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P16879

- FES_MOUSE

UniProt

P16879 - FES_MOUSE

Protein

Tyrosine-protein kinase Fes/Fps

Gene

Fes

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (15 Jan 2008)
      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 TRIM28.3 Publications

    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-713. Present in an inactive form in the absence of activating stimuli.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei590 – 5901ATPPROSITE-ProRule annotation
    Active sitei683 – 6831Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi567 – 5759ATPPROSITE-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 binding Source: IntAct
    6. protein kinase activity Source: MGI
    7. 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. protein autophosphorylation Source: Ensembl
    7. regulation of cell adhesion Source: UniProtKB
    8. regulation of cell differentiation Source: UniProtKB
    9. regulation of cell motility Source: UniProtKB
    10. regulation of cell proliferation Source: UniProtKB
    11. regulation of cell shape Source: UniProtKB
    12. regulation of mast cell degranulation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Lipid-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 3474.
    ReactomeiREACT_188578. Signaling by SCF-KIT.

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:95514. Fes.

    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: Reactome
    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

    Disruption phenotypei

    No visible phenotype. Mice are fertile and healthy, display slightly reduced numbers of myeloid cells and are more sensitive to lipopolysaccharide (LPS). Mice lacking both Fps/Fes and Fer activity are viable and fertile, but produce fewer offspring than normal. They display elevated levels of circulating neutrophils, erythrocytes and platelets, while other cell counts are normal.2 Publications

    Keywords - Diseasei

    Proto-oncogene, Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 822822Tyrosine-protein kinase Fes/FpsPRO_0000088089Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei67 – 671PhosphoserineBy similarity
    Modified residuei261 – 2611PhosphotyrosineBy similarity
    Modified residuei421 – 4211PhosphothreonineBy similarity
    Modified residuei713 – 7131Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei716 – 7161PhosphoserineBy similarity

    Post-translational modificationi

    Autophosphorylated on Tyr-713 in response to FGF2. Phosphorylated by LYN in response to FCER1 activation. Phosphorylated by HCK By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiP16879.

    PTM databases

    PhosphoSiteiP16879.

    Expressioni

    Gene expression databases

    BgeeiP16879.
    CleanExiMM_FES.
    GenevestigatoriP16879.

    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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    H2-K1P019013EBI-771815,EBI-1265227
    Ptpn11P352352EBI-771815,EBI-397236

    Protein-protein interaction databases

    BioGridi199634. 1 interaction.
    IntActiP16879. 3 interactions.
    MINTiMINT-1520684.

    Structurei

    3D structure databases

    ProteinModelPortaliP16879.
    SMRiP16879. Positions 1-402, 449-821.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 9696FCHPROSITE-ProRule annotationAdd
    BLAST
    Domaini460 – 54990SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini561 – 818258Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 300300Important for interaction with membranes containing phosphoinositidesBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili133 – 16533Sequence AnalysisAdd
    BLAST
    Coiled coili320 – 36950Sequence 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

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00750000117264.
    HOGENOMiHOG000059550.
    HOVERGENiHBG005655.
    InParanoidiP16879.
    KOiK07527.
    OMAiYQGFLRQ.
    OrthoDBiEOG708VXW.
    PhylomeDBiP16879.
    TreeFamiTF315363.

    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.

    P16879-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGFSSELCSP QGHGAVQQMQ EAELRLLEGM RKWMAQRVKS DREYAGLLHH    50
    MSLQDSGGQS WSSGPDSPVS QSWAEITSQT ENLSRVLRQH AEDLNSGPLS 100
    KLSVLIRERQ HLRKTYNEQW QQLQQELTKT HSQDIEKLKT QYRTLVRDST 150
    QARRKYQEAS KDKDRDKAKD KYVRSLWKLF AHHNRYVLGV RAAQLHHHHH 200
    HRFMLPGLLQ SLQDLHEEMA GILKDILQEY LEISSLVQDD VASIHRELAA 250
    AAARIQPEFE YLGFLRQYGS TPDVPPCVTF DESLLEDGEQ LEPGELQLNE 300
    LTLESVQHTL TSVTDELAVA TKEVLSRQEM VSQLQRELQS EEQNTHPRER 350
    VQLLSKRQML QEAIQGLQIA LCSQDKLQAQ QELLQSKMEQ LGTGEPPAVP 400
    LLQDDRHSTS STEQEREGGR TPTLEILKSH FSGIFRPKFS IPPPLQLVPE 450
    VQKPLYEQLW YHGAIPRAEV AELLTHSGDF LVRESQGKQE YVLSVMWDGQ 500
    PRHFIIQSSD NLYRLEGDGF PSIPLLITHL LSSQQPLTKK SGVVLFRAVP 550
    KDKWVLKHED LVLGEQIGRG NFGEVFSGRL RADNTPVAVK SCRETLPPDL 600
    KAKFLQEARI LKQYNHPNIV RLIGVCTQKQ PIYIVMELVQ GGDFLTFLRT 650
    EGARLRVKTL LQMVGDAAAG MEYLESKCCI HRDLAARNCL VTEKNVLKIS 700
    DFGMSREEAD GIYAASAGLR QVPVKWTAPE ALNYGRYSSE SDVWSFGILL 750
    WETFSLGASP YPNLTNQQTR EFVEKGHRLP CPELCPDAVF RLMEQCWAYE 800
    PGQRPSFSII CQELHSIRKR HR 822
    Length:822
    Mass (Da):93,779
    Last modified:January 15, 2008 - v2
    Checksum:i939280C56ACF25EE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti110 – 1112QH → HS in CAA31138. (PubMed:3060793)Curated
    Sequence conflicti413 – 4142Missing in CAA31138. (PubMed:3060793)Curated
    Sequence conflicti413 – 4142Missing in AAN33122. (PubMed:11909942)Curated
    Sequence conflicti467 – 4671R → W in CAA31138. (PubMed:3060793)Curated
    Sequence conflicti477 – 4771S → T in CAA31138. (PubMed:3060793)Curated
    Sequence conflicti477 – 4771S → T in AAN33122. (PubMed:11909942)Curated
    Sequence conflicti500 – 5001Q → H in CAA31138. (PubMed:3060793)Curated
    Sequence conflicti500 – 5001Q → H in AAN33122. (PubMed:11909942)Curated
    Sequence conflicti509 – 5091S → L in CAA31138. (PubMed:3060793)Curated
    Sequence conflicti509 – 5091S → L in AAN33122. (PubMed:11909942)Curated
    Sequence conflicti664 – 6641V → M in CAA31138. (PubMed:3060793)Curated
    Sequence conflicti716 – 7172SA → CS in CAA31138. (PubMed:3060793)Curated
    Sequence conflicti716 – 7172SA → CS in AAA40012. (PubMed:2482828)Curated
    Sequence conflicti749 – 7491L → P in AAA40012. (PubMed:2482828)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12616 mRNA. Translation: CAA31138.1.
    AF542394 Genomic DNA. Translation: AAN33122.1.
    M33421 mRNA. Translation: AAA40012.1.
    AK143639 mRNA. Translation: BAE25475.1.
    AK170418 mRNA. Translation: BAE41784.1.
    BC129919 mRNA. Translation: AAI29920.1.
    CCDSiCCDS39999.1.
    PIRiI48347.
    RefSeqiNP_034324.2. NM_010194.2.
    XP_006540667.1. XM_006540604.1.
    UniGeneiMm.48757.

    Genome annotation databases

    EnsembliENSMUST00000080932; ENSMUSP00000079733; ENSMUSG00000053158.
    GeneIDi14159.
    KEGGimmu:14159.
    UCSCiuc009ias.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12616 mRNA. Translation: CAA31138.1 .
    AF542394 Genomic DNA. Translation: AAN33122.1 .
    M33421 mRNA. Translation: AAA40012.1 .
    AK143639 mRNA. Translation: BAE25475.1 .
    AK170418 mRNA. Translation: BAE41784.1 .
    BC129919 mRNA. Translation: AAI29920.1 .
    CCDSi CCDS39999.1.
    PIRi I48347.
    RefSeqi NP_034324.2. NM_010194.2.
    XP_006540667.1. XM_006540604.1.
    UniGenei Mm.48757.

    3D structure databases

    ProteinModelPortali P16879.
    SMRi P16879. Positions 1-402, 449-821.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199634. 1 interaction.
    IntActi P16879. 3 interactions.
    MINTi MINT-1520684.

    PTM databases

    PhosphoSitei P16879.

    Proteomic databases

    PRIDEi P16879.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000080932 ; ENSMUSP00000079733 ; ENSMUSG00000053158 .
    GeneIDi 14159.
    KEGGi mmu:14159.
    UCSCi uc009ias.1. mouse.

    Organism-specific databases

    CTDi 2242.
    MGIi MGI:95514. Fes.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117264.
    HOGENOMi HOG000059550.
    HOVERGENi HBG005655.
    InParanoidi P16879.
    KOi K07527.
    OMAi YQGFLRQ.
    OrthoDBi EOG708VXW.
    PhylomeDBi P16879.
    TreeFami TF315363.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 3474.
    Reactomei REACT_188578. Signaling by SCF-KIT.

    Miscellaneous databases

    NextBioi 285286.
    PROi P16879.
    SOURCEi Search...

    Gene expression databases

    Bgeei P16879.
    CleanExi MM_FES.
    Genevestigatori P16879.

    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. "Isolation and structural analysis of murine c-fes cDNA clones."
      Wilks A.F., Kurban R.R.
      Oncogene 3:289-294(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Enhanced endotoxin sensitivity in fps/fes-null mice with minimal defects in hematopoietic homeostasis."
      Zirngibl R.A., Senis Y., Greer P.A.
      Mol. Cell. Biol. 22:2472-2486(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE.
      Strain: 129/SvJ.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Spleen.
    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].
    5. "The application of the polymerase chain reaction to cloning members of the protein tyrosine kinase family."
      Wilks A.F., Kurban R.R., Hovens C.M., Ralph S.J.
      Gene 85:67-74(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 680-749.
    6. "Fps/Fes and Fer protein-tyrosine kinases play redundant roles in regulating hematopoiesis."
      Senis Y.A., Craig A.W., Greer P.A.
      Exp. Hematol. 31:673-681(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    7. "Fer and Fps/Fes participate in a Lyn-dependent pathway from FcepsilonRI to platelet-endothelial cell adhesion molecule 1 to limit mast cell activation."
      Udell C.M., Samayawardhena L.A., Kawakami Y., Kawakami T., Craig A.W.
      J. Biol. Chem. 281:20949-20957(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MAST CELL ACTIVATION AND PHOSPHORYLATION OF PECAM1, PHOSPHORYLATION, ENZYME REGULATION.
    8. "The tyrosine kinase FES is an essential effector of KITD816V proliferation signal."
      Voisset E., Lopez S., Dubreuil P., De Sepulveda P.
      Blood 110:2593-2599(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH KIT, PHOSPHORYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
    9. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-713, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    10. "Fps/Fes protein-tyrosine kinase regulates mast cell adhesion and migration downstream of Kit and beta1 integrin receptors."
      Smith J.A., Samayawardhena L.A., Craig A.W.
      Cell. Signal. 22:427-436(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiFES_MOUSE
    AccessioniPrimary (citable) accession number: P16879
    Secondary accession number(s): Q3TD20, Q62122, Q8CG02
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 135 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3