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P34152

- FAK1_MOUSE

UniProt

P34152 - FAK1_MOUSE

Protein

Focal adhesion kinase 1

Gene

Ptk2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 3 (20 May 2008)
      Previous versions | rss
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    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 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.By similarity

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.3 PublicationsPROSITE-ProRule annotation

    Enzyme regulationi

    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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei492 – 4921ATPPROSITE-ProRule annotation
    Active sitei584 – 5841Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi466 – 4727ATPPROSITE-ProRule annotation
    Nucleotide bindingi538 – 5403ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. angiogenesis Source: MGI
    2. blood vessel development Source: MGI
    3. cellular component movement Source: MGI
    4. central nervous system neuron axonogenesis Source: MGI
    5. endothelial cell migration Source: MGI
    6. ephrin receptor signaling pathway Source: UniProtKB
    7. establishment of nucleus localization Source: MGI
    8. extracellular matrix organization Source: MGI
    9. growth hormone receptor signaling pathway Source: Ensembl
    10. integrin-mediated signaling pathway Source: UniProtKB
    11. microtubule cytoskeleton organization Source: MGI
    12. negative regulation of anoikis Source: Ensembl
    13. negative regulation of apoptotic process Source: UniProtKB
    14. negative regulation of axonogenesis Source: MGI
    15. negative regulation of cell-cell adhesion Source: Ensembl
    16. negative regulation of organ growth Source: MGI
    17. negative regulation of synapse assembly Source: MGI
    18. neuron migration Source: MGI
    19. peptidyl-tyrosine phosphorylation Source: UniProtKB
    20. positive regulation of cell migration Source: UniProtKB
    21. positive regulation of cell proliferation Source: UniProtKB
    22. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    23. positive regulation of protein kinase activity Source: UniProtKB
    24. positive regulation of protein kinase B signaling Source: UniProtKB
    25. positive regulation of protein phosphorylation Source: UniProtKB
    26. positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
    27. protein autophosphorylation Source: UniProtKB
    28. regulation of cell adhesion mediated by integrin Source: UniProtKB
    29. regulation of cell proliferation Source: UniProtKB
    30. regulation of cell shape Source: UniProtKB
    31. regulation of osteoblast differentiation Source: UniProtKB
    32. signal complex assembly Source: InterPro
    33. vasculogenesis Source: MGI

    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. 3474.
    ReactomeiREACT_198374. Regulation of actin dynamics for phagocytic cup formation.
    REACT_224460. Apoptotic cleavage of cellular proteins.

    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
    Protein-tyrosine kinase 2
    p125FAK
    pp125FAK
    Gene namesi
    Name:Ptk2
    Synonyms:Fadk, Fak, Fak1, Kiaa4203
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:95481. Ptk2.

    Subcellular locationi

    GO - Cellular componenti

    1. apical plasma membrane Source: MGI
    2. cytosol Source: Reactome
    3. focal adhesion Source: MGI
    4. lamellipodium Source: MGI
    5. microtubule organizing center Source: UniProtKB-SubCell
    6. nucleus Source: UniProtKB
    7. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Disruption phenotypei

    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.4 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi428 – 4281Y → 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. 3 Publications
    Mutagenesisi614 – 6152YY → FF: Strongly reduced enzyme activity; when associated with F-428.
    Mutagenesisi963 – 9631Y → F: Abolishes interaction with GRB2. 2 Publications
    Mutagenesisi1072 – 10721L → S: Loss of interaction with ARHGEF28. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 10901089Focal adhesion kinase 1PRO_0000088078Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei5 – 51PhosphotyrosineBy similarity
    Modified residuei13 – 131PhosphothreonineBy similarity
    Modified residuei29 – 291PhosphoserineBy similarity
    Cross-linki152 – 152Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei428 – 4281Phosphotyrosine; by autocatalysis5 Publications
    Modified residuei438 – 4381Phosphotyrosine2 Publications
    Modified residuei608 – 6081PhosphotyrosineBy similarity
    Modified residuei614 – 6141Phosphotyrosine; by RET and SRC5 Publications
    Modified residuei615 – 6151Phosphotyrosine; by RET and SRC5 Publications
    Modified residuei618 – 6181PhosphoserineBy similarity
    Modified residuei760 – 7601PhosphoserineBy similarity
    Modified residuei770 – 7701Phosphoserine; by CDK51 Publication
    Modified residuei899 – 8991Phosphotyrosine1 Publication
    Modified residuei948 – 9481Phosphoserine1 Publication
    Modified residuei952 – 9521PhosphothreonineBy similarity
    Modified residuei963 – 9631Phosphotyrosine; by SRC5 Publications

    Post-translational modificationi

    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 ZFYVE21.14 Publications
    Sumoylated; this enhances autophosphorylation.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP34152.
    PaxDbiP34152.
    PRIDEiP34152.

    PTM databases

    PhosphoSiteiP34152.

    Expressioni

    Developmental stagei

    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.

    Gene expression databases

    BgeeiP34152.
    CleanExiMM_PTK2.
    GenevestigatoriP34152.

    Interactioni

    Subunit structurei

    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).By similarity22 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    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.

    Protein-protein interaction databases

    BioGridi199587. 10 interactions.
    IntActiP34152. 21 interactions.
    MINTiMINT-141959.

    Structurei

    Secondary structure

    1
    1090
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi960 – 98021
    Helixi985 – 9873
    Helixi989 – 100921
    Helixi1010 – 10123
    Helixi1018 – 104427
    Helixi1048 – 108134

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K40X-ray2.25A959-1084[»]
    1KKYmodel-B959-1084[»]
    1KL0model-A959-1084[»]
    ProteinModelPortaliP34152.
    SMRiP34152. Positions 34-764, 959-1084.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP34152.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 355321FERMPROSITE-ProRule annotationAdd
    BLAST
    Domaini469 – 718250Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni745 – 1090346Interaction with TGFB1I1By similarityAdd
    BLAST
    Regioni950 – 1090141Interaction with ARHGEF28Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi750 – 77122Pro-richAdd
    BLAST
    Compositional biasi901 – 95151Pro-richAdd
    BLAST

    Domaini

    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.

    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.
    HOVERGENiHBG004018.
    InParanoidiP34152.
    KOiK05725.
    OMAiVQTNHYQ.
    OrthoDBiEOG7ZSHSB.
    PhylomeDBiP34152.
    TreeFamiTF316643.

    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 (9)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 9 isoformsi produced by alternative promoter usage and alternative splicing. Align

    Isoform 1 (identifier: P34152-1) [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 NHTPSSSTKT HLGTGMERSP GAMERVLKVF HYFESSSEPT     50
    TWASIIRHGD ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV 100
    DMGVSSVREK YELAHPPEEW KYELRIRYLP KGFLNQFTED KPTLNFFYQQ 150
    VKSDYMQEIA DQVDQEIALK LGCLEIRRSY WEMRGNALEK KSNYEVLEKD 200
    VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI LKFFEILSPV 250
    YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFNQVQ 300
    TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL 350
    VNGATQSFII RPQKEGERAL PSIPKLANSE KQGMRTHAVS VSHCQHKVKK 400
    ARRFLPLVFC SLEPPPTDEI SGDETDDYAE IIDEEDTYTM PSKSYGIDEA 450
    RDYEIQRERI ELGRCIGEGQ FGDVHQGVYL SPENPALAVA IKTCKNCTSD 500
    SVREKFLQEA LTMRQFDHPH IVKLIGVITE NPVWIIMELC TLGELRSFLQ 550
    VRKYSLDLAS LILYAYQLST ALAYLESKRF VHRDIAARNV LVSSNDCVKL 600
    GDFGLSRYME DSTYYKASKG KLPIKWMAPE SINFRRFTSA SDVWMFGVCM 650
    WEILMHGVKP FQGVKNNDVI GRIENGERLP MPPNCPPTLY SLMTKCWAYD 700
    PSRRPRFTEL KAQLSTILEE EKVQQEERMR MESRRQATVS WDSGGSDEAP 750
    PKPSRPGYPS PRSSEGFYPS PQHMVQTNHY QVSGYPGSHG IPAMAGSIYQ 800
    GQASLLDQTE LWNHRPQEMS MWQPSVEDSA ALDLRGMGQV LPPHLMEERL 850
    IRQQQEMEED QRWLEKEERF LKPDVRLSRG SIDREDGSFQ GPTGNQHIYQ 900
    PVGKPDPAAP PKKPPRPGAP GHLSNLSSIS SPADSYNEGV KLQPQEISPP 950
    PTANLDRSND KVYENVTGLV KAVIEMSSKI QPAPPEEYVP MVKEVGLALR 1000
    TLLATVDETI PALPASTHRE IEMAQKLLNS DLGELISKMK LAQQYVMTSL 1050
    QQEYKKQMLT AAHALAVDAK NLLDVIDQAR LKMLGQTRPH 1090
    Length:1,090
    Mass (Da):123,537
    Last modified:May 20, 2008 - v3
    Checksum:i7C795105A9B9DCA6
    GO
    Isoform 2 (identifier: P34152-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         443-450: KSYGIDEA → T

    Show »
    Length:1,083
    Mass (Da):122,774
    Checksum:iE536A38627B90A83
    GO
    Isoform 3 (identifier: P34152-3) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:1,052
    Mass (Da):119,243
    Checksum:i4B7453C5D81F0F63
    GO
    Isoform 4 (identifier: P34152-4) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:1,055
    Mass (Da):119,682
    Checksum:iAFB79846FA73ED6F
    GO
    Isoform 5 (identifier: P34152-5) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:957
    Mass (Da):108,608
    Checksum:iD277A4D65AE6012A
    GO
    Isoform 6 (identifier: P34152-6) [UniParc]FASTAAdd to Basket

    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.Curated Contains a phosphotyrosine at position 397.Curated

    Show »
    Length:916
    Mass (Da):104,070
    Checksum:iF2DA51E8CC785229
    GO
    Isoform 7 (identifier: P34152-7) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:509
    Mass (Da):57,697
    Checksum:iA406369629607D5D
    GO
    Isoform 8 (identifier: P34152-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         199-1090: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:198
    Mass (Da):23,064
    Checksum:i2732777636068833
    GO
    Isoform 9 (identifier: P34152-9) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:360
    Mass (Da):39,930
    Checksum:i6C5E4C5486C62265
    GO

    Sequence cautioni

    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
    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti32 – 321A → T in BC030180. (PubMed:15489334)Curated
    Sequence conflicti42 – 421Y → H in AAA37592. (PubMed:1528852)Curated
    Sequence conflicti87 – 871L → V in BAB24058. (PubMed:16141072)Curated
    Sequence conflicti128 – 1281Y → D in BAB24058. (PubMed:16141072)Curated
    Sequence conflicti146 – 1461F → V in BAB24058. (PubMed:16141072)Curated
    Sequence conflicti157 – 1571Q → L in BC030180. (PubMed:15489334)Curated
    Sequence conflicti225 – 2251Q → H in BAC37757. (PubMed:16141072)Curated
    Sequence conflicti250 – 2501V → M in BAC37757. (PubMed:16141072)Curated
    Sequence conflicti800 – 8001Q → P in BC030180. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 730730Missing in isoform 9. CuratedVSP_042171Add
    BLAST
    Alternative sequencei199 – 1090892Missing in isoform 8. 1 PublicationVSP_033998Add
    BLAST
    Alternative sequencei392 – 3921S → SGVS in isoform 5. 1 PublicationVSP_033999
    Alternative sequencei393 – 42331Missing in isoform 3, isoform 4 and isoform 6. 4 PublicationsVSP_004975Add
    BLAST
    Alternative sequencei393 – 41725Missing in isoform 7. 1 PublicationVSP_034000Add
    BLAST
    Alternative sequencei443 – 4508KSYGIDEA → T in isoform 2, isoform 3, isoform 4 and isoform 6. 4 PublicationsVSP_004976
    Alternative sequencei511 – 53424LTMRQ…ENPVW → SEVIFASKKIQLGPGIFDII CLSA in isoform 7. 1 PublicationVSP_034001Add
    BLAST
    Alternative sequencei535 – 1090556Missing in isoform 7. 1 PublicationVSP_034002Add
    BLAST
    Alternative sequencei941 – 9411K → KPWR in isoform 4. 1 PublicationVSP_034003
    Alternative sequencei942 – 95413LQPQE…PPTAN → VGICACAMWSVPC in isoform 5 and isoform 6. 2 PublicationsVSP_034004Add
    BLAST
    Alternative sequencei955 – 1090136Missing in isoform 5 and isoform 6. 2 PublicationsVSP_034005Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , AF025648, AF025649, AF025650, AF025651 Genomic DNA. Translation: AAB95262.1.
    AF025652
    , AF025648, AF025649, AF025650 Genomic DNA. Translation: AAB95263.1.
    U77074 Genomic DNA. Translation: AAB51229.1.
    CCDSiCCDS37099.1. [P34152-3]
    CCDS49631.1. [P34152-6]
    PIRiA46166.
    RefSeqiNP_001123881.1. NM_001130409.1. [P34152-6]
    NP_032008.2. NM_007982.2. [P34152-3]
    XP_006520496.1. XM_006520433.1. [P34152-4]
    UniGeneiMm.254494.

    Genome annotation databases

    EnsembliENSMUST00000110036; ENSMUSP00000105663; ENSMUSG00000022607. [P34152-3]
    ENSMUST00000170939; ENSMUSP00000126764; ENSMUSG00000022607. [P34152-6]
    GeneIDi14083.
    KEGGimmu:14083.
    UCSCiuc007wbw.2. mouse. [P34152-4]
    uc007wbx.2. mouse. [P34152-3]
    uc007wby.2. mouse. [P34152-5]
    uc007wbz.2. mouse. [P34152-6]
    uc007wca.1. mouse. [P34152-8]

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , AF025648 , AF025649 , AF025650 , AF025651 Genomic DNA. Translation: AAB95262.1 .
    AF025652
    , AF025648 , AF025649 , AF025650 Genomic DNA. Translation: AAB95263.1 .
    U77074 Genomic DNA. Translation: AAB51229.1 .
    CCDSi CCDS37099.1. [P34152-3 ]
    CCDS49631.1. [P34152-6 ]
    PIRi A46166.
    RefSeqi NP_001123881.1. NM_001130409.1. [P34152-6 ]
    NP_032008.2. NM_007982.2. [P34152-3 ]
    XP_006520496.1. XM_006520433.1. [P34152-4 ]
    UniGenei Mm.254494.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1K40 X-ray 2.25 A 959-1084 [» ]
    1KKY model - B 959-1084 [» ]
    1KL0 model - A 959-1084 [» ]
    ProteinModelPortali P34152.
    SMRi P34152. Positions 34-764, 959-1084.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199587. 10 interactions.
    IntActi P34152. 21 interactions.
    MINTi MINT-141959.

    Chemistry

    ChEMBLi CHEMBL1075288.

    PTM databases

    PhosphoSitei P34152.

    Proteomic databases

    MaxQBi P34152.
    PaxDbi P34152.
    PRIDEi P34152.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000110036 ; ENSMUSP00000105663 ; ENSMUSG00000022607 . [P34152-3 ]
    ENSMUST00000170939 ; ENSMUSP00000126764 ; ENSMUSG00000022607 . [P34152-6 ]
    GeneIDi 14083.
    KEGGi mmu:14083.
    UCSCi uc007wbw.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

    CTDi 5747.
    MGIi MGI:95481. Ptk2.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000115459.
    HOVERGENi HBG004018.
    InParanoidi P34152.
    KOi K05725.
    OMAi VQTNHYQ.
    OrthoDBi EOG7ZSHSB.
    PhylomeDBi P34152.
    TreeFami TF316643.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 3474.
    Reactomei REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
    REACT_224460. Apoptotic cleavage of cellular proteins.

    Miscellaneous databases

    ChiTaRSi PTK2. mouse.
    EvolutionaryTracei P34152.
    NextBioi 285100.
    PROi P34152.
    SOURCEi Search...

    Gene expression databases

    Bgeei P34152.
    CleanExi MM_PTK2.
    Genevestigatori P34152.

    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. "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.
      , 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. 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. 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. 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. 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. 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.

    Entry informationi

    Entry nameiFAK1_MOUSE
    AccessioniPrimary (citable) accession number: P34152
    Secondary accession number(s): O08578
    , Q5DTH7, Q8C513, Q8CFH7, Q8CHM2, Q8K2S0, Q9DAW3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 171 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3