert M.,
Gelman M., Girault J.A.;
"Alternatively spliced focal adhesion kinase in rat brain with
increased autophosphorylation activity.";
J. Biol. Chem. 272:28720-28725(1997).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 391-417.
STRAIN=129/SvJ;
Asano H., Komiyama H.K., Grant S.G.;
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
[9]
FUNCTION IN INTEGRIN SIGNALING AND ACTIVATION OF MAP KINASES,
INTERACTION WITH GRB2; BCAR1; SHC1 AND SRC, PHOSPHORYLATION AT
TYR-963, AND MUTAGENESIS OF TYR-963.
PubMed=7997267; DOI=10.1038/372786a0;
Schlaepfer D.D., Hanks S.K., Hunter T., van der Geer P.;
"Integrin-mediated signal transduction linked to Ras pathway by GRB2
binding to focal adhesion kinase.";
Nature 372:786-791(1994).
[10]
INTERACTION WITH TLN1.
PubMed=7622520; DOI=10.1074/jbc.270.28.16995;
Chen H.C., Appeddu P.A., Parsons J.T., Hildebrand J.D., Schaller M.D.,
Guan J.L.;
"Interaction of focal adhesion kinase with cytoskeletal protein
talin.";
J. Biol. Chem. 270:16995-16999(1995).
[11]
PHOSPHORYLATION AT TYR-428; TYR-438; TYR-614 AND TYR-615,
AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-428 AND
614-TYR-615, AND ENZYME REGULATION.
PubMed=7529876; DOI=10.1128/MCB.15.2.954;
Calalb M.B., Polte T.R., Hanks S.K.;
"Tyrosine phosphorylation of focal adhesion kinase at sites in the
catalytic domain regulates kinase activity: a role for Src family
kinases.";
Mol. Cell. Biol. 15:954-963(1995).
[12]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=7478517;
Furuta Y., Ilic D., Kanazawa S., Takeda N., Yamamoto T., Aizawa S.;
"Mesodermal defect in late phase of gastrulation by a targeted
mutation of focal adhesion kinase, FAK.";
Oncogene 11:1989-1995(1995).
[13]
INTERACTION WITH PIK3R1, MUTAGENESIS OF TYR-428, AND PHOSPHORYLATION
AT TYR-428.
PubMed=8824286; DOI=10.1074/jbc.271.42.26329;
Chen H.C., Appeddu P.A., Isoda H., Guan J.L.;
"Phosphorylation of tyrosine 397 in focal adhesion kinase is required
for binding phosphatidylinositol 3-kinase.";
J. Biol. Chem. 271:26329-26334(1996).
[14]
PHOSPHORYLATION AT TYR-963, MUTAGENESIS OF TYR-963, AND INTERACTION
WITH GRB2.
PubMed=8816475; DOI=10.1128/MCB.16.10.5623;
Schlaepfer D.D., Hunter T.;
"Evidence for in vivo phosphorylation of the Grb2 SH2-domain binding
site on focal adhesion kinase by Src-family protein-tyrosine
kinases.";
Mol. Cell. Biol. 16:5623-5633(1996).
[15]
FUNCTION IN PHOSPHORYLATION OF SHC1 AND ACTIVATION OF MAPK1/ERK2,
PHOSPHORYLATION AT TYR-963, AND INTERACTION WITH GRB2.
PubMed=9148935; DOI=10.1074/jbc.272.20.13189;
Schlaepfer D.D., Hunter T.;
"Focal adhesion kinase overexpression enhances ras-dependent integrin
signaling to ERK2/mitogen-activated protein kinase through
interactions with and activation of c-Src.";
J. Biol. Chem. 272:13189-13195(1997).
[16]
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).
[17]
INTERACTION WITH SORBS1.
PubMed=9461600; DOI=10.1074/jbc.273.7.4073;
Ribon V., Herrera R., Kay B.K., Saltiel A.R.;
"A role for CAP, a novel, multifunctional Src homology 3 domain-
containing protein in formation of actin stress fibers and focal
adhesions.";
J. Biol. Chem. 273:4073-4080(1998).
[18]
INTERACTION WITH TGFB1I1.
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).
[19]
FUNCTION IN CELL SPREADING; MIGRATION AND PHOSPHORYLATION OF BCAR1,
CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF TYR-428 AND
614-TYR-TYR-615, AND PHOSPHORYLATION AT TYR-428; TYR-614 AND TYR-615.
PubMed=10373530; DOI=10.1128/MCB.19.7.4806;
Owen J.D., Ruest P.J., Fry D.W., Hanks S.K.;
"Induced focal adhesion kinase (FAK) expression in FAK-null cells
enhances cell spreading and migration requiring both auto- and
activation loop phosphorylation sites and inhibits adhesion-dependent
tyrosine phosphorylation of Pyk2.";
Mol. Cell. Biol. 19:4806-4818(1999).
[20]
INTERACTION WITH BCAR3.
PubMed=10896938; DOI=10.1074/jbc.M003074200;
Gotoh T., Cai D., Tian X., Feig L.A., Lerner A.;
"p130Cas regulates the activity of AND-34, a novel Ral, Rap1, and R-
Ras guanine nucleotide exchange factor.";
J. Biol. Chem. 275:30118-30123(2000).
[21]
FUNCTION, AND PHOSPHORYLATION AT TYR-428.
PubMed=10806474; DOI=10.1038/35010517;
Sieg D.J., Hauck C.R., Ilic D., Klingbeil C.K., Schaefer E.,
Damsky C.H., Schlaepfer D.D.;
"FAK integrates growth-factor and integrin signals to promote cell
migration.";
Nat. Cell Biol. 2:249-256(2000).
[22]
INTERACTION WITH STAT1, AND FUNCTION IN STAT1 PHOSPHORYLATION.
PubMed=11278462; DOI=10.1074/jbc.M009063200;
Xie B., Zhao J., Kitagawa M., Durbin J., Madri J.A., Guan J.L.,
Fu X.Y.;
"Focal adhesion kinase activates Stat1 in integrin-mediated cell
migration and adhesion.";
J. Biol. Chem. 276:19512-19523(2001).
[23]
FUNCTION IN PHOSPHORYLATION OF ACTN1.
PubMed=11369769; DOI=10.1074/jbc.M101678200;
Izaguirre G., Aguirre L., Hu Y.P., Lee H.Y., Schlaepfer D.D.,
Aneskievich B.J., Haimovich B.;
"The cytoskeletal/non-muscle isoform of alpha-actinin is
phosphorylated on its actin-binding domain by the focal adhesion
kinase.";
J. Biol. Chem. 276:28676-28685(2001).
[24]
PHOSPHORYLATION AT TYR-428; TYR-438; TYR-614; TYR-615; TYR-899 AND
TYR-963.
PubMed=11420674; DOI=10.1038/sj.onc.1204359;
Nakamura K., Yano H., Schaefer E., Sabe H.;
"Different modes and qualities of tyrosine phosphorylation of Fak and
Pyk2 during epithelial-mesenchymal transdifferentiation and cell
migration: analysis of specific phosphorylation events using site-
directed antibodies.";
Oncogene 20:2626-2635(2001).
[25]
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).
[26]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-770.
PubMed=12941275; DOI=10.1016/S0092-8674(03)00605-6;
Xie Z., Sanada K., Samuels B.A., Shih H., Tsai L.H.;
"Serine 732 phosphorylation of FAK by Cdk5 is important for
microtubule organization, nuclear movement, and neuronal migration.";
Cell 114:469-482(2003).
[27]
INTERACTION WITH SHB.
PubMed=12464388; DOI=10.1016/S0898-6568(02)00076-1;
Holmqvist K., Cross M.J., Riley D., Welsh M.;
"The Shb adaptor protein causes Src-dependent cell spreading and
activation of focal adhesion kinase in murine brain endothelial
cells.";
Cell. Signal. 15:171-179(2003).
[28]
FUNCTION, INTERACTION WITH ARHGEF28, AND MUTAGENESIS OF LEU-1072.
PubMed=12702722; DOI=10.1074/jbc.M302381200;
Zhai J., Lin H., Nie Z., Wu J., Canete-Soler R., Schlaepfer W.W.,
Schlaepfer D.D.;
"Direct interaction of focal adhesion kinase with p190RhoGEF.";
J. Biol. Chem. 278:24865-24873(2003).
[29]
INTERACTION WITH PIAS1.
PubMed=14500712; DOI=10.1074/jbc.M308562200;
Kadare G., Toutant M., Formstecher E., Corvol J.C., Carnaud M.,
Boutterin M.C., Girault J.A.;
"PIAS1-mediated sumoylation of focal adhesion kinase activates its
autophosphorylation.";
J. Biol. Chem. 278:47434-47440(2003).
[30]
INTERACTION WITH LPXN.
PubMed=12674328; DOI=10.1359/jbmr.2003.18.4.669;
Gupta A., Lee B.S., Khadeer M.A., Tang Z., Chellaiah M., Abu-Amer Y.,
Goldknopf J., Hruska K.A.;
"Leupaxin is a critical adaptor protein in the adhesion zone of the
osteoclast.";
J. Bone Miner. Res. 18:669-685(2003).
[31]
INTERACTION WITH WASL, AND PHOSPHORYLATION OF WASL.
PubMed=14676198; DOI=10.1074/jbc.M310739200;
Wu X., Suetsugu S., Cooper L.A., Takenawa T., Guan J.L.;
"Focal adhesion kinase regulation of N-WASP subcellular localization
and function.";
J. Biol. Chem. 279:9565-9576(2004).
[32]
INTERACTION WITH DCC.
PubMed=15494733; DOI=10.1038/nn1330;
Ren X.R., Ming G.L., Xie Y., Hong Y., Sun D.M., Zhao Z.Q., Feng Z.,
Wang Q., Shim S., Chen Z.F., Song H.J., Mei L., Xiong W.C.;
"Focal adhesion kinase in netrin-1 signaling.";
Nat. Neurosci. 7:1204-1212(2004).
[33]
INTERACTION WITH DCC.
PubMed=15494734; DOI=10.1038/nn1329;
Li W., Lee J., Vikis H.G., Lee S.H., Liu G., Aurandt J., Shen T.L.,
Fearon E.R., Guan J.L., Han M., Rao Y., Hong K., Guan K.L.;
"Activation of FAK and Src are receptor-proximal events required for
netrin signaling.";
Nat. Neurosci. 7:1213-1221(2004).
[34]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=15967814; DOI=10.1083/jcb.200411155;
Shen T.L., Park A.Y., Alcaraz A., Peng X., Jang I., Koni P.,
Flavell R.A., Gu H., Guan J.L.;
"Conditional knockout of focal adhesion kinase in endothelial cells
reveals its role in angiogenesis and vascular development in late
embryogenesis.";
J. Cell Biol. 169:941-952(2005).
[35]
FUNCTION.
PubMed=16000375; DOI=10.1091/mbc.E05-02-0131;
Brown M.C., Cary L.A., Jamieson J.S., Cooper J.A., Turner C.E.;
"Src and FAK kinases cooperate to phosphorylate paxillin kinase
linker, stimulate its focal adhesion localization, and regulate cell
spreading and protrusiveness.";
Mol. Biol. Cell 16:4316-4328(2005).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-397 (ISOFORMS 3; 4 AND
6), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[37]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=16391003; DOI=10.1083/jcb.200506184;
Braren R., Hu H., Kim Y.H., Beggs H.E., Reichardt L.F., Wang R.;
"Endothelial FAK is essential for vascular network stability, cell
survival, and lamellipodial formation.";
J. Cell Biol. 172:151-162(2006).
[38]
FUNCTION IN CELL SPREADING; PHOSPHORYLATION OF ARHGEF7; RAC1 TARGETING
TO FOCAL ADHESIONS AND RAC1 ACTIVATION, AND INTERACTION WITH ARHGEF7.
PubMed=17093062; DOI=10.1091/mbc.E06-03-0207;
Chang F., Lemmon C.A., Park D., Romer L.H.;
"FAK potentiates Rac1 activation and localization to matrix adhesion
sites: a role for betaPIX.";
Mol. Biol. Cell 18:253-264(2007).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-614 AND TYR-615, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[40]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-614; TYR-615 AND
TYR-963, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[41]
DISRUPTION PHENOTYPE, FUNCTION IN REGULATION OF P53/TP53 LEVELS; CELL
PROLIFERATION AND CELL SURVIVAL, INTERACTION WITH MDM2, 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).
[42]
DEVELOPMENTAL STAGE (ISOFORM 9).
PubMed=19372463; DOI=10.1161/CIRCRESAHA.109.195941;
DiMichele L.A., Hakim Z.S., Sayers R.L., Rojas M., Schwartz R.J.,
Mack C.P., Taylor J.M.;
"Transient expression of FRNK reveals stage-specific requirement for
focal adhesion kinase activity in cardiac growth.";
Circ. Res. 104:1201-1208(2009).
[43]
FUNCTION IN PHOSPHORYLATION OF GRB7, AND INTERACTION WITH GRB7.
PubMed=19473962; DOI=10.1074/jbc.M109.018259;
Chu P.Y., Huang L.Y., Hsu C.H., Liang C.C., Guan J.L., Hung T.H.,
Shen T.L.;
"Tyrosine phosphorylation of growth factor receptor-bound protein-7 by
focal adhesion kinase in the regulation of cell migration,
proliferation, and tumorigenesis.";
J. Biol. Chem. 284:20215-20226(2009).
[44]
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).
[45]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; TYR-614 AND TYR-615,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[46]
FUNCTION.
PubMed=22056317; DOI=10.1016/j.yjmcc.2011.10.015;
Clemente C.F., Xavier-Neto J., Dalla Costa A.P., Consonni S.R.,
Antunes J.E., Rocco S.A., Pereira M.B., Judice C.C., Strauss B.,
Joazeiro P.P., Matos-Souza J.R., Franchini K.G.;
"Focal adhesion kinase governs cardiac concentric hypertrophic growth
by activating the AKT and mTOR pathways.";
J. Mol. Cell. Cardiol. 52:493-501(2012).
[47]
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).
[48]
REVIEW ON FUNCTION; SUBUNIT; PHOSPHORYLATION AND ENZYME REGULATION.
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).
[49]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 959-1084, AND INTERACTION
WITH PXN.
PubMed=11799401; DOI=10.1038/nsb755;
Hayashi I., Vuori K., Liddington R.C.;
"The focal adhesion targeting (FAT) region of focal adhesion kinase is
a four-helix bundle that binds paxillin.";
Nat. Struct. Biol. 9:101-106(2002).
-!- 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 9 (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 (By similarity). {ECO:0000250,
ECO:0000269|PubMed:10373530, ECO:0000269|PubMed:10806474,
ECO:0000269|PubMed:11278462, ECO:0000269|PubMed:11369769,
ECO:0000269|PubMed:12702722, ECO:0000269|PubMed:12941275,
ECO:0000269|PubMed:15967814, ECO:0000269|PubMed:16000375,
ECO:0000269|PubMed:16391003, ECO:0000269|PubMed:17093062,
ECO:0000269|PubMed:18206965, ECO:0000269|PubMed:19147981,
ECO:0000269|PubMed:19473962, ECO:0000269|PubMed:22056317,
ECO:0000269|PubMed:7478517, ECO:0000269|PubMed:7997267,
ECO:0000269|PubMed:9148935}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:10373530,
ECO:0000269|PubMed:1528852, ECO:0000269|PubMed:7529876}.
-!- ENZYME REGULATION: Subject to autoinhibition, mediated by
interactions between the FERM domain and the kinase domain.
Activated by autophosphorylation at Tyr-428. This promotes
interaction with SRC and phosphorylation at Tyr-614 and Tyr-615 in
the kinase activation loop by SRC. Phosphorylation at Tyr-428,
Tyr-614 and Tyr-615 is required for maximal kinase activity.
{ECO:0000269|PubMed:7529876}.
-!- SUBUNIT: Interacts with GIT1. Component of a complex that contains
at least FER, CTTN and PTK2/FAK1. Interacts with BMX. Interacts
with STEAP4. Interacts with ZFYVE21. Interacts with ESR1.
Interacts with 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) (By similarity).
Interacts with MISP (By similarity). 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. Interacts with STAT1. Interacts
with WASL. Interacts with ARHGEF7. Interacts with DCC. Interacts
(via first Pro-rich region) with CAS family members (via SH3
domain), including BCAR1, BCAR3, CASS4 and NEDD9. Interacts with
SORBS1. Interacts with ARHGEF28. Interacts with SHB. Interacts
with PXN and TLN1. Interacts with TGFB1I1. Interacts with PIK3R1
or PIK3R2. Interacts with SRC, GRB2 and GRB7. Interacts with LPXN
(via LD motif 3). Interacts with CD36. Interacts with EMP2;
regulates PTK2 activation and localization (By similarity).
{ECO:0000250|UniProtKB:Q05397, ECO:0000269|PubMed:10896938,
ECO:0000269|PubMed:11278462, ECO:0000269|PubMed:11799401,
ECO:0000269|PubMed:12221124, ECO:0000269|PubMed:12464388,
ECO:0000269|PubMed:12674328, ECO:0000269|PubMed:12702722,
ECO:0000269|PubMed:14500712, ECO:0000269|PubMed:14676198,
ECO:0000269|PubMed:15494733, ECO:0000269|PubMed:15494734,
ECO:0000269|PubMed:17093062, ECO:0000269|PubMed:18206965,
ECO:0000269|PubMed:19473962, ECO:0000269|PubMed:7622520,
ECO:0000269|PubMed:7997267, ECO:0000269|PubMed:8816475,
ECO:0000269|PubMed:8824286, ECO:0000269|PubMed:9148935,
ECO:0000269|PubMed:9422762, ECO:0000269|PubMed:9461600,
ECO:0000269|PubMed:9756887}.
-!- INTERACTION:
Q61140:Bcar1; NbExp=3; IntAct=EBI-77070, EBI-77088;
P54763:Ephb2; NbExp=3; IntAct=EBI-77070, EBI-537711;
P62993:GRB2 (xeno); NbExp=3; IntAct=EBI-77070, EBI-401755;
P11627:L1cam; NbExp=4; IntAct=EBI-77070, EBI-397964;
P97333:Nrp1; NbExp=2; IntAct=EBI-77070, EBI-1555129;
P18031:PTPN1 (xeno); NbExp=2; IntAct=EBI-77070, EBI-968788;
Q8VI36:Pxn; NbExp=4; IntAct=EBI-77070, EBI-983394;
P12931:SRC (xeno); NbExp=2; IntAct=EBI-77070, EBI-621482;
-!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell
membrane; Peripheral membrane protein; Cytoplasmic side.
Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome. Nucleus
{ECO:0000250}. Note=Constituent of focal adhesions. Detected at
microtubules.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=9;
Name=1;
IsoId=P34152-1; Sequence=Displayed;
Name=2;
IsoId=P34152-2; Sequence=VSP_004976;
Name=3;
IsoId=P34152-3; Sequence=VSP_004975, VSP_004976;
Note=Peptide 386-413 identified and sequenced in Ref.6. Contains
a phosphotyrosine at position 397.
{ECO:0000244|PubMed:15592455};
Name=4;
IsoId=P34152-4; Sequence=VSP_004975, VSP_004976, VSP_034003;
Note=No experimental confirmation available. Contains a
phosphotyrosine at position 397. {ECO:0000244|PubMed:15592455};
Name=5;
IsoId=P34152-5; Sequence=VSP_033999, VSP_034004, VSP_034005;
Name=6;
IsoId=P34152-6; Sequence=VSP_004975, VSP_004976, VSP_034004,
VSP_034005;
Note=No experimental confirmation available. Ref.5 (BC030180)
sequence differs from that shown due to a stop codon in position
912 which was translated as Trp to extend the sequence. Contains
a phosphotyrosine at position 397. {ECO:0000244|PubMed:15592455,
ECO:0000305};
Name=7;
IsoId=P34152-7; Sequence=VSP_034000, VSP_034001, VSP_034002;
Note=No experimental confirmation available.;
Name=8;
IsoId=P34152-8; Sequence=VSP_033998;
Note=No experimental confirmation available.;
Name=9; Synonyms=FRNK;
IsoId=P34152-9; Sequence=VSP_042171;
Note=Produced by alternative promoter usage.;
-!- DEVELOPMENTAL STAGE: Isoform 9 is detected in neonate myocardium;
levels are low directly after birth, high five to fifteen days
after birth, and not detectable in adult (at protein level).
Isoform 9 is detected in neonate myocardium; levels are high
directly after birth, decrease during the first week of life and
are low thereafter.
-!- DOMAIN: The first Pro-rich domain interacts with the SH3 domain of
CAS family members, such as BCAR1 and NEDD9.
-!- DOMAIN: The C-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-428 is the major autophosphorylation
site, but other kinases can also phosphorylate this residue.
Phosphorylation at Tyr-428 promotes interaction with SRC and SRC
family members, leading to phosphorylation at Tyr-614, Tyr-615 and
at additional tyrosine residues. FGR promotes phosphorylation at
Tyr-428 and Tyr-614. FER promotes phosphorylation at Tyr-615, Tyr-
899 and Tyr-963, even when cells are not adherent. Tyr-428, Tyr-
614 and Ser-760 are phosphorylated only when cells are adherent.
Phosphorylation at Tyr-428 is important for interaction with BMX,
PIK3R1 and SHC1. Phosphorylation at Tyr-963 is important for
interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is
recruited to PTK2 via EPHA2 (tyrosine phosphorylated).
Microtubule-induced dephosphorylation at Tyr-428 is crucial for
the induction of focal adhesion disassembly; this
dephosphorylation could be catalyzed by PTPN11 and regulated by
ZFYVE21. {ECO:0000269|PubMed:10373530,
ECO:0000269|PubMed:10806474, ECO:0000269|PubMed:11420674,
ECO:0000269|PubMed:12941275, ECO:0000269|PubMed:14676198,
ECO:0000269|PubMed:1528852, ECO:0000269|PubMed:7529876,
ECO:0000269|PubMed:7997267, ECO:0000269|PubMed:8816475,
ECO:0000269|PubMed:8824286, ECO:0000269|PubMed:9148935,
ECO:0000269|Ref.6}.
-!- PTM: Sumoylated; this enhances autophosphorylation. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Embryonically lethal. Embryos die at about
8.5 dpc, despite normal implantation. Embryos do not develop a
normal head fold, neural tube or heart tube. Endothelial-specific
gene disruption is lethal at about 11 dpc, due to defects in
embryonic angiogenesis. {ECO:0000269|PubMed:15967814,
ECO:0000269|PubMed:16391003, ECO:0000269|PubMed:18206965,
ECO:0000269|PubMed:7478517}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. FAK subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=BAC37757.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAD90317.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; M95408; AAA37592.1; -; mRNA.
EMBL; AB030035; BAC53924.1; -; mRNA.
EMBL; AB011499; BAC53890.1; -; mRNA.
EMBL; AK005468; BAB24058.1; -; mRNA.
EMBL; AK079821; BAC37757.1; ALT_INIT; mRNA.
EMBL; AK220543; BAD90317.1; ALT_INIT; mRNA.
EMBL; BC030180; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AF025652; AAB95262.1; -; Genomic_DNA.
EMBL; AF025648; AAB95262.1; JOINED; Genomic_DNA.
EMBL; AF025649; AAB95262.1; JOINED; Genomic_DNA.
EMBL; AF025650; AAB95262.1; JOINED; Genomic_DNA.
EMBL; AF025651; AAB95262.1; JOINED; Genomic_DNA.
EMBL; AF025652; AAB95263.1; -; Genomic_DNA.
EMBL; AF025648; AAB95263.1; JOINED; Genomic_DNA.
EMBL; AF025649; AAB95263.1; JOINED; Genomic_DNA.
EMBL; AF025650; AAB95263.1; JOINED; Genomic_DNA.
EMBL; U77074; AAB51229.1; -; Genomic_DNA.
CCDS; CCDS37099.1; -. [P34152-3]
CCDS; CCDS49631.1; -. [P34152-6]
PIR; A46166; A46166.
RefSeq; NP_001123881.1; NM_001130409.1. [P34152-6]
RefSeq; NP_032008.2; NM_007982.2. [P34152-3]
RefSeq; XP_006520496.1; XM_006520433.2. [P34152-4]
UniGene; Mm.254494; -.
PDB; 1K40; X-ray; 2.25 A; A=959-1084.
PDB; 1KKY; Model; -; B=959-1084.
PDB; 1KL0; Model; -; A=959-1084.
PDB; 5F28; X-ray; 2.90 A; E/F/G=942-1090.
PDBsum; 1K40; -.
PDBsum; 1KKY; -.
PDBsum; 1KL0; -.
PDBsum; 5F28; -.
ProteinModelPortal; P34152; -.
SMR; P34152; -.
BioGrid; 199587; 11.
DIP; DIP-31045N; -.
ELM; P34152; -.
IntAct; P34152; 22.
MINT; MINT-141959; -.
STRING; 10090.ENSMUSP00000105663; -.
BindingDB; P34152; -.
ChEMBL; CHEMBL1075288; -.
iPTMnet; P34152; -.
PhosphoSitePlus; P34152; -.
SwissPalm; P34152; -.
MaxQB; P34152; -.
PaxDb; P34152; -.
PeptideAtlas; P34152; -.
PRIDE; P34152; -.
Ensembl; ENSMUST00000110036; ENSMUSP00000105663; ENSMUSG00000022607. [P34152-3]
Ensembl; ENSMUST00000170939; ENSMUSP00000126764; ENSMUSG00000022607. [P34152-6]
GeneID; 14083; -.
KEGG; mmu:14083; -.
UCSC; uc007wbw.2; mouse. [P34152-4]
UCSC; uc007wbx.2; mouse. [P34152-3]
UCSC; uc007wby.2; mouse. [P34152-5]
UCSC; uc007wbz.2; mouse. [P34152-6]
UCSC; uc007wca.1; mouse. [P34152-8]
CTD; 5747; -.
MGI; MGI:95481; Ptk2.
eggNOG; KOG4257; Eukaryota.
eggNOG; ENOG410ZH9Y; LUCA.
GeneTree; ENSGT00760000118799; -.
HOVERGEN; HBG004018; -.
InParanoid; P34152; -.
KO; K05725; -.
OMA; VQTNHYQ; -.
OrthoDB; EOG091G03BN; -.
PhylomeDB; P34152; -.
TreeFam; TF316643; -.
BRENDA; 2.7.10.2; 3474.
Reactome; R-MMU-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-MMU-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-MMU-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-MMU-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-MMU-375165; NCAM signaling for neurite out-growth.
Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
Reactome; R-MMU-3928663; EPHA-mediated growth cone collapse.
Reactome; R-MMU-418885; DCC mediated attractive signaling.
Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
Reactome; R-MMU-8874081; MET activates PTK2 signaling.
ChiTaRS; Ptk2; mouse.
EvolutionaryTrace; P34152; -.
PRO; PR:P34152; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000022607; -.
CleanEx; MM_PTK2; -.
Genevisible; P34152; MM.
GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
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; IDA:MGI.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0001725; C:stress fiber; ISO:MGI.
GO; GO:0003779; F:actin binding; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008432; F:JUN kinase binding; ISO:MGI.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IMP:UniProtKB.
GO; GO:0004672; F:protein kinase activity; TAS:Reactome.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0005102; F:receptor binding; IBA:GO_Central.
GO; GO:0042169; F:SH2 domain binding; ISO:MGI.
GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
GO; GO:0001525; P:angiogenesis; IMP:MGI.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0001568; P:blood vessel development; IMP:MGI.
GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:MGI.
GO; GO:0021955; P:central nervous system neuron axonogenesis; IMP:MGI.
GO; GO:0043542; P:endothelial cell migration; IMP:MGI.
GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IBA:GO_Central.
GO; GO:0040023; P:establishment of nucleus localization; IDA:MGI.
GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
GO; GO:0060396; P:growth hormone receptor signaling pathway; ISO:MGI.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:MGI.
GO; GO:2000811; P:negative regulation of anoikis; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0050771; P:negative regulation of axonogenesis; IMP:MGI.
GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISO:MGI.
GO; GO:0046621; P:negative regulation of organ growth; IGI:MGI.
GO; GO:0051964; P:negative regulation of synapse assembly; IMP:MGI.
GO; GO:0001764; P:neuron migration; IDA:MGI.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:2000060; P:positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
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; ISS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
GO; GO:0010632; P:regulation of epithelial cell migration; ISO:MGI.
GO; GO:0051893; P:regulation of focal adhesion assembly; ISO:MGI.
GO; GO:0045667; P:regulation of osteoblast differentiation; ISS:UniProtKB.
GO; GO:0001932; P:regulation of protein phosphorylation; ISO:MGI.
GO; GO:1900024; P:regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
GO; GO:0007172; P:signal complex assembly; IEA:InterPro.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:MGI.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0001570; P:vasculogenesis; IMP:MGI.
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;
Reference proteome; Transferase; Tyrosine-protein kinase;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.6}.
CHAIN 2 1090 Focal adhesion kinase 1.
/FTId=PRO_0000088078.
DOMAIN 35 355 FERM. {ECO:0000255|PROSITE-
ProRule:PRU00084}.
DOMAIN 469 718 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 466 472 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 538 540 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 745 1090 Interaction with TGFB1I1. {ECO:0000250}.
REGION 950 1090 Interaction with ARHGEF28.
{ECO:0000269|PubMed:12702722}.
COMPBIAS 750 771 Pro-rich.
COMPBIAS 901 951 Pro-rich.
ACT_SITE 584 584 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 492 492 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.6}.
MOD_RES 5 5 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q05397}.
MOD_RES 13 13 Phosphothreonine.
{ECO:0000250|UniProtKB:Q05397}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000250|UniProtKB:Q05397}.
MOD_RES 54 54 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 428 428 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:10373530,
ECO:0000269|PubMed:10806474,
ECO:0000269|PubMed:11420674,
ECO:0000269|PubMed:7529876,
ECO:0000269|PubMed:8824286}.
MOD_RES 438 438 Phosphotyrosine.
{ECO:0000269|PubMed:11420674,
ECO:0000269|PubMed:7529876}.
MOD_RES 608 608 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q05397}.
MOD_RES 614 614 Phosphotyrosine; by RET and SRC.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:18034455,
ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:10373530,
ECO:0000269|PubMed:11420674,
ECO:0000269|PubMed:7529876}.
MOD_RES 615 615 Phosphotyrosine; by RET and SRC.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:18034455,
ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:10373530,
ECO:0000269|PubMed:11420674,
ECO:0000269|PubMed:7529876}.
MOD_RES 618 618 Phosphoserine.
{ECO:0000250|UniProtKB:Q05397}.
MOD_RES 760 760 Phosphoserine.
{ECO:0000250|UniProtKB:Q05397}.
MOD_RES 770 770 Phosphoserine; by CDK5.
{ECO:0000269|PubMed:12941275}.
MOD_RES 881 881 Phosphoserine.
{ECO:0000250|UniProtKB:Q05397}.
MOD_RES 899 899 Phosphotyrosine.
{ECO:0000269|PubMed:11420674}.
MOD_RES 948 948 Phosphoserine. {ECO:0000269|Ref.6}.
MOD_RES 952 952 Phosphothreonine.
{ECO:0000250|UniProtKB:Q05397}.
MOD_RES 963 963 Phosphotyrosine; by SRC.
{ECO:0000244|PubMed:18034455,
ECO:0000269|PubMed:11420674,
ECO:0000269|PubMed:7997267,
ECO:0000269|PubMed:8816475,
ECO:0000269|PubMed:9148935}.
CROSSLNK 152 152 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
VAR_SEQ 1 730 Missing (in isoform 9). {ECO:0000305}.
/FTId=VSP_042171.
VAR_SEQ 199 1090 Missing (in isoform 8).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_033998.
VAR_SEQ 392 392 S -> SGVS (in isoform 5).
{ECO:0000303|Ref.2}.
/FTId=VSP_033999.
VAR_SEQ 393 423 Missing (in isoform 3, isoform 4 and
isoform 6). {ECO:0000303|PubMed:1528852,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|Ref.4}.
/FTId=VSP_004975.
VAR_SEQ 393 417 Missing (in isoform 7).
{ECO:0000303|Ref.2}.
/FTId=VSP_034000.
VAR_SEQ 443 450 KSYGIDEA -> T (in isoform 2, isoform 3,
isoform 4 and isoform 6).
{ECO:0000303|PubMed:1528852,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|Ref.4}.
/FTId=VSP_004976.
VAR_SEQ 511 534 LTMRQFDHPHIVKLIGVITENPVW -> SEVIFASKKIQLG
PGIFDIICLSA (in isoform 7).
{ECO:0000303|Ref.2}.
/FTId=VSP_034001.
VAR_SEQ 535 1090 Missing (in isoform 7).
{ECO:0000303|Ref.2}.
/FTId=VSP_034002.
VAR_SEQ 941 941 K -> KPWR (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_034003.
VAR_SEQ 942 954 LQPQEISPPPTAN -> VGICACAMWSVPC (in
isoform 5 and isoform 6).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2}.
/FTId=VSP_034004.
VAR_SEQ 955 1090 Missing (in isoform 5 and isoform 6).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2}.
/FTId=VSP_034005.
MUTAGEN 428 428 Y->F: Strongly reduced enzyme activity;
when associated with 614-F-F-615.
Abolishes activation of MAPK1/ERK2 in
response to integrin signaling. Abolishes
activation of SRC. Abolishes interaction
with PIK3R1.
{ECO:0000269|PubMed:10373530,
ECO:0000269|PubMed:7529876,
ECO:0000269|PubMed:8824286}.
MUTAGEN 614 615 YY->FF: Strongly reduced enzyme activity;
when associated with F-428.
{ECO:0000269|PubMed:10373530,
ECO:0000269|PubMed:7529876}.
MUTAGEN 963 963 Y->F: Abolishes interaction with GRB2.
{ECO:0000269|PubMed:7997267,
ECO:0000269|PubMed:8816475}.
MUTAGEN 1072 1072 L->S: Loss of interaction with ARHGEF28.
{ECO:0000269|PubMed:12702722}.
CONFLICT 32 32 A -> T (in Ref. 5; BC030180).
{ECO:0000305}.
CONFLICT 42 42 Y -> H (in Ref. 1; AAA37592).
{ECO:0000305}.
CONFLICT 87 87 L -> V (in Ref. 3; BAB24058).
{ECO:0000305}.
CONFLICT 128 128 Y -> D (in Ref. 3; BAB24058).
{ECO:0000305}.
CONFLICT 146 146 F -> V (in Ref. 3; BAB24058).
{ECO:0000305}.
CONFLICT 157 157 Q -> L (in Ref. 5; BC030180).
{ECO:0000305}.
CONFLICT 225 225 Q -> H (in Ref. 3; BAC37757).
{ECO:0000305}.
CONFLICT 250 250 V -> M (in Ref. 3; BAC37757).
{ECO:0000305}.
CONFLICT 800 800 Q -> P (in Ref. 5; BC030180).
{ECO:0000305}.
HELIX 960 980 {ECO:0000244|PDB:1K40}.
HELIX 985 987 {ECO:0000244|PDB:1K40}.
HELIX 989 1009 {ECO:0000244|PDB:1K40}.
HELIX 1010 1012 {ECO:0000244|PDB:1K40}.
HELIX 1015 1017 {ECO:0000244|PDB:5F28}.
HELIX 1018 1044 {ECO:0000244|PDB:1K40}.
HELIX 1048 1081 {ECO:0000244|PDB:1K40}.
SEQUENCE 1090 AA; 123537 MW; 7C795105A9B9DCA6 CRC64;
MAAAYLDPNL NHTPSSSTKT HLGTGMERSP GAMERVLKVF HYFESSSEPT TWASIIRHGD
ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW
KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMQEIA DQVDQEIALK LGCLEIRRSY
WEMRGNALEK KSNYEVLEKD VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI
LKFFEILSPV YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFNQVQ
TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL VNGATQSFII
RPQKEGERAL PSIPKLANSE KQGMRTHAVS VSHCQHKVKK ARRFLPLVFC SLEPPPTDEI
SGDETDDYAE IIDEEDTYTM PSKSYGIDEA RDYEIQRERI ELGRCIGEGQ FGDVHQGVYL
SPENPALAVA IKTCKNCTSD SVREKFLQEA LTMRQFDHPH IVKLIGVITE NPVWIIMELC
TLGELRSFLQ VRKYSLDLAS LILYAYQLST ALAYLESKRF VHRDIAARNV LVSSNDCVKL
GDFGLSRYME DSTYYKASKG KLPIKWMAPE SINFRRFTSA SDVWMFGVCM WEILMHGVKP
FQGVKNNDVI GRIENGERLP MPPNCPPTLY SLMTKCWAYD PSRRPRFTEL KAQLSTILEE
EKVQQEERMR MESRRQATVS WDSGGSDEAP PKPSRPGYPS PRSSEGFYPS PQHMVQTNHY
QVSGYPGSHG IPAMAGSIYQ GQASLLDQTE LWNHRPQEMS MWQPSVEDSA ALDLRGMGQV
LPPHLMEERL IRQQQEMEED QRWLEKEERF LKPDVRLSRG SIDREDGSFQ GPTGNQHIYQ
PVGKPDPAAP PKKPPRPGAP GHLSNLSSIS SPADSYNEGV KLQPQEISPP PTANLDRSND
KVYENVTGLV KAVIEMSSKI QPAPPEEYVP MVKEVGLALR TLLATVDETI PALPASTHRE
IEMAQKLLNS DLGELISKMK LAQQYVMTSL QQEYKKQMLT AAHALAVDAK NLLDVIDQAR
LKMLGQTRPH


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