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Focal adhesion kinase 1 (FADK 1) (EC 2.7.10.2) (Focal adhesion kinase-related nonkinase) (FRNK) (p41/p43FRNK) (Protein-tyrosine kinase 2) (p125FAK) (pp125FAK)

 FAK1_CHICK              Reviewed;        1053 AA.
Q00944;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 2.
20-JUN-2018, entry version 176.
RecName: Full=Focal adhesion kinase 1;
Short=FADK 1;
EC=2.7.10.2;
AltName: Full=Focal adhesion kinase-related nonkinase;
Short=FRNK;
Short=p41/p43FRNK;
AltName: Full=Protein-tyrosine kinase 2;
AltName: Full=p125FAK;
AltName: Full=pp125FAK;
Name=PTK2; Synonyms=FAK, FAK1;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 26-1053 (ISOFORM 1).
TISSUE=Embryo;
PubMed=1594631; DOI=10.1073/pnas.89.11.5192;
Schaller M.D., Borgman C.A., Cobb B.S., Vines R.R., Reynolds A.B.,
Parsons J.T.;
"pp125FAK a structurally distinctive protein-tyrosine kinase
associated with focal adhesions.";
Proc. Natl. Acad. Sci. U.S.A. 89:5192-5196(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-63 (ISOFORM 1).
TISSUE=Embryo;
PubMed=8439308; DOI=10.1006/bbrc.1993.1160;
Devor B.B., Zhang X., Patel S.K., Polte T.R., Hanks S.K.;
"Chicken and mouse focal adhesion kinases are similar in structure at
their amino termini.";
Biochem. Biophys. Res. Commun. 190:1084-1089(1993).
[3]
ALTERNATIVE PROMOTER USAGE, IDENTIFICATION OF ISOFORM 2,
PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=8423801; DOI=10.1128/MCB.13.2.785;
Schaller M.D., Borgman C.A., Parsons J.T.;
"Autonomous expression of a noncatalytic domain of the focal adhesion-
associated protein tyrosine kinase pp125FAK.";
Mol. Cell. Biol. 13:785-791(1993).
[4]
INTERACTION WITH ARHGAP26.
PubMed=8649427; DOI=10.1128/MCB.16.6.3169;
Hildebrand J.D., Taylor J.M., Parsons J.T.;
"An SH3 domain-containing GTPase-activating protein for Rho and Cdc42
associates with focal adhesion kinase.";
Mol. Cell. Biol. 16:3169-3178(1996).
[5]
INTERACTION WITH PIK3R1 AND SRC, AND MUTAGENESIS OF ASP-395.
PubMed=10212207; DOI=10.1074/jbc.274.18.12361;
Reiske H.R., Kao S.C., Cary L.A., Guan J.L., Lai J.F., Chen H.C.;
"Requirement of phosphatidylinositol 3-kinase in focal adhesion
kinase-promoted cell migration.";
J. Biol. Chem. 274:12361-12366(1999).
[6]
INTERACTION WITH GRB7.
PubMed=12021278; DOI=10.1074/jbc.M203085200;
Shen T.L., Han D.C., Guan J.L.;
"Association of Grb7 with phosphoinositides and its role in the
regulation of cell migration.";
J. Biol. Chem. 277:29069-29077(2002).
[7]
PHOSPHORYLATION AT TYR-397; TYR-576 AND TYR-863.
PubMed=12370821; DOI=10.1038/sj.onc.1205904;
Leu T.H., Maa M.C.;
"Tyr-863 phosphorylation enhances focal adhesion kinase
autophosphorylation at Tyr-397.";
Oncogene 21:6992-7000(2002).
[8]
FUNCTION, AND 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).
[9]
FUNCTION, AND 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).
[10]
FUNCTION.
PubMed=15494732; DOI=10.1038/nn1331;
Liu G., Beggs H., Jurgensen C., Park H.T., Tang H., Gorski J.,
Jones K.R., Reichardt L.F., Wu J., Rao Y.;
"Netrin requires focal adhesion kinase and Src family kinases for axon
outgrowth and attraction.";
Nat. Neurosci. 7:1222-1232(2004).
[11]
INTERACTION WITH THE ARP2/3 COMPLEX.
PubMed=17721515; DOI=10.1038/ncb1626;
Serrels B., Serrels A., Brunton V.G., Holt M., McLean G.W., Gray C.H.,
Jones G.E., Frame M.C.;
"Focal adhesion kinase controls actin assembly via a FERM-mediated
interaction with the Arp2/3 complex.";
Nat. Cell Biol. 9:1046-1056(2007).
[12]
FUNCTION.
PubMed=20705914; DOI=10.1161/ATVBAHA.110.212761;
Koshman Y.E., Kim T., Chu M., Engman S.J., Iyengar R., Robia S.L.,
Samarel A.M.;
"FRNK inhibition of focal adhesion kinase-dependent signaling and
migration in vascular smooth muscle cells.";
Arterioscler. Thromb. Vasc. Biol. 30:2226-2233(2010).
[13]
FUNCTION.
PubMed=21852560; DOI=10.1161/ATVBAHA.111.235549;
Koshman Y.E., Chu M., Engman S.J., Kim T., Iyengar R., Robia S.L.,
Samarel A.M.;
"Focal adhesion kinase-related nonkinase inhibits vascular smooth
muscle cell invasion by focal adhesion targeting, tyrosine 168
phosphorylation, and competition for p130Cas Binding.";
Arterioscler. Thromb. Vasc. Biol. 31:2432-2440(2011).
[14]
PHOSPHORYLATION AT SER-911, AND FUNCTION.
PubMed=21937583; DOI=10.1093/cvr/cvr247;
Chu M., Iyengar R., Koshman Y.E., Kim T., Russell B., Martin J.L.,
Heroux A.L., Robia S.L., Samarel A.M.;
"Serine-910 phosphorylation of focal adhesion kinase is critical for
sarcomere reorganization in cardiomyocyte hypertrophy.";
Cardiovasc. Res. 92:409-419(2011).
[15]
STRUCTURE BY NMR OF 916-1053.
PubMed=11909967; DOI=10.1128/MCB.22.8.2751-2760.2002;
Liu G., Guibao C.D., Zheng J.;
"Structural insight into the mechanisms of targeting and signaling of
focal adhesion kinase.";
Mol. Cell. Biol. 22:2751-2760(2002).
[16]
STRUCTURE BY NMR OF 920-1053 IN COMPLEX WITH PXN, AND INTERACTION WITH
PXN.
PubMed=14662767; DOI=10.1074/jbc.M309808200;
Gao G., Prutzman K.C., King M.L., Scheswohl D.M., DeRose E.F.,
London R.E., Schaller M.D., Campbell S.L.;
"NMR solution structure of the focal adhesion targeting domain of
focal adhesion kinase in complex with a paxillin LD peptide: evidence
for a two-site binding model.";
J. Biol. Chem. 279:8441-8451(2004).
[17]
STRUCTURE BY NMR OF 920-1053.
PubMed=15130480; DOI=10.1016/j.str.2004.02.028;
Prutzman K.C., Gao G., King M.L., Iyer V.V., Mueller G.A.,
Schaller M.D., Campbell S.L.;
"The focal adhesion targeting domain of focal adhesion kinase contains
a hinge region that modulates tyrosine 926 phosphorylation.";
Structure 12:881-891(2004).
[18]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 31-405.
PubMed=16221668; DOI=10.1074/jbc.M509188200;
Ceccarelli D.F., Song H.K., Poy F., Schaller M.D., Eck M.J.;
"Crystal structure of the FERM domain of focal adhesion kinase.";
J. Biol. Chem. 281:252-259(2006).
[19]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 411-686 IN COMPLEXES WITH
STAUROSPORINE AND ATP ANALOG, ENZYME REGULATION, AND PHOSPHORYLATION
AT TYR-576 AND TYR-577.
PubMed=17574028; DOI=10.1016/j.cell.2007.05.041;
Lietha D., Cai X., Ceccarelli D.F., Li Y., Schaller M.D., Eck M.J.;
"Structural basis for the autoinhibition of focal adhesion kinase.";
Cell 129:1177-1187(2007).
[20]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 411-686 IN COMPLEX WITH
TAE226.
PubMed=19030106; DOI=10.1371/journal.pone.0003800;
Lietha D., Eck M.J.;
"Crystal structures of the FAK kinase in complex with TAE226 and
related bis-anilino pyrimidine inhibitors reveal a helical DFG
conformation.";
PLoS ONE 3:E3800-E3800(2008).
-!- 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, 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), ephrin
receptors, 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. Regulates P53/TP53 activity and
stability. Phosphorylates SRC; this increases SRC kinase activity.
Isoform 2 (FRNK) does not contain a kinase domain and inhibits
PTK2/FAK1 phosphorylation and signaling.
{ECO:0000269|PubMed:15494732, ECO:0000269|PubMed:15494733,
ECO:0000269|PubMed:15494734, ECO:0000269|PubMed:20705914,
ECO:0000269|PubMed:21852560, ECO:0000269|PubMed:21937583}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- 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 TAE226.
{ECO:0000269|PubMed:17574028}.
-!- SUBUNIT: Interacts with ARHGAP26, GRB7, DCC, PIK3R1, PXN and SRC.
Interacts with the ARP2/3 complex. {ECO:0000269|PubMed:10212207,
ECO:0000269|PubMed:12021278, ECO:0000269|PubMed:14662767,
ECO:0000269|PubMed:15494733, ECO:0000269|PubMed:15494734,
ECO:0000269|PubMed:17721515, ECO:0000269|PubMed:19030106,
ECO:0000269|PubMed:8649427}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-2896409, EBI-2896409;
P61157:ACTR3 (xeno); NbExp=5; IntAct=EBI-2896409, EBI-351419;
P08581:MET (xeno); NbExp=5; IntAct=EBI-2896409, EBI-1039152;
P49024:PXN; NbExp=2; IntAct=EBI-2896409, EBI-2896280;
P00523:SRC; NbExp=3; IntAct=EBI-2896409, EBI-848039;
-!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
{ECO:0000269|PubMed:8423801}. Cell membrane
{ECO:0000269|PubMed:8423801}; Peripheral membrane protein
{ECO:0000269|PubMed:8423801}; Cytoplasmic side
{ECO:0000269|PubMed:8423801}. Cytoplasm, perinuclear region
{ECO:0000269|PubMed:8423801}. Cytoplasm, cytoskeleton
{ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing
center, centrosome {ECO:0000250}. Nucleus
{ECO:0000269|PubMed:8423801}. Note=Constituent of focal adhesions.
Detected at microtubules (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage; Named isoforms=2;
Name=1;
IsoId=Q00944-1; Sequence=Displayed;
Name=2; Synonyms=FRNK;
IsoId=Q00944-2; Sequence=VSP_042173;
-!- 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. Isoform 2 is phosphorylated on
serine or threonine residues, but apparently not on tyrosine
residues. {ECO:0000269|PubMed:12370821,
ECO:0000269|PubMed:17574028, ECO:0000269|PubMed:21937583,
ECO:0000269|PubMed:8423801}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. FAK subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; M86656; AAA48765.1; -; mRNA.
EMBL; L08402; AAA48766.1; -; mRNA.
PIR; A45388; A45388.
PIR; PC1239; PC1239.
RefSeq; NP_990766.1; NM_205435.1. [Q00944-1]
UniGene; Gga.15614; -.
PDB; 1KTM; NMR; -; A=916-1053.
PDB; 1PV3; NMR; -; A=920-1053.
PDB; 1QVX; NMR; -; A=920-1053.
PDB; 2AEH; X-ray; 2.53 A; A/B=31-399.
PDB; 2AL6; X-ray; 2.35 A; A/B=31-405.
PDB; 2J0J; X-ray; 2.80 A; A=31-686.
PDB; 2J0K; X-ray; 3.00 A; A/B=31-686.
PDB; 2J0L; X-ray; 2.30 A; A=411-686.
PDB; 2J0M; X-ray; 2.80 A; A=31-399, B=411-686.
PDB; 2JKK; X-ray; 2.00 A; A=411-686.
PDB; 2JKM; X-ray; 2.31 A; A=411-686.
PDB; 2JKO; X-ray; 1.65 A; A=411-686.
PDB; 2JKQ; X-ray; 2.60 A; A=411-686.
PDB; 2L6F; NMR; -; A=916-1053.
PDB; 2L6G; NMR; -; A=916-1053.
PDB; 2L6H; NMR; -; A=916-1053.
PDB; 3ZDT; X-ray; 3.15 A; A/B=31-405.
PDB; 4BRX; X-ray; 2.05 A; A=411-686.
PDB; 4C7T; X-ray; 2.05 A; A=411-686.
PDB; 4CYE; X-ray; 3.20 A; A/B=31-405.
PDB; 4D4R; X-ray; 1.55 A; A/B=411-686.
PDB; 4D4S; X-ray; 2.00 A; A/B=411-686.
PDB; 4D4V; X-ray; 2.10 A; A/B=411-686.
PDB; 4D4Y; X-ray; 1.80 A; A/B=411-686.
PDB; 4D55; X-ray; 2.30 A; A=411-686.
PDB; 4D58; X-ray; 1.95 A; A/B=411-686.
PDB; 4D5H; X-ray; 1.75 A; A/B=411-686.
PDB; 4D5K; X-ray; 1.75 A; A/B=411-686.
PDBsum; 1KTM; -.
PDBsum; 1PV3; -.
PDBsum; 1QVX; -.
PDBsum; 2AEH; -.
PDBsum; 2AL6; -.
PDBsum; 2J0J; -.
PDBsum; 2J0K; -.
PDBsum; 2J0L; -.
PDBsum; 2J0M; -.
PDBsum; 2JKK; -.
PDBsum; 2JKM; -.
PDBsum; 2JKO; -.
PDBsum; 2JKQ; -.
PDBsum; 2L6F; -.
PDBsum; 2L6G; -.
PDBsum; 2L6H; -.
PDBsum; 3ZDT; -.
PDBsum; 4BRX; -.
PDBsum; 4C7T; -.
PDBsum; 4CYE; -.
PDBsum; 4D4R; -.
PDBsum; 4D4S; -.
PDBsum; 4D4V; -.
PDBsum; 4D4Y; -.
PDBsum; 4D55; -.
PDBsum; 4D58; -.
PDBsum; 4D5H; -.
PDBsum; 4D5K; -.
ProteinModelPortal; Q00944; -.
SMR; Q00944; -.
BioGrid; 676665; 2.
ELM; Q00944; -.
IntAct; Q00944; 11.
STRING; 9031.ENSGALP00000026014; -.
iPTMnet; Q00944; -.
PaxDb; Q00944; -.
PRIDE; Q00944; -.
Ensembl; ENSGALT00000072414; ENSGALP00000044406; ENSGALG00000031741. [Q00944-1]
GeneID; 396416; -.
KEGG; gga:396416; -.
CTD; 5747; -.
eggNOG; KOG4257; Eukaryota.
eggNOG; ENOG410ZH9Y; LUCA.
GeneTree; ENSGT00760000118799; -.
HOGENOM; HOG000069938; -.
HOVERGEN; HBG004018; -.
InParanoid; Q00944; -.
KO; K05725; -.
OMA; VQTNHYQ; -.
OrthoDB; EOG091G03BN; -.
PhylomeDB; Q00944; -.
BRENDA; 2.7.10.2; 1306.
Reactome; R-GGA-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-GGA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-GGA-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-GGA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-GGA-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-GGA-375165; NCAM signaling for neurite out-growth.
Reactome; R-GGA-3928662; EPHB-mediated forward signaling.
Reactome; R-GGA-418885; DCC mediated attractive signaling.
Reactome; R-GGA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-GGA-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-GGA-5673001; RAF/MAP kinase cascade.
Reactome; R-GGA-8874081; MET activates PTK2 signaling.
EvolutionaryTrace; Q00944; -.
PRO; PR:Q00944; -.
Proteomes; UP000000539; Chromosome 2.
Bgee; ENSGALG00000016171; -.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0005623; C:cell; IDA:AgBase.
GO; GO:0005737; C:cytoplasm; IDA:AgBase.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005925; C:focal adhesion; IDA:AgBase.
GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0042383; C:sarcolemma; IDA:AgBase.
GO; GO:0001725; C:stress fiber; IEA:Ensembl.
GO; GO:0003779; F:actin binding; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IMP:AgBase.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005178; F:integrin binding; IPI:AgBase.
GO; GO:0008432; F:JUN kinase binding; IEA:Ensembl.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0002020; F:protease binding; IPI:AgBase.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:AgBase.
GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
GO; GO:0007015; P:actin filament organization; IMP:AgBase.
GO; GO:0060055; P:angiogenesis involved in wound healing; IMP:AgBase.
GO; GO:0021955; P:central nervous system neuron axonogenesis; IEA:Ensembl.
GO; GO:0043542; P:endothelial cell migration; IEA:Ensembl.
GO; GO:0048013; P:ephrin receptor signaling pathway; IEA:Ensembl.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IBA:GO_Central.
GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
GO; GO:0060396; P:growth hormone receptor signaling pathway; IEA:Ensembl.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
GO; GO:2000811; P:negative regulation of anoikis; IMP:AgBase.
GO; GO:0010507; P:negative regulation of autophagy; IEA:Ensembl.
GO; GO:0050771; P:negative regulation of axonogenesis; IEA:Ensembl.
GO; GO:0022408; P:negative regulation of cell-cell adhesion; IEA:Ensembl.
GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IMP:AgBase.
GO; GO:0046621; P:negative regulation of organ growth; IEA:Ensembl.
GO; GO:0031953; P:negative regulation of protein autophosphorylation; IMP:AgBase.
GO; GO:0051964; P:negative regulation of synapse assembly; IEA:Ensembl.
GO; GO:0007097; P:nuclear migration; IEA:Ensembl.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:AgBase.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; IMP:AgBase.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
GO; GO:0032092; P:positive regulation of protein binding; IMP:AgBase.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IMP:AgBase.
GO; GO:1904237; P:positive regulation of substrate-dependent cell migration, cell attachment to substrate; IMP:AgBase.
GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IDA:AgBase.
GO; GO:0021852; P:pyramidal neuron migration; IMP:AgBase.
GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IEA:Ensembl.
GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
GO; GO:0010632; P:regulation of epithelial cell migration; IEA:Ensembl.
GO; GO:0045667; P:regulation of osteoblast differentiation; IEA:Ensembl.
GO; GO:1900024; P:regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
GO; GO:0035994; P:response to muscle stretch; IDA:AgBase.
GO; GO:0009268; P:response to pH; IMP:AgBase.
GO; GO:0007172; P:signal complex assembly; IEA:InterPro.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
GO; GO:0044319; P:wound healing, spreading of cells; IMP:AgBase.
CDD; cd14473; FERM_B-lobe; 1.
Gene3D; 1.20.80.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR019749; Band_41_domain.
InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
InterPro; IPR035963; FERM_2.
InterPro; IPR019748; FERM_central.
InterPro; IPR000299; FERM_domain.
InterPro; IPR036137; Focal_adhe_kin_target_dom_sf.
InterPro; IPR005189; Focal_adhesion_kin_target_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR029071; Ubiquitin-like_domsf.
Pfam; PF00373; FERM_M; 1.
Pfam; 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; 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; Alternative promoter usage; Angiogenesis; ATP-binding;
Cell junction; Cell membrane; Complete proteome; Cytoplasm;
Cytoskeleton; Developmental protein; Kinase; Membrane;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Transferase; Tyrosine-protein kinase.
CHAIN 1 1053 Focal adhesion kinase 1.
/FTId=PRO_0000088076.
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:0000305}.
NP_BIND 500 502 ATP. {ECO:0000305}.
COMPBIAS 712 733 Pro-rich.
COMPBIAS 865 914 Pro-rich.
ACT_SITE 546 546 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 454 454 ATP. {ECO:0000305}.
MOD_RES 397 397 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12370821}.
MOD_RES 407 407 Phosphotyrosine. {ECO:0000250}.
MOD_RES 576 576 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:12370821,
ECO:0000269|PubMed:17574028}.
MOD_RES 577 577 Phosphotyrosine; by SRC. {ECO:0000250}.
MOD_RES 863 863 Phosphotyrosine.
{ECO:0000269|PubMed:12370821}.
MOD_RES 911 911 Phosphoserine.
{ECO:0000269|PubMed:21937583}.
MOD_RES 926 926 Phosphotyrosine. {ECO:0000250}.
VAR_SEQ 1 692 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_042173.
MUTAGEN 395 395 D->A: Abolishes interaction with PIK3R1.
{ECO:0000269|PubMed:10212207}.
STRAND 36 40 {ECO:0000244|PDB:2AL6}.
HELIX 49 51 {ECO:0000244|PDB:2AL6}.
STRAND 53 58 {ECO:0000244|PDB:2AL6}.
HELIX 64 74 {ECO:0000244|PDB:2AL6}.
HELIX 80 82 {ECO:0000244|PDB:2AL6}.
STRAND 83 89 {ECO:0000244|PDB:2AL6}.
STRAND 95 98 {ECO:0000244|PDB:2AL6}.
STRAND 100 103 {ECO:0000244|PDB:2J0M}.
HELIX 104 112 {ECO:0000244|PDB:2AL6}.
HELIX 117 119 {ECO:0000244|PDB:2AL6}.
STRAND 120 126 {ECO:0000244|PDB:2AL6}.
HELIX 133 137 {ECO:0000244|PDB:2AL6}.
HELIX 141 158 {ECO:0000244|PDB:2AL6}.
TURN 159 162 {ECO:0000244|PDB:2AL6}.
HELIX 165 179 {ECO:0000244|PDB:2AL6}.
TURN 180 182 {ECO:0000244|PDB:2AL6}.
HELIX 187 189 {ECO:0000244|PDB:2AL6}.
HELIX 191 199 {ECO:0000244|PDB:2AL6}.
TURN 200 202 {ECO:0000244|PDB:2J0J}.
HELIX 203 205 {ECO:0000244|PDB:2AL6}.
HELIX 209 213 {ECO:0000244|PDB:2AL6}.
HELIX 217 229 {ECO:0000244|PDB:2AL6}.
TURN 230 233 {ECO:0000244|PDB:2AL6}.
HELIX 236 247 {ECO:0000244|PDB:2AL6}.
TURN 248 250 {ECO:0000244|PDB:2AL6}.
STRAND 256 262 {ECO:0000244|PDB:2AL6}.
STRAND 264 266 {ECO:0000244|PDB:2AL6}.
STRAND 268 275 {ECO:0000244|PDB:2AL6}.
TURN 276 278 {ECO:0000244|PDB:2AL6}.
STRAND 279 285 {ECO:0000244|PDB:2AL6}.
STRAND 290 294 {ECO:0000244|PDB:2AL6}.
HELIX 296 298 {ECO:0000244|PDB:2AL6}.
STRAND 299 305 {ECO:0000244|PDB:2AL6}.
STRAND 308 310 {ECO:0000244|PDB:2AL6}.
STRAND 314 320 {ECO:0000244|PDB:2AL6}.
STRAND 327 333 {ECO:0000244|PDB:2AL6}.
HELIX 334 352 {ECO:0000244|PDB:2AL6}.
STRAND 398 402 {ECO:0000244|PDB:2AL6}.
HELIX 412 414 {ECO:0000244|PDB:2J0J}.
HELIX 419 421 {ECO:0000244|PDB:4D4R}.
STRAND 422 431 {ECO:0000244|PDB:4D4R}.
STRAND 434 441 {ECO:0000244|PDB:4D4R}.
STRAND 444 446 {ECO:0000244|PDB:2J0L}.
STRAND 449 455 {ECO:0000244|PDB:4D4R}.
TURN 457 460 {ECO:0000244|PDB:4D4R}.
HELIX 462 475 {ECO:0000244|PDB:4D4R}.
STRAND 486 490 {ECO:0000244|PDB:4D4R}.
STRAND 492 494 {ECO:0000244|PDB:4D4R}.
STRAND 496 500 {ECO:0000244|PDB:4D4R}.
HELIX 507 514 {ECO:0000244|PDB:4D4R}.
TURN 515 517 {ECO:0000244|PDB:4D4R}.
HELIX 520 539 {ECO:0000244|PDB:4D4R}.
HELIX 549 551 {ECO:0000244|PDB:4D4R}.
STRAND 552 556 {ECO:0000244|PDB:4D4R}.
STRAND 559 562 {ECO:0000244|PDB:4D4R}.
HELIX 567 570 {ECO:0000244|PDB:4D5H}.
HELIX 572 575 {ECO:0000244|PDB:4D4R}.
HELIX 577 579 {ECO:0000244|PDB:4D4R}.
HELIX 586 588 {ECO:0000244|PDB:4D4R}.
HELIX 591 596 {ECO:0000244|PDB:4D4R}.
HELIX 601 616 {ECO:0000244|PDB:4D4R}.
TURN 617 619 {ECO:0000244|PDB:4D4R}.
TURN 622 625 {ECO:0000244|PDB:4D4R}.
HELIX 628 630 {ECO:0000244|PDB:4D4R}.
HELIX 631 636 {ECO:0000244|PDB:4D4R}.
HELIX 649 658 {ECO:0000244|PDB:4D4R}.
HELIX 663 665 {ECO:0000244|PDB:4D4R}.
HELIX 669 684 {ECO:0000244|PDB:4D4R}.
TURN 919 921 {ECO:0000244|PDB:1KTM}.
HELIX 922 941 {ECO:0000244|PDB:1KTM}.
TURN 942 945 {ECO:0000244|PDB:1KTM}.
HELIX 948 975 {ECO:0000244|PDB:1KTM}.
TURN 978 980 {ECO:0000244|PDB:1PV3}.
HELIX 982 1005 {ECO:0000244|PDB:1KTM}.
STRAND 1008 1012 {ECO:0000244|PDB:1KTM}.
HELIX 1014 1047 {ECO:0000244|PDB:1KTM}.
SEQUENCE 1053 AA; 119207 MW; 8051154219B953B9 CRC64;
MAAAYLDPNL NHTPSSSAKT HLGTGMERSP GAMERVLKVF HYFENSSEPT TWASIIRHGD
ATDVRGIIQK IVDCHKVKNV ACYGLRLSHL QSEEVHWLHL DMGVSNVREK FELAHPPEEW
KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKNDYMLEIA DQVDQEIALK LGCLEIRRSY
GEMRGNALEK KSNYEVLEKD VGLRRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI
LKFFEILSPV YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGANP THLADFNQVQ
TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL VNGATQSFII
RPQKEGERAL PSIPKLANNE KQGVRSHTVS VSETDDYAEI IDEEDTYTMP STRDYEIQRE
RIELGRCIGE GQFGDVHQGI YMSPENPAMA VAIKTCKNCT SDSVREKFLQ EALTMRQFDH
PHIVKLIGVI TENPVWIIME LCTLGELRSF LQVRKFSLDL ASLILYAYQL STALAYLESK
RFVHRDIAAR NVLVSATDCV KLGDFGLSRY MEDSTYYKAS KGKLPIKWMA PESINFRRFT
SASDVWMFGV CMWEILMHGV KPFQGVKNND VIGRIENGER LPMPPNCPPT LYSLMTKCWA
YDPSRRPRFT ELKAQLSTIL EEEKLQQEER MRMESRRQVT VSWDSGGSDE APPKPSRPGY
PSPRSSEGFY PSPQHMVQPN HYQVSGYSGS HGIPAMAGSI YPGQASLLDQ TDSWNHRPQE
VSAWQPNMED SGTLDVRGMG QVLPTHLMEE RLIRQQQEME EDQRWLEKEE RFLVMKPDVR
LSRGSIERED GGLQGPAGNQ HIYQPVGKPD HAAPPKKPPR PGAPHLGSLA SLNSPVDSYN
EGVKIKPQEI SPPPTANLDR SNDKVYENVT GLVKAVIEMS SKIQPAPPEE YVPMVKEVGL
ALRTLLATVD ESLPVLPAST HREIEMAQKL LNSDLAELIN KMKLAQQYVM TSLQQEYKKQ
MLTAAHALAV DAKNLLDVID QARLKMISQS RPH


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