Focal adhesion kinase 1 - Mus musculus (Mouse)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Focal adhesion kinase 1
Short name=FADK 1
EC=2.7.10.2

Alternative name(s):
Focal adhesion kinase-related nonkinase
Short name=FRNK
Protein-tyrosine kinase 2
p125FAK
pp125FAK

Gene names

Name:	Ptk2
Synonyms:	Fadk, Fak, Fak1, Kiaa4203

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1090 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.9 Ref.12 Ref.15 Ref.19 Ref.21 Ref.22 Ref.23 Ref.26 Ref.28 Ref.34 Ref.35 Ref.36 Ref.37 Ref.40 Ref.43 Ref.44 Ref.45
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.1 Ref.11 Ref.19
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. Ref.11
Subunit structure	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 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). Ref.9 Ref.10 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.22 Ref.25 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.37 Ref.40 Ref.43 Ref.48
Subcellular location	Cell junction › focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm › perinuclear region. Cytoplasm › cytoskeleton. Cytoplasm › cytoskeleton › centrosome. Nucleus By similarity. Note: Constituent of focal adhesions. Detected at microtubules. Ref.1 Ref.26 Ref.40
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. Ref.42
Domain	The first Pro-rich domain interacts with the SH3 domain of CAS family members, such as BCAR1 and NEDD9. The C-terminal region is the site of focal adhesion targeting (FAT) sequence which mediates the localization of FAK1 to focal adhesions.
Post-translational modification	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. Ref.1 Ref.6 Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 Ref.19 Ref.21 Ref.24 Ref.26 Ref.31 Sumoylated; this enhances autophosphorylation By similarity.
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. Ref.12 Ref.34 Ref.36 Ref.40
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. FAK subfamily. Contains 1 FERM domain. Contains 1 protein kinase domain.
Sequence caution	The sequence BAC37757.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAD90317.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. Isoform 6: The sequence BC030180 differs from that shown. Reason: a stop codon in position 912 which was translated as Trp to extend the sequence

Ontologies

Keywords
Biological process	Angiogenesis
Cellular component	Cell junction Cell membrane Cytoplasm Cytoskeleton Membrane Nucleus
Coding sequence diversity	Alternative promoter usage Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Transferase Tyrosine-protein kinase
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	JNK cascade Inferred from electronic annotation. Source: Compara angiogenesis Inferred from mutant phenotype Ref.34. Source: MGI cellular chloride ion homeostasis Inferred from electronic annotation. Source: Compara central nervous system neuron axonogenesis Inferred from mutant phenotype PubMed 15378065. Source: MGI endothelial cell migration Inferred from mutant phenotype Ref.34. Source: MGI ephrin receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB establishment of nucleus localization Inferred from direct assay Ref.26. Source: MGI extracellular matrix organization Inferred from mutant phenotype PubMed 14642275. Source: MGI fat cell differentiation Inferred from electronic annotation. Source: Compara growth hormone receptor signaling pathway Inferred from electronic annotation. Source: Compara integrin-mediated signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB microtubule cytoskeleton organization Inferred from direct assay Ref.26. Source: MGI negative regulation of anoikis Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of axonogenesis Inferred from mutant phenotype PubMed 15378065. Source: MGI negative regulation of cell migration Inferred from electronic annotation. Source: Compara negative regulation of cell-cell adhesion Inferred from electronic annotation. Source: Compara negative regulation of organ growth Inferred from genetic interaction PubMed 16374517. Source: MGI negative regulation of synapse assembly Inferred from mutant phenotype PubMed 15378065. Source: MGI neuron migration Inferred from direct assay Ref.26. Source: MGI peptidyl-tyrosine phosphorylation Inferred from direct assay Ref.11. Source: UniProtKB positive regulation of cell adhesion Inferred from electronic annotation. Source: Compara positive regulation of cell growth Inferred from electronic annotation. Source: Compara positive regulation of cell migration Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell proliferation Inferred from mutant phenotype Ref.40. Source: UniProtKB positive regulation of glial cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of phagocytosis Inferred from electronic annotation. Source: Compara positive regulation of phosphatidylinositol 3-kinase cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of protein kinase B signaling cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of protein kinase activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Inferred from mutant phenotype Ref.40. Source: UniProtKB positive regulation of smooth muscle cell migration Inferred from electronic annotation. Source: Compara positive regulation of smooth muscle cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of synaptic transmission Inferred from electronic annotation. Source: Compara positive regulation of vasodilation Inferred from electronic annotation. Source: Compara protein autophosphorylation Inferred from direct assay Ref.11. Source: UniProtKB regulation of cell adhesion mediated by integrin Inferred from sequence or structural similarity. Source: UniProtKB regulation of cell shape Inferred from sequence or structural similarity. Source: UniProtKB regulation of osteoblast differentiation Inferred from sequence or structural similarity. Source: UniProtKB response to arsenic-containing substance Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to estradiol stimulus Inferred from electronic annotation. Source: Compara response to glucose stimulus Inferred from electronic annotation. Source: Compara response to mechanical stimulus Inferred from electronic annotation. Source: Compara signal complex assembly Inferred from electronic annotation. Source: InterPro vasculogenesis Inferred from mutant phenotype Ref.34. Source: MGI
Cellular_component	apical plasma membrane Inferred from direct assay PubMed 10742111. Source: MGI basolateral plasma membrane Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome focal adhesion Inferred from direct assay PubMed 10699171 PubMed 11784865 PubMed 15728191 PubMed 16405917. Source: MGI intercalated disc Inferred from electronic annotation. Source: Compara lamellipodium Inferred from direct assay PubMed 15728191. Source: MGI microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear body Inferred from electronic annotation. Source: Compara nucleolus Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay Ref.40. Source: UniProtKB perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell sarcolemma Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB signal transducer activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Bcar1	Q61140	2	EBI-77070,EBI-77088
Ephb2	P54763	3	EBI-77070,EBI-537711

Alternative products

This entry describes 9 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]

Isoform 1 (identifier: P34152-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P34152-2) The sequence of this isoform differs from the canonical sequence as follows: 443-450: KSYGIDEA → T

Isoform 3 (identifier: P34152-3) The sequence of this isoform differs from the canonical sequence as follows: 393-423: Missing. 443-450: KSYGIDEA → T
Note: Peptide 386-413 identified and sequenced in Ref.6.

Isoform 4 (identifier: P34152-4) The sequence of this isoform differs from the canonical sequence as follows: 393-423: Missing. 443-450: KSYGIDEA → T 941-941: K → KPWR
Note: No experimental confirmation available.

Isoform 5 (identifier: P34152-5) The sequence of this isoform differs from the canonical sequence as follows: 392-392: S → SGVS 942-954: LQPQEISPPPTAN → VGICACAMWSVPC 955-1090: Missing.

Isoform 6 (identifier: P34152-6) The sequence of this isoform differs from the canonical sequence as follows: 393-423: Missing. 443-450: KSYGIDEA → T 942-954: LQPQEISPPPTAN → VGICACAMWSVPC 955-1090: Missing.
Note: No experimental confirmation available.

Isoform 7 (identifier: P34152-7) The sequence of this isoform differs from the canonical sequence as follows: 393-417: Missing. 511-534: LTMRQFDHPHIVKLIGVITENPVW → SEVIFASKKIQLGPGIFDIICLSA 535-1090: Missing.
Note: No experimental confirmation available.

Isoform 8 (identifier: P34152-8) The sequence of this isoform differs from the canonical sequence as follows: 199-1090: Missing.
Note: No experimental confirmation available.

Isoform 9 (identifier: P34152-9) Also known as: FRNK; The sequence of this isoform differs from the canonical sequence as follows: 1-730: Missing.
Note: Produced by alternative promoter usage.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

Removed Ref.6

Chain

2 – 1090

1089

Focal adhesion kinase 1

PRO_0000088078

Regions

Domain

35 – 355

321

FERM

Domain

469 – 718

250

Protein kinase

Nucleotide binding

466 – 472

7

ATP By similarity

Nucleotide binding

538 – 540

3

ATP By similarity

Region

745 – 1090

346

Interaction with TGFB1I1 By similarity

Region

950 – 1090

141

Interaction with ARHGEF28

Compositional bias

750 – 771

22

Pro-rich

Compositional bias

901 – 951

51

Pro-rich

Sites

Active site

584

1

Proton acceptor By similarity

Binding site

492

1

ATP By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.6

Modified residue

5

1

Phosphotyrosine By similarity

Modified residue

13

1

Phosphothreonine By similarity

Modified residue

29

1

Phosphoserine By similarity

Modified residue

428

1

Phosphotyrosine; by autocatalysis Ref.11 Ref.13 Ref.19 Ref.21 Ref.24

Modified residue

438

1

Phosphotyrosine Ref.11 Ref.24

Modified residue

608

1

Phosphotyrosine By similarity

Modified residue

614

1

Phosphotyrosine; by RET and SRC Ref.11 Ref.19 Ref.24 Ref.39 Ref.41

Modified residue

615

1

Phosphotyrosine; by RET and SRC Ref.11 Ref.19 Ref.24 Ref.39 Ref.41

Modified residue

618

1

Phosphoserine By similarity

Modified residue

760

1

Phosphoserine By similarity

Modified residue

770

1

Phosphoserine; by CDK5 Ref.26

Modified residue

899

1

Phosphotyrosine Ref.24

Modified residue

948

1

Phosphoserine Ref.6 Ref.38

Modified residue

952

1

Phosphothreonine By similarity

Modified residue

963

1

Phosphotyrosine; by SRC Ref.9 Ref.14 Ref.15 Ref.24 Ref.41

Cross-link

152

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence

1 – 730

730

Missing in isoform 9.

VSP_042171

Alternative sequence

199 – 1090

892

Missing in isoform 8.

VSP_033998

Alternative sequence

392

1

S → SGVS in isoform 5.

VSP_033999

Alternative sequence

393 – 423

31

Missing in isoform 3, isoform 4 and isoform 6.

VSP_004975

Alternative sequence

393 – 417

25

Missing in isoform 7.

VSP_034000

Alternative sequence

443 – 450

8

KSYGIDEA → T in isoform 2, isoform 3, isoform 4 and isoform 6.

VSP_004976

Alternative sequence

511 – 534

24

LTMRQ…ENPVW → SEVIFASKKIQLGPGIFDII CLSA in isoform 7.

VSP_034001

Alternative sequence

535 – 1090

556

Missing in isoform 7.

VSP_034002

Alternative sequence

941

1

K → KPWR in isoform 4.

VSP_034003

Alternative sequence

942 – 954

13

LQPQE…PPTAN → VGICACAMWSVPC in isoform 5 and isoform 6.

VSP_034004

Alternative sequence

955 – 1090

136

Missing in isoform 5 and isoform 6.

VSP_034005

Experimental info

Mutagenesis

428

1

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. Ref.11 Ref.13 Ref.19

Mutagenesis

614 – 615

2

YY → FF: Strongly reduced enzyme activity; when associated with F-428.

Mutagenesis

963

1

Y → F: Abolishes interaction with GRB2. Ref.9 Ref.14

Mutagenesis

1072

1

L → S: Loss of interaction with ARHGEF28. Ref.28

Sequence conflict

32

1

A → T in BC030180. Ref.5

Sequence conflict

42

1

Y → H in AAA37592. Ref.1

Sequence conflict

87

1

L → V in BAB24058. Ref.3

Sequence conflict

128

1

Y → D in BAB24058. Ref.3

Sequence conflict

146

1

F → V in BAB24058. Ref.3

Sequence conflict

157

1

Q → L in BC030180. Ref.5

Sequence conflict

225

1

Q → H in BAC37757. Ref.3

Sequence conflict

250

1

V → M in BAC37757. Ref.3

Sequence conflict

800

1

Q → P in BC030180. Ref.5

Secondary structure

1

.

1090

Helix Strand Turn

Details...

Sequences

Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified May 20, 2008. Version 3. Checksum: 7C795105A9B9DCA6 Show »	FASTA	1,090	123,537
10 20 30 40 50 60 MAAAYLDPNL NHTPSSSTKT HLGTGMERSP GAMERVLKVF HYFESSSEPT TWASIIRHGD 70 80 90 100 110 120 ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW 130 140 150 160 170 180 KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMQEIA DQVDQEIALK LGCLEIRRSY 190 200 210 220 230 240 WEMRGNALEK KSNYEVLEKD VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI 250 260 270 280 290 300 LKFFEILSPV YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFNQVQ 310 320 330 340 350 360 TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL VNGATQSFII 370 380 390 400 410 420 RPQKEGERAL PSIPKLANSE KQGMRTHAVS VSHCQHKVKK ARRFLPLVFC SLEPPPTDEI 430 440 450 460 470 480 SGDETDDYAE IIDEEDTYTM PSKSYGIDEA RDYEIQRERI ELGRCIGEGQ FGDVHQGVYL 490 500 510 520 530 540 SPENPALAVA IKTCKNCTSD SVREKFLQEA LTMRQFDHPH IVKLIGVITE NPVWIIMELC 550 560 570 580 590 600 TLGELRSFLQ VRKYSLDLAS LILYAYQLST ALAYLESKRF VHRDIAARNV LVSSNDCVKL 610 620 630 640 650 660 GDFGLSRYME DSTYYKASKG KLPIKWMAPE SINFRRFTSA SDVWMFGVCM WEILMHGVKP 670 680 690 700 710 720 FQGVKNNDVI GRIENGERLP MPPNCPPTLY SLMTKCWAYD PSRRPRFTEL KAQLSTILEE 730 740 750 760 770 780 EKVQQEERMR MESRRQATVS WDSGGSDEAP PKPSRPGYPS PRSSEGFYPS PQHMVQTNHY 790 800 810 820 830 840 QVSGYPGSHG IPAMAGSIYQ GQASLLDQTE LWNHRPQEMS MWQPSVEDSA ALDLRGMGQV 850 860 870 880 890 900 LPPHLMEERL IRQQQEMEED QRWLEKEERF LKPDVRLSRG SIDREDGSFQ GPTGNQHIYQ 910 920 930 940 950 960 PVGKPDPAAP PKKPPRPGAP GHLSNLSSIS SPADSYNEGV KLQPQEISPP PTANLDRSND 970 980 990 1000 1010 1020 KVYENVTGLV KAVIEMSSKI QPAPPEEYVP MVKEVGLALR TLLATVDETI PALPASTHRE 1030 1040 1050 1060 1070 1080 IEMAQKLLNS DLGELISKMK LAQQYVMTSL QQEYKKQMLT AAHALAVDAK NLLDVIDQAR 1090 LKMLGQTRPH « Hide
Isoform 2 [UniParc]. Checksum: E536A38627B90A83 Show »	FASTA	1,083	122,774
10 20 30 40 50 60 MAAAYLDPNL NHTPSSSTKT HLGTGMERSP GAMERVLKVF HYFESSSEPT TWASIIRHGD 70 80 90 100 110 120 ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW 130 140 150 160 170 180 KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMQEIA DQVDQEIALK LGCLEIRRSY 190 200 210 220 230 240 WEMRGNALEK KSNYEVLEKD VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI 250 260 270 280 290 300 LKFFEILSPV YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFNQVQ 310 320 330 340 350 360 TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL VNGATQSFII 370 380 390 400 410 420 RPQKEGERAL PSIPKLANSE KQGMRTHAVS VSHCQHKVKK ARRFLPLVFC SLEPPPTDEI 430 440 450 460 470 480 SGDETDDYAE IIDEEDTYTM PSTRDYEIQR ERIELGRCIG EGQFGDVHQG VYLSPENPAL 490 500 510 520 530 540 AVAIKTCKNC TSDSVREKFL QEALTMRQFD HPHIVKLIGV ITENPVWIIM ELCTLGELRS 550 560 570 580 590 600 FLQVRKYSLD LASLILYAYQ LSTALAYLES KRFVHRDIAA RNVLVSSNDC VKLGDFGLSR 610 620 630 640 650 660 YMEDSTYYKA SKGKLPIKWM APESINFRRF TSASDVWMFG VCMWEILMHG VKPFQGVKNN 670 680 690 700 710 720 DVIGRIENGE RLPMPPNCPP TLYSLMTKCW AYDPSRRPRF TELKAQLSTI LEEEKVQQEE 730 740 750 760 770 780 RMRMESRRQA TVSWDSGGSD EAPPKPSRPG YPSPRSSEGF YPSPQHMVQT NHYQVSGYPG 790 800 810 820 830 840 SHGIPAMAGS IYQGQASLLD QTELWNHRPQ EMSMWQPSVE DSAALDLRGM GQVLPPHLME 850 860 870 880 890 900 ERLIRQQQEM EEDQRWLEKE ERFLKPDVRL SRGSIDREDG SFQGPTGNQH IYQPVGKPDP 910 920 930 940 950 960 AAPPKKPPRP GAPGHLSNLS SISSPADSYN EGVKLQPQEI SPPPTANLDR SNDKVYENVT 970 980 990 1000 1010 1020 GLVKAVIEMS SKIQPAPPEE YVPMVKEVGL ALRTLLATVD ETIPALPAST HREIEMAQKL 1030 1040 1050 1060 1070 1080 LNSDLGELIS KMKLAQQYVM TSLQQEYKKQ MLTAAHALAV DAKNLLDVID QARLKMLGQT RPH « Hide
Isoform 3 [UniParc]. Checksum: 4B7453C5D81F0F63 Show »	FASTA	1,052	119,243
10 20 30 40 50 60 MAAAYLDPNL NHTPSSSTKT HLGTGMERSP GAMERVLKVF HYFESSSEPT TWASIIRHGD 70 80 90 100 110 120 ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW 130 140 150 160 170 180 KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMQEIA DQVDQEIALK LGCLEIRRSY 190 200 210 220 230 240 WEMRGNALEK KSNYEVLEKD VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI 250 260 270 280 290 300 LKFFEILSPV YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFNQVQ 310 320 330 340 350 360 TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL VNGATQSFII 370 380 390 400 410 420 RPQKEGERAL PSIPKLANSE KQGMRTHAVS VSETDDYAEI IDEEDTYTMP STRDYEIQRE 430 440 450 460 470 480 RIELGRCIGE GQFGDVHQGV YLSPENPALA VAIKTCKNCT SDSVREKFLQ EALTMRQFDH 490 500 510 520 530 540 PHIVKLIGVI TENPVWIIME LCTLGELRSF LQVRKYSLDL ASLILYAYQL STALAYLESK 550 560 570 580 590 600 RFVHRDIAAR NVLVSSNDCV KLGDFGLSRY MEDSTYYKAS KGKLPIKWMA PESINFRRFT 610 620 630 640 650 660 SASDVWMFGV CMWEILMHGV KPFQGVKNND VIGRIENGER LPMPPNCPPT LYSLMTKCWA 670 680 690 700 710 720 YDPSRRPRFT ELKAQLSTIL EEEKVQQEER MRMESRRQAT VSWDSGGSDE APPKPSRPGY 730 740 750 760 770 780 PSPRSSEGFY PSPQHMVQTN HYQVSGYPGS HGIPAMAGSI YQGQASLLDQ TELWNHRPQE 790 800 810 820 830 840 MSMWQPSVED SAALDLRGMG QVLPPHLMEE RLIRQQQEME EDQRWLEKEE RFLKPDVRLS 850 860 870 880 890 900 RGSIDREDGS FQGPTGNQHI YQPVGKPDPA APPKKPPRPG APGHLSNLSS ISSPADSYNE 910 920 930 940 950 960 GVKLQPQEIS PPPTANLDRS NDKVYENVTG LVKAVIEMSS KIQPAPPEEY VPMVKEVGLA 970 980 990 1000 1010 1020 LRTLLATVDE TIPALPASTH REIEMAQKLL NSDLGELISK MKLAQQYVMT SLQQEYKKQM 1030 1040 1050 LTAAHALAVD AKNLLDVIDQ ARLKMLGQTR PH « Hide
Isoform 4 [UniParc]. Checksum: AFB79846FA73ED6F Show »	FASTA	1,055	119,682
10 20 30 40 50 60 MAAAYLDPNL NHTPSSSTKT HLGTGMERSP GAMERVLKVF HYFESSSEPT TWASIIRHGD 70 80 90 100 110 120 ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW 130 140 150 160 170 180 KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMQEIA DQVDQEIALK LGCLEIRRSY 190 200 210 220 230 240 WEMRGNALEK KSNYEVLEKD VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI 250 260 270 280 290 300 LKFFEILSPV YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFNQVQ 310 320 330 340 350 360 TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL VNGATQSFII 370 380 390 400 410 420 RPQKEGERAL PSIPKLANSE KQGMRTHAVS VSETDDYAEI IDEEDTYTMP STRDYEIQRE 430 440 450 460 470 480 RIELGRCIGE GQFGDVHQGV YLSPENPALA VAIKTCKNCT SDSVREKFLQ EALTMRQFDH 490 500 510 520 530 540 PHIVKLIGVI TENPVWIIME LCTLGELRSF LQVRKYSLDL ASLILYAYQL STALAYLESK 550 560 570 580 590 600 RFVHRDIAAR NVLVSSNDCV KLGDFGLSRY MEDSTYYKAS KGKLPIKWMA PESINFRRFT 610 620 630 640 650 660 SASDVWMFGV CMWEILMHGV KPFQGVKNND VIGRIENGER LPMPPNCPPT LYSLMTKCWA 670 680 690 700 710 720 YDPSRRPRFT ELKAQLSTIL EEEKVQQEER MRMESRRQAT VSWDSGGSDE APPKPSRPGY 730 740 750 760 770 780 PSPRSSEGFY PSPQHMVQTN HYQVSGYPGS HGIPAMAGSI YQGQASLLDQ TELWNHRPQE 790 800 810 820 830 840 MSMWQPSVED SAALDLRGMG QVLPPHLMEE RLIRQQQEME EDQRWLEKEE RFLKPDVRLS 850 860 870 880 890 900 RGSIDREDGS FQGPTGNQHI YQPVGKPDPA APPKKPPRPG APGHLSNLSS ISSPADSYNE 910 920 930 940 950 960 GVKPWRLQPQ EISPPPTANL DRSNDKVYEN VTGLVKAVIE MSSKIQPAPP EEYVPMVKEV 970 980 990 1000 1010 1020 GLALRTLLAT VDETIPALPA STHREIEMAQ KLLNSDLGEL ISKMKLAQQY VMTSLQQEYK 1030 1040 1050 KQMLTAAHAL AVDAKNLLDV IDQARLKMLG QTRPH « Hide
Isoform 5 [UniParc]. Checksum: D277A4D65AE6012A Show »	FASTA	957	108,608
10 20 30 40 50 60 MAAAYLDPNL NHTPSSSTKT HLGTGMERSP GAMERVLKVF HYFESSSEPT TWASIIRHGD 70 80 90 100 110 120 ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW 130 140 150 160 170 180 KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMQEIA DQVDQEIALK LGCLEIRRSY 190 200 210 220 230 240 WEMRGNALEK KSNYEVLEKD VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI 250 260 270 280 290 300 LKFFEILSPV YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFNQVQ 310 320 330 340 350 360 TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL VNGATQSFII 370 380 390 400 410 420 RPQKEGERAL PSIPKLANSE KQGMRTHAVS VSGVSHCQHK VKKARRFLPL VFCSLEPPPT 430 440 450 460 470 480 DEISGDETDD YAEIIDEEDT YTMPSKSYGI DEARDYEIQR ERIELGRCIG EGQFGDVHQG 490 500 510 520 530 540 VYLSPENPAL AVAIKTCKNC TSDSVREKFL QEALTMRQFD HPHIVKLIGV ITENPVWIIM 550 560 570 580 590 600 ELCTLGELRS FLQVRKYSLD LASLILYAYQ LSTALAYLES KRFVHRDIAA RNVLVSSNDC 610 620 630 640 650 660 VKLGDFGLSR YMEDSTYYKA SKGKLPIKWM APESINFRRF TSASDVWMFG VCMWEILMHG 670 680 690 700 710 720 VKPFQGVKNN DVIGRIENGE RLPMPPNCPP TLYSLMTKCW AYDPSRRPRF TELKAQLSTI 730 740 750 760 770 780 LEEEKVQQEE RMRMESRRQA TVSWDSGGSD EAPPKPSRPG YPSPRSSEGF YPSPQHMVQT 790 800 810 820 830 840 NHYQVSGYPG SHGIPAMAGS IYQGQASLLD QTELWNHRPQ EMSMWQPSVE DSAALDLRGM 850 860 870 880 890 900 GQVLPPHLME ERLIRQQQEM EEDQRWLEKE ERFLKPDVRL SRGSIDREDG SFQGPTGNQH 910 920 930 940 950 IYQPVGKPDP AAPPKKPPRP GAPGHLSNLS SISSPADSYN EGVKVGICAC AMWSVPC « Hide
Isoform 6 [UniParc]. Checksum: F2DA51E8CC785229 Show »	FASTA	916	104,070
10 20 30 40 50 60 MAAAYLDPNL NHTPSSSTKT HLGTGMERSP GAMERVLKVF HYFESSSEPT TWASIIRHGD 70 80 90 100 110 120 ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW 130 140 150 160 170 180 KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMQEIA DQVDQEIALK LGCLEIRRSY 190 200 210 220 230 240 WEMRGNALEK KSNYEVLEKD VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI 250 260 270 280 290 300 LKFFEILSPV YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFNQVQ 310 320 330 340 350 360 TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL VNGATQSFII 370 380 390 400 410 420 RPQKEGERAL PSIPKLANSE KQGMRTHAVS VSETDDYAEI IDEEDTYTMP STRDYEIQRE 430 440 450 460 470 480 RIELGRCIGE GQFGDVHQGV YLSPENPALA VAIKTCKNCT SDSVREKFLQ EALTMRQFDH 490 500 510 520 530 540 PHIVKLIGVI TENPVWIIME LCTLGELRSF LQVRKYSLDL ASLILYAYQL STALAYLESK 550 560 570 580 590 600 RFVHRDIAAR NVLVSSNDCV KLGDFGLSRY MEDSTYYKAS KGKLPIKWMA PESINFRRFT 610 620 630 640 650 660 SASDVWMFGV CMWEILMHGV KPFQGVKNND VIGRIENGER LPMPPNCPPT LYSLMTKCWA 670 680 690 700 710 720 YDPSRRPRFT ELKAQLSTIL EEEKVQQEER MRMESRRQAT VSWDSGGSDE APPKPSRPGY 730 740 750 760 770 780 PSPRSSEGFY PSPQHMVQTN HYQVSGYPGS HGIPAMAGSI YQGQASLLDQ TELWNHRPQE 790 800 810 820 830 840 MSMWQPSVED SAALDLRGMG QVLPPHLMEE RLIRQQQEME EDQRWLEKEE RFLKPDVRLS 850 860 870 880 890 900 RGSIDREDGS FQGPTGNQHI YQPVGKPDPA APPKKPPRPG APGHLSNLSS ISSPADSYNE 910 GVKVGICACA MWSVPC « Hide
Isoform 7 [UniParc]. Checksum: A406369629607D5D Show »	FASTA	509	57,697
10 20 30 40 50 60 MAAAYLDPNL NHTPSSSTKT HLGTGMERSP GAMERVLKVF HYFESSSEPT TWASIIRHGD 70 80 90 100 110 120 ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW 130 140 150 160 170 180 KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMQEIA DQVDQEIALK LGCLEIRRSY 190 200 210 220 230 240 WEMRGNALEK KSNYEVLEKD VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI 250 260 270 280 290 300 LKFFEILSPV YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFNQVQ 310 320 330 340 350 360 TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL VNGATQSFII 370 380 390 400 410 420 RPQKEGERAL PSIPKLANSE KQGMRTHAVS VSDEISGDET DDYAEIIDEE DTYTMPSKSY 430 440 450 460 470 480 GIDEARDYEI QRERIELGRC IGEGQFGDVH QGVYLSPENP ALAVAIKTCK NCTSDSVREK 490 500 FLQEASEVIF ASKKIQLGPG IFDIICLSA « Hide
Isoform 8 [UniParc]. Checksum: 2732777636068833 Show »	FASTA	198	23,064
10 20 30 40 50 60 MAAAYLDPNL NHTPSSSTKT HLGTGMERSP GAMERVLKVF HYFESSSEPT TWASIIRHGD 70 80 90 100 110 120 ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW 130 140 150 160 170 180 KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMQEIA DQVDQEIALK LGCLEIRRSY 190 WEMRGNALEK KSNYEVLE « Hide
Isoform 9 (FRNK) [UniParc]. Checksum: 6C5E4C5486C62265 Show »	FASTA	360	39,930
10 20 30 40 50 60 MESRRQATVS WDSGGSDEAP PKPSRPGYPS PRSSEGFYPS PQHMVQTNHY QVSGYPGSHG 70 80 90 100 110 120 IPAMAGSIYQ GQASLLDQTE LWNHRPQEMS MWQPSVEDSA ALDLRGMGQV LPPHLMEERL 130 140 150 160 170 180 IRQQQEMEED QRWLEKEERF LKPDVRLSRG SIDREDGSFQ GPTGNQHIYQ PVGKPDPAAP 190 200 210 220 230 240 PKKPPRPGAP GHLSNLSSIS SPADSYNEGV KLQPQEISPP PTANLDRSND KVYENVTGLV 250 260 270 280 290 300 KAVIEMSSKI QPAPPEEYVP MVKEVGLALR TLLATVDETI PALPASTHRE IEMAQKLLNS 310 320 330 340 350 360 DLGELISKMK LAQQYVMTSL QQEYKKQMLT AAHALAVDAK NLLDVIDQAR LKMLGQTRPH « Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin." Hanks S.K., Calalb M.B., Harper M.C., Patel S.K. Proc. Natl. Acad. Sci. U.S.A. 89:8487-8491(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, PHOSPHORYLATION. Strain: BALB/c. Tissue: Embryo.
[2]	"Focal adhesion kinase." Yamakawa N. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 7). Strain: BALB/c. Tissue: Brain and Embryo.
[3]	"The transcriptional landscape of the mammalian genome." 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. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 8). Strain: C57BL/6J. Tissue: Placenta and Thymus.
[4]	"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." Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H. Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Fetal brain.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). Strain: Czech II. Tissue: Mammary tumor.
[6]	Bienvenut W.V., Sandilands E., Serrels B., Brunton V.G., Sumpton D.P., Frame M.C. Submitted (MAR-2008) to UniProtKB Cited for: 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, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[7]	"Alternatively spliced focal adhesion kinase in rat brain with increased autophosphorylation activity." Burgaya F., Toutant M., Studler J.-M., Costa A., Le Bert M., Gelman M., Girault J.A. J. Biol. Chem. 272:28720-28725(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 391-460 (ISOFORMS 1 AND 2). Strain: ICR X Swiss Webster.
[8]	Asano H., Komiyama H.K., Grant S.G. Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 391-417. Strain: 129/SvJ.
[9]	"Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase." Schlaepfer D.D., Hanks S.K., Hunter T., van der Geer P. Nature 372:786-791(1994) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN INTEGRIN SIGNALING AND ACTIVATION OF MAP KINASES, INTERACTION WITH GRB2; BCAR1; SHC1 AND SRC, PHOSPHORYLATION AT TYR-963, MUTAGENESIS OF TYR-963.
[10]	"Interaction of focal adhesion kinase with cytoskeletal protein talin." Chen H.C., Appeddu P.A., Parsons J.T., Hildebrand J.D., Schaller M.D., Guan J.L. J. Biol. Chem. 270:16995-16999(1995) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TLN1.
[11]	"Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases." Calalb M.B., Polte T.R., Hanks S.K. Mol. Cell. Biol. 15:954-963(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-428; TYR-438; TYR-614 AND TYR-615, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-428 AND 614-TYR-615, ENZYME REGULATION.
[12]	"Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK." Furuta Y., Ilic D., Kanazawa S., Takeda N., Yamamoto T., Aizawa S. Oncogene 11:1989-1995(1995) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[13]	"Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding phosphatidylinositol 3-kinase." Chen H.C., Appeddu P.A., Isoda H., Guan J.L. J. Biol. Chem. 271:26329-26334(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PIK3R1, MUTAGENESIS OF TYR-428, PHOSPHORYLATION AT TYR-428.
[14]	"Evidence for in vivo phosphorylation of the Grb2 SH2-domain binding site on focal adhesion kinase by Src-family protein-tyrosine kinases." Schlaepfer D.D., Hunter T. Mol. Cell. Biol. 16:5623-5633(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-963, MUTAGENESIS OF TYR-963, INTERACTION WITH GRB2.
[15]	"Focal adhesion kinase overexpression enhances ras-dependent integrin signaling to ERK2/mitogen-activated protein kinase through interactions with and activation of c-Src." Schlaepfer D.D., Hunter T. J. Biol. Chem. 272:13189-13195(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF SHC1 AND ACTIVATION OF MAPK1/ERK2, PHOSPHORYLATION AT TYR-963, INTERACTION WITH GRB2.
[16]	"Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions." Matsuya M., Sasaki H., Aoto H., Mitaka T., Nagura K., Ohba T., Ishino M., Takahashi S., Suzuki R., Sasaki T. J. Biol. Chem. 273:1003-1014(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TGFB1I1.
[17]	"A role for CAP, a novel, multifunctional Src homology 3 domain-containing protein in formation of actin stress fibers and focal adhesions." Ribon V., Herrera R., Kay B.K., Saltiel A.R. J. Biol. Chem. 273:4073-4080(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SORBS1.
[18]	"Interaction of Hic-5, A senescence-related protein, with focal adhesion kinase." Fujita H., Kamiguchi K., Cho D., Shibanuma M., Morimoto C., Tachibana K. J. Biol. Chem. 273:26516-26521(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TGFB1I1.
[19]	"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." Owen J.D., Ruest P.J., Fry D.W., Hanks S.K. Mol. Cell. Biol. 19:4806-4818(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CELL SPREADING; MIGRATION AND PHOSPHORYLATION OF BCAR1, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF TYR-428 AND 614-TYR-TYR-615, PHOSPHORYLATION AT TYR-428; TYR-614 AND TYR-615.
[20]	"p130Cas regulates the activity of AND-34, a novel Ral, Rap1, and R-Ras guanine nucleotide exchange factor." Gotoh T., Cai D., Tian X., Feig L.A., Lerner A. J. Biol. Chem. 275:30118-30123(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BCAR3.
[21]	"FAK integrates growth-factor and integrin signals to promote cell migration." Sieg D.J., Hauck C.R., Ilic D., Klingbeil C.K., Schaefer E., Damsky C.H., Schlaepfer D.D. Nat. Cell Biol. 2:249-256(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT TYR-428.
[22]	"Focal adhesion kinase activates Stat1 in integrin-mediated cell migration and adhesion." Xie B., Zhao J., Kitagawa M., Durbin J., Madri J.A., Guan J.L., Fu X.Y. J. Biol. Chem. 276:19512-19523(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH STAT1, FUNCTION IN STAT1 PHOSPHORYLATION.
[23]	"The cytoskeletal/non-muscle isoform of alpha-actinin is phosphorylated on its actin-binding domain by the focal adhesion kinase." Izaguirre G., Aguirre L., Hu Y.P., Lee H.Y., Schlaepfer D.D., Aneskievich B.J., Haimovich B. J. Biol. Chem. 276:28676-28685(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF ACTN1.
[24]	"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." Nakamura K., Yano H., Schaefer E., Sabe H. Oncogene 20:2626-2635(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-428; TYR-438; TYR-614; TYR-615; TYR-899 AND TYR-963.
[25]	"Regulation of focal adhesion kinase by a novel protein inhibitor FIP200." Abbi S., Ueda H., Zheng C., Cooper L.A., Zhao J., Christopher R., Guan J.L. Mol. Biol. Cell 13:3178-3191(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RB1CC1.
[26]	"Serine 732 phosphorylation of FAK by Cdk5 is important for microtubule organization, nuclear movement, and neuronal migration." Xie Z., Sanada K., Samuels B.A., Shih H., Tsai L.H. Cell 114:469-482(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-770.
[27]	"The Shb adaptor protein causes Src-dependent cell spreading and activation of focal adhesion kinase in murine brain endothelial cells." Holmqvist K., Cross M.J., Riley D., Welsh M. Cell. Signal. 15:171-179(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SHB.
[28]	"Direct interaction of focal adhesion kinase with p190RhoGEF." Zhai J., Lin H., Nie Z., Wu J., Canete-Soler R., Schlaepfer W.W., Schlaepfer D.D. J. Biol. Chem. 278:24865-24873(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ARHGEF28, MUTAGENESIS OF LEU-1072.
[29]	"PIAS1-mediated sumoylation of focal adhesion kinase activates its autophosphorylation." Kadare G., Toutant M., Formstecher E., Corvol J.C., Carnaud M., Boutterin M.C., Girault J.A. J. Biol. Chem. 278:47434-47440(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PIAS1.
[30]	"Leupaxin is a critical adaptor protein in the adhesion zone of the osteoclast." Gupta A., Lee B.S., Khadeer M.A., Tang Z., Chellaiah M., Abu-Amer Y., Goldknopf J., Hruska K.A. J. Bone Miner. Res. 18:669-685(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LPXN.
[31]	"Focal adhesion kinase regulation of N-WASP subcellular localization and function." Wu X., Suetsugu S., Cooper L.A., Takenawa T., Guan J.L. J. Biol. Chem. 279:9565-9576(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH WASL, PHOSPHORYLATION OF WASL.
[32]	"Focal adhesion kinase in netrin-1 signaling." 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. Nat. Neurosci. 7:1204-1212(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DCC.
[33]	"Activation of FAK and Src are receptor-proximal events required for netrin signaling." 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. Nat. Neurosci. 7:1213-1221(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DCC.
[34]	"Conditional knockout of focal adhesion kinase in endothelial cells reveals its role in angiogenesis and vascular development in late embryogenesis." Shen T.L., Park A.Y., Alcaraz A., Peng X., Jang I., Koni P., Flavell R.A., Gu H., Guan J.L. J. Cell Biol. 169:941-952(2005) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[35]	"Src and FAK kinases cooperate to phosphorylate paxillin kinase linker, stimulate its focal adhesion localization, and regulate cell spreading and protrusiveness." Brown M.C., Cary L.A., Jamieson J.S., Cooper J.A., Turner C.E. Mol. Biol. Cell 16:4316-4328(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[36]	"Endothelial FAK is essential for vascular network stability, cell survival, and lamellipodial formation." Braren R., Hu H., Kim Y.H., Beggs H.E., Reichardt L.F., Wang R. J. Cell Biol. 172:151-162(2006) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[37]	"FAK potentiates Rac1 activation and localization to matrix adhesion sites: a role for betaPIX." Chang F., Lemmon C.A., Park D., Romer L.H. Mol. Biol. Cell 18:253-264(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CELL SPREADING; PHOSPHORYLATION OF ARHGEF7; RAC1 TARGETING TO FOCAL ADHESIONS AND RAC1 ACTIVATION, INTERACTION WITH ARHGEF7.
[38]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-948, MASS SPECTROMETRY. Tissue: Brain cortex.
[39]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-614 AND TYR-615, MASS SPECTROMETRY. Tissue: Liver.
[40]	"Nuclear FAK promotes cell proliferation and survival through FERM-enhanced p53 degradation." 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. Mol. Cell 29:9-22(2008) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION IN REGULATION OF P53/TP53 LEVELS; CELL PROLIFERATION AND CELL SURVIVAL, INTERACTION WITH MDM2, SUBCELLULAR LOCATION.
[41]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-614; TYR-615 AND TYR-963, MASS SPECTROMETRY. Tissue: Brain.
[42]	"Transient expression of FRNK reveals stage-specific requirement for focal adhesion kinase activity in cardiac growth." DiMichele L.A., Hakim Z.S., Sayers R.L., Rojas M., Schwartz R.J., Mack C.P., Taylor J.M. Circ. Res. 104:1201-1208(2009) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE (ISOFORM 9).
[43]	"Tyrosine phosphorylation of growth factor receptor-bound protein-7 by focal adhesion kinase in the regulation of cell migration, proliferation, and tumorigenesis." Chu P.Y., Huang L.Y., Hsu C.H., Liang C.C., Guan J.L., Hung T.H., Shen T.L. J. Biol. Chem. 284:20215-20226(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF GRB7, INTERACTION WITH GRB7.
[44]	"Ras- and PI3K-dependent breast tumorigenesis in mice and humans requires focal adhesion kinase signaling." Pylayeva Y., Gillen K.M., Gerald W., Beggs H.E., Reichardt L.F., Giancotti F.G. J. Clin. Invest. 119:252-266(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN SRC-MEDIATED PHOSPHORYLATION OF BCAR1, ROLE IN DISEASE.
[45]	"Focal adhesion kinase governs cardiac concentric hypertrophic growth by activating the AKT and mTOR pathways." 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. J. Mol. Cell. Cardiol. 52:493-501(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[46]	"The role of focal adhesion kinase in early development." Chatzizacharias N.A., Kouraklis G.P., Theocharis S.E. Histol. Histopathol. 25:1039-1055(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ROLE IN DEVELOPMENT.
[47]	"Focal adhesion kinase: exploring Fak structure to gain insight into function." Hall J.E., Fu W., Schaller M.D. Int. Rev. Cell Mol. Biol. 288:185-225(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION; SUBUNIT; PHOSPHORYLATION AND ENZYME REGULATION.
[48]	"The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin." Hayashi I., Vuori K., Liddington R.C. Nat. Struct. Biol. 9:101-106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 959-1084, INTERACTION WITH PXN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M95408 mRNA. Translation: AAA37592.1.
AB030035 mRNA. Translation: BAC53924.1.
AB011499 mRNA. Translation: BAC53890.1.
AK005468 mRNA. Translation: BAB24058.1.
AK079821 mRNA. Translation: BAC37757.1. Different initiation.
AK220543 mRNA. Translation: BAD90317.1. Different initiation.
BC030180 mRNA. No translation available.
AF025652

AF025651 Genomic DNA. Translation: AAB95262.1.
AF025652

AF025650 Genomic DNA. Translation: AAB95263.1.
U77074 Genomic DNA. Translation: AAB51229.1.

IPI

IPI00113563.
IPI00230629.
IPI00338858.
IPI00625418.
IPI00875543.
IPI00895208.
IPI00895269.
IPI00895396.

PIR

A46166.

RefSeq

NP_001123881.1. NM_001130409.1.
NP_032008.2. NM_007982.2.

UniGene

Mm.254494.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K40	X-ray	2.25	A	959-1084	[»]
1KKY	model	-	B	959-1084	[»]
1KL0	model	-	A	959-1084	[»]

ProteinModelPortal

P34152.

SMR

P34152. Positions 33-742, 959-1084.

ModBase

Search...

Protein-protein interaction databases

IntAct

P34152. 5 interactions.

MINT

MINT-141959.

PTM databases

PhosphoSite

P34152.

Proteomic databases

PaxDb

P34152.

PRIDE

P34152.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000110036; ENSMUSP00000105663; ENSMUSG00000022607.
ENSMUST00000170939; ENSMUSP00000126764; ENSMUSG00000022607.

GeneID

14083.

KEGG

mmu:14083.

UCSC

uc007wbw.2. mouse.
uc007wbx.2. mouse.
uc007wby.2. mouse.
uc007wbz.2. mouse.
uc007wca.1. mouse.

Organism-specific databases

CTD

5747.

MGI

MGI:95481. Ptk2.

Rouge

Search...

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00620000087791.

HOVERGEN

HBG004018.

InParanoid

P34152.

KO

K05725.

OMA

VQTNHYQ.

OrthoDB

EOG4WH8K1.

Enzyme and pathway databases

BRENDA

2.7.10.2. 3474.

Reactome

REACT_127416. Developmental Biology.

Gene expression databases

Bgee

P34152.

CleanEx

MM_PTK2.

Genevestigator

P34152.

GermOnline

ENSMUSG00000022607. Mus musculus.

Family and domain databases

InterPro

IPR019749. Band_41_domain.
IPR019748. FERM_central.
IPR000299. FERM_domain.
IPR005189. Focal_adhesion_kin_target_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]

Pfam

PF00373. FERM_M. 1 hit.
PF03623. Focal_AT. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]

PRINTS

PR00109. TYRKINASE.

ProDom

PD006413. Focal_adhesion_target_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00295. B41. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF47031. FERM_3-hlx. 1 hit.
SSF68993. Focal_AT. 1 hit.
SSF56112. Kinase_like. 1 hit.

PROSITE

PS00660. FERM_1. False negative.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1075288.

ChiTaRS

PTK2. mouse.

EvolutionaryTrace

P34152.

NextBio

285100.

SOURCE

Search...

Entry information

Entry name

FAK1_MOUSE

Accession

Primary (citable) accession number: P34152
Secondary accession number(s): O08578

Q9DAW3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	May 20, 2008
Last modified:	May 1, 2013
This is version 156 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents