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P14238

- FES_FELCA

UniProt

P14238 - FES_FELCA

Protein

Tyrosine-protein kinase Fes/Fps

Gene

FES

Organism
Felis catus (Cat) (Felis silvestris catus)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Tyrosine-protein kinase that acts downstream of cell surface receptors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, cell attachment and cell spreading. Plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Acts down-stream of the activated FCER1 receptor and the mast/stem cell growth factor receptor KIT. Plays a role in the regulation of mast cell degranulation. Plays a role in the regulation of cell differentiation and promotes neurite outgrowth in response to NGF signaling. Plays a role in cell scattering and cell migration in response to HGF-induced activation of EZR. Phosphorylates BCR and down-regulates BCR kinase activity. Phosphorylates HCLS1/HS1, PECAM1, STAT3 and TRIM28 By similarity.By similarity

    Catalytic activityi

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

    Enzyme regulationi

    Kinase activity is tightly regulated. Activated in response to signaling from a cell surface receptor. Activation probably requires binding of a substrate via the SH2 domain, plus autophosphorylation at Tyr-711. Present in an inactive form in the absence of activating stimuli By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei588 – 5881ATPPROSITE-ProRule annotation
    Active sitei681 – 6811Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi565 – 5739ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. immunoglobulin receptor binding Source: UniProtKB
    3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
    4. phosphatidylinositol binding Source: UniProtKB
    5. protein tyrosine kinase activity Source: UniProtKB

    GO - Biological processi

    1. peptidyl-tyrosine phosphorylation Source: UniProtKB
    2. positive regulation of actin cytoskeleton reorganization Source: UniProtKB
    3. positive regulation of microtubule polymerization Source: UniProtKB
    4. positive regulation of myeloid cell differentiation Source: UniProtKB
    5. positive regulation of neuron projection development Source: UniProtKB
    6. regulation of cell adhesion Source: UniProtKB
    7. regulation of cell differentiation Source: UniProtKB
    8. regulation of cell motility Source: UniProtKB
    9. regulation of cell proliferation Source: UniProtKB
    10. regulation of cell shape Source: UniProtKB
    11. regulation of mast cell degranulation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Lipid-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase Fes/Fps (EC:2.7.10.2)
    Alternative name(s):
    Proto-oncogene c-Fes
    Gene namesi
    Name:FES
    Synonyms:FPS
    OrganismiFelis catus (Cat) (Felis silvestris catus)
    Taxonomic identifieri9685 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis
    ProteomesiUP000011712: Unplaced

    Subcellular locationi

    Cytoplasmcytosol By similarity. Cytoplasmcytoskeleton By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cytoplasmic vesicle By similarity. Golgi apparatus By similarity. Cell junctionfocal adhesion By similarity
    Note: Distributed throughout the cytosol when the kinase is not activated. Association with microtubules requires activation of the kinase activity. Shuttles between focal adhesions and cell-cell contacts in epithelial cells. Recruited to the lateral cell membrane in polarized epithelial cells by interaction with phosphorylated EZR. Detected at tubular membrane structures in the cytoplasm and at the cell periphery By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
    3. cytosol Source: UniProtKB-SubCell
    4. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
    5. focal adhesion Source: UniProtKB
    6. Golgi apparatus Source: UniProtKB-SubCell
    7. microtubule cytoskeleton Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Golgi apparatus, Membrane

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene, Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 820820Tyrosine-protein kinase Fes/FpsPRO_0000088085Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei65 – 651PhosphoserineBy similarity
    Modified residuei259 – 2591PhosphotyrosineBy similarity
    Modified residuei419 – 4191PhosphothreonineBy similarity
    Modified residuei711 – 7111Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei714 – 7141PhosphoserineBy similarity

    Post-translational modificationi

    Autophosphorylated on Tyr-711 in response to FGF2. Phosphorylated by LYN in response to FCER1 activation. Phosphorylated by HCK By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiP14238.

    Interactioni

    Subunit structurei

    Homooligomer. Interacts with BCR. Interacts (when activated, via coiled coil domain) with TRIM28. Interacts (via SH2 domain) with phosphorylated EZR, MS4A2/FCER1B and HCLS1/HS1. Interacts with phosphorylated KIT. Interacts with FLT3. Interacts (via FCH domain) with soluble tubulin. Interacts (via SH2 domain) with microtubules By similarity.By similarity

    Protein-protein interaction databases

    STRINGi9685.ENSFCAP00000005663.

    Structurei

    3D structure databases

    ProteinModelPortaliP14238.
    SMRiP14238. Positions 447-819.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 9494FCHPROSITE-ProRule annotationAdd
    BLAST
    Domaini458 – 54790SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini559 – 820262Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 298298Important for interaction with membranes containing phosphoinositidesBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili123 – 16341Sequence AnalysisAdd
    BLAST
    Coiled coili318 – 38972Sequence AnalysisAdd
    BLAST

    Domaini

    The coiled coil domains are important for regulating the kinase activity. They mediate homooligomerization and probably also interaction with other proteins By similarity.By similarity
    The N-terminal region including the first coiled coil domain mediates interaction with phosphoinositide-containing membranes.By similarity

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. Fes/fps subfamily.PROSITE-ProRule annotation
    Contains 1 FCH domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, SH2 domain

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG005655.

    Family and domain databases

    Gene3Di3.30.505.10. 1 hit.
    InterProiIPR001060. FCH_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR016250. Tyr-prot_kinase_Fes/Fps.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view]
    PfamiPF00611. FCH. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000632. TyrPK_fps. 1 hit.
    PRINTSiPR00401. SH2DOMAIN.
    PR00109. TYRKINASE.
    SMARTiSM00055. FCH. 1 hit.
    SM00252. SH2. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50133. FCH. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P14238-1 [UniParc]FASTAAdd to Basket

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    MGFSSELCSP QGHGAVQQMQ EAELRLLEGM RKWMAQRVKS DREYAGLLHH    50
    MSLQDGGGRG TGPYSPISQS WAEITSQTEG LSRLLRQHAE DLNSGPLSKL 100
    GLLIRERQQL RKTYSEQWQQ LQQELTKTHN QDIEKLKSQY RALARDSAQA 150
    RRKYQEASKD KDRDKAKDKY VRSLWKLFAH HNRYVLGVRA AQLHHHHHHQ 200
    LMLPGLLQSL QDLHQEMACI LKEILQEYLE ISSLVQDEVV AIHLEMAAAV 250
    ARIQPEAEYQ GFLRQYGSTP DVPPCVTFDE SLLEEGEPLE PGELQLNELT 300
    VESVQHTLTS VTDELTVATQ TVLSRQEAVA QLQRELQNEE QNTHPRERVQ 350
    LLAKKQVLQE ALQALQVALC SQAKLQAQRE LLQAKLEQLG PGEPPPVLLL 400
    QDDRHSTSSS EQEREGGRTP TLEILKSHIS GIFRPKFSLP PPLQLVPEVQ 450
    KPLHEQLWYH GALPRAEVAE LLTHSGDFLV RESQGKQEYV LSVLWDGQPR 500
    HFIIESADNL YRLEGDGFAS IPLLVDHLLR SQQPLTKKSG IVLNRAVPKD 550
    KWVLNHEDLV LGEQIGRGNF GEVFSGRLRA DNTLVAVKSC RETLPPDIKA 600
    KFLQEAKILK QYSHPNIVRL IGVCTQKQPI YIVMELVQGG DFLTFLRTEG 650
    ARLRMKTLLQ MVGDAAAGME YLESKCCIHR DLAARNCLVT EKNVLKISDF 700
    GMSREEADGI YAASGGLRQV PVKWTAPEAL NYGRYSSESD VWSFGILLWE 750
    TFSLGASPYP NLSNQQTREF VEKGGRLPCP ELCPDAVFRL MEQCWAYEPG 800
    QRPSFSAIYQ ELQSIRKRHR 820
    Length:820
    Mass (Da):92,975
    Last modified:February 1, 1996 - v2
    Checksum:iF3A52B750236834E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16705
    , M16666, M16667, M16668, M16669, M16670, M16671, M16706, M16672, M16673, M16674, M16698, M16700, M16701, M16702, M16704 Genomic DNA. Translation: AAA30808.1.
    PIRiA27824. TVCTFF.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16705
    , M16666 , M16667 , M16668 , M16669 , M16670 , M16671 , M16706 , M16672 , M16673 , M16674 , M16698 , M16700 , M16701 , M16702 , M16704 Genomic DNA. Translation: AAA30808.1 .
    PIRi A27824. TVCTFF.

    3D structure databases

    ProteinModelPortali P14238.
    SMRi P14238. Positions 447-819.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9685.ENSFCAP00000005663.

    Proteomic databases

    PRIDEi P14238.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG005655.

    Family and domain databases

    Gene3Di 3.30.505.10. 1 hit.
    InterProi IPR001060. FCH_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR016250. Tyr-prot_kinase_Fes/Fps.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view ]
    Pfami PF00611. FCH. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000632. TyrPK_fps. 1 hit.
    PRINTSi PR00401. SH2DOMAIN.
    PR00109. TYRKINASE.
    SMARTi SM00055. FCH. 1 hit.
    SM00252. SH2. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50133. FCH. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of the feline c-fes/fps proto-oncogene: genesis of a retroviral oncogene."
      Roebroek A.J.M., Schalken J.A., Onnekink C., Bloemers H.P.J., van de Ven W.J.M.
      J. Virol. 61:2009-2016(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiFES_FELCA
    AccessioniPrimary (citable) accession number: P14238
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 113 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3