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Q05397 (FAK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 175. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 phosphatase 1 regulatory subunit 71
Short name=PPP1R71
Protein-tyrosine kinase 2
p125FAK
pp125FAK
Gene names
Name:PTK2
Synonyms:FAK, FAK1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1052 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription. Ref.9 Ref.10 Ref.11 Ref.14 Ref.15 Ref.17 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.35 Ref.37 Ref.40 Ref.42 Ref.46 Ref.50 Ref.51 Ref.52 Ref.54 Ref.58

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.9 Ref.10 Ref.64

Enzyme regulation

Subject to autoinhibition, mediated by interactions between the FERM domain and the kinase domain. Activated by autophosphorylation at Tyr-397. This promotes interaction with SRC and phosphorylation at Tyr-576 and Tyr-577 in the kinase activation loop. Phosphorylation at Tyr-576 and Tyr-577 is required for maximal kinase activity. Inhibited by TAC544, TAE226, PF-573,228 and PF-562,271. Ref.9 Ref.22 Ref.23 Ref.25 Ref.40 Ref.52

Subunit structure

Interacts (via first Pro-rich region) with CAS family members (via SH3 domain), including BCAR1, BCAR3, CASS4 and NEDD9. Interacts with GIT1. Interacts with SORBS1. Interacts with ARHGEF28. Interacts with SHB. Interacts with PXN and TLN1. Interacts with STAT1. Interacts with DCC. Interacts with WASL. Interacts with ARHGEF7. Interacts with GRB2 and GRB7 By similarity. Component of a complex that contains at least FER, CTTN and PTK2/FAK1. Interacts with BMX. Interacts with TGFB1I1. Interacts with STEAP4. Interacts with ZFYVE21. Interacts with ESR1. Interacts with PIK3R1 or PIK3R2. Interacts with SRC, FGR, FLT4 and RET. Interacts with EPHA2 in resting cells; activation of EPHA2 recruits PTPN11, leading to dephosphorylation of PTK2/FAK1 and dissociation of the complex. Interacts with EPHA1 (kinase activity-dependent). Interacts with CD4; this interaction requires the presence of HIV-1 gp120. Interacts with PIAS1. Interacts with ARHGAP26 and SHC1. Interacts with RB1CC1; this inhibits PTK2/FAK1 activity and activation of downstream signaling pathways. Interacts with P53/TP53 and MDM2. Interacts with LPXN (via LD motif 3). Interacts with MISP. Interacts with CIB1 isoform 2. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.16 Ref.18 Ref.26 Ref.27 Ref.28 Ref.30 Ref.34 Ref.36 Ref.38 Ref.41 Ref.43 Ref.46 Ref.47 Ref.60 Ref.63 Ref.65

Subcellular location

Cell junctionfocal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcell cortex. Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Nucleus. Note: Constituent of focal adhesions. Detected at microtubules. Ref.9 Ref.16 Ref.28 Ref.29 Ref.65

Tissue specificity

Detected in B and T-lymphocytes. Isoform 1 and isoform 6 are detected in lung fibroblasts (at protein level). Ubiquitous. Ref.1 Ref.2 Ref.6 Ref.42

Developmental stage

Isoform 6 is detected in cultured cells, immediately after seeding and before formation of focal adhesions (at protein level). Ref.20

Domain

The Pro-rich regions interact with the SH3 domain of CAS family members, such as BCAR1 and NEDD9, and with the GTPase activating protein ARHGAP26.

The carboxy-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-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine residues. FGR promotes phosphorylation at Tyr-397 and Tyr-576. FER promotes phosphorylation at Tyr-577, Tyr-861 and Tyr-925, even when cells are not adherent. Tyr-397, Tyr-576 and Ser-722 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-397 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-925 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21. Ref.9 Ref.10 Ref.11 Ref.13 Ref.15 Ref.22 Ref.23 Ref.25 Ref.34 Ref.43 Ref.46 Ref.64

Sumoylated; this enhances autophosphorylation By similarity.

Involvement in disease

Aberrant PTK2/FAK1 expression may play a role in cancer cell proliferation, migration and invasion, in tumor formation and metastasis. PTK2/FAK1 overexpression is seen in many types of cancer. Ref.11 Ref.22 Ref.23 Ref.25 Ref.37 Ref.40 Ref.50 Ref.52 Ref.54

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. FAK subfamily.

Contains 1 FERM domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processAngiogenesis
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   Coding sequence diversityAlternative promoter usage
Alternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Transferase
Tyrosine-protein kinase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

angiogenesis

Traceable author statement Ref.56. Source: UniProtKB

apoptotic process

Traceable author statement. Source: Reactome

axon guidance

Traceable author statement Ref.49. Source: UniProtKB

blood coagulation

Traceable author statement. Source: Reactome

cell motility

Traceable author statement Ref.49. Source: UniProtKB

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

central nervous system neuron axonogenesis

Inferred from electronic annotation. Source: Ensembl

embryo development

Traceable author statement Ref.56. Source: UniProtKB

endothelial cell migration

Inferred from electronic annotation. Source: Ensembl

ephrin receptor signaling pathway

Inferred from direct assay Ref.9. Source: UniProtKB

establishment of cell polarity

Traceable author statement Ref.53. Source: UniProtKB

establishment of nucleus localization

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Inferred from electronic annotation. Source: Ensembl

growth hormone receptor signaling pathway

Inferred from direct assay PubMed 10925297. Source: BHF-UCL

heart morphogenesis

Traceable author statement Ref.56. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

integrin-mediated signaling pathway

Inferred from mutant phenotype Ref.10. Source: UniProtKB

microtubule cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

negative regulation of anoikis

Inferred from mutant phenotype PubMed 22402981. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype Ref.14. Source: UniProtKB

negative regulation of axonogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell-cell adhesion

Inferred from direct assay PubMed 21703394. Source: BHF-UCL

negative regulation of organ growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of synapse assembly

Inferred from electronic annotation. Source: Ensembl

netrin-activated signaling pathway

Traceable author statement Ref.49. Source: UniProtKB

neuron migration

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.9Ref.10. Source: UniProtKB

placenta development

Traceable author statement Ref.56. Source: UniProtKB

platelet activation

Traceable author statement. Source: Reactome

positive regulation of cell migration

Inferred from direct assay Ref.10. Source: UniProtKB

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phosphatidylinositol 3-kinase activity

Traceable author statement Ref.49. Source: UniProtKB

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from mutant phenotype Ref.14. Source: UniProtKB

positive regulation of protein kinase B signaling

Inferred from mutant phenotype Ref.14. Source: UniProtKB

positive regulation of protein kinase activity

Inferred from mutant phenotype Ref.10. Source: UniProtKB

positive regulation of protein phosphorylation

Inferred from mutant phenotype Ref.14. Source: UniProtKB

positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.9Ref.10. Source: UniProtKB

regulation of Rho GTPase activity

Traceable author statement Ref.53. Source: UniProtKB

regulation of cell adhesion mediated by integrin

Inferred from direct assay Ref.9. Source: UniProtKB

regulation of cell proliferation

Inferred from mutant phenotype Ref.29. Source: UniProtKB

regulation of cell shape

Inferred from mutant phenotype Ref.9Ref.14. Source: UniProtKB

regulation of cytoskeleton organization

Traceable author statement Ref.49. Source: UniProtKB

regulation of endothelial cell migration

Traceable author statement Ref.56. Source: UniProtKB

regulation of focal adhesion assembly

Traceable author statement Ref.50Ref.53. Source: UniProtKB

regulation of osteoblast differentiation

Inferred from mutant phenotype Ref.24. Source: UniProtKB

signal complex assembly

Inferred from electronic annotation. Source: InterPro

vasculogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: Ensembl

cell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoskeleton

Traceable author statement PubMed 10801330. Source: ProtInc

cytosol

Inferred from direct assay Ref.16. Source: UniProtKB

focal adhesion

Inferred from direct assay Ref.9Ref.16. Source: UniProtKB

lamellipodium

Inferred from electronic annotation. Source: Ensembl

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.16. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

JUN kinase binding

Inferred from direct assay PubMed 10925297. Source: BHF-UCL

SH2 domain binding

Inferred from physical interaction PubMed 15077193. Source: UniProtKB

actin binding

Inferred from direct assay PubMed 16803572. Source: BHF-UCL

non-membrane spanning protein tyrosine kinase activity

Inferred from direct assay Ref.9Ref.10. Source: UniProtKB

protein kinase activity

Traceable author statement. Source: Reactome

protein kinase binding

Inferred from physical interaction Ref.38. Source: UniProtKB

signal transducer activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q05397-1)

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: Q05397-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-181: Missing.
     182-189: EMRGNALE → MSDYWVVG
     472-472: A → ACHYTSLHWNWCRYISDPNVDACPDPRNAE
     834-854: Missing.
Isoform 3 (identifier: Q05397-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-181: Missing.
     182-189: EMRGNALE → MSDYWVVG
     472-472: A → ACHYTSLHWNWCRYISDPNVDACPDPRNAE
     677-706: STILEEEKAQQEERMRMESRRQATVSWDSG → FQNPAQMLPASGRLPNQPCPERENYSFATF
     707-1052: Missing.
Isoform 4 (identifier: Q05397-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-181: Missing.
     182-189: EMRGNALE → MSDYWVVG
     472-472: A → ACHYTSLHWNWCRYISDPNVDACPDPRNAE
     579-583: ASKGK → GKKSG
     584-1052: Missing.
Isoform 5 (identifier: Q05397-5)

The sequence of this isoform differs from the canonical sequence as follows:
     868-868: D → GKEEKNWAERN
     903-903: K → KPWR
Isoform 6 (identifier: Q05397-6)

Also known as: FRNK;

The sequence of this isoform differs from the canonical sequence as follows:
     1-692: Missing.
Note: Produced by alternative promoter usage.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 10521051Focal adhesion kinase 1
PRO_0000088077

Regions

Domain35 – 355321FERM
Domain422 – 680259Protein kinase
Nucleotide binding428 – 4347ATP
Nucleotide binding500 – 5023ATP
Region707 – 1052346Interaction with TGFB1I1
Region912 – 1052141Interaction with ARHGEF28 By similarity
Compositional bias712 – 73322Pro-rich
Compositional bias863 – 91351Pro-rich

Sites

Active site5461Proton acceptor By similarity
Binding site4541ATP

Amino acid modifications

Modified residue21N-acetylalanine Ref.5 Ref.33 Ref.39
Modified residue51Phosphotyrosine Ref.39
Modified residue131Phosphothreonine Ref.31 Ref.39
Modified residue291Phosphoserine Ref.31 Ref.39
Modified residue3971Phosphotyrosine; by autocatalysis Ref.13 Ref.15 Ref.22 Ref.23 Ref.25 Ref.34 Ref.39 Ref.43
Modified residue4071Phosphotyrosine Ref.13 Ref.15
Modified residue5701Phosphotyrosine Ref.39
Modified residue5761Phosphotyrosine; by RET and SRC Ref.15 Ref.34 Ref.46
Modified residue5771Phosphotyrosine; by RET and SRC Ref.13 Ref.34 Ref.46
Modified residue5801Phosphoserine Ref.39
Modified residue7221Phosphoserine Ref.34
Modified residue7321Phosphoserine; by CDK5
Modified residue8611Phosphotyrosine Ref.13 Ref.22 Ref.34
Modified residue8871Phosphoserine Ref.31
Modified residue9101Phosphoserine Ref.31 Ref.32 Ref.39 Ref.44
Modified residue9141Phosphothreonine Ref.44
Modified residue9251Phosphotyrosine Ref.13 Ref.34
Cross-link152Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence1 – 692692Missing in isoform 6.
VSP_042168
Alternative sequence1 – 181181Missing in isoform 2, isoform 3 and isoform 4.
VSP_004967
Alternative sequence182 – 1898EMRGNALE → MSDYWVVG in isoform 2, isoform 3 and isoform 4.
VSP_004968
Alternative sequence4721A → ACHYTSLHWNWCRYISDPNV DACPDPRNAE in isoform 2, isoform 3 and isoform 4.
VSP_004969
Alternative sequence579 – 5835ASKGK → GKKSG in isoform 4.
VSP_004971
Alternative sequence584 – 1052469Missing in isoform 4.
VSP_004972
Alternative sequence677 – 70630STILE…SWDSG → FQNPAQMLPASGRLPNQPCP ERENYSFATF in isoform 3.
VSP_004973
Alternative sequence707 – 1052346Missing in isoform 3.
VSP_004974
Alternative sequence834 – 85421Missing in isoform 2.
VSP_004970
Alternative sequence8681D → GKEEKNWAERN in isoform 5.
VSP_042169
Alternative sequence9031K → KPWR in isoform 5.
VSP_042170
Natural variant2921H → P. Ref.66
VAR_041682
Natural variant2921H → Q. Ref.66
VAR_041683
Natural variant7931V → A in a glioblastoma multiforme sample; somatic mutation. Ref.66
VAR_041684
Natural variant10301D → E. Ref.66
VAR_041685
Natural variant10441K → E in a metastatic melanoma sample; somatic mutation. Ref.66
VAR_041686

Experimental info

Mutagenesis3971Y → F: Abolishes autophosphorylation. Abolishes interaction with SRC and activation of BMX. Ref.10
Mutagenesis9281V → G: Loss of interaction with TGFB1I1. Ref.8
Mutagenesis10341L → S: Loss of interaction with TGFB1I1. Ref.8
Sequence conflict1841R → L in BAG65198. Ref.3
Sequence conflict2111L → I in BAG65198. Ref.3
Sequence conflict7781P → S in AAA35819. Ref.2

Secondary structure

........................................................................ 1052
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: D8A4C15138AB0243

FASTA1,052119,233
        10         20         30         40         50         60 
MAAAYLDPNL NHTPNSSTKT HLGTGMERSP GAMERVLKVF HYFESNSEPT TWASIIRHGD 

        70         80         90        100        110        120 
ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW 

       130        140        150        160        170        180 
KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMLEIA 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 THLADFTQVQ 

       310        320        330        340        350        360 
TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL VNGTSQSFII 

       370        380        390        400        410        420 
RPQKEGERAL PSIPKLANSE KQGMRTHAVS VSETDDYAEI IDEEDTYTMP STRDYEIQRE 

       430        440        450        460        470        480 
RIELGRCIGE GQFGDVHQGI YMSPENPALA 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 EEEKAQQEER MRMESRRQAT VSWDSGGSDE APPKPSRPGY 

       730        740        750        760        770        780 
PSPRSSEGFY PSPQHMVQTN HYQVSGYPGS HGITAMAGSI YPGQASLLDQ TDSWNHRPQE 

       790        800        810        820        830        840 
IAMWQPNVED STVLDLRGIG QVLPTHLMEE RLIRQQQEME EDQRWLEKEE RFLKPDVRLS 

       850        860        870        880        890        900 
RGSIDREDGS LQGPIGNQHI YQPVGKPDPA APPKKPPRPG APGHLGSLAS LSSPADSYNE 

       910        920        930        940        950        960 
GVKLQPQEIS PPPTANLDRS NDKVYENVTG LVKAVIEMSS KIQPAPPEEY VPMVKEVGLA 

       970        980        990       1000       1010       1020 
LRTLLATVDE TIPLLPASTH REIEMAQKLL NSDLGELINK MKLAQQYVMT SLQQEYKKQM 

      1030       1040       1050 
LTAAHALAVD AKNLLDVIDQ ARLKMLGQTR PH 

« Hide

Isoform 2 [UniParc].

Checksum: 64783EFF1FF4FCCB
Show »

FASTA87999,358
Isoform 3 [UniParc].

Checksum: 3960D6100B580E7D
Show »

FASTA55463,201
Isoform 4 [UniParc].

Checksum: 9C8013A49B83C690
Show »

FASTA43148,967
Isoform 5 [UniParc].

Checksum: 3FC0C66C4CF858D8
Show »

FASTA1,065120,900
Isoform 6 (FRNK) [UniParc].

Checksum: 0BD7ACE4EAEE63C0
Show »

FASTA36039,874

References

« Hide 'large scale' references
[1]"Human T and B lymphocytes express a structurally conserved focal adhesion kinase, pp125FAK."
Whitney G.S., Chan P.Y., Blake J., Cosand W.L., Neubauer M.G., Aruffo A., Kanner S.B.
DNA Cell Biol. 12:823-830(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: T-cell.
[2]"Expression of an N-terminally truncated form of human focal adhesion kinase in brain."
Andre E., Becker-Andre M.
Biochem. Biophys. Res. Commun. 190:140-147(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), TISSUE SPECIFICITY.
Tissue: Brain.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Trachea.
[4]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Bienvenut W.V., Glen H., Brunton V.G., Frame M.C.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-19; 192-199; 222-236; 243-252; 350-364; 414-419; 468-476; 562-569; 674-690; 798-811; 832-838; 904-933; 963-981; 989-1000 AND 1003-1042, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Osteosarcoma.
[6]"A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes."
Lee S.-T., Strunk K.M., Spritz R.A.
Oncogene 8:3403-3410(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 552-602, TISSUE SPECIFICITY.
Tissue: Melanocyte.
[7]"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.
[8]"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, MUTAGENESIS OF VAL-928 AND LEU-1034.
[9]"Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation."
Miao H., Burnett E., Kinch M., Simon E., Wang B.
Nat. Cell Biol. 2:62-69(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PXN PHOSPHORYLATION; REGULATION OF CELL SHAPE AND MIGRATION, INTERACTION WITH EPHA2, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, ENZYME REGULATION, DEPHOSPHORYLATION BY PTPN11, SUBCELLULAR LOCATION.
[10]"Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain."
Chen R., Kim O., Li M., Xiong X., Guan J.L., Kung H.J., Chen H., Shimizu Y., Qiu Y.
Nat. Cell Biol. 3:439-444(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL MIGRATION AND ACTIVATION OF BMX, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF TYR-397, INTERACTION WITH BMX.
[11]"Focal adhesion kinase enhances signaling through the Shc/extracellular signal-regulated kinase pathway in anaplastic astrocytoma tumor biopsy samples."
Hecker T.P., Grammer J.R., Gillespie G.Y., Stewart J. Jr., Gladson C.L.
Cancer Res. 62:2699-2707(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF SHC1, AUTOPHOSPHORYLATION, INTERACTION WITH SHC1 AND SRC, ROLE IN DISEASE.
[12]"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.
[13]"Site-specific phosphorylation of platelet focal adhesion kinase by low-density lipoprotein."
Relou I.A.M., Bax L.A.B., Van Rijn H.J.M., Akkerman J.-W.N.
Biochem. J. 369:407-416(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-397; TYR-407; TYR-577; TYR-861 AND TYR-925, INTERACTION WITH FGR.
[14]"Focal adhesion kinase is upstream of phosphatidylinositol 3-kinase/Akt in regulating fibroblast survival in response to contraction of type I collagen matrices via a beta 1 integrin viability signaling pathway."
Xia H., Nho R.S., Kahm J., Kleidon J., Henke C.A.
J. Biol. Chem. 279:33024-33034(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN INTEGRIN SIGNALING; REGULATION OF APOPTOSIS; REGULATION OF CELL SHAPE AND ACTIVATION OF PHOSPHATIDYLINOSITOL KINASE AND AKT1 SIGNALING PATHWAY.
[15]"The proto-oncogene Fgr regulates cell migration and this requires its plasma membrane localization."
Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L., Lowell C.A., Berton G.
Exp. Cell Res. 302:253-269(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN REGULATION OF CELL MIGRATION, PHOSPHORYLATION AT TYR-407; TYR-397 AND TYR-576.
[16]"Direct interaction of the N-terminal domain of focal adhesion kinase with the N-terminal transactivation domain of p53."
Golubovskaya V.M., Finch R., Cance W.G.
J. Biol. Chem. 280:25008-25021(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH P53/TP53, SUBCELLULAR LOCATION.
[17]"Microtubule-induced focal adhesion disassembly is mediated by dynamin and focal adhesion kinase."
Ezratty E.J., Partridge M.A., Gundersen G.G.
Nat. Cell Biol. 7:581-590(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN FOCAL ADHESION DISASSEMBLY.
[18]"Vascular endothelial growth factor receptor-3 and focal adhesion kinase bind and suppress apoptosis in breast cancer cells."
Garces C.A., Kurenova E.V., Golubovskaya V.M., Cance W.G.
Cancer Res. 66:1446-1454(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FLT4.
[19]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Expression of FAK-related non-kinase (FRNK) coincides with morphological change in the early stage of cell adhesion."
Nagoshi Y., Yamamoto G., Irie T., Tachikawa T.
Med. Mol. Morphol. 39:154-160(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE PROMOTER USAGE, IDENTIFICATION OF ISOFORM 6, DEVELOPMENTAL STAGE (ISOFORM 6).
[21]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Therapeutic efficacy of a novel focal adhesion kinase inhibitor TAE226 in ovarian carcinoma."
Halder J., Lin Y.G., Merritt W.M., Spannuth W.A., Nick A.M., Honda T., Kamat A.A., Han L.Y., Kim T.J., Lu C., Tari A.M., Bornmann W., Fernandez A., Lopez-Berestein G., Sood A.K.
Cancer Res. 67:10976-10983(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, ROLE IN DISEASE, PHOSPHORYLATION AT TYR-397 AND TYR-861.
[23]"Cellular characterization of a novel focal adhesion kinase inhibitor."
Slack-Davis J.K., Martin K.H., Tilghman R.W., Iwanicki M., Ung E.J., Autry C., Luzzio M.J., Cooper B., Kath J.C., Roberts W.G., Parsons J.T.
J. Biol. Chem. 282:14845-14852(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, ROLE IN DISEASE, PHOSPHORYLATION AT TYR-397.
[24]"Activation of FAK is necessary for the osteogenic differentiation of human mesenchymal stem cells on laminin-5."
Salasznyk R.M., Klees R.F., Boskey A., Plopper G.E.
J. Cell. Biochem. 100:499-514(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN OSTEOBLAST DIFFERENTIATION.
[25]"Inhibition of both focal adhesion kinase and insulin-like growth factor-I receptor kinase suppresses glioma proliferation in vitro and in vivo."
Liu T.J., LaFortune T., Honda T., Ohmori O., Hatakeyama S., Meyer T., Jackson D., de Groot J., Yung W.K.
Mol. Cancer Ther. 6:1357-1367(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, ROLE IN DISEASE, PHOSPHORYLATION AT TYR-397.
[26]"The LIM protein leupaxin is enriched in smooth muscle and functions as an serum response factor cofactor to induce smooth muscle cell gene transcription."
Sundberg-Smith L.J., DiMichele L.A., Sayers R.L., Mack C.P., Taylor J.M.
Circ. Res. 102:1502-1511(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LPXN.
[27]"Etk/BMX, a Btk family tyrosine kinase, and Mal contribute to the cross-talk between MyD88 and FAK pathways."
Semaan N., Alsaleh G., Gottenberg J.E., Wachsmann D., Sibilia J.
J. Immunol. 180:3485-3491(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BMX.
[28]"A novel Cas family member, HEPL, regulates FAK and cell spreading."
Singh M.K., Dadke D., Nicolas E., Serebriiskii I.G., Apostolou S., Canutescu A., Egleston B.L., Golemis E.A.
Mol. Biol. Cell 19:1627-1636(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CASS4.
[29]"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: FUNCTION IN REGULATION OF P53/TP53 LEVELS; CELL PROLIFERATION AND CELL SURVIVAL, SUBCELLULAR LOCATION.
[30]"Regulation of estrogen rapid signaling through arginine methylation by PRMT1."
Le Romancer M., Treilleux I., Leconte N., Robin-Lespinasse Y., Sentis S., Bouchekioua-Bouzaghou K., Goddard S., Gobert-Gosse S., Corbo L.
Mol. Cell 31:212-221(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ESR1; PIK3R1 AND/OR PIK3R2 AND SRC.
[31]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; SER-29; SER-887 AND SER-910, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[32]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[33]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[34]"Specific tyrosine phosphorylation of focal adhesion kinase mediated by Fer tyrosine kinase in suspended hepatocytes."
Oh M.A., Choi S., Lee M.J., Choi M.C., Lee S.A., Ko W., Cance W.G., Oh E.S., Buday L., Kim S.H., Lee J.W.
Biochim. Biophys. Acta 1793:781-791(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-397; TYR-576; TYR-577; SER-722; TYR-861 AND TYR-925, IDENTIFICATION IN A COMPLEX WITH CTTN AND FER.
[35]"Paxillin-Y118 phosphorylation contributes to the control of Src-induced anchorage-independent growth by FAK and adhesion."
Sachdev S., Bu Y., Gelman I.H.
BMC Cancer 9:12-12(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SRC-MEDIATED PHOSPHORYLATION OF PXN.
[36]"STEAP4 regulates focal adhesion kinase activation and CpG motifs within STEAP4 promoter region are frequently methylated in DU145, human androgen-independent prostate cancer cells."
Tamura T., Chiba J.
Int. J. Mol. Med. 24:599-604(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STEAP4.
[37]"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.
[38]"EphA1 interacts with integrin-linked kinase and regulates cell morphology and motility."
Yamazaki T., Masuda J., Omori T., Usui R., Akiyama H., Maru Y.
J. Cell Sci. 122:243-255(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EPHA1.
[39]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-5; THR-13; SER-29; TYR-397; TYR-570; SER-580 AND SER-910, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[40]"Bioluminescent imaging study: FAK inhibitor, PF-562,271, preclinical study in PC3M-luc-C6 local implant and metastasis xenograft models."
Sun H., Pisle S., Gardner E.R., Figg W.D.
Cancer Biol. Ther. 10:38-43(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN DISEASE, ENZYME REGULATION.
[41]"LIM domain-containing adaptor, leupaxin, localizes in focal adhesion and suppresses the integrin-induced tyrosine phosphorylation of paxillin."
Tanaka T., Moriwaki K., Murata S., Miyasaka M.
Cancer Sci. 101:363-368(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LPXN.
[42]"Downregulation of FAK-related non-kinase mediates the migratory phenotype of human fibrotic lung fibroblasts."
Cai G.Q., Zheng A., Tang Q., White E.S., Chou C.F., Gladson C.L., Olman M.A., Ding Q.
Exp. Cell Res. 316:1600-1609(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION (ISOFORM 6), TISSUE SPECIFICITY.
[43]"ZF21 protein regulates cell adhesion and motility."
Nagano M., Hoshino D., Sakamoto T., Kawasaki N., Koshikawa N., Seiki M.
J. Biol. Chem. 285:21013-21022(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZFYVE21, DEPHOSPHORYLATION AT TYR-397.
[44]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910 AND THR-914, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[45]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[46]"Focal adhesion kinase (FAK) binds RET kinase via its FERM domain, priming a direct and reciprocal RET-FAK transactivation mechanism."
Plaza-Menacho I., Morandi A., Mologni L., Boender P., Gambacorti-Passerini C., Magee A.I., Hofstra R.M.W., Knowles P., McDonald N.Q., Isacke C.M.
J. Biol. Chem. 286:17292-17302(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RET, FUNCTION IN RET PHOSPHORYLATION, PHOSPHORYLATION AT TYR-576 AND TYR-577.
[47]"A novel splice variant of calcium and integrin-binding protein 1 mediates protein kinase D2-stimulated tumour growth by regulating angiogenesis."
Armacki M., Joodi G., Nimmagadda S.C., de Kimpe L., Pusapati G.V., Vandoninck S., Van Lint J., Illing A., Seufferlein T.
Oncogene 0:0-0(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CIB1 ISOFORM 2.
Tissue: Brain.
[48]"Signaling through focal adhesion kinase."
Schlaepfer D.D., Hauck C.R., Sieg D.J.
Prog. Biophys. Mol. Biol. 71:435-478(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON SIGNALING AND ON DIRECT PTK2/FAK1 SUBSTRATES.
[49]"Netrin-integrin signaling in epithelial morphogenesis, axon guidance and vascular patterning."
Nikolopoulos S.N., Giancotti F.G.
Cell Cycle 4:E131-E135(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION IN NETRIN SIGNALING.
[50]"Integrin-regulated FAK-Src signaling in normal and cancer cells."
Mitra S.K., Schlaepfer D.D.
Curr. Opin. Cell Biol. 18:516-523(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION IN CELL MIGRATION; FOCAL ADHESION TURNOVER AND ACTIVATION OF SIGNALING PATHWAYS, ROLE IN DISEASE.
[51]"Focal adhesion kinase: an essential kinase in the regulation of cardiovascular functions."
Vadali K., Cai X., Schaller M.D.
IUBMB Life 59:709-716(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[52]"FERM control of FAK function: implications for cancer therapy."
Lim S.T., Mikolon D., Stupack D.G., Schlaepfer D.D.
Cell Cycle 7:2306-2314(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ROLE IN INTEGRIN SIGNALING AND IN REGULATION OF P53/TP53 ACTIVITIES, ROLE IN DISEASE, ENZYME REGULATION.
[53]"Focal adhesion kinase: switching between GAPs and GEFs in the regulation of cell motility."
Tomar A., Schlaepfer D.D.
Curr. Opin. Cell Biol. 21:676-683(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION IN REGULATION OF RHO FAMILY GTPASE ACTIVITY.
[54]"Focal adhesion kinase and cancer."
Golubovskaya V.M., Kweh F.A., Cance W.G.
Histol. Histopathol. 24:503-510(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON EXPRESSION IN CANCER, ROLE IN DISEASE.
[55]"Focal adhesion kinase and p53 signal transduction pathways in cancer."
Golubovskaya V.M., Cance W.
Front. Biosci. 15:901-912(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION IN REGULATION OF P53/TP53.
[56]"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.
[57]"Integrin signaling through FAK in the regulation of mammary stem cells and breast cancer."
Guan J.L.
IUBMB Life 62:268-276(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION IN INTEGRIN SIGNALING AND ACTIVATION OF DOWNSTREAM SIGNALING PATHWAYS.
[58]"Cellular functions of FAK kinases: insight into molecular mechanisms and novel functions."
Schaller M.D.
J. Cell Sci. 123:1007-1013(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SIGNALING.
[59]"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; ENZYME REGULATION AND ROLE IN DISEASE.
[60]"MISP is a novel Plk1 substrate required for proper spindle orientation and mitotic progression."
Zhu M., Settele F., Kotak S., Sanchez-Pulido L., Ehret L., Ponting C.P., Goenczy P., Hoffmann I.
J. Cell Biol. 200:773-787(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MISP.
[61]"The structural basis of localization and signaling by the focal adhesion targeting domain."
Arold S.T., Hoellerer M.K., Noble M.E.
Structure 10:319-327(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 891-1052, IDENTIFICATION BY MASS SPECTROMETRY.
[62]"Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography."
Nowakowski J., Cronin C.N., McRee D.E., Knuth M.W., Nelson C.G., Pavletich N.P., Rogers J., Sang B.C., Scheibe D.N., Swanson R.V., Thompson D.A.
Structure 10:1659-1667(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 411-686 IN COMPLEX WITH ATP.
[63]"Molecular recognition of paxillin LD motifs by the focal adhesion targeting domain."
Hoellerer M.K., Noble M.E., Labesse G., Campbell I.D., Werner J.M., Arold S.T.
Structure 11:1207-1217(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 892-1052 IN COMPLEX WITH PXN, INTERACTION WITH PXN.
[64]"Antitumor activity and pharmacology of a selective focal adhesion kinase inhibitor, PF-562,271."
Roberts W.G., Ung E., Whalen P., Cooper B., Hulford C., Autry C., Richter D., Emerson E., Lin J., Kath J., Coleman K., Yao L., Martinez-Alsina L., Lorenzen M., Berliner M., Luzzio M., Patel N., Schmitt E. expand/collapse author list , LaGreca S., Jani J., Wessel M., Marr E., Griffor M., Vajdos F.
Cancer Res. 68:1935-1944(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 414-689 IN COMPLEX WITH INHIBITOR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION.
[65]"Structural basis for the interaction between focal adhesion kinase and CD4."
Garron M.L., Arthos J., Guichou J.F., McNally J., Cicala C., Arold S.T.
J. Mol. Biol. 375:1320-1328(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.82 ANGSTROMS) OF 891-1052 IN COMPLEX WITH CD4, SUBCELLULAR LOCATION, INTERACTION WITH CD4.
[66]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] PRO-292; GLN-292; ALA-793; GLU-1030 AND GLU-1044.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L13616 mRNA. Translation: AAA58469.1.
L05186 mRNA. Translation: AAA35819.1.
AK304356 mRNA. Translation: BAG65198.1.
AC067931 Genomic DNA. No translation available.
AC100860 Genomic DNA. No translation available.
AC105009 Genomic DNA. No translation available.
AC105235 Genomic DNA. No translation available.
PIRI53012.
PC1225.
RefSeqNP_001186578.1. NM_001199649.1.
NP_722560.1. NM_153831.3.
UniGeneHs.395482.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K04X-ray1.95A891-1052[»]
1K05X-ray2.90A/B/C891-1052[»]
1MP8X-ray1.60A411-686[»]
1OW6X-ray2.35A/B/C892-1052[»]
1OW7X-ray2.60A/B/C892-1052[»]
1OW8X-ray2.85A/B/C892-1052[»]
2ETMX-ray2.30A/B411-689[»]
2IJMX-ray2.19A/B411-689[»]
2RA7X-ray1.99A921-1048[»]
3B71X-ray2.82A/B/C891-1052[»]
3BZ3X-ray2.20A414-689[»]
3PXKX-ray1.79A/B411-689[»]
3S9OX-ray2.60A/B/C891-1052[»]
4EBVX-ray1.67A411-686[»]
4EBWX-ray2.65A411-686[»]
4GU6X-ray1.95A/B411-689[»]
4GU9X-ray2.40A/B410-686[»]
4I4EX-ray1.55A411-686[»]
4I4FX-ray1.75A411-686[»]
4K8AX-ray2.91A/B410-686[»]
4K9YX-ray2.00A410-686[»]
4KABX-ray2.71A/B410-686[»]
4KAOX-ray2.39A/B410-689[»]
ProteinModelPortalQ05397.
SMRQ05397. Positions 33-715, 908-1049.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111719. 97 interactions.
IntActQ05397. 51 interactions.
MINTMINT-92695.
STRING9606.ENSP00000341189.

Chemistry

BindingDBQ05397.
ChEMBLCHEMBL2695.
GuidetoPHARMACOLOGY2180.

PTM databases

PhosphoSiteQ05397.

Polymorphism databases

DMDM3183518.

Proteomic databases

PaxDbQ05397.
PRIDEQ05397.

Protocols and materials databases

DNASU5747.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000340930; ENSP00000341189; ENSG00000169398. [Q05397-5]
ENST00000521059; ENSP00000429474; ENSG00000169398. [Q05397-1]
ENST00000522684; ENSP00000429911; ENSG00000169398. [Q05397-1]
GeneID5747.
KEGGhsa:5747.
UCSCuc003yvq.3. human. [Q05397-2]
uc003yvu.3. human. [Q05397-1]
uc011ljp.2. human. [Q05397-6]
uc011ljr.2. human. [Q05397-5]

Organism-specific databases

CTD5747.
GeneCardsGC08M141667.
HGNCHGNC:9611. PTK2.
HPACAB004036.
HPA001842.
MIM600758. gene.
neXtProtNX_Q05397.
PharmGKBPA33955.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000069938.
HOVERGENHBG004018.
InParanoidQ05397.
KOK05725.
OrthoDBEOG7ZSHSB.
PhylomeDBQ05397.
TreeFamTF316643.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_578. Apoptosis.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkQ05397.

Gene expression databases

ArrayExpressQ05397.
BgeeQ05397.
CleanExHS_PTK2.
GenevestigatorQ05397.

Family and domain databases

InterProIPR019749. Band_41_domain.
IPR019748. FERM_central.
IPR000299. FERM_domain.
IPR005189. Focal_adhesion_kin_target_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamPF00373. FERM_M. 1 hit.
PF03623. Focal_AT. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
ProDomPD006413. Focal_adhesion_target_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00295. B41. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF47031. SSF47031. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF68993. SSF68993. 1 hit.
PROSITEPS00661. 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]
ProtoNetSearch...

Other

ChiTaRSPTK2. human.
EvolutionaryTraceQ05397.
GeneWikiPTK2.
GenomeRNAi5747.
NextBio22380.
PMAP-CutDBQ05397.
PROQ05397.
SOURCESearch...

Entry information

Entry nameFAK1_HUMAN
AccessionPrimary (citable) accession number: Q05397
Secondary accession number(s): B4E2N6 expand/collapse secondary AC list , F5H4S4, Q14291, Q9UD85
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 175 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM