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P14234

- FGR_MOUSE

UniProt

P14234 - FGR_MOUSE

Protein

Tyrosine-protein kinase Fgr

Gene

Fgr

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors devoid of kinase activity and contributes to the regulation of immune responses, including neutrophil, monocyte, macrophage and mast cell functions, cytoskeleton remodeling in response to extracellular stimuli, phagocytosis, cell adhesion and migration. Promotes mast cell degranulation, release of inflammatory cytokines and IgE-mediated anaphylaxis. Acts downstream of receptors that bind the Fc region of immunoglobulins, such as MS4A2/FCER1B, FCER1G and FCGR2. Acts downstream of ITGB1 and ITGB2, and regulates actin cytoskeleton reorganization, cell spreading and adhesion. Depending on the context, activates or inhibits cellular responses. Functions as negative regulator of ITGB2 signaling, phagocytosis and SYK activity in monocytes (PubMed:11672534). Required for normal ITGB1 and ITGB2 signaling, normal cell spreading and adhesion in neutrophils and macrophages (PubMed:8666673 and PubMed:9687507). Functions as positive regulator of cell migration and regulates cytoskeleton reorganization via RAC1 activation (PubMed:15561106). Phosphorylates SYK (in vitro) and promotes SYK-dependent activation of AKT1 and MAP kinase signaling (PubMed:21746961). Phosphorylates PLD2 in antigen-stimulated mast cells, leading to PLD2 activation and the production of the signaling molecules lysophosphatidic acid and diacylglycerol. Promotes activation of PIK3R1. Phosphorylates FASLG, and thereby regulates its ubiquitination and subsequent internalization. Phosphorylates ABL1. Promotes phosphorylation of CBL, CTTN, PIK3R1, PTK2/FAK1, PTK2B/PYK2 and VAV2. Phosphorylates HCLS1 that has already been phosphorylated by SYK, but not unphosphorylated HCLS1.8 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Activated by autophosphorylation. Prior phosphorylation at Tyr-511 by SRC inhibits ulterior autophosphorylation at Tyr-400. Activated by phorbol myristate acetate, phosphatidic acid and poly-Lys. Binding (via SH2 domain) of HCLS1 that is already phosphorylated by SYK strongly increases kinase activity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei279 – 2791ATPPROSITE-ProRule annotation
    Active sitei370 – 3701Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi257 – 2659ATPPROSITE-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. phosphotyrosine binding Source: UniProtKB
    5. protein binding Source: IntAct
    6. protein kinase binding Source: UniProtKB

    GO - Biological processi

    1. defense response to Gram-positive bacterium Source: UniProtKB
    2. innate immune response Source: UniProtKB-KW
    3. integrin-mediated signaling pathway Source: UniProtKB
    4. peptidyl-tyrosine phosphorylation Source: UniProtKB
    5. positive regulation of cell migration Source: UniProtKB
    6. positive regulation of cytokine secretion Source: UniProtKB
    7. positive regulation of mast cell degranulation Source: UniProtKB
    8. positive regulation of phosphatidylinositol 3-kinase activity Source: Ensembl
    9. positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
    10. protein autophosphorylation Source: Ensembl
    11. regulation of actin cytoskeleton organization Source: UniProtKB
    12. regulation of cell shape Source: UniProtKB
    13. regulation of innate immune response Source: UniProtKB
    14. regulation of phagocytosis Source: UniProtKB
    15. regulation of protein kinase activity Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Immunity, Innate immunity

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 3474.
    ReactomeiREACT_196487. FCGR activation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase Fgr (EC:2.7.10.2)
    Alternative name(s):
    Proto-oncogene c-Fgr
    p55-Fgr
    Gene namesi
    Name:Fgr
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:95527. Fgr.

    Subcellular locationi

    Cell membrane 1 Publication; Lipid-anchor 1 Publication; Cytoplasmic side 1 Publication. Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cell projectionruffle membrane 1 Publication. Cytoplasmcytosol 1 Publication. Cytoplasmcytoskeleton 1 Publication. Mitochondrion inner membrane By similarity. Mitochondrion intermembrane space By similarity
    Note: Detected in mitochondrial intermembrane space and at inner membranes By similarity. Colocalizes with actin fibers at membrane ruffles. Detected at plasma membrane lipid rafts.By similarity

    GO - Cellular componenti

    1. cytoskeleton Source: UniProtKB-SubCell
    2. cytosol Source: UniProtKB-SubCell
    3. mitochondrial inner membrane Source: UniProtKB-SubCell
    4. mitochondrial intermembrane space Source: UniProtKB-SubCell
    5. plasma membrane Source: UniProtKB
    6. ruffle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype. Mice lacking both Fgr and Hck are normal and fertile, but show increased susceptibility to infection with Listeria monocytogenes. In addition, their polymorphonuclear leukocytes show defects in cell spreading and adhesion.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1 – 77Missing: Abolishes localization at the cell membrane. 1 Publication
    Mutagenesisi279 – 2791K → R: Loss of kinase activity. 2 Publications

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedCurated
    Chaini2 – 517516Tyrosine-protein kinase FgrPRO_0000088092Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine1 Publication
    Lipidationi3 – 31S-palmitoyl cysteine1 Publication
    Lipidationi6 – 61S-palmitoyl cysteine1 Publication
    Modified residuei13 – 131Phosphoserine1 Publication
    Modified residuei32 – 321PhosphotyrosineBy similarity
    Modified residuei400 – 4001Phosphotyrosine; alternate1 Publication
    Modified residuei400 – 4001Phosphotyrosine; by autocatalysis; alternateBy similarity
    Modified residuei511 – 5111Phosphotyrosine; by SRCBy similarity

    Post-translational modificationi

    Ubiquitinated. Becomes ubiquitinated in response to ITGB2 signaling; this does not lead to degradation By similarity.By similarity
    Phosphorylated. Autophosphorylated on tyrosine residues. Becomes phosphorylated in response to FCGR2 engagement, cell adhesion and signaling by ITGB2. Prior phosphorylation at Tyr-511 by SRC inhibits ulterior autophosphorylation at Tyr-400 By similarity.By similarity

    Keywords - PTMi

    Lipoprotein, Myristate, Palmitate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP14234.
    PaxDbiP14234.
    PRIDEiP14234.

    PTM databases

    PhosphoSiteiP14234.

    Expressioni

    Gene expression databases

    BgeeiP14234.
    GenevestigatoriP14234.

    Interactioni

    Subunit structurei

    Interacts with ITGB1, ITGB2, MS4A2/FCER1B, FCER1G and FCGR2. Interacts (via SH2 domain) with SYK (tyrosine phosphorylated). Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts with PTK2/FAK1. Interacts (via SH2 domain) with HCLS1 (tyrosine phosphorylated by SYK). Interacts with SIRPA and PTPNS1. Interacts (not phosphorylated on tyrosine residues) with CBL; FGR tyrosine phosphorylation promotes dissociation By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ClnkQ9QZE23EBI-7587024,EBI-8040679

    Protein-protein interaction databases

    BioGridi199663. 1 interaction.
    IntActiP14234. 3 interactions.
    MINTiMINT-85500.
    STRINGi10090.ENSMUSP00000030693.

    Structurei

    3D structure databases

    ProteinModelPortaliP14234.
    SMRiP14234. Positions 37-515.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini65 – 12662SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini132 – 22998SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini251 – 504254Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH2 domain, SH3 domain

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00620000087702.
    HOGENOMiHOG000233858.
    HOVERGENiHBG008761.
    InParanoidiQ8BGM0.
    KOiK08891.
    OMAiTWNGSTK.
    OrthoDBiEOG7GTT2V.
    TreeFamiTF351634.

    Family and domain databases

    Gene3Di3.30.505.10. 1 hit.
    InterProiIPR028459. FGR.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR001452. SH3_domain.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view]
    PANTHERiPTHR24418:SF224. PTHR24418:SF224. 1 hit.
    PfamiPF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    PR00109. TYRKINASE.
    SMARTiSM00252. SH2. 1 hit.
    SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P14234-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGCVFCKKLE PASKEDVGLE GDFRSQTAEE RYFPDPTQGR TSSVFPQPTS    50
    PAFLNTGNMR SISGTGVTIF VALYDYEART GDDLTFTKGE KFHILNNTEY 100
    DWWEARSLSS GHRGYVPSNY VAPVDSIQAE EWYFGKISRK DAERQLLSSG 150
    NPQGAFLIRE SETTKGAYSL SIRDWDQNRG DHIKHYKIRK LDTGGYYITT 200
    RAQFDSIQDL VRHYMEVNDG LCYLLTAPCT TTKPQTLGLA KDAWEIDRNS 250
    IALERRLGTG CFGDVWLGTW NCSTKVAVKT LKPGTMSPKA FLEEAQIMKL 300
    LRHDKLVQLY AVVSEEPIYI VTEFMCYGSL LDFLKDREGQ NLMLPHLVDM 350
    AAQVAEGMAY MERMNYIHRD LRAANILVGE YLICKIADFG LARLIEDNEY 400
    NPQQGTKFPI KWTAPEAALF GRFTVKSDVW SFGILLTELI TKGRVPYPGM 450
    NNREVLEQVE HGYHMPCPPG CPASLYEVME QAWRLDPEER PTFEYLQSFL 500
    EDYFTSTEPQ YQPGDQT 517
    Length:517
    Mass (Da):58,867
    Last modified:July 27, 2011 - v2
    Checksum:i87DF5B19BF3F4734
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti33 – 331F → Y in CAA34463. (PubMed:2674853)Curated
    Sequence conflicti33 – 331F → Y in CAA36437. (PubMed:2179817)Curated
    Sequence conflicti41 – 411T → N in CAA34463. (PubMed:2674853)Curated
    Sequence conflicti212 – 2121R → Q in CAA34463. (PubMed:2674853)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16440 mRNA. Translation: CAA34463.1.
    X52191 mRNA. Translation: CAA36437.1.
    AK036438 mRNA. Translation: BAC29429.1.
    AK036476 mRNA. Translation: BAC29445.1.
    AK038141 mRNA. Translation: BAC29939.1.
    AK155902 mRNA. Translation: BAE33493.1.
    AL627184 Genomic DNA. Translation: CAM14378.1.
    CH466552 Genomic DNA. Translation: EDL30081.1.
    CH466552 Genomic DNA. Translation: EDL30082.1.
    CCDSiCCDS18739.1.
    PIRiA43807.
    RefSeqiNP_034338.3. NM_010208.4.
    XP_006538607.1. XM_006538544.1.
    XP_006538608.1. XM_006538545.1.
    UniGeneiMm.271665.

    Genome annotation databases

    EnsembliENSMUST00000030693; ENSMUSP00000030693; ENSMUSG00000028874.
    ENSMUST00000171223; ENSMUSP00000128411; ENSMUSG00000028874.
    GeneIDi14191.
    KEGGimmu:14191.
    UCSCiuc012dmj.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16440 mRNA. Translation: CAA34463.1 .
    X52191 mRNA. Translation: CAA36437.1 .
    AK036438 mRNA. Translation: BAC29429.1 .
    AK036476 mRNA. Translation: BAC29445.1 .
    AK038141 mRNA. Translation: BAC29939.1 .
    AK155902 mRNA. Translation: BAE33493.1 .
    AL627184 Genomic DNA. Translation: CAM14378.1 .
    CH466552 Genomic DNA. Translation: EDL30081.1 .
    CH466552 Genomic DNA. Translation: EDL30082.1 .
    CCDSi CCDS18739.1.
    PIRi A43807.
    RefSeqi NP_034338.3. NM_010208.4.
    XP_006538607.1. XM_006538544.1.
    XP_006538608.1. XM_006538545.1.
    UniGenei Mm.271665.

    3D structure databases

    ProteinModelPortali P14234.
    SMRi P14234. Positions 37-515.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199663. 1 interaction.
    IntActi P14234. 3 interactions.
    MINTi MINT-85500.
    STRINGi 10090.ENSMUSP00000030693.

    Chemistry

    ChEMBLi CHEMBL2034795.

    PTM databases

    PhosphoSitei P14234.

    Proteomic databases

    MaxQBi P14234.
    PaxDbi P14234.
    PRIDEi P14234.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030693 ; ENSMUSP00000030693 ; ENSMUSG00000028874 .
    ENSMUST00000171223 ; ENSMUSP00000128411 ; ENSMUSG00000028874 .
    GeneIDi 14191.
    KEGGi mmu:14191.
    UCSCi uc012dmj.1. mouse.

    Organism-specific databases

    CTDi 2268.
    MGIi MGI:95527. Fgr.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00620000087702.
    HOGENOMi HOG000233858.
    HOVERGENi HBG008761.
    InParanoidi Q8BGM0.
    KOi K08891.
    OMAi TWNGSTK.
    OrthoDBi EOG7GTT2V.
    TreeFami TF351634.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 3474.
    Reactomei REACT_196487. FCGR activation.

    Miscellaneous databases

    NextBioi 285410.
    PROi P14234.
    SOURCEi Search...

    Gene expression databases

    Bgeei P14234.
    Genevestigatori P14234.

    Family and domain databases

    Gene3Di 3.30.505.10. 1 hit.
    InterProi IPR028459. FGR.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR001452. SH3_domain.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view ]
    PANTHERi PTHR24418:SF224. PTHR24418:SF224. 1 hit.
    Pfami PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    PR00109. TYRKINASE.
    SMARTi SM00252. SH2. 1 hit.
    SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the murine c-fgr proto-oncogene cDNA and induction of c-fgr expression by proliferation and activation factors in normal bone marrow-derived monocytic cells."
      Yi T.L., Willman C.L.
      Oncogene 4:1081-1087(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: DBA/2J.
    2. "Molecular cloning and sequencing of the murine c-fgr gene."
      King F.J., Cole M.D.
      Oncogene 5:337-344(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Monocytic leukemia.
    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.
      Tissue: Bone and Thymus.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "Functional overlap in the src gene family: inactivation of hck and fgr impairs natural immunity."
      Lowell C.A., Soriano P., Varmus H.E.
      Genes Dev. 8:387-398(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION IN IMMUNITY TO LISTERIA INFECTION.
    7. "Deficiency of Src family kinases p59/61hck and p58c-fgr results in defective adhesion-dependent neutrophil functions."
      Lowell C.A., Fumagalli L., Berton G.
      J. Cell Biol. 133:895-910(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION IN CELL ADHESION AND INTEGRIN SIGNALING.
    8. "A beta 1 integrin signaling pathway involving Src-family kinases, Cbl and PI-3 kinase is required for macrophage spreading and migration."
      Meng F., Lowell C.A.
      EMBO J. 17:4391-4403(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ITGB1 SIGNALING, FUNCTION IN PHOSPHORYLATION OF CBL, INTERACTION WITH CBL.
    9. "Negative regulation of phagocytosis in murine macrophages by the Src kinase family member, Fgr."
      Gresham H.D., Dale B.M., Potter J.W., Chang P.W., Vines C.M., Lowell C.A., Lagenaur C.F., Willman C.L.
      J. Exp. Med. 191:515-528(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIRPA AND PTPNS1, MUTAGENESIS OF LYS-279, FUNCTION AS NEGATIVE REGULATOR OF PHAGOCYTOSIS.
    10. "Inhibition of beta 2 integrin receptor and Syk kinase signaling in monocytes by the Src family kinase Fgr."
      Vines C.M., Potter J.W., Xu Y., Geahlen R.L., Costello P.S., Tybulewicz V.L., Lowell C.A., Chang P.W., Gresham H.D., Willman C.L.
      Immunity 15:507-519(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS NEGATIVE REGULATOR OF SYK AND INTEGRIN SIGNALING, INTERACTION WITH SYK.
    11. "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; ACTIVATION OF RAC1 AND IN PHOSPHORYLATION OF PIK3R1; PTK2/FAK1; VAV2; PTK2B/PYK2 AND CTTN, CATALYTIC ACTIVITY, INTERACTION WITH PTK2/FAK1, MYRISTOYLATION, PALMITOYLATION, MUTAGENESIS OF 1-MET--LYS-7, SUBCELLULAR LOCATION.
    12. "Identification of Y589 and Y599 in the juxtamembrane domain of Flt3 as ligand-induced autophosphorylation sites involved in binding of Src family kinases and the protein tyrosine phosphatase SHP2."
      Heiss E., Masson K., Sundberg C., Pedersen M., Sun J., Bengtsson S., Ronnstrand L.
      Blood 108:1542-1550(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FLT3.
    13. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND TYR-400, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "c-Abl and Src-family kinases cross-talk in regulation of myeloid cell migration."
      Baruzzi A., Iacobucci I., Soverini S., Lowell C.A., Martinelli G., Berton G.
      FEBS Lett. 584:15-21(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF CELL MIGRATION, INTERACTION WITH ABL1; ITGB1 AND ITGB2.
    15. "The Src family kinase Fgr is critical for activation of mast cells and IgE-mediated anaphylaxis in mice."
      Lee J.H., Kim J.W., Kim do K., Kim H.S., Park H.J., Park D.K., Kim A.R., Kim B., Beaven M.A., Park K.L., Kim Y.M., Choi W.S.
      J. Immunol. 187:1807-1815(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF SYK; MAST CELL DEGRANULATION AND RELEASE OF CYTOKINES, INTERACTION WITH FCER1G.

    Entry informationi

    Entry nameiFGR_MOUSE
    AccessioniPrimary (citable) accession number: P14234
    Secondary accession number(s): Q61404, Q8BGM0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 145 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