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O35346

- FAK1_RAT

UniProt

O35346 - FAK1_RAT

Protein

Focal adhesion kinase 1

Gene

Ptk2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      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 2 (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.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 by SRC. Phosphorylation at Tyr-397, Tyr-576 and Tyr-577 is required for maximal kinase activity.

    Sites

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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi428 – 4347ATPPROSITE-ProRule annotation
    Nucleotide bindingi500 – 5023ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. integrin binding Source: RGD
    4. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
    5. phosphatidylinositol 3-kinase binding Source: RGD
    6. protein binding Source: IntAct
    7. protein complex binding Source: RGD
    8. protein tyrosine kinase activity Source: RGD
    9. signal transducer activity Source: InterPro

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. cellular chloride ion homeostasis Source: RGD
    3. ephrin receptor signaling pathway Source: UniProtKB
    4. fat cell differentiation Source: RGD
    5. integrin-mediated signaling pathway Source: UniProtKB
    6. JNK cascade Source: RGD
    7. MAPK cascade Source: RGD
    8. negative regulation of apoptotic process Source: RGD
    9. negative regulation of cell migration Source: RGD
    10. peptidyl-tyrosine phosphorylation Source: UniProtKB
    11. positive regulation of cell adhesion Source: RGD
    12. positive regulation of cell growth Source: RGD
    13. positive regulation of cell migration Source: RGD
    14. positive regulation of cell proliferation Source: UniProtKB
    15. positive regulation of glial cell proliferation Source: RGD
    16. positive regulation of phagocytosis Source: RGD
    17. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    18. positive regulation of protein kinase activity Source: UniProtKB
    19. positive regulation of protein kinase B signaling Source: UniProtKB
    20. positive regulation of protein phosphorylation Source: UniProtKB
    21. positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
    22. positive regulation of smooth muscle cell migration Source: RGD
    23. positive regulation of smooth muscle cell proliferation Source: RGD
    24. positive regulation of synaptic transmission Source: RGD
    25. positive regulation of vasodilation Source: RGD
    26. protein autophosphorylation Source: UniProtKB
    27. regulation of cell adhesion mediated by integrin Source: UniProtKB
    28. regulation of cell proliferation Source: UniProtKB
    29. regulation of cell shape Source: UniProtKB
    30. regulation of osteoblast differentiation Source: UniProtKB
    31. response to arsenic-containing substance Source: RGD
    32. response to drug Source: RGD
    33. response to estradiol Source: RGD
    34. response to glucose Source: RGD
    35. response to mechanical stimulus Source: RGD
    36. response to organic cyclic compound Source: RGD
    37. response to organic substance Source: RGD
    38. response to organonitrogen compound Source: RGD
    39. 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. 5301.
    ReactomeiREACT_196755. Regulation of actin dynamics for phagocytic cup formation.

    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:Fak, Fak1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3443. Ptk2.

    Subcellular locationi

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

    GO - Cellular componenti

    1. apical plasma membrane Source: RGD
    2. basolateral plasma membrane Source: RGD
    3. cytosol Source: UniProtKB
    4. focal adhesion Source: RGD
    5. intercalated disc Source: RGD
    6. microtubule organizing center Source: UniProtKB-SubCell
    7. nuclear body Source: RGD
    8. nucleolus Source: RGD
    9. nucleus Source: RGD
    10. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    11. sarcolemma Source: RGD

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi152 – 1521K → R: Abolishes sumoylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 10551054Focal adhesion kinase 1PRO_0000088079Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    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)
    Modified residuei397 – 3971Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei407 – 4071PhosphotyrosineBy similarity
    Modified residuei570 – 5701PhosphotyrosineBy similarity
    Modified residuei576 – 5761Phosphotyrosine; by RET and SRCBy similarity
    Modified residuei577 – 5771Phosphotyrosine; by RET and SRCBy similarity
    Modified residuei580 – 5801PhosphoserineBy similarity
    Modified residuei722 – 7221Phosphoserine2 Publications
    Modified residuei732 – 7321Phosphoserine; by CDK5By similarity
    Modified residuei861 – 8611PhosphotyrosineBy similarity
    Modified residuei913 – 9131Phosphoserine2 Publications
    Modified residuei917 – 9171PhosphothreonineBy similarity
    Modified residuei928 – 9281PhosphotyrosineBy 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. FGR promotes phosphorylation at Tyr-397 and Tyr-576. FER promotes phosphorylation at Tyr-577, Tyr-861 and Tyr-928, even when cells are not adherent. Tyr-397, Tyr-576 and Ser-722 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-397 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-928 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21 By similarity.By similarity
    Sumoylated; this enhances autophosphorylation.3 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiO35346.
    PRIDEiO35346.

    PTM databases

    PhosphoSiteiO35346.

    Expressioni

    Gene expression databases

    GenevestigatoriO35346.

    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 PIK3R1 or PIK3R2. 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). Interacts with P53/TP53. Interacts (via first Pro-rich region) with CAS family members (via SH3 domain), including BCAR1, BCAR3, CASS4 and NEDD9. Interacts with TGFB1I1. Interacts with SRC, GRB2 and GRB7. Interacts with ARHGEF28. Interacts with SHB. Interacts with PXN and TLN1. Interacts with SORBS1. Interacts with STAT1. Interacts with WASL. Interacts with ARHGAP26 and SHC1. Interacts with RB1CC1; this inhibits PTK2/FAK1 activity and activation of downstream signaling pathways. Interacts with ARHGEF7. Interacts with MDM2 By similarity. Interacts with PIAS1. Interacts with DCC. Interacts with LPXN (via LD motif 3) By similarity. Interacts with MISP By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself12EBI-6252940,EBI-6252940
    Ptrh2Q5XI863EBI-6252940,EBI-6252926

    Protein-protein interaction databases

    BioGridi247643. 5 interactions.
    DIPiDIP-41330N.
    IntActiO35346. 4 interactions.
    MINTiMINT-208164.

    Structurei

    3D structure databases

    ProteinModelPortaliO35346.
    SMRiO35346. Positions 33-686, 911-1052.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni707 – 1055349Interaction with TGFB1I1By similarityAdd
    BLAST
    Regioni915 – 1055141Interaction with ARHGEF28By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi712 – 73322Pro-richAdd
    BLAST
    Compositional biasi863 – 91654Pro-richAdd
    BLAST

    Domaini

    The first Pro-rich domain interacts with the SH3 domain of CAS family members, such as BCAR1 and NEDD9.By similarity
    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.
    HOGENOMiHOG000069938.
    HOVERGENiHBG004018.
    KOiK05725.
    PhylomeDBiO35346.

    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.

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

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

    Isoform 1 (identifier: O35346-1) [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 HLGTGTERSP GAMERVLKVF HYFESSNEPT     50
    TWASIIRHGD ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV 100
    DMGVSSVREK YELAHPPEEW KYELRIRYLP KGFLNQFTED KPTLNFFYQQ 150
    VKSDYMLEIA DQVDQDIALK LGCLEIRRSY WEMRGNALEK KSNYEVLEKD 200
    VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI LKFFEILSPV 250
    YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFNQVQ 300
    TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL 350
    VNGATQSFII RPQKEGERAL PSIPKLANNE KQGMRTHAVS VSETDDYAEI 400
    IDEEDTYTMP STRDYEIQRE RIELGRCIGE GQFGDVHQGV YLSPENPALA 450
    VAIKTCKNCT SDSVREKFLQ EALTMRQFDH PHIVKLIGVI TENPVWIIME 500
    LCTLGELRSF LQVRKYSLDL ASLILYAYQL STALAYLESK RFVHRDIAAR 550
    NVLVSSNDCV KLGDFGLSRY MEDSTYYKAS KGKLPIKWMA PESINFRRFT 600
    SASDVWMFGV CMWEILMHGV KPFQGVKNND VIGRIENGER LPMPPNCPPT 650
    LYSLMTKCWA YDPSRRPRFT ELKAQLSTIL EEEKVQQEER MRMESRRQAT 700
    VSWDSGGSDE APPKPSRPGY PSPRSSEGFY PSPQHMVQTN HYQISGYPGS 750
    HGIPAMAGSI YPGQASLLDQ TELWNHRPQE MSMWQPSVED SAALDLRGMG 800
    QVLPPHLMEE RLIRQQQEME EDQRWLEKEE RFLKPDVRLS RGSIDREDGS 850
    FQGPTGNQHI YQPVGKPDPA APPKKPPRPG APGHLSNLSS ISSPAESYNE 900
    GVKPWRLQPQ EISPPPTANL DRSNDKVYEN VTGLVKAVIE MSSKIQPAPP 950
    EEYVPMVKEV GLALRTLLAT VDETIPILPA STHREIEMAQ KLLNSDLGEL 1000
    ISKMKLAQQY VMTSLQQEYK KQMLTAAHAL AVDAKNLLDV IDQARLKMLG 1050
    QTRPH 1055
    Length:1,055
    Mass (Da):119,717
    Last modified:January 1, 1998 - v1
    Checksum:i3AFB4ED682D14A33
    GO
    Isoform 2 (identifier: O35346-2) [UniParc]FASTAAdd to Basket

    Also known as: FRNK

    The sequence of this isoform differs from the canonical sequence as follows:
         2-692: Missing.

    Show »
    Length:364
    Mass (Da):40,540
    Checksum:iE41D2940196AE032
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 692691Missing in isoform 2. CuratedVSP_042172Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF020777 mRNA. Translation: AAB72203.1.
    U43942 mRNA. Translation: AAA86280.1.
    RefSeqiNP_037213.1. NM_013081.2. [O35346-1]
    UniGeneiRn.2809.

    Genome annotation databases

    GeneIDi25614.
    KEGGirno:25614.
    UCSCiRGD:3443. rat. [O35346-1]

    Keywords - Coding sequence diversityi

    Alternative promoter usage

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF020777 mRNA. Translation: AAB72203.1 .
    U43942 mRNA. Translation: AAA86280.1 .
    RefSeqi NP_037213.1. NM_013081.2. [O35346-1 ]
    UniGenei Rn.2809.

    3D structure databases

    ProteinModelPortali O35346.
    SMRi O35346. Positions 33-686, 911-1052.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 247643. 5 interactions.
    DIPi DIP-41330N.
    IntActi O35346. 4 interactions.
    MINTi MINT-208164.

    Chemistry

    ChEMBLi CHEMBL5773.

    PTM databases

    PhosphoSitei O35346.

    Proteomic databases

    PaxDbi O35346.
    PRIDEi O35346.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 25614.
    KEGGi rno:25614.
    UCSCi RGD:3443. rat. [O35346-1 ]

    Organism-specific databases

    CTDi 5747.
    RGDi 3443. Ptk2.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000069938.
    HOVERGENi HBG004018.
    KOi K05725.
    PhylomeDBi O35346.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 5301.
    Reactomei REACT_196755. Regulation of actin dynamics for phagocytic cup formation.

    Miscellaneous databases

    NextBioi 607363.
    PROi O35346.

    Gene expression databases

    Genevestigatori O35346.

    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. "Cloning of focal adhesion kinase, pp125FAK, from rat brain reveals multiple transcripts with different patterns of expression."
      Burgaya F., Girault J.A.
      Brain Res. Mol. Brain Res. 37:63-73(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: Sprague-Dawley.
      Tissue: Corpus striatum.
    2. Sasaki T., Nagura K., Sasaki H.
      Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 350-528 (ISOFORM 1).
      Strain: Wistar.
    3. "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.
    4. "Subcellular redistribution of focal adhesion kinase and its related nonkinase in hypertrophic myocardium."
      Yi X.P., Wang X., Gerdes A.M., Li F.
      Hypertension 41:1317-1323(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-722 AND SER-913, CHARACTERIZATION OF ISOFORM 2.
    5. Cited for: INTERACTION WITH ARHGEF28.
    6. "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: SUMOYLATION AT LYS-152, MUTAGENESIS OF LYS-152, INTERACTION WITH PIAS1, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT TYR-397, SUBCELLULAR LOCATION.
    7. Cited for: FUNCTION, INTERACTION WITH DCC.
    8. "Nuclear compartmentalization of FAK and FRNK in cardiac myocytes."
      Yi X.P., Zhou J., Huber L., Qu J., Wang X., Gerdes A.M., Li F.
      Am. J. Physiol. 290:H2509-H2515(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, CHARACTERIZATION OF ISOFORM 2.

    Entry informationi

    Entry nameiFAK1_RAT
    AccessioniPrimary (citable) accession number: O35346
    Secondary accession number(s): Q62900
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 143 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3