Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q00944

- FAK1_CHICK

UniProt

Q00944 - FAK1_CHICK

Protein

Focal adhesion kinase 1

Gene

PTK2

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (01 Feb 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development, embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), ephrin receptors, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Regulates P53/TP53 activity and stability. Phosphorylates SRC; this increases SRC kinase activity. Isoform 2 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling.6 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Enzyme regulationi

    Subject to autoinhibition, mediated by interactions between the FERM domain and the kinase domain. Activated by autophosphorylation at Tyr-397. This promotes interaction with SRC and phosphorylation at Tyr-576 and Tyr-577 in the kinase activation loop. Phosphorylation at Tyr-576 and Tyr-577 is required for maximal kinase activity. Inhibited by TAE226.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei454 – 4541ATPCurated
    Active sitei546 – 5461Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi428 – 4347ATPCurated
    Nucleotide bindingi500 – 5023ATPCurated

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
    4. protein binding Source: IntAct
    5. signal transducer activity Source: InterPro

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. signal complex assembly Source: InterPro

    Keywords - Molecular functioni

    Developmental protein, Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Angiogenesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 1306.
    ReactomeiREACT_197606. Regulation of actin dynamics for phagocytic cup formation.
    REACT_204997. Netrin mediated repulsion signals.
    REACT_207020. DCC mediated attractive signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Focal adhesion kinase 1 (EC:2.7.10.2)
    Short name:
    FADK 1
    Alternative name(s):
    Focal adhesion kinase-related nonkinase
    Short name:
    FRNK
    Short name:
    p41/p43FRNK
    Protein-tyrosine kinase 2
    p125FAK
    pp125FAK
    Gene namesi
    Name:PTK2
    Synonyms:FAK, FAK1
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Chromosome 2

    Subcellular locationi

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

    GO - Cellular componenti

    1. focal adhesion Source: UniProtKB-SubCell
    2. microtubule organizing center Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB-SubCell
    4. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    5. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi395 – 3951D → A: Abolishes interaction with PIK3R1. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10531053Focal adhesion kinase 1PRO_0000088076Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei397 – 3971Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei407 – 4071PhosphotyrosineBy similarity
    Modified residuei576 – 5761Phosphotyrosine; by SRC3 Publications
    Modified residuei577 – 5771Phosphotyrosine; by SRCBy similarity
    Modified residuei863 – 8631Phosphotyrosine2 Publications
    Modified residuei911 – 9111Phosphoserine2 Publications
    Modified residuei926 – 9261PhosphotyrosineBy similarity

    Post-translational modificationi

    Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine residues. Isoform 2 is phosphorylated on serine or threonine residues, but apparently not on tyrosine residues.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ00944.
    PRIDEiQ00944.

    Interactioni

    Subunit structurei

    Interacts with ARHGAP26, GRB7, DCC, PIK3R1, PXN and SRC. Interacts with the ARP2/3 complex.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-2896409,EBI-2896409
    ACTR3P611575EBI-2896409,EBI-351419From a different organism.
    METP085815EBI-2896409,EBI-1039152From a different organism.
    PXNP490242EBI-2896409,EBI-2896280
    SRCP005233EBI-2896409,EBI-848039

    Protein-protein interaction databases

    BioGridi676665. 2 interactions.
    IntActiQ00944. 11 interactions.
    MINTiMINT-1517788.

    Structurei

    Secondary structure

    1
    1053
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi36 – 405
    Helixi49 – 513
    Beta strandi53 – 586
    Helixi64 – 7411
    Helixi80 – 823
    Beta strandi83 – 897
    Beta strandi95 – 984
    Beta strandi100 – 1034
    Helixi104 – 1129
    Helixi117 – 1193
    Beta strandi120 – 1267
    Helixi133 – 1375
    Helixi141 – 15818
    Turni159 – 1624
    Helixi165 – 17915
    Turni180 – 1823
    Helixi187 – 1893
    Helixi191 – 1999
    Turni200 – 2023
    Helixi203 – 2053
    Helixi209 – 2135
    Helixi217 – 22913
    Turni230 – 2334
    Helixi236 – 24712
    Turni248 – 2503
    Beta strandi256 – 2627
    Beta strandi264 – 2663
    Beta strandi268 – 2758
    Turni276 – 2783
    Beta strandi279 – 2857
    Beta strandi290 – 2945
    Helixi296 – 2983
    Beta strandi299 – 3057
    Beta strandi308 – 3103
    Beta strandi314 – 3207
    Beta strandi327 – 3337
    Helixi334 – 35219
    Beta strandi398 – 4025
    Helixi412 – 4143
    Helixi419 – 4213
    Beta strandi422 – 4309
    Beta strandi432 – 44110
    Beta strandi444 – 4463
    Beta strandi448 – 4558
    Turni457 – 4604
    Helixi462 – 47615
    Beta strandi486 – 4905
    Beta strandi492 – 4943
    Beta strandi496 – 5005
    Helixi507 – 5137
    Turni514 – 5174
    Helixi520 – 53920
    Helixi549 – 5513
    Beta strandi552 – 5565
    Beta strandi559 – 5624
    Helixi565 – 5684
    Beta strandi573 – 5753
    Helixi586 – 5883
    Helixi591 – 5966
    Helixi601 – 61616
    Turni617 – 6193
    Turni622 – 6254
    Helixi628 – 6303
    Helixi631 – 6366
    Helixi649 – 65810
    Helixi663 – 6653
    Helixi669 – 68517
    Turni919 – 9213
    Helixi922 – 94120
    Turni942 – 9454
    Helixi948 – 97528
    Turni978 – 9803
    Helixi982 – 100524
    Beta strandi1008 – 10125
    Helixi1014 – 104734

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KTMNMR-A916-1053[»]
    1PV3NMR-A920-1053[»]
    1QVXNMR-A920-1053[»]
    2AEHX-ray2.53A/B31-399[»]
    2AL6X-ray2.35A/B31-405[»]
    2J0JX-ray2.80A31-686[»]
    2J0KX-ray3.00A/B31-686[»]
    2J0LX-ray2.30A411-686[»]
    2J0MX-ray2.80A31-399[»]
    B411-686[»]
    2JKKX-ray2.00A411-686[»]
    2JKMX-ray2.31A411-686[»]
    2JKOX-ray1.65A411-686[»]
    2JKQX-ray2.60A411-686[»]
    2L6FNMR-A916-1053[»]
    2L6GNMR-A916-1053[»]
    2L6HNMR-A916-1053[»]
    3ZDTX-ray3.15A/B31-405[»]
    4BRXX-ray2.05A411-686[»]
    4C7TX-ray2.05A411-686[»]
    4CYEX-ray3.20A/B31-405[»]
    ProteinModelPortaliQ00944.
    SMRiQ00944. Positions 33-686, 916-1053.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ00944.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 355321FERMPROSITE-ProRule annotationAdd
    BLAST
    Domaini422 – 680259Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi712 – 73322Pro-richAdd
    BLAST
    Compositional biasi865 – 91450Pro-richAdd
    BLAST

    Domaini

    The carboxy-terminal region is the site of focal adhesion targeting (FAT) sequence which mediates the localization of FAK1 to focal adhesions.

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. FAK subfamily.PROSITE-ProRule annotation
    Contains 1 FERM domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00740000115459.
    HOGENOMiHOG000069938.
    HOVERGENiHBG004018.
    KOiK05725.
    PhylomeDBiQ00944.

    Family and domain databases

    InterProiIPR019749. 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.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF00373. FERM_M. 1 hit.
    PF03623. Focal_AT. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PRINTSiPR00109. TYRKINASE.
    ProDomiPD006413. Focal_adhesion_target_reg. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00295. B41. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47031. SSF47031. 1 hit.
    SSF54236. SSF54236. 1 hit.
    SSF56112. SSF56112. 1 hit.
    SSF68993. SSF68993. 1 hit.
    PROSITEiPS00661. 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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative promoter usage. Align

    Isoform 1 (identifier: Q00944-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAAAYLDPNL NHTPSSSAKT HLGTGMERSP GAMERVLKVF HYFENSSEPT     50
    TWASIIRHGD ATDVRGIIQK IVDCHKVKNV ACYGLRLSHL QSEEVHWLHL 100
    DMGVSNVREK FELAHPPEEW KYELRIRYLP KGFLNQFTED KPTLNFFYQQ 150
    VKNDYMLEIA DQVDQEIALK LGCLEIRRSY GEMRGNALEK KSNYEVLEKD 200
    VGLRRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI LKFFEILSPV 250
    YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGANP THLADFNQVQ 300
    TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL 350
    VNGATQSFII RPQKEGERAL PSIPKLANNE KQGVRSHTVS VSETDDYAEI 400
    IDEEDTYTMP STRDYEIQRE RIELGRCIGE GQFGDVHQGI YMSPENPAMA 450
    VAIKTCKNCT SDSVREKFLQ EALTMRQFDH PHIVKLIGVI TENPVWIIME 500
    LCTLGELRSF LQVRKFSLDL ASLILYAYQL STALAYLESK RFVHRDIAAR 550
    NVLVSATDCV KLGDFGLSRY MEDSTYYKAS KGKLPIKWMA PESINFRRFT 600
    SASDVWMFGV CMWEILMHGV KPFQGVKNND VIGRIENGER LPMPPNCPPT 650
    LYSLMTKCWA YDPSRRPRFT ELKAQLSTIL EEEKLQQEER MRMESRRQVT 700
    VSWDSGGSDE APPKPSRPGY PSPRSSEGFY PSPQHMVQPN HYQVSGYSGS 750
    HGIPAMAGSI YPGQASLLDQ TDSWNHRPQE VSAWQPNMED SGTLDVRGMG 800
    QVLPTHLMEE RLIRQQQEME EDQRWLEKEE RFLVMKPDVR LSRGSIERED 850
    GGLQGPAGNQ HIYQPVGKPD HAAPPKKPPR PGAPHLGSLA SLNSPVDSYN 900
    EGVKIKPQEI SPPPTANLDR SNDKVYENVT GLVKAVIEMS SKIQPAPPEE 950
    YVPMVKEVGL ALRTLLATVD ESLPVLPAST HREIEMAQKL LNSDLAELIN 1000
    KMKLAQQYVM TSLQQEYKKQ MLTAAHALAV DAKNLLDVID QARLKMISQS 1050
    RPH 1053
    Length:1,053
    Mass (Da):119,207
    Last modified:February 1, 1994 - v2
    Checksum:i8051154219B953B9
    GO
    Isoform 2 (identifier: Q00944-2) [UniParc]FASTAAdd to Basket

    Also known as: FRNK

    The sequence of this isoform differs from the canonical sequence as follows:
         1-692: Missing.

    Show »
    Length:361
    Mass (Da):40,032
    Checksum:i61E6AD4B50CCCC49
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 692692Missing in isoform 2. CuratedVSP_042173Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86656 mRNA. Translation: AAA48765.1.
    L08402 mRNA. Translation: AAA48766.1.
    PIRiA45388.
    PC1239.
    RefSeqiNP_990766.1. NM_205435.1. [Q00944-1]
    UniGeneiGga.15614.

    Genome annotation databases

    EnsembliENSGALT00000026060; ENSGALP00000026013; ENSGALG00000016171. [Q00944-1]
    GeneIDi396416.
    KEGGigga:396416.

    Keywords - Coding sequence diversityi

    Alternative promoter usage

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86656 mRNA. Translation: AAA48765.1 .
    L08402 mRNA. Translation: AAA48766.1 .
    PIRi A45388.
    PC1239.
    RefSeqi NP_990766.1. NM_205435.1. [Q00944-1 ]
    UniGenei Gga.15614.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KTM NMR - A 916-1053 [» ]
    1PV3 NMR - A 920-1053 [» ]
    1QVX NMR - A 920-1053 [» ]
    2AEH X-ray 2.53 A/B 31-399 [» ]
    2AL6 X-ray 2.35 A/B 31-405 [» ]
    2J0J X-ray 2.80 A 31-686 [» ]
    2J0K X-ray 3.00 A/B 31-686 [» ]
    2J0L X-ray 2.30 A 411-686 [» ]
    2J0M X-ray 2.80 A 31-399 [» ]
    B 411-686 [» ]
    2JKK X-ray 2.00 A 411-686 [» ]
    2JKM X-ray 2.31 A 411-686 [» ]
    2JKO X-ray 1.65 A 411-686 [» ]
    2JKQ X-ray 2.60 A 411-686 [» ]
    2L6F NMR - A 916-1053 [» ]
    2L6G NMR - A 916-1053 [» ]
    2L6H NMR - A 916-1053 [» ]
    3ZDT X-ray 3.15 A/B 31-405 [» ]
    4BRX X-ray 2.05 A 411-686 [» ]
    4C7T X-ray 2.05 A 411-686 [» ]
    4CYE X-ray 3.20 A/B 31-405 [» ]
    ProteinModelPortali Q00944.
    SMRi Q00944. Positions 33-686, 916-1053.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 676665. 2 interactions.
    IntActi Q00944. 11 interactions.
    MINTi MINT-1517788.

    Proteomic databases

    PaxDbi Q00944.
    PRIDEi Q00944.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSGALT00000026060 ; ENSGALP00000026013 ; ENSGALG00000016171 . [Q00944-1 ]
    GeneIDi 396416.
    KEGGi gga:396416.

    Organism-specific databases

    CTDi 5747.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000115459.
    HOGENOMi HOG000069938.
    HOVERGENi HBG004018.
    KOi K05725.
    PhylomeDBi Q00944.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 1306.
    Reactomei REACT_197606. Regulation of actin dynamics for phagocytic cup formation.
    REACT_204997. Netrin mediated repulsion signals.
    REACT_207020. DCC mediated attractive signaling.

    Miscellaneous databases

    EvolutionaryTracei Q00944.
    NextBioi 20816457.
    PROi Q00944.

    Family and domain databases

    InterProi IPR019749. 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.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF00373. FERM_M. 1 hit.
    PF03623. Focal_AT. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PRINTSi PR00109. TYRKINASE.
    ProDomi PD006413. Focal_adhesion_target_reg. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00295. B41. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47031. SSF47031. 1 hit.
    SSF54236. SSF54236. 1 hit.
    SSF56112. SSF56112. 1 hit.
    SSF68993. SSF68993. 1 hit.
    PROSITEi PS00661. FERM_2. 1 hit.
    PS50057. FERM_3. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions."
      Schaller M.D., Borgman C.A., Cobb B.S., Vines R.R., Reynolds A.B., Parsons J.T.
      Proc. Natl. Acad. Sci. U.S.A. 89:5192-5196(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-1053 (ISOFORM 1).
      Tissue: Embryo.
    2. "Chicken and mouse focal adhesion kinases are similar in structure at their amino termini."
      Devor B.B., Zhang X., Patel S.K., Polte T.R., Hanks S.K.
      Biochem. Biophys. Res. Commun. 190:1084-1089(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-63 (ISOFORM 1).
      Tissue: Embryo.
    3. "Autonomous expression of a noncatalytic domain of the focal adhesion-associated protein tyrosine kinase pp125FAK."
      Schaller M.D., Borgman C.A., Parsons J.T.
      Mol. Cell. Biol. 13:785-791(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE PROMOTER USAGE, IDENTIFICATION OF ISOFORM 2, PHOSPHORYLATION, SUBCELLULAR LOCATION.
    4. "An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase."
      Hildebrand J.D., Taylor J.M., Parsons J.T.
      Mol. Cell. Biol. 16:3169-3178(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARHGAP26.
    5. "Requirement of phosphatidylinositol 3-kinase in focal adhesion kinase-promoted cell migration."
      Reiske H.R., Kao S.C., Cary L.A., Guan J.L., Lai J.F., Chen H.C.
      J. Biol. Chem. 274:12361-12366(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIK3R1 AND SRC, MUTAGENESIS OF ASP-395.
    6. "Association of Grb7 with phosphoinositides and its role in the regulation of cell migration."
      Shen T.L., Han D.C., Guan J.L.
      J. Biol. Chem. 277:29069-29077(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRB7.
    7. "Tyr-863 phosphorylation enhances focal adhesion kinase autophosphorylation at Tyr-397."
      Leu T.H., Maa M.C.
      Oncogene 21:6992-7000(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-397; TYR-576 AND TYR-863.
    8. Cited for: FUNCTION, INTERACTION WITH DCC.
    9. "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: FUNCTION, INTERACTION WITH DCC.
    10. "Netrin requires focal adhesion kinase and Src family kinases for axon outgrowth and attraction."
      Liu G., Beggs H., Jurgensen C., Park H.T., Tang H., Gorski J., Jones K.R., Reichardt L.F., Wu J., Rao Y.
      Nat. Neurosci. 7:1222-1232(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Focal adhesion kinase controls actin assembly via a FERM-mediated interaction with the Arp2/3 complex."
      Serrels B., Serrels A., Brunton V.G., Holt M., McLean G.W., Gray C.H., Jones G.E., Frame M.C.
      Nat. Cell Biol. 9:1046-1056(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH THE ARP2/3 COMPLEX.
    12. "FRNK inhibition of focal adhesion kinase-dependent signaling and migration in vascular smooth muscle cells."
      Koshman Y.E., Kim T., Chu M., Engman S.J., Iyengar R., Robia S.L., Samarel A.M.
      Arterioscler. Thromb. Vasc. Biol. 30:2226-2233(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Focal adhesion kinase-related nonkinase inhibits vascular smooth muscle cell invasion by focal adhesion targeting, tyrosine 168 phosphorylation, and competition for p130Cas Binding."
      Koshman Y.E., Chu M., Engman S.J., Kim T., Iyengar R., Robia S.L., Samarel A.M.
      Arterioscler. Thromb. Vasc. Biol. 31:2432-2440(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Serine-910 phosphorylation of focal adhesion kinase is critical for sarcomere reorganization in cardiomyocyte hypertrophy."
      Chu M., Iyengar R., Koshman Y.E., Kim T., Russell B., Martin J.L., Heroux A.L., Robia S.L., Samarel A.M.
      Cardiovasc. Res. 92:409-419(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-911, FUNCTION.
    15. "Structural insight into the mechanisms of targeting and signaling of focal adhesion kinase."
      Liu G., Guibao C.D., Zheng J.
      Mol. Cell. Biol. 22:2751-2760(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 916-1053.
    16. "NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: evidence for a two-site binding model."
      Gao G., Prutzman K.C., King M.L., Scheswohl D.M., DeRose E.F., London R.E., Schaller M.D., Campbell S.L.
      J. Biol. Chem. 279:8441-8451(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 920-1053 IN COMPLEX WITH PXN, INTERACTION WITH PXN.
    17. "The focal adhesion targeting domain of focal adhesion kinase contains a hinge region that modulates tyrosine 926 phosphorylation."
      Prutzman K.C., Gao G., King M.L., Iyer V.V., Mueller G.A., Schaller M.D., Campbell S.L.
      Structure 12:881-891(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 920-1053.
    18. "Crystal structure of the FERM domain of focal adhesion kinase."
      Ceccarelli D.F., Song H.K., Poy F., Schaller M.D., Eck M.J.
      J. Biol. Chem. 281:252-259(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 31-405.
    19. "Structural basis for the autoinhibition of focal adhesion kinase."
      Lietha D., Cai X., Ceccarelli D.F., Li Y., Schaller M.D., Eck M.J.
      Cell 129:1177-1187(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 411-686 IN COMPLEXES WITH STAUROSPORINE AND ATP ANALOG, ENZYME REGULATION, PHOSPHORYLATION AT TYR-576 AND TYR-577.
    20. "Crystal structures of the FAK kinase in complex with TAE226 and related bis-anilino pyrimidine inhibitors reveal a helical DFG conformation."
      Lietha D., Eck M.J.
      PLoS ONE 3:E3800-E3800(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 411-686 IN COMPLEX WITH TAE226.

    Entry informationi

    Entry nameiFAK1_CHICK
    AccessioniPrimary (citable) accession number: Q00944
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 139 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3