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Q05397

- FAK1_HUMAN

UniProt

Q05397 - FAK1_HUMAN

Protein

Focal adhesion kinase 1

Gene

PTK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 180 (01 Oct 2014)
      Sequence version 2 (15 Jul 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 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription.23 Publications

    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-397. This promotes interaction with SRC and phosphorylation at Tyr-576 and Tyr-577 in the kinase activation loop. Phosphorylation at Tyr-576 and Tyr-577 is required for maximal kinase activity. Inhibited by TAC544, TAE226, PF-573,228 and PF-562,271.6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei454 – 4541ATP1 PublicationPROSITE-ProRule annotation
    Active sitei546 – 5461Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi428 – 4347ATP1 PublicationPROSITE-ProRule annotation
    Nucleotide bindingi500 – 5023ATP1 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. actin binding Source: BHF-UCL
    2. ATP binding Source: UniProtKB-KW
    3. JUN kinase binding Source: BHF-UCL
    4. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein kinase activity Source: Reactome
    7. protein kinase binding Source: UniProtKB
    8. SH2 domain binding Source: UniProtKB
    9. signal transducer activity Source: InterPro

    GO - Biological processi

    1. angiogenesis Source: UniProtKB
    2. apoptotic process Source: Reactome
    3. axon guidance Source: UniProtKB
    4. blood coagulation Source: Reactome
    5. cell motility Source: UniProtKB
    6. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
    7. central nervous system neuron axonogenesis Source: Ensembl
    8. embryo development Source: UniProtKB
    9. endothelial cell migration Source: Ensembl
    10. ephrin receptor signaling pathway Source: UniProtKB
    11. establishment of cell polarity Source: UniProtKB
    12. establishment of nucleus localization Source: Ensembl
    13. extracellular matrix organization Source: Ensembl
    14. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    15. growth hormone receptor signaling pathway Source: BHF-UCL
    16. heart morphogenesis Source: UniProtKB
    17. innate immune response Source: Reactome
    18. integrin-mediated signaling pathway Source: UniProtKB
    19. microtubule cytoskeleton organization Source: Ensembl
    20. negative regulation of anoikis Source: UniProtKB
    21. negative regulation of apoptotic process Source: UniProtKB
    22. negative regulation of axonogenesis Source: Ensembl
    23. negative regulation of cell-cell adhesion Source: BHF-UCL
    24. negative regulation of organ growth Source: Ensembl
    25. negative regulation of synapse assembly Source: Ensembl
    26. netrin-activated signaling pathway Source: UniProtKB
    27. neuron migration Source: Ensembl
    28. peptidyl-tyrosine phosphorylation Source: UniProtKB
    29. placenta development Source: UniProtKB
    30. platelet activation Source: Reactome
    31. positive regulation of cell migration Source: UniProtKB
    32. positive regulation of cell proliferation Source: UniProtKB
    33. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
    34. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    35. positive regulation of protein kinase activity Source: UniProtKB
    36. positive regulation of protein kinase B signaling Source: UniProtKB
    37. positive regulation of protein phosphorylation Source: UniProtKB
    38. positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
    39. protein autophosphorylation Source: UniProtKB
    40. regulation of cell adhesion mediated by integrin Source: UniProtKB
    41. regulation of cell proliferation Source: UniProtKB
    42. regulation of cell shape Source: UniProtKB
    43. regulation of cytoskeleton organization Source: UniProtKB
    44. regulation of endothelial cell migration Source: UniProtKB
    45. regulation of focal adhesion assembly Source: UniProtKB
    46. regulation of osteoblast differentiation Source: UniProtKB
    47. regulation of Rho GTPase activity Source: UniProtKB
    48. signal complex assembly Source: InterPro
    49. vasculogenesis Source: Ensembl

    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. 2681.
    ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
    REACT_15381. p130Cas linkage to MAPK signaling for integrins.
    REACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_18334. NCAM signaling for neurite out-growth.
    REACT_22351. DCC mediated attractive signaling.
    REACT_22384. Netrin mediated repulsion signals.
    REACT_23916. Signal regulatory protein (SIRP) family interactions.
    SignaLinkiQ05397.

    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 phosphatase 1 regulatory subunit 71
    Short name:
    PPP1R71
    Protein-tyrosine kinase 2
    p125FAK
    pp125FAK
    Gene namesi
    Name:PTK2
    Synonyms:FAK, FAK1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:9611. PTK2.

    Subcellular locationi

    GO - Cellular componenti

    1. apical plasma membrane Source: Ensembl
    2. cell cortex Source: UniProtKB-SubCell
    3. cytoskeleton Source: ProtInc
    4. cytosol Source: UniProtKB
    5. focal adhesion Source: UniProtKB
    6. lamellipodium Source: Ensembl
    7. microtubule organizing center Source: UniProtKB-SubCell
    8. nucleus Source: UniProtKB

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Involvement in diseasei

    Aberrant PTK2/FAK1 expression may play a role in cancer cell proliferation, migration and invasion, in tumor formation and metastasis. PTK2/FAK1 overexpression is seen in many types of cancer.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi397 – 3971Y → F: Abolishes autophosphorylation. Abolishes interaction with SRC and activation of BMX. 1 Publication
    Mutagenesisi928 – 9281V → G: Loss of interaction with TGFB1I1. 1 Publication
    Mutagenesisi1034 – 10341L → S: Loss of interaction with TGFB1I1. 1 Publication

    Organism-specific databases

    PharmGKBiPA33955.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 10521051Focal adhesion kinase 1PRO_0000088077Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei5 – 51Phosphotyrosine1 Publication
    Modified residuei13 – 131Phosphothreonine2 Publications
    Modified residuei29 – 291Phosphoserine2 Publications
    Cross-linki152 – 152Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei397 – 3971Phosphotyrosine; by autocatalysis7 Publications
    Modified residuei407 – 4071Phosphotyrosine2 Publications
    Modified residuei570 – 5701Phosphotyrosine1 Publication
    Modified residuei576 – 5761Phosphotyrosine; by RET and SRC3 Publications
    Modified residuei577 – 5771Phosphotyrosine; by RET and SRC3 Publications
    Modified residuei580 – 5801Phosphoserine1 Publication
    Modified residuei722 – 7221Phosphoserine1 Publication
    Modified residuei732 – 7321Phosphoserine; by CDK5By similarity
    Modified residuei861 – 8611Phosphotyrosine3 Publications
    Modified residuei887 – 8871Phosphoserine1 Publication
    Modified residuei910 – 9101Phosphoserine4 Publications
    Modified residuei914 – 9141Phosphothreonine1 Publication
    Modified residuei925 – 9251Phosphotyrosine2 Publications

    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-925, even when cells are not adherent. Tyr-397, Tyr-576 and Ser-722 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-397 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-925 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21.11 Publications
    Sumoylated; this enhances autophosphorylation.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ05397.
    PaxDbiQ05397.
    PRIDEiQ05397.

    PTM databases

    PhosphoSiteiQ05397.

    Miscellaneous databases

    PMAP-CutDBQ05397.

    Expressioni

    Tissue specificityi

    Detected in B and T-lymphocytes. Isoform 1 and isoform 6 are detected in lung fibroblasts (at protein level). Ubiquitous.4 Publications

    Developmental stagei

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

    Gene expression databases

    ArrayExpressiQ05397.
    BgeeiQ05397.
    CleanExiHS_PTK2.
    GenevestigatoriQ05397.

    Organism-specific databases

    HPAiCAB004036.
    HPA001842.

    Interactioni

    Subunit structurei

    Interacts (via first Pro-rich region) with CAS family members (via SH3 domain), including BCAR1, BCAR3, CASS4 and NEDD9. Interacts with GIT1. Interacts with SORBS1. Interacts with ARHGEF28. Interacts with SHB. Interacts with PXN and TLN1. Interacts with STAT1. Interacts with DCC. Interacts with WASL. Interacts with ARHGEF7. Interacts with GRB2 and GRB7 By similarity. Component of a complex that contains at least FER, CTTN and PTK2/FAK1. Interacts with BMX. Interacts with TGFB1I1. Interacts with STEAP4. Interacts with ZFYVE21. Interacts with ESR1. Interacts with PIK3R1 or PIK3R2. Interacts with SRC, FGR, FLT4 and RET. Interacts with EPHA2 in resting cells; activation of EPHA2 recruits PTPN11, leading to dephosphorylation of PTK2/FAK1 and dissociation of the complex. Interacts with EPHA1 (kinase activity-dependent). Interacts with CD4; this interaction requires the presence of HIV-1 gp120. Interacts with PIAS1. Interacts with ARHGAP26 and SHC1. Interacts with RB1CC1; this inhibits PTK2/FAK1 activity and activation of downstream signaling pathways. Interacts with P53/TP53 and MDM2. Interacts with LPXN (via LD motif 3). Interacts with MISP. Interacts with CIB1 isoform 2.By similarity25 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCAR1P569452EBI-702142,EBI-702093
    CRKLP461092EBI-702142,EBI-910
    EPHA2P293173EBI-702142,EBI-702104
    ERBB2P046262EBI-702142,EBI-641062
    FLT1P179482EBI-702142,EBI-1026718
    PTPN23Q9H3S74EBI-702142,EBI-724478
    PTRH2Q9Y3E52EBI-702142,EBI-1056751
    PXNP4902315EBI-702142,EBI-702209
    SRCP129317EBI-702142,EBI-621482
    SrcP054805EBI-702142,EBI-298680From a different organism.
    TGFB1I1O432942EBI-702142,EBI-1051449
    Tgfb1i1Q622193EBI-702142,EBI-642844From a different organism.
    TNS3Q68CZ23EBI-702142,EBI-1220488
    TP53P0463713EBI-702142,EBI-366083

    Protein-protein interaction databases

    BioGridi111719. 99 interactions.
    IntActiQ05397. 58 interactions.
    MINTiMINT-92695.
    STRINGi9606.ENSP00000341189.

    Structurei

    Secondary structure

    1
    1052
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi35 – 406
    Helixi49 – 513
    Beta strandi53 – 586
    Helixi64 – 7310
    Turni74 – 763
    Helixi80 – 823
    Beta strandi83 – 897
    Beta strandi95 – 984
    Helixi104 – 11411
    Helixi117 – 1193
    Beta strandi120 – 1267
    Helixi133 – 1375
    Helixi141 – 15818
    Helixi165 – 17915
    Helixi185 – 1873
    Beta strandi188 – 1903
    Helixi191 – 1944
    Helixi197 – 2015
    Turni204 – 2063
    Helixi209 – 2146
    Turni217 – 2193
    Helixi220 – 2289
    Helixi229 – 2313
    Helixi236 – 24712
    Helixi248 – 2503
    Beta strandi256 – 2627
    Beta strandi264 – 2663
    Beta strandi268 – 2758
    Turni276 – 2783
    Beta strandi279 – 2835
    Beta strandi290 – 2945
    Helixi296 – 2983
    Beta strandi299 – 3068
    Beta strandi308 – 3114
    Beta strandi314 – 3207
    Beta strandi327 – 3337
    Helixi334 – 35118
    Helixi413 – 4153
    Helixi419 – 4213
    Beta strandi422 – 4309
    Beta strandi432 – 44110
    Beta strandi444 – 4463
    Beta strandi448 – 4558
    Turni457 – 4604
    Helixi462 – 4687
    Helixi470 – 4767
    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
    Helixi570 – 5734
    Helixi574 – 5763
    Helixi586 – 5883
    Helixi591 – 5966
    Helixi601 – 61616
    Turni617 – 6193
    Turni622 – 6254
    Helixi628 – 6303
    Helixi631 – 6366
    Helixi649 – 65810
    Helixi663 – 6653
    Helixi669 – 68416
    Helixi685 – 6873
    Beta strandi915 – 9173
    Helixi923 – 94220
    Helixi947 – 9493
    Helixi950 – 97122
    Helixi972 – 9743
    Helixi977 – 9793
    Helixi980 – 100627
    Turni1007 – 10093
    Beta strandi1010 – 10123
    Helixi1013 – 104533

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K04X-ray1.95A891-1052[»]
    1K05X-ray2.90A/B/C891-1052[»]
    1MP8X-ray1.60A411-686[»]
    1OW6X-ray2.35A/B/C892-1052[»]
    1OW7X-ray2.60A/B/C892-1052[»]
    1OW8X-ray2.85A/B/C892-1052[»]
    2ETMX-ray2.30A/B411-689[»]
    2IJMX-ray2.19A/B411-689[»]
    2RA7X-ray1.99A921-1048[»]
    3B71X-ray2.82A/B/C891-1052[»]
    3BZ3X-ray2.20A414-689[»]
    3PXKX-ray1.79A/B411-689[»]
    3S9OX-ray2.60A/B/C891-1052[»]
    4EBVX-ray1.67A411-686[»]
    4EBWX-ray2.65A411-686[»]
    4GU6X-ray1.95A/B411-689[»]
    4GU9X-ray2.40A/B410-686[»]
    4I4EX-ray1.55A411-686[»]
    4I4FX-ray1.75A411-686[»]
    4K8AX-ray2.91A/B410-686[»]
    4K9YX-ray2.00A410-686[»]
    4KABX-ray2.71A/B410-686[»]
    4KAOX-ray2.39A/B410-689[»]
    4NY0X-ray2.80A/B/C/D31-405[»]
    ProteinModelPortaliQ05397.
    SMRiQ05397. Positions 34-715, 908-1049.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ05397.

    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 – 1052346Interaction with TGFB1I1Add
    BLAST
    Regioni912 – 1052141Interaction with ARHGEF28By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi712 – 73322Pro-richAdd
    BLAST
    Compositional biasi863 – 91351Pro-richAdd
    BLAST

    Domaini

    The Pro-rich regions interact with the SH3 domain of CAS family members, such as BCAR1 and NEDD9, and with the GTPase activating protein ARHGAP26.
    The carboxy-terminal region is the site of focal adhesion targeting (FAT) sequence which mediates the localization of FAK1 to focal adhesions.

    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.
    InParanoidiQ05397.
    KOiK05725.
    OrthoDBiEOG7ZSHSB.
    PhylomeDBiQ05397.
    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 (6)i

    Sequence statusi: Complete.

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

    This entry describes 6 isoformsi produced by alternative promoter usage and alternative splicing. Align

    Isoform 1 (identifier: Q05397-1) [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 NHTPNSSTKT HLGTGMERSP GAMERVLKVF HYFESNSEPT     50
    TWASIIRHGD ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV 100
    DMGVSSVREK YELAHPPEEW KYELRIRYLP KGFLNQFTED KPTLNFFYQQ 150
    VKSDYMLEIA DQVDQEIALK LGCLEIRRSY WEMRGNALEK KSNYEVLEKD 200
    VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI LKFFEILSPV 250
    YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFTQVQ 300
    TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL 350
    VNGTSQSFII RPQKEGERAL PSIPKLANSE KQGMRTHAVS VSETDDYAEI 400
    IDEEDTYTMP STRDYEIQRE RIELGRCIGE GQFGDVHQGI YMSPENPALA 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 EEEKAQQEER MRMESRRQAT 700
    VSWDSGGSDE APPKPSRPGY PSPRSSEGFY PSPQHMVQTN HYQVSGYPGS 750
    HGITAMAGSI YPGQASLLDQ TDSWNHRPQE IAMWQPNVED STVLDLRGIG 800
    QVLPTHLMEE RLIRQQQEME EDQRWLEKEE RFLKPDVRLS RGSIDREDGS 850
    LQGPIGNQHI YQPVGKPDPA APPKKPPRPG APGHLGSLAS LSSPADSYNE 900
    GVKLQPQEIS PPPTANLDRS NDKVYENVTG LVKAVIEMSS KIQPAPPEEY 950
    VPMVKEVGLA LRTLLATVDE TIPLLPASTH REIEMAQKLL NSDLGELINK 1000
    MKLAQQYVMT SLQQEYKKQM LTAAHALAVD AKNLLDVIDQ ARLKMLGQTR 1050
    PH 1052
    Length:1,052
    Mass (Da):119,233
    Last modified:July 15, 1998 - v2
    Checksum:iD8A4C15138AB0243
    GO
    Isoform 2 (identifier: Q05397-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:879
    Mass (Da):99,358
    Checksum:i64783EFF1FF4FCCB
    GO
    Isoform 3 (identifier: Q05397-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:554
    Mass (Da):63,201
    Checksum:i3960D6100B580E7D
    GO
    Isoform 4 (identifier: Q05397-4) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:431
    Mass (Da):48,967
    Checksum:i9C8013A49B83C690
    GO
    Isoform 5 (identifier: Q05397-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         868-868: D → GKEEKNWAERN
         903-903: K → KPWR

    Show »
    Length:1,065
    Mass (Da):120,900
    Checksum:i3FC0C66C4CF858D8
    GO
    Isoform 6 (identifier: Q05397-6) [UniParc]FASTAAdd to Basket

    Also known as: FRNK

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

    Note: Produced by alternative promoter usage.

    Show »
    Length:360
    Mass (Da):39,874
    Checksum:i0BD7ACE4EAEE63C0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti184 – 1841R → L in BAG65198. (PubMed:14702039)Curated
    Sequence conflicti211 – 2111L → I in BAG65198. (PubMed:14702039)Curated
    Sequence conflicti778 – 7781P → S in AAA35819. (PubMed:8422239)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti292 – 2921H → P.1 Publication
    VAR_041682
    Natural varianti292 – 2921H → Q.1 Publication
    VAR_041683
    Natural varianti793 – 7931V → A in a glioblastoma multiforme sample; somatic mutation. 1 Publication
    VAR_041684
    Natural varianti1030 – 10301D → E.1 Publication
    VAR_041685
    Natural varianti1044 – 10441K → E in a metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_041686

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 692692Missing in isoform 6. CuratedVSP_042168Add
    BLAST
    Alternative sequencei1 – 181181Missing in isoform 2, isoform 3 and isoform 4. 1 PublicationVSP_004967Add
    BLAST
    Alternative sequencei182 – 1898EMRGNALE → MSDYWVVG in isoform 2, isoform 3 and isoform 4. 1 PublicationVSP_004968
    Alternative sequencei472 – 4721A → ACHYTSLHWNWCRYISDPNV DACPDPRNAE in isoform 2, isoform 3 and isoform 4. 1 PublicationVSP_004969
    Alternative sequencei579 – 5835ASKGK → GKKSG in isoform 4. 1 PublicationVSP_004971
    Alternative sequencei584 – 1052469Missing in isoform 4. 1 PublicationVSP_004972Add
    BLAST
    Alternative sequencei677 – 70630STILE…SWDSG → FQNPAQMLPASGRLPNQPCP ERENYSFATF in isoform 3. 1 PublicationVSP_004973Add
    BLAST
    Alternative sequencei707 – 1052346Missing in isoform 3. 1 PublicationVSP_004974Add
    BLAST
    Alternative sequencei834 – 85421Missing in isoform 2. 1 PublicationVSP_004970Add
    BLAST
    Alternative sequencei868 – 8681D → GKEEKNWAERN in isoform 5. 1 PublicationVSP_042169
    Alternative sequencei903 – 9031K → KPWR in isoform 5. 1 PublicationVSP_042170

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L13616 mRNA. Translation: AAA58469.1.
    L05186 mRNA. Translation: AAA35819.1.
    AK304356 mRNA. Translation: BAG65198.1.
    AC067931 Genomic DNA. No translation available.
    AC100860 Genomic DNA. No translation available.
    AC105009 Genomic DNA. No translation available.
    AC105235 Genomic DNA. No translation available.
    CCDSiCCDS56557.1. [Q05397-5]
    CCDS6381.1. [Q05397-1]
    PIRiI53012.
    PC1225.
    RefSeqiNP_001186578.1. NM_001199649.1. [Q05397-5]
    NP_722560.1. NM_153831.3. [Q05397-1]
    UniGeneiHs.395482.

    Genome annotation databases

    EnsembliENST00000340930; ENSP00000341189; ENSG00000169398. [Q05397-5]
    ENST00000521059; ENSP00000429474; ENSG00000169398. [Q05397-1]
    ENST00000522684; ENSP00000429911; ENSG00000169398. [Q05397-1]
    GeneIDi5747.
    KEGGihsa:5747.
    UCSCiuc003yvq.3. human. [Q05397-2]
    uc003yvu.3. human. [Q05397-1]
    uc011ljp.2. human. [Q05397-6]
    uc011ljr.2. human. [Q05397-5]

    Polymorphism databases

    DMDMi3183518.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L13616 mRNA. Translation: AAA58469.1 .
    L05186 mRNA. Translation: AAA35819.1 .
    AK304356 mRNA. Translation: BAG65198.1 .
    AC067931 Genomic DNA. No translation available.
    AC100860 Genomic DNA. No translation available.
    AC105009 Genomic DNA. No translation available.
    AC105235 Genomic DNA. No translation available.
    CCDSi CCDS56557.1. [Q05397-5 ]
    CCDS6381.1. [Q05397-1 ]
    PIRi I53012.
    PC1225.
    RefSeqi NP_001186578.1. NM_001199649.1. [Q05397-5 ]
    NP_722560.1. NM_153831.3. [Q05397-1 ]
    UniGenei Hs.395482.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1K04 X-ray 1.95 A 891-1052 [» ]
    1K05 X-ray 2.90 A/B/C 891-1052 [» ]
    1MP8 X-ray 1.60 A 411-686 [» ]
    1OW6 X-ray 2.35 A/B/C 892-1052 [» ]
    1OW7 X-ray 2.60 A/B/C 892-1052 [» ]
    1OW8 X-ray 2.85 A/B/C 892-1052 [» ]
    2ETM X-ray 2.30 A/B 411-689 [» ]
    2IJM X-ray 2.19 A/B 411-689 [» ]
    2RA7 X-ray 1.99 A 921-1048 [» ]
    3B71 X-ray 2.82 A/B/C 891-1052 [» ]
    3BZ3 X-ray 2.20 A 414-689 [» ]
    3PXK X-ray 1.79 A/B 411-689 [» ]
    3S9O X-ray 2.60 A/B/C 891-1052 [» ]
    4EBV X-ray 1.67 A 411-686 [» ]
    4EBW X-ray 2.65 A 411-686 [» ]
    4GU6 X-ray 1.95 A/B 411-689 [» ]
    4GU9 X-ray 2.40 A/B 410-686 [» ]
    4I4E X-ray 1.55 A 411-686 [» ]
    4I4F X-ray 1.75 A 411-686 [» ]
    4K8A X-ray 2.91 A/B 410-686 [» ]
    4K9Y X-ray 2.00 A 410-686 [» ]
    4KAB X-ray 2.71 A/B 410-686 [» ]
    4KAO X-ray 2.39 A/B 410-689 [» ]
    4NY0 X-ray 2.80 A/B/C/D 31-405 [» ]
    ProteinModelPortali Q05397.
    SMRi Q05397. Positions 34-715, 908-1049.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111719. 99 interactions.
    IntActi Q05397. 58 interactions.
    MINTi MINT-92695.
    STRINGi 9606.ENSP00000341189.

    Chemistry

    BindingDBi Q05397.
    ChEMBLi CHEMBL2695.
    GuidetoPHARMACOLOGYi 2180.

    PTM databases

    PhosphoSitei Q05397.

    Polymorphism databases

    DMDMi 3183518.

    Proteomic databases

    MaxQBi Q05397.
    PaxDbi Q05397.
    PRIDEi Q05397.

    Protocols and materials databases

    DNASUi 5747.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000340930 ; ENSP00000341189 ; ENSG00000169398 . [Q05397-5 ]
    ENST00000521059 ; ENSP00000429474 ; ENSG00000169398 . [Q05397-1 ]
    ENST00000522684 ; ENSP00000429911 ; ENSG00000169398 . [Q05397-1 ]
    GeneIDi 5747.
    KEGGi hsa:5747.
    UCSCi uc003yvq.3. human. [Q05397-2 ]
    uc003yvu.3. human. [Q05397-1 ]
    uc011ljp.2. human. [Q05397-6 ]
    uc011ljr.2. human. [Q05397-5 ]

    Organism-specific databases

    CTDi 5747.
    GeneCardsi GC08M141667.
    HGNCi HGNC:9611. PTK2.
    HPAi CAB004036.
    HPA001842.
    MIMi 600758. gene.
    neXtProti NX_Q05397.
    PharmGKBi PA33955.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000069938.
    HOVERGENi HBG004018.
    InParanoidi Q05397.
    KOi K05725.
    OrthoDBi EOG7ZSHSB.
    PhylomeDBi Q05397.
    TreeFami TF316643.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 2681.
    Reactomei REACT_107. Apoptotic cleavage of cellular proteins.
    REACT_15381. p130Cas linkage to MAPK signaling for integrins.
    REACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_18334. NCAM signaling for neurite out-growth.
    REACT_22351. DCC mediated attractive signaling.
    REACT_22384. Netrin mediated repulsion signals.
    REACT_23916. Signal regulatory protein (SIRP) family interactions.
    SignaLinki Q05397.

    Miscellaneous databases

    ChiTaRSi PTK2. human.
    EvolutionaryTracei Q05397.
    GeneWikii PTK2.
    GenomeRNAii 5747.
    NextBioi 22380.
    PMAP-CutDB Q05397.
    PROi Q05397.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q05397.
    Bgeei Q05397.
    CleanExi HS_PTK2.
    Genevestigatori Q05397.

    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. "Human T and B lymphocytes express a structurally conserved focal adhesion kinase, pp125FAK."
      Whitney G.S., Chan P.Y., Blake J., Cosand W.L., Neubauer M.G., Aruffo A., Kanner S.B.
      DNA Cell Biol. 12:823-830(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: T-cell.
    2. "Expression of an N-terminally truncated form of human focal adhesion kinase in brain."
      Andre E., Becker-Andre M.
      Biochem. Biophys. Res. Commun. 190:140-147(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), TISSUE SPECIFICITY.
      Tissue: Brain.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
      Tissue: Trachea.
    4. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Bienvenut W.V., Glen H., Brunton V.G., Frame M.C.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-19; 192-199; 222-236; 243-252; 350-364; 414-419; 468-476; 562-569; 674-690; 798-811; 832-838; 904-933; 963-981; 989-1000 AND 1003-1042, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Osteosarcoma.
    6. "A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes."
      Lee S.-T., Strunk K.M., Spritz R.A.
      Oncogene 8:3403-3410(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 552-602, TISSUE SPECIFICITY.
      Tissue: Melanocyte.
    7. "Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions."
      Matsuya M., Sasaki H., Aoto H., Mitaka T., Nagura K., Ohba T., Ishino M., Takahashi S., Suzuki R., Sasaki T.
      J. Biol. Chem. 273:1003-1014(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TGFB1I1.
    8. "Interaction of Hic-5, A senescence-related protein, with focal adhesion kinase."
      Fujita H., Kamiguchi K., Cho D., Shibanuma M., Morimoto C., Tachibana K.
      J. Biol. Chem. 273:26516-26521(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TGFB1I1, MUTAGENESIS OF VAL-928 AND LEU-1034.
    9. "Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation."
      Miao H., Burnett E., Kinch M., Simon E., Wang B.
      Nat. Cell Biol. 2:62-69(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PXN PHOSPHORYLATION; REGULATION OF CELL SHAPE AND MIGRATION, INTERACTION WITH EPHA2, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, ENZYME REGULATION, DEPHOSPHORYLATION BY PTPN11, SUBCELLULAR LOCATION.
    10. "Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain."
      Chen R., Kim O., Li M., Xiong X., Guan J.L., Kung H.J., Chen H., Shimizu Y., Qiu Y.
      Nat. Cell Biol. 3:439-444(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL MIGRATION AND ACTIVATION OF BMX, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF TYR-397, INTERACTION WITH BMX.
    11. "Focal adhesion kinase enhances signaling through the Shc/extracellular signal-regulated kinase pathway in anaplastic astrocytoma tumor biopsy samples."
      Hecker T.P., Grammer J.R., Gillespie G.Y., Stewart J. Jr., Gladson C.L.
      Cancer Res. 62:2699-2707(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF SHC1, AUTOPHOSPHORYLATION, INTERACTION WITH SHC1 AND SRC, ROLE IN DISEASE.
    12. "Regulation of focal adhesion kinase by a novel protein inhibitor FIP200."
      Abbi S., Ueda H., Zheng C., Cooper L.A., Zhao J., Christopher R., Guan J.L.
      Mol. Biol. Cell 13:3178-3191(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RB1CC1.
    13. "Site-specific phosphorylation of platelet focal adhesion kinase by low-density lipoprotein."
      Relou I.A.M., Bax L.A.B., Van Rijn H.J.M., Akkerman J.-W.N.
      Biochem. J. 369:407-416(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-397; TYR-407; TYR-577; TYR-861 AND TYR-925, INTERACTION WITH FGR.
    14. "Focal adhesion kinase is upstream of phosphatidylinositol 3-kinase/Akt in regulating fibroblast survival in response to contraction of type I collagen matrices via a beta 1 integrin viability signaling pathway."
      Xia H., Nho R.S., Kahm J., Kleidon J., Henke C.A.
      J. Biol. Chem. 279:33024-33034(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN INTEGRIN SIGNALING; REGULATION OF APOPTOSIS; REGULATION OF CELL SHAPE AND ACTIVATION OF PHOSPHATIDYLINOSITOL KINASE AND AKT1 SIGNALING PATHWAY.
    15. "The proto-oncogene Fgr regulates cell migration and this requires its plasma membrane localization."
      Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L., Lowell C.A., Berton G.
      Exp. Cell Res. 302:253-269(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF CELL MIGRATION, PHOSPHORYLATION AT TYR-407; TYR-397 AND TYR-576.
    16. "Direct interaction of the N-terminal domain of focal adhesion kinase with the N-terminal transactivation domain of p53."
      Golubovskaya V.M., Finch R., Cance W.G.
      J. Biol. Chem. 280:25008-25021(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH P53/TP53, SUBCELLULAR LOCATION.
    17. "Microtubule-induced focal adhesion disassembly is mediated by dynamin and focal adhesion kinase."
      Ezratty E.J., Partridge M.A., Gundersen G.G.
      Nat. Cell Biol. 7:581-590(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN FOCAL ADHESION DISASSEMBLY.
    18. "Vascular endothelial growth factor receptor-3 and focal adhesion kinase bind and suppress apoptosis in breast cancer cells."
      Garces C.A., Kurenova E.V., Golubovskaya V.M., Cance W.G.
      Cancer Res. 66:1446-1454(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FLT4.
    19. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "Expression of FAK-related non-kinase (FRNK) coincides with morphological change in the early stage of cell adhesion."
      Nagoshi Y., Yamamoto G., Irie T., Tachikawa T.
      Med. Mol. Morphol. 39:154-160(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE PROMOTER USAGE, IDENTIFICATION OF ISOFORM 6, DEVELOPMENTAL STAGE (ISOFORM 6).
    21. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: ENZYME REGULATION, ROLE IN DISEASE, PHOSPHORYLATION AT TYR-397 AND TYR-861.
    23. Cited for: FUNCTION, ENZYME REGULATION, ROLE IN DISEASE, PHOSPHORYLATION AT TYR-397.
    24. "Activation of FAK is necessary for the osteogenic differentiation of human mesenchymal stem cells on laminin-5."
      Salasznyk R.M., Klees R.F., Boskey A., Plopper G.E.
      J. Cell. Biochem. 100:499-514(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN OSTEOBLAST DIFFERENTIATION.
    25. "Inhibition of both focal adhesion kinase and insulin-like growth factor-I receptor kinase suppresses glioma proliferation in vitro and in vivo."
      Liu T.J., LaFortune T., Honda T., Ohmori O., Hatakeyama S., Meyer T., Jackson D., de Groot J., Yung W.K.
      Mol. Cancer Ther. 6:1357-1367(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, ROLE IN DISEASE, PHOSPHORYLATION AT TYR-397.
    26. "The LIM protein leupaxin is enriched in smooth muscle and functions as an serum response factor cofactor to induce smooth muscle cell gene transcription."
      Sundberg-Smith L.J., DiMichele L.A., Sayers R.L., Mack C.P., Taylor J.M.
      Circ. Res. 102:1502-1511(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LPXN.
    27. "Etk/BMX, a Btk family tyrosine kinase, and Mal contribute to the cross-talk between MyD88 and FAK pathways."
      Semaan N., Alsaleh G., Gottenberg J.E., Wachsmann D., Sibilia J.
      J. Immunol. 180:3485-3491(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BMX.
    28. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CASS4.
    29. "Nuclear FAK promotes cell proliferation and survival through FERM-enhanced p53 degradation."
      Lim S.T., Chen X.L., Lim Y., Hanson D.A., Vo T.T., Howerton K., Larocque N., Fisher S.J., Schlaepfer D.D., Ilic D.
      Mol. Cell 29:9-22(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF P53/TP53 LEVELS; CELL PROLIFERATION AND CELL SURVIVAL, SUBCELLULAR LOCATION.
    30. Cited for: INTERACTION WITH ESR1; PIK3R1 AND/OR PIK3R2 AND SRC.
    31. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; SER-29; SER-887 AND SER-910, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    32. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    33. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    34. "Specific tyrosine phosphorylation of focal adhesion kinase mediated by Fer tyrosine kinase in suspended hepatocytes."
      Oh M.A., Choi S., Lee M.J., Choi M.C., Lee S.A., Ko W., Cance W.G., Oh E.S., Buday L., Kim S.H., Lee J.W.
      Biochim. Biophys. Acta 1793:781-791(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-397; TYR-576; TYR-577; SER-722; TYR-861 AND TYR-925, IDENTIFICATION IN A COMPLEX WITH CTTN AND FER.
    35. "Paxillin-Y118 phosphorylation contributes to the control of Src-induced anchorage-independent growth by FAK and adhesion."
      Sachdev S., Bu Y., Gelman I.H.
      BMC Cancer 9:12-12(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SRC-MEDIATED PHOSPHORYLATION OF PXN.
    36. "STEAP4 regulates focal adhesion kinase activation and CpG motifs within STEAP4 promoter region are frequently methylated in DU145, human androgen-independent prostate cancer cells."
      Tamura T., Chiba J.
      Int. J. Mol. Med. 24:599-604(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STEAP4.
    37. "Ras- and PI3K-dependent breast tumorigenesis in mice and humans requires focal adhesion kinase signaling."
      Pylayeva Y., Gillen K.M., Gerald W., Beggs H.E., Reichardt L.F., Giancotti F.G.
      J. Clin. Invest. 119:252-266(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SRC-MEDIATED PHOSPHORYLATION OF BCAR1, ROLE IN DISEASE.
    38. "EphA1 interacts with integrin-linked kinase and regulates cell morphology and motility."
      Yamazaki T., Masuda J., Omori T., Usui R., Akiyama H., Maru Y.
      J. Cell Sci. 122:243-255(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EPHA1.
    39. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-5; THR-13; SER-29; TYR-397; TYR-570; SER-580 AND SER-910, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    40. "Bioluminescent imaging study: FAK inhibitor, PF-562,271, preclinical study in PC3M-luc-C6 local implant and metastasis xenograft models."
      Sun H., Pisle S., Gardner E.R., Figg W.D.
      Cancer Biol. Ther. 10:38-43(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN DISEASE, ENZYME REGULATION.
    41. "LIM domain-containing adaptor, leupaxin, localizes in focal adhesion and suppresses the integrin-induced tyrosine phosphorylation of paxillin."
      Tanaka T., Moriwaki K., Murata S., Miyasaka M.
      Cancer Sci. 101:363-368(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LPXN.
    42. "Downregulation of FAK-related non-kinase mediates the migratory phenotype of human fibrotic lung fibroblasts."
      Cai G.Q., Zheng A., Tang Q., White E.S., Chou C.F., Gladson C.L., Olman M.A., Ding Q.
      Exp. Cell Res. 316:1600-1609(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (ISOFORM 6), TISSUE SPECIFICITY.
    43. Cited for: INTERACTION WITH ZFYVE21, DEPHOSPHORYLATION AT TYR-397.
    44. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910 AND THR-914, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    45. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    46. "Focal adhesion kinase (FAK) binds RET kinase via its FERM domain, priming a direct and reciprocal RET-FAK transactivation mechanism."
      Plaza-Menacho I., Morandi A., Mologni L., Boender P., Gambacorti-Passerini C., Magee A.I., Hofstra R.M.W., Knowles P., McDonald N.Q., Isacke C.M.
      J. Biol. Chem. 286:17292-17302(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RET, FUNCTION IN RET PHOSPHORYLATION, PHOSPHORYLATION AT TYR-576 AND TYR-577.
    47. "A novel splice variant of calcium and integrin-binding protein 1 mediates protein kinase D2-stimulated tumour growth by regulating angiogenesis."
      Armacki M., Joodi G., Nimmagadda S.C., de Kimpe L., Pusapati G.V., Vandoninck S., Van Lint J., Illing A., Seufferlein T.
      Oncogene 33:1167-1180(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CIB1 ISOFORM 2.
      Tissue: Brain.
    48. Cited for: REVIEW ON SIGNALING AND ON DIRECT PTK2/FAK1 SUBSTRATES.
    49. "Netrin-integrin signaling in epithelial morphogenesis, axon guidance and vascular patterning."
      Nikolopoulos S.N., Giancotti F.G.
      Cell Cycle 4:E131-E135(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION IN NETRIN SIGNALING.
    50. "Integrin-regulated FAK-Src signaling in normal and cancer cells."
      Mitra S.K., Schlaepfer D.D.
      Curr. Opin. Cell Biol. 18:516-523(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION IN CELL MIGRATION; FOCAL ADHESION TURNOVER AND ACTIVATION OF SIGNALING PATHWAYS, ROLE IN DISEASE.
    51. "Focal adhesion kinase: an essential kinase in the regulation of cardiovascular functions."
      Vadali K., Cai X., Schaller M.D.
      IUBMB Life 59:709-716(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    52. "FERM control of FAK function: implications for cancer therapy."
      Lim S.T., Mikolon D., Stupack D.G., Schlaepfer D.D.
      Cell Cycle 7:2306-2314(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON ROLE IN INTEGRIN SIGNALING AND IN REGULATION OF P53/TP53 ACTIVITIES, ROLE IN DISEASE, ENZYME REGULATION.
    53. "Focal adhesion kinase: switching between GAPs and GEFs in the regulation of cell motility."
      Tomar A., Schlaepfer D.D.
      Curr. Opin. Cell Biol. 21:676-683(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION IN REGULATION OF RHO FAMILY GTPASE ACTIVITY.
    54. "Focal adhesion kinase and cancer."
      Golubovskaya V.M., Kweh F.A., Cance W.G.
      Histol. Histopathol. 24:503-510(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON EXPRESSION IN CANCER, ROLE IN DISEASE.
    55. "Focal adhesion kinase and p53 signal transduction pathways in cancer."
      Golubovskaya V.M., Cance W.
      Front. Biosci. 15:901-912(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION IN REGULATION OF P53/TP53.
    56. "The role of focal adhesion kinase in early development."
      Chatzizacharias N.A., Kouraklis G.P., Theocharis S.E.
      Histol. Histopathol. 25:1039-1055(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON ROLE IN DEVELOPMENT.
    57. "Integrin signaling through FAK in the regulation of mammary stem cells and breast cancer."
      Guan J.L.
      IUBMB Life 62:268-276(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION IN INTEGRIN SIGNALING AND ACTIVATION OF DOWNSTREAM SIGNALING PATHWAYS.
    58. "Cellular functions of FAK kinases: insight into molecular mechanisms and novel functions."
      Schaller M.D.
      J. Cell Sci. 123:1007-1013(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SIGNALING.
    59. "Focal adhesion kinase: exploring Fak structure to gain insight into function."
      Hall J.E., Fu W., Schaller M.D.
      Int. Rev. Cell Mol. Biol. 288:185-225(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION; SUBUNIT; PHOSPHORYLATION; ENZYME REGULATION AND ROLE IN DISEASE.
    60. "MISP is a novel Plk1 substrate required for proper spindle orientation and mitotic progression."
      Zhu M., Settele F., Kotak S., Sanchez-Pulido L., Ehret L., Ponting C.P., Goenczy P., Hoffmann I.
      J. Cell Biol. 200:773-787(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MISP.
    61. "The structural basis of localization and signaling by the focal adhesion targeting domain."
      Arold S.T., Hoellerer M.K., Noble M.E.
      Structure 10:319-327(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 891-1052, IDENTIFICATION BY MASS SPECTROMETRY.
    62. "Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography."
      Nowakowski J., Cronin C.N., McRee D.E., Knuth M.W., Nelson C.G., Pavletich N.P., Rogers J., Sang B.C., Scheibe D.N., Swanson R.V., Thompson D.A.
      Structure 10:1659-1667(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 411-686 IN COMPLEX WITH ATP.
    63. "Molecular recognition of paxillin LD motifs by the focal adhesion targeting domain."
      Hoellerer M.K., Noble M.E., Labesse G., Campbell I.D., Werner J.M., Arold S.T.
      Structure 11:1207-1217(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 892-1052 IN COMPLEX WITH PXN, INTERACTION WITH PXN.
    64. Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 414-689 IN COMPLEX WITH INHIBITOR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION.
    65. "Structural basis for the interaction between focal adhesion kinase and CD4."
      Garron M.L., Arthos J., Guichou J.F., McNally J., Cicala C., Arold S.T.
      J. Mol. Biol. 375:1320-1328(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.82 ANGSTROMS) OF 891-1052 IN COMPLEX WITH CD4, SUBCELLULAR LOCATION, INTERACTION WITH CD4.
    66. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] PRO-292; GLN-292; ALA-793; GLU-1030 AND GLU-1044.

    Entry informationi

    Entry nameiFAK1_HUMAN
    AccessioniPrimary (citable) accession number: Q05397
    Secondary accession number(s): B4E2N6
    , F5H4S4, Q14291, Q9UD85
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 180 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3