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P70600

- FAK2_RAT

UniProt

P70600 - FAK2_RAT

Protein

Protein-tyrosine kinase 2-beta

Gene

Ptk2b

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    Functioni

    Non-receptor protein-tyrosine kinase that regulates reorganization of the actin cytoskeleton, cell polarization, cell migration, adhesion, spreading and bone remodeling. Plays a role in the regulation of the humoral immune response, and is required for normal levels of marginal B-cells in the spleen and normal migration of splenic B-cells. Required for normal macrophage polarization and migration towards sites of inflammation. Regulates cytoskeleton rearrangement and cell spreading in T-cells, and contributes to the regulation of T-cell responses. Promotes osteoclastic bone resorption; this requires both PTK2B/PYK2 and SRC. May inhibit differentiation and activity of osteoprogenitor cells. Functions in signaling downstream of integrin and collagen receptors, immune receptors, G-protein coupled receptors (GPCR), cytokine, chemokine and growth factor receptors, and mediates responses to cellular stress. 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 of the AKT1 signaling cascade. Promotes activation of NOS3. Regulates production of the cellular messenger cGMP. Promotes activation of the MAP kinase signaling cascade, including activation of MAPK1/ERK2, MAPK3/ERK1 and MAPK8/JNK1. Promotes activation of Rho family GTPases, such as RHOA and RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Acts as a scaffold, binding to both PDPK1 and SRC, thereby allowing SRC to phosphorylate PDPK1 at 'Tyr-9, 'Tyr-373', and 'Tyr-376' By similarity. Promotes phosphorylation of NMDA receptors by SRC family members, and thereby contributes to the regulation of NMDA receptor ion channel activity and intracellular Ca2+ levels. May also regulate potassium ion transport by phosphorylation of potassium channel subunits. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ASAP1, NPHP1, KCNA2 and SHC1. Promotes phosphorylation of ASAP2, RHOU and PXN; this requires both SRC and PTK2/PYK2 By similarity.By similarity

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 PublicationPROSITE-ProRule annotation

    Enzyme regulationi

    Activated in response to stimuli that lead to increased intracellular Ca2+ levels; this activation is indirect and may be mediated by calcium-mediated production of reactive oxygen species (ROS). Activated by autophosphorylation at Tyr-402; this creates a binding site for SRC family kinases and leads to phosphorylation at additional tyrosine residues. Phosphorylation at Tyr-402, Tyr-579 and Tyr-580 is required for optimal kinase activity By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei457 – 4571ATPPROSITE-ProRule annotation
    Active sitei549 – 5491Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi431 – 4399ATPPROSITE-ProRule annotation
    Nucleotide bindingi503 – 5097ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. 3-phosphoinositide-dependent protein kinase binding Source: RGD
    2. ATP binding Source: UniProtKB-KW
    3. calmodulin-dependent protein kinase activity Source: Alzheimers_University_of_Toronto
    4. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
    5. protein binding Source: RGD
    6. protein complex binding Source: RGD
    7. signal transducer activity Source: InterPro

    GO - Biological processi

    1. actin filament organization Source: RGD
    2. activation of Janus kinase activity Source: RGD
    3. activation of Rac GTPase activity Source: RGD
    4. angiogenesis Source: RGD
    5. blood vessel endothelial cell migration Source: RGD
    6. bone resorption Source: UniProtKB
    7. cell adhesion Source: RGD
    8. cell differentiation Source: RGD
    9. cell surface receptor signaling pathway Source: UniProtKB
    10. cellular defense response Source: Alzheimers_University_of_Toronto
    11. cellular response to retinoic acid Source: Ensembl
    12. chemokine-mediated signaling pathway Source: UniProtKB
    13. epidermal growth factor receptor signaling pathway Source: RGD
    14. focal adhesion assembly Source: RGD
    15. glial cell proliferation Source: RGD
    16. integrin-mediated signaling pathway Source: UniProtKB
    17. ionotropic glutamate receptor signaling pathway Source: Alzheimers_University_of_Toronto
    18. long-term synaptic potentiation Source: Alzheimers_University_of_Toronto
    19. MAPK cascade Source: RGD
    20. marginal zone B cell differentiation Source: UniProtKB
    21. negative regulation of apoptotic process Source: UniProtKB
    22. negative regulation of bone mineralization Source: UniProtKB
    23. negative regulation of cell proliferation Source: UniProtKB
    24. negative regulation of muscle cell apoptotic process Source: RGD
    25. negative regulation of myeloid cell differentiation Source: Ensembl
    26. negative regulation of neuron apoptotic process Source: Alzheimers_University_of_Toronto
    27. negative regulation of ossification Source: RGD
    28. negative regulation of potassium ion transport Source: Ensembl
    29. neuron projection development Source: RGD
    30. oocyte maturation Source: RGD
    31. peptidyl-tyrosine autophosphorylation Source: Alzheimers_University_of_Toronto
    32. peptidyl-tyrosine phosphorylation Source: Alzheimers_University_of_Toronto
    33. positive regulation of actin filament polymerization Source: UniProtKB
    34. positive regulation of angiogenesis Source: Ensembl
    35. positive regulation of B cell chemotaxis Source: UniProtKB
    36. positive regulation of cell growth Source: RGD
    37. positive regulation of cell-matrix adhesion Source: UniProtKB
    38. positive regulation of cell migration Source: RGD
    39. positive regulation of cell proliferation Source: RGD
    40. positive regulation of cytosolic calcium ion concentration Source: RGD
    41. positive regulation of endothelial cell migration Source: Ensembl
    42. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    43. positive regulation of excitatory postsynaptic membrane potential Source: Alzheimers_University_of_Toronto
    44. positive regulation of JNK cascade Source: UniProtKB
    45. positive regulation of JUN kinase activity Source: RGD
    46. positive regulation of neuron projection development Source: Ensembl
    47. positive regulation of nitric-oxide synthase activity Source: Ensembl
    48. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
    49. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
    50. positive regulation of protein kinase activity Source: UniProtKB
    51. positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
    52. positive regulation of reactive oxygen species metabolic process Source: RGD
    53. positive regulation of synaptic transmission, glutamatergic Source: Alzheimers_University_of_Toronto
    54. positive regulation of translation Source: RGD
    55. regulation of actin cytoskeleton reorganization Source: UniProtKB
    56. regulation of calcium-mediated signaling Source: Ensembl
    57. regulation of cell adhesion Source: UniProtKB
    58. regulation of cell shape Source: UniProtKB
    59. regulation of cGMP biosynthetic process Source: Ensembl
    60. regulation of cGMP-mediated signaling Source: Ensembl
    61. regulation of establishment of cell polarity Source: UniProtKB
    62. regulation of inositol trisphosphate biosynthetic process Source: UniProtKB
    63. regulation of macrophage chemotaxis Source: UniProtKB
    64. regulation of nitric oxide biosynthetic process Source: Ensembl
    65. regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: Alzheimers_University_of_Toronto
    66. regulation of release of sequestered calcium ion into cytosol Source: UniProtKB
    67. response to calcium ion Source: RGD
    68. response to cAMP Source: RGD
    69. response to cocaine Source: RGD
    70. response to drug Source: RGD
    71. response to ethanol Source: RGD
    72. response to glucose Source: RGD
    73. response to hormone Source: RGD
    74. response to hydrogen peroxide Source: RGD
    75. response to hypoxia Source: RGD
    76. response to immobilization stress Source: RGD
    77. response to lithium ion Source: RGD
    78. response to mechanical stimulus Source: RGD
    79. response to organonitrogen compound Source: RGD
    80. response to osmotic stress Source: RGD
    81. response to reactive oxygen species Source: RGD
    82. signal complex assembly Source: InterPro
    83. sprouting angiogenesis Source: UniProtKB
    84. stress fiber assembly Source: RGD
    85. tumor necrosis factor-mediated signaling pathway Source: Ensembl
    86. vascular endothelial growth factor receptor signaling pathway Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Adaptive immunity, Angiogenesis, Immunity

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 5301.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein-tyrosine kinase 2-beta (EC:2.7.10.2)
    Alternative name(s):
    Calcium-dependent tyrosine kinase
    Short name:
    CADTK
    Calcium-regulated non-receptor proline-rich tyrosine kinase
    Cell adhesion kinase beta
    Short name:
    CAK-beta
    Short name:
    CAKB
    Focal adhesion kinase 2
    Short name:
    FADK 2
    Proline-rich tyrosine kinase 2
    Gene namesi
    Name:Ptk2b
    Synonyms:Fak2, Pyk2
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 15

    Organism-specific databases

    RGDi628758. Ptk2b.

    Subcellular locationi

    Cytoplasm 1 Publication. Cytoplasmperinuclear region By similarity. Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cell projectionlamellipodium By similarity. Cytoplasmcell cortex By similarity. Nucleus By similarity
    Note: Colocalizes with integrins at the cell periphery. Interaction with NPHP1 induces the membrane-association of the kinase. Colocalizes with PXN at the microtubule-organizing center. The tyrosine phosphorylated form is detected at cell-cell contacts By similarity.By similarity
    Isoform 2 : Cell junctionfocal adhesion
    Note: Localizes to focal adhesions, but not isoform 1 and isoform 3.

    GO - Cellular componenti

    1. apical dendrite Source: Alzheimers_University_of_Toronto
    2. axon Source: RGD
    3. cell body Source: Alzheimers_University_of_Toronto
    4. cell cortex Source: RGD
    5. dendrite Source: Alzheimers_University_of_Toronto
    6. focal adhesion Source: RGD
    7. growth cone Source: Alzheimers_University_of_Toronto
    8. lamellipodium Source: UniProtKB
    9. membrane raft Source: RGD
    10. neuronal cell body Source: Alzheimers_University_of_Toronto
    11. N-methyl-D-aspartate selective glutamate receptor complex Source: Alzheimers_University_of_Toronto
    12. nucleus Source: RGD
    13. perinuclear region of cytoplasm Source: RGD
    14. postsynaptic density Source: Alzheimers_University_of_Toronto

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10091009Protein-tyrosine kinase 2-betaPRO_0000088083Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei361 – 3611PhosphoserineBy similarity
    Modified residuei375 – 3751PhosphoserineBy similarity
    Modified residuei399 – 3991PhosphoserineBy similarity
    Modified residuei402 – 4021Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei440 – 4401PhosphotyrosineBy similarity
    Modified residuei579 – 5791Phosphotyrosine; by SRC, LYN and LCK1 Publication
    Modified residuei580 – 5801Phosphotyrosine; by SRC, LYN and LCK2 Publications
    Modified residuei722 – 7221PhosphotyrosineBy similarity
    Modified residuei762 – 7621PhosphoserineBy similarity
    Modified residuei765 – 7651PhosphothreonineBy similarity
    Modified residuei834 – 8341PhosphotyrosineBy similarity
    Modified residuei839 – 8391PhosphoserineBy similarity
    Modified residuei842 – 8421PhosphothreonineBy similarity
    Modified residuei849 – 8491PhosphotyrosineBy similarity
    Modified residuei866 – 8661PhosphoserineBy similarity
    Modified residuei881 – 8811PhosphotyrosineBy similarity

    Post-translational modificationi

    Phosphorylated on tyrosine residues in response to various stimuli that elevate the intracellular calcium concentration; this activation is indirect and may be mediated by production of reactive oxygen species (ROS). Tyr-402 is the major autophosphorylation site, but other kinases can also phosphorylate Tyr-402. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-402 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-579; Tyr-580 and Tyr-881. Phosphorylation at Tyr-881 is important for interaction with GRB2. Phosphorylated on tyrosine residues upon activation of FGR and PKC. Recruitment by NPHP1 to cell matrix adhesions initiates Tyr-402 phosphorylation. In monocytes, adherence to substrata is required for tyrosine phosphorylation and kinase activation. Angiotensin II, thapsigargin and L-alpha-lysophosphatidic acid (LPA) also induce autophosphorylation and increase kinase activity. Phosphorylation by MYLK promotes ITGB2 activation and is thus essential to trigger neutrophil transmigration during lung injury. Dephosphorylated by PTPN12 By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP70600.
    PRIDEiP70600.

    PTM databases

    PhosphoSiteiP70600.

    Expressioni

    Tissue specificityi

    Highly expressed in pulmonary vein endothelial cells, lung and brain (at protein level). Isoform 1 is expressed at high levels in the brain (hippocampus, cerebral cortex and olfactory bulb) and poorly in the spleen and other tissues, whereas isoforms 2 and 3 are expressed in the spleen and brain (highest in cerebellum).1 Publication

    Gene expression databases

    GenevestigatoriP70600.

    Interactioni

    Subunit structurei

    Homodimer, or homooligomer. Interacts with NPHP1, ASAP1, ASAP2, ARHGAP26, SKAP2 and TGFB1I1. The Tyr-402 phosphorylated form interacts with SRC (via SH2 domain) and SRC family members. Forms a signaling complex with EPHA1, LCK and phosphatidylinositol 3-kinase; upon activation by EFNA1. Interacts with GRB2 (via SH2 domain). Interacts with P53/TP53 and MDM2. Interacts with MYLK. Interacts with BCAR1. Interacts with RB1CC1. Interacts with RHOU. Interacts with VAV1. Interacts with PDPK1. Interacts with LPXN and PTPN12 By similarity. Interacts with SIRPA and SH2D3C. Interacts (hypophosphorylated) with PXN. Interacts with ARHGAP10.By similarity4 Publications

    Protein-protein interaction databases

    BioGridi248405. 4 interactions.
    MINTiMINT-266266.

    Structurei

    3D structure databases

    ProteinModelPortaliP70600.
    SMRiP70600. Positions 415-692, 869-999.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini39 – 359321FERMPROSITE-ProRule annotationAdd
    BLAST
    Domaini425 – 683259Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni801 – 1009209Interaction with TGFB1I1Add
    BLAST
    Regioni868 – 1009142Focal adhesion targeting (FAT)Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi701 – 76767Pro-richAdd
    BLAST
    Compositional biasi831 – 86939Pro-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00740000115459.
    HOGENOMiHOG000069938.
    HOVERGENiHBG004018.
    InParanoidiP70600.
    KOiK05871.
    OMAiQMLTASH.
    OrthoDBiEOG7ZSHSB.
    PhylomeDBiP70600.
    TreeFamiTF316643.

    Family and domain databases

    Gene3Di1.20.80.10. 1 hit.
    InterProiIPR019749. Band_41_domain.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    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.
    PROSITEiPS50057. 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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P70600-1) [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

    MSGVSEPLSR VKVGTLRPPE GPPEPMVVVP VDVEKEDVRI LKVCFYSNSF     50
    NPGKNFKLVK CTVQTEIQEI ITSILLSGRI GPNIQLAECY GLRLKHMKSD 100
    EIHWLHPQMT VGEVQDKYEC LHVEAEWRYD LQIRYLPEDF MESLKEDRTT 150
    LLYFYQQLRN DYMQRYASKV SEGMALQLGC LELRRFFKDM PHNALDKKSN 200
    FELLEKEVGL DLFFPKQMQE NLKPKQFRKM IQQTFQQYAS LREEECVMKF 250
    FNTLAGFANI DQETYRCELI QGWNITVDLV IGPKGIRQLT SQDTKPTCLA 300
    EFKQIRSIRC LPLEETQAVL QLGIEGAPQS LSIKTSSLAE AENMADLIDG 350
    YCRLQGEHKG SLIIHAKKDG EKRNSLPQIP TLNLESRRSH LSESCSIESD 400
    IYAEIPDETL RRPGGPQYGV AREDVVLNRI LGEGFFGEVY EGVYTNHKGE 450
    KINVAVKTCK KDCTLDNKEK FMSEAVIMKN LDHPHIVKLI GIIEEEPTWI 500
    VMELYPYGEL GHYLERNKNS LKVPTLVLYA LQICKAMAYL ESINCVHRDI 550
    AVRNILVASP ECVKLGDFGL SRYIEDEDYY KASVTRLPIK WMSPESINFR 600
    RFTTASDVWM FAVCMWEILS FGKQPFFWLE NKDVIGVLEK GDRLPKPELC 650
    PPVLYTLMTR CWDYDPSDRP RFTELVCSLS DIYQMERDIA IEQERNARYR 700
    PPKILEPTAF QEPPPKPSRP KYKHPPQTNL LAPKLQFQVP EGLCASSPTL 750
    TSPMEYPSPV NSLHTPPLHR HNVFKRHSMR EEDFIRPSSR EEAQQLWEAE 800
    KIKMRQVLDR QQKQMVEDSQ WLRREERCLD PMVYMNDKSP LTPEKEAGYT 850
    EFTGPPQKPP RLGAQSIQPT ANLDRTDDLV YHNVMTLVEA VLELKNKLSQ 900
    LPPEEYVVVV KNVGLNLRKL IGSVDDLLPS LPASSRTEIE GTQKLLNKDL 950
    AELINKMRLA QQNAVTSLSE DCKRQMLTAS HTLAVDAKNL LDAVDQAKVV 1000
    ANLAHPPAE 1009
    Length:1,009
    Mass (Da):115,784
    Last modified:February 1, 1997 - v1
    Checksum:iD435A475BCA49E9B
    GO
    Isoform 2 (identifier: P70600-2) [UniParc]FASTAAdd to Basket

    Also known as: PRNK

    The sequence of this isoform differs from the canonical sequence as follows:
         1-771: Missing.
         772-780: NVFKRHSMR → MGLIVLSSQ

    Show »
    Length:238
    Mass (Da):26,808
    Checksum:i223D384D7CE2F9F4
    GO
    Isoform 3 (identifier: P70600-3) [UniParc]FASTAAdd to Basket

    Also known as: PYK2s

    The sequence of this isoform differs from the canonical sequence as follows:
         739-780: Missing.

    Show »
    Length:967
    Mass (Da):111,093
    Checksum:iCE6F8A2223E69167
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti205 – 2051E → A in BAA08290. (PubMed:7673154)Curated
    Sequence conflicti807 – 8071V → F in AAC28340. (PubMed:9645946)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 771771Missing in isoform 2. 1 PublicationVSP_004982Add
    BLAST
    Alternative sequencei739 – 78042Missing in isoform 3. 1 PublicationVSP_004984Add
    BLAST
    Alternative sequencei772 – 7809NVFKRHSMR → MGLIVLSSQ in isoform 2. 1 PublicationVSP_004983

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U69109 mRNA. Translation: AAC52895.1.
    D45854 mRNA. Translation: BAA08290.1.
    AF063890 mRNA. Translation: AAC28340.1.
    BC101921 mRNA. Translation: AAI01922.1.
    PIRiA57434.
    RefSeqiNP_059014.2. NM_017318.2. [P70600-1]
    XP_006252205.1. XM_006252143.1. [P70600-1]
    XP_006252206.1. XM_006252144.1. [P70600-1]
    XP_006252207.1. XM_006252145.1. [P70600-3]
    UniGeneiRn.11025.

    Genome annotation databases

    EnsembliENSRNOT00000030007; ENSRNOP00000031615; ENSRNOG00000027839. [P70600-1]
    ENSRNOT00000030036; ENSRNOP00000036813; ENSRNOG00000027839. [P70600-3]
    GeneIDi50646.
    KEGGirno:50646.
    UCSCiRGD:628758. rat. [P70600-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U69109 mRNA. Translation: AAC52895.1 .
    D45854 mRNA. Translation: BAA08290.1 .
    AF063890 mRNA. Translation: AAC28340.1 .
    BC101921 mRNA. Translation: AAI01922.1 .
    PIRi A57434.
    RefSeqi NP_059014.2. NM_017318.2. [P70600-1 ]
    XP_006252205.1. XM_006252143.1. [P70600-1 ]
    XP_006252206.1. XM_006252144.1. [P70600-1 ]
    XP_006252207.1. XM_006252145.1. [P70600-3 ]
    UniGenei Rn.11025.

    3D structure databases

    ProteinModelPortali P70600.
    SMRi P70600. Positions 415-692, 869-999.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 248405. 4 interactions.
    MINTi MINT-266266.

    Chemistry

    ChEMBLi CHEMBL1075222.

    PTM databases

    PhosphoSitei P70600.

    Proteomic databases

    PaxDbi P70600.
    PRIDEi P70600.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000030007 ; ENSRNOP00000031615 ; ENSRNOG00000027839 . [P70600-1 ]
    ENSRNOT00000030036 ; ENSRNOP00000036813 ; ENSRNOG00000027839 . [P70600-3 ]
    GeneIDi 50646.
    KEGGi rno:50646.
    UCSCi RGD:628758. rat. [P70600-1 ]

    Organism-specific databases

    CTDi 2185.
    RGDi 628758. Ptk2b.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000115459.
    HOGENOMi HOG000069938.
    HOVERGENi HBG004018.
    InParanoidi P70600.
    KOi K05871.
    OMAi QMLTASH.
    OrthoDBi EOG7ZSHSB.
    PhylomeDBi P70600.
    TreeFami TF316643.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 5301.

    Miscellaneous databases

    NextBioi 610458.
    PROi P70600.

    Gene expression databases

    Genevestigatori P70600.

    Family and domain databases

    Gene3Di 1.20.80.10. 1 hit.
    InterProi IPR019749. Band_41_domain.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    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 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. "Activation of a novel calcium-dependent protein-tyrosine kinase. Correlation with c-Jun N-terminal kinase but not mitogen-activated protein kinase activation."
      Yu H., Li X., Marchetto G.S., Dy R., Hunter D., Calvo B., Dawson T.L., Wilm M., Anderegg R.J., Graves L.M., Earp H.S.
      J. Biol. Chem. 271:29993-29998(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 310-334; 553-572; 672-687 AND 989-998.
      Tissue: Liver epithelium.
    2. "Cloning and characterization of cell adhesion kinase beta, a novel protein-tyrosine kinase of the focal adhesion kinase subfamily."
      Sasaki H., Nagura K., Ishino M., Tobioka H., Kotani K., Sasaki T.
      J. Biol. Chem. 270:21206-21219(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: Sprague-Dawley.
      Tissue: Brain.
    3. "Expression and characterization of splice variants of PYK2, a focal adhesion kinase-related protein."
      Xiong W.-C., Macklem M., Parsons J.T.
      J. Cell Sci. 111:1981-1991(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION, DOMAIN FAT.
      Tissue: Hippocampus.
    4. "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 1).
      Tissue: Prostate.
    5. "Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions."
      Lev S., Moreno H., Martinez R., Canoll P., Peles E., Musacchio J.M., Plowman G.D., Rudy B., Schlessinger J.
      Nature 376:737-745(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION.
    6. "A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation."
      Dikic I., Tokiwa G., Lev S., Courtneidge S.A., Schlessinger J.
      Nature 383:547-550(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN G-PROTEIN COUPLED RECEPTOR SIGNALING AND PHOSPHORYLATION OF SRC, INTERACTION WITH SRC, PHOSPHORYLATION.
    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. "Pyk2/CAKbeta tyrosine kinase activity-mediated angiogenesis of pulmonary vascular endothelial cells."
      Tang H., Hao Q., Fitzgerald T., Sasaki T., Landon E.J., Inagami T.
      J. Biol. Chem. 277:5441-5447(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ANGIOGENESIS; CELL MIGRATION; CELL SPREADING AND REORGANIZATION OF THE ACTIN CYTOSKELETON, TISSUE SPECIFICITY.
    9. "Metabotropic glutamate receptor 1-induced upregulation of NMDA receptor current: mediation through the Pyk2/Src-family kinase pathway in cortical neurons."
      Heidinger V., Manzerra P., Wang X.Q., Strasser U., Yu S.P., Choi D.W., Behrens M.M.
      J. Neurosci. 22:5452-5461(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SRC-MEDIATED PHOSPHORYLATION OF NMDA RECEPTORS AND REGULATON OF NMDA RECEPTOR CHANNEL ACTIVITY.
    10. "Differential regulation of Pyk2 phosphorylation at Tyr-402 and Tyr-580 in intestinal epithelial cells: roles of calcium, Src, Rho kinase, and the cytoskeleton."
      Wu S.S., Jacamo R.O., Vong S.K., Rozengurt E.
      Cell. Signal. 18:1932-1940(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT TYR-402 AND TYR-580, CATALYTIC ACTIVITY.
    11. Cited for: AUTOPHOSPHORYLATION, INTERACTION WITH DLG4.
    12. "PYK2 signaling is required for PDGF-dependent vascular smooth muscle cell proliferation."
      Perez J., Torres R.A., Rocic P., Cismowski M.J., Weber D.S., Darley-Usmar V.M., Lucchesi P.A.
      Am. J. Physiol. 301:C242-C251(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "The Pyk2 FERM regulates Pyk2 complex formation and phosphorylation."
      Riggs D., Yang Z., Kloss J., Loftus J.C.
      Cell. Signal. 23:288-296(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-402; TYR-579 AND TYR-580, SUBUNIT.

    Entry informationi

    Entry nameiFAK2_RAT
    AccessioniPrimary (citable) accession number: P70600
    Secondary accession number(s): O88489, Q3T1H4, Q63201
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 144 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, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3