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P34152 (FAK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 166. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·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-tyrosine kinase 2
p125FAK
pp125FAK
Gene names
Name:Ptk2
Synonyms:Fadk, Fak, Fak1, Kiaa4203
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1090 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 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.37 Ref.38 Ref.41 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 MISP By similarity. Interacts with PIAS1. Interacts with ARHGAP26 and SHC1. Interacts with RB1CC1; this inhibits PTK2/FAK1 activity and activation of downstream signaling pathways. Interacts with P53/TP53. Interacts with STAT1. Interacts with WASL. Interacts with ARHGEF7. Interacts with DCC. Interacts (via first Pro-rich region) with CAS family members (via SH3 domain), including BCAR1, BCAR3, CASS4 and NEDD9. Interacts with SORBS1. Interacts with ARHGEF28. Interacts with SHB. Interacts with PXN and TLN1. Interacts with TGFB1I1. Interacts with PIK3R1 or PIK3R2. Interacts with SRC, GRB2 and GRB7. Interacts with LPXN (via LD motif 3). 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.38 Ref.41 Ref.43 Ref.48

Subcellular location

Cell junctionfocal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmperinuclear region. Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Nucleus By similarity. Note: Constituent of focal adhesions. Detected at microtubules. Ref.1 Ref.26 Ref.41

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.37 Ref.41

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 processAngiogenesis
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   Coding sequence diversityAlternative promoter usage
Alternative splicing
   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_processangiogenesis

Inferred from mutant phenotype Ref.34. Source: MGI

blood vessel development

Inferred from mutant phenotype PubMed 12595342Ref.34. Source: MGI

cellular component movement

Traceable author statement PubMed 11784865. Source: MGI

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

growth hormone receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

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-cell adhesion

Inferred from electronic annotation. Source: Ensembl

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 migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation

Inferred from mutant phenotype Ref.41. Source: UniProtKB

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein kinase B signaling

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 phosphorylation

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.41. Source: UniProtKB

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 proliferation

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

signal complex assembly

Inferred from electronic annotation. Source: InterPro

vasculogenesis

Inferred from mutant phenotype Ref.34. Source: MGI

   Cellular_componentapical plasma membrane

Inferred from direct assay PubMed 10742111. Source: MGI

cytosol

Traceable author statement. Source: Reactome

focal adhesion

Inferred from direct assay PubMed 10699171PubMed 11784865PubMed 15728191PubMed 16405917. Source: MGI

lamellipodium

Inferred from direct assay PubMed 15728191. Source: MGI

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.41. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein tyrosine kinase activity

Inferred from direct assay Ref.11. Source: UniProtKB

signal transducer activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Bcar1Q611403EBI-77070,EBI-77088
Ephb2P547633EBI-77070,EBI-537711
GRB2P629933EBI-77070,EBI-401755From a different organism.
L1camP116274EBI-77070,EBI-397964
Nrp1P973332EBI-77070,EBI-1555129
PTPN1P180312EBI-77070,EBI-968788From a different organism.
PxnQ8VI363EBI-77070,EBI-983394
SRCP129312EBI-77070,EBI-621482From a different organism.

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. Contains a phosphotyrosine at position 397.
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. Contains a phosphotyrosine at position 397.
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. Contains a phosphotyrosine at position 397.
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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 10901089Focal adhesion kinase 1
PRO_0000088078

Regions

Domain35 – 355321FERM
Domain469 – 718250Protein kinase
Nucleotide binding466 – 4727ATP By similarity
Nucleotide binding538 – 5403ATP By similarity
Region745 – 1090346Interaction with TGFB1I1 By similarity
Region950 – 1090141Interaction with ARHGEF28
Compositional bias750 – 77122Pro-rich
Compositional bias901 – 95151Pro-rich

Sites

Active site5841Proton acceptor By similarity
Binding site4921ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.6
Modified residue51Phosphotyrosine By similarity
Modified residue131Phosphothreonine By similarity
Modified residue291Phosphoserine By similarity
Modified residue4281Phosphotyrosine; by autocatalysis Ref.11 Ref.13 Ref.19 Ref.21 Ref.24
Modified residue4381Phosphotyrosine Ref.11 Ref.24
Modified residue6081Phosphotyrosine By similarity
Modified residue6141Phosphotyrosine; by RET and SRC Ref.11 Ref.19 Ref.24 Ref.39 Ref.40
Modified residue6151Phosphotyrosine; by RET and SRC Ref.11 Ref.19 Ref.24 Ref.39 Ref.40
Modified residue6181Phosphoserine By similarity
Modified residue7601Phosphoserine By similarity
Modified residue7701Phosphoserine; by CDK5 Ref.26
Modified residue8991Phosphotyrosine Ref.24
Modified residue9481Phosphoserine Ref.6
Modified residue9521Phosphothreonine By similarity
Modified residue9631Phosphotyrosine; by SRC Ref.9 Ref.14 Ref.15 Ref.24 Ref.40
Cross-link152Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence1 – 730730Missing in isoform 9.
VSP_042171
Alternative sequence199 – 1090892Missing in isoform 8.
VSP_033998
Alternative sequence3921S → SGVS in isoform 5.
VSP_033999
Alternative sequence393 – 42331Missing in isoform 3, isoform 4 and isoform 6.
VSP_004975
Alternative sequence393 – 41725Missing in isoform 7.
VSP_034000
Alternative sequence443 – 4508KSYGIDEA → T in isoform 2, isoform 3, isoform 4 and isoform 6.
VSP_004976
Alternative sequence511 – 53424LTMRQ…ENPVW → SEVIFASKKIQLGPGIFDII CLSA in isoform 7.
VSP_034001
Alternative sequence535 – 1090556Missing in isoform 7.
VSP_034002
Alternative sequence9411K → KPWR in isoform 4.
VSP_034003
Alternative sequence942 – 95413LQPQE…PPTAN → VGICACAMWSVPC in isoform 5 and isoform 6.
VSP_034004
Alternative sequence955 – 1090136Missing in isoform 5 and isoform 6.
VSP_034005

Experimental info

Mutagenesis4281Y → 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
Mutagenesis614 – 6152YY → FF: Strongly reduced enzyme activity; when associated with F-428.
Mutagenesis9631Y → F: Abolishes interaction with GRB2. Ref.9 Ref.14
Mutagenesis10721L → S: Loss of interaction with ARHGEF28. Ref.28
Sequence conflict321A → T in BC030180. Ref.5
Sequence conflict421Y → H in AAA37592. Ref.1
Sequence conflict871L → V in BAB24058. Ref.3
Sequence conflict1281Y → D in BAB24058. Ref.3
Sequence conflict1461F → V in BAB24058. Ref.3
Sequence conflict1571Q → L in BC030180. Ref.5
Sequence conflict2251Q → H in BAC37757. Ref.3
Sequence conflict2501V → M in BAC37757. Ref.3
Sequence conflict8001Q → P in BC030180. Ref.5

Secondary structure

............ 1090
Helix Strand Turn

Details...

Sequences

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

Last modified May 20, 2008. Version 3.
Checksum: 7C795105A9B9DCA6

FASTA1,090123,537
        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 »

FASTA1,083122,774
Isoform 3 [UniParc].

Checksum: 4B7453C5D81F0F63
Show »

FASTA1,052119,243
Isoform 4 [UniParc].

Checksum: AFB79846FA73ED6F
Show »

FASTA1,055119,682
Isoform 5 [UniParc].

Checksum: D277A4D65AE6012A
Show »

FASTA957108,608
Isoform 6 [UniParc].

Checksum: F2DA51E8CC785229
Show »

FASTA916104,070
Isoform 7 [UniParc].

Checksum: A406369629607D5D
Show »

FASTA50957,697
Isoform 8 [UniParc].

Checksum: 2732777636068833
Show »

FASTA19823,064
Isoform 9 (FRNK) [UniParc].

Checksum: 6C5E4C5486C62265
Show »

FASTA36039,930

References

« Hide '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. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
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, IDENTIFICATION BY 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]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-397 (ISOFORMS 3; 4 AND 6), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[37]"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.
[38]"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.
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[40]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[41]"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.
[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 expand/collapse EMBL AC list , AF025648, AF025649, AF025650, AF025651 Genomic DNA. Translation: AAB95262.1.
AF025652 expand/collapse EMBL AC list , AF025648, AF025649, AF025650 Genomic DNA. Translation: AAB95263.1.
U77074 Genomic DNA. Translation: AAB51229.1.
PIRA46166.
RefSeqNP_001123881.1. NM_001130409.1.
NP_032008.2. NM_007982.2.
XP_006520496.1. XM_006520433.1.
UniGeneMm.254494.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K40X-ray2.25A959-1084[»]
1KKYmodel-B959-1084[»]
1KL0model-A959-1084[»]
ProteinModelPortalP34152.
SMRP34152. Positions 33-764, 959-1084.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199587. 10 interactions.
IntActP34152. 21 interactions.
MINTMINT-141959.

Chemistry

ChEMBLCHEMBL1075288.

PTM databases

PhosphoSiteP34152.

Proteomic databases

PaxDbP34152.
PRIDEP34152.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000110036; ENSMUSP00000105663; ENSMUSG00000022607. [P34152-3]
ENSMUST00000170939; ENSMUSP00000126764; ENSMUSG00000022607. [P34152-6]
GeneID14083.
KEGGmmu:14083.
UCSCuc007wbw.2. mouse. [P34152-4]
uc007wbx.2. mouse. [P34152-3]
uc007wby.2. mouse. [P34152-5]
uc007wbz.2. mouse. [P34152-6]
uc007wca.1. mouse. [P34152-8]

Organism-specific databases

CTD5747.
MGIMGI:95481. Ptk2.
RougeSearch...

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00740000115459.
HOVERGENHBG004018.
InParanoidP34152.
KOK05725.
OMAVQTNHYQ.
OrthoDBEOG7ZSHSB.
PhylomeDBP34152.
TreeFamTF316643.

Enzyme and pathway databases

BRENDA2.7.10.2. 3474.
ReactomeREACT_188576. Developmental Biology.

Gene expression databases

BgeeP34152.
CleanExMM_PTK2.
GenevestigatorP34152.

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. mouse.
EvolutionaryTraceP34152.
NextBio285100.
PROP34152.
SOURCESearch...

Entry information

Entry nameFAK1_MOUSE
AccessionPrimary (citable) accession number: P34152
Secondary accession number(s): O08578 expand/collapse secondary AC list , Q5DTH7, Q8C513, Q8CFH7, Q8CHM2, Q8K2S0, Q9DAW3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: May 20, 2008
Last modified: April 16, 2014
This is version 166 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

MGD cross-references

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