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P09769

- FGR_HUMAN

UniProt

P09769 - FGR_HUMAN

Protein

Tyrosine-protein kinase Fgr

Gene

FGR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 2 (01 Jan 1990)
      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, FCGR2A and/or FCGR2B. 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. Required for normal ITGB1 and ITGB2 signaling, normal cell spreading and adhesion in neutrophils and macrophages. Functions as positive regulator of cell migration and regulates cytoskeleton reorganization via RAC1 activation. Phosphorylates SYK (in vitro) and promotes SYK-dependent activation of AKT1 and MAP kinase signaling. 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 HCLS1.4 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.3 PublicationsPROSITE-ProRule annotation

    Enzyme regulationi

    Activated by autophosphorylation. Prior phosphorylation at Tyr-523 by SRC inhibits ulterior autophosphorylation at Tyr-412. 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.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei291 – 2911ATPPROSITE-ProRule annotation
    Active sitei382 – 3821Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi269 – 2779ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. Fc-gamma receptor I complex binding Source: UniProtKB
    3. immunoglobulin receptor binding Source: UniProtKB
    4. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
    5. phosphotyrosine binding Source: UniProtKB
    6. protein binding Source: IntAct
    7. protein kinase binding Source: UniProtKB
    8. protein tyrosine kinase activity Source: UniProtKB

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. defense response to Gram-positive bacterium Source: UniProtKB
    3. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    4. immune response-regulating cell surface receptor signaling pathway Source: UniProtKB
    5. innate immune response Source: Reactome
    6. integrin-mediated signaling pathway Source: UniProtKB
    7. peptidyl-tyrosine phosphorylation Source: UniProtKB
    8. positive regulation of cell migration Source: UniProtKB
    9. positive regulation of cytokine secretion Source: UniProtKB
    10. positive regulation of mast cell degranulation Source: UniProtKB
    11. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
    12. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    13. protein autophosphorylation Source: UniProtKB
    14. protein phosphorylation Source: ProtInc
    15. regulation of cell shape Source: UniProtKB
    16. regulation of innate immune response Source: UniProtKB
    17. regulation of phagocytosis Source: UniProtKB
    18. regulation of protein kinase activity Source: UniProtKB
    19. response to virus Source: ProtInc

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Immunity, Innate immunity

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_160274. FCGR activation.
    REACT_23879. Platelet sensitization by LDL.
    SignaLinkiP09769.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase Fgr (EC:2.7.10.2)
    Alternative name(s):
    Gardner-Rasheed feline sarcoma viral (v-fgr) oncogene homolog
    Proto-oncogene c-Fgr
    p55-Fgr
    p58-Fgr
    p58c-Fgr
    Gene namesi
    Name:FGR
    Synonyms:SRC2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3697. FGR.

    Subcellular locationi

    Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projectionruffle membrane. Cytoplasmcytosol. Cytoplasmcytoskeleton. 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. actin cytoskeleton Source: Ensembl
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. mitochondrial inner membrane Source: UniProtKB-SubCell
    5. mitochondrial intermembrane space Source: UniProtKB-SubCell
    6. plasma membrane Source: UniProtKB
    7. ruffle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Involvement in diseasei

    Mutations that cause aberrant kinase activation can confer oncogene activity and promote aberrant cell proliferation.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi523 – 5231Y → F: Strongly increased catalytic activity. Functions as oncogene. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA28135.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 529528Tyrosine-protein kinase FgrPRO_0000088091Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity
    Lipidationi3 – 31S-palmitoyl cysteineBy similarity
    Lipidationi6 – 61S-palmitoyl cysteineBy similarity
    Modified residuei34 – 341Phosphotyrosine1 Publication
    Modified residuei412 – 4121Phosphotyrosine1 Publication
    Modified residuei523 – 5231Phosphotyrosine; by SRC1 Publication

    Post-translational modificationi

    Ubiquitinated. Becomes ubiquitinated in response to ITGB2 signaling; this does not lead to degradation.1 Publication
    Phosphorylated. Autophosphorylated on tyrosine residues. Becomes phosphorylated in response to FCGR2A and/or FCGR2B engagement, cell adhesion and signaling by ITGB2. Prior phosphorylation at Tyr-523 by SRC inhibits ulterior autophosphorylation at Tyr-412.3 Publications

    Keywords - PTMi

    Lipoprotein, Myristate, Palmitate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP09769.
    PRIDEiP09769.

    PTM databases

    PhosphoSiteiP09769.

    Expressioni

    Tissue specificityi

    Detected in neutrophils, monocytes and natural killer cells (at protein level). Detected in monocytes and large lymphocytes.3 Publications

    Gene expression databases

    ArrayExpressiP09769.
    BgeeiP09769.
    CleanExiHS_FGR.
    GenevestigatoriP09769.

    Organism-specific databases

    HPAiCAB018959.
    HPA002024.

    Interactioni

    Subunit structurei

    Interacts with ITGB1, ITGB2, MS4A2/FCER1B, FCER1G, FCGR2A and/or FCGR2B. 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. Interacts with PIK3R1 and FASLG By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ALOX5P099172EBI-1383732,EBI-79934
    ARP102753EBI-1383732,EBI-608057
    ERBB2P046263EBI-1383732,EBI-641062
    HSP90AB1P082382EBI-1383732,EBI-352572
    KITP107212EBI-1383732,EBI-1379503
    METP085812EBI-1383732,EBI-1039152

    Protein-protein interaction databases

    BioGridi108559. 20 interactions.
    DIPiDIP-1049N.
    IntActiP09769. 12 interactions.
    MINTiMINT-1209880.
    STRINGi9606.ENSP00000363115.

    Structurei

    3D structure databases

    ProteinModelPortaliP09769.
    SMRiP09769. Positions 78-527.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini77 – 13862SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini144 – 24198SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini263 – 516254Protein 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.
    HOGENOMiHOG000233858.
    HOVERGENiHBG008761.
    InParanoidiP09769.
    KOiK08891.
    OMAiTWNGSTK.
    OrthoDBiEOG7GTT2V.
    PhylomeDBiP09769.
    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.

    P09769-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGCVFCKKLE PVATAKEDAG LEGDFRSYGA ADHYGPDPTK ARPASSFAHI    50
    PNYSNFSSQA INPGFLDSGT IRGVSGIGVT LFIALYDYEA RTEDDLTFTK 100
    GEKFHILNNT EGDWWEARSL SSGKTGCIPS NYVAPVDSIQ AEEWYFGKIG 150
    RKDAERQLLS PGNPQGAFLI RESETTKGAY SLSIRDWDQT RGDHVKHYKI 200
    RKLDMGGYYI TTRVQFNSVQ ELVQHYMEVN DGLCNLLIAP CTIMKPQTLG 250
    LAKDAWEISR SSITLERRLG TGCFGDVWLG TWNGSTKVAV KTLKPGTMSP 300
    KAFLEEAQVM KLLRHDKLVQ LYAVVSEEPI YIVTEFMCHG SLLDFLKNPE 350
    GQDLRLPQLV DMAAQVAEGM AYMERMNYIH RDLRAANILV GERLACKIAD 400
    FGLARLIKDD EYNPCQGSKF PIKWTAPEAA LFGRFTIKSD VWSFGILLTE 450
    LITKGRIPYP GMNKREVLEQ VEQGYHMPCP PGCPASLYEA MEQTWRLDPE 500
    ERPTFEYLQS FLEDYFTSAE PQYQPGDQT 529
    Length:529
    Mass (Da):59,479
    Last modified:January 1, 1990 - v2
    Checksum:i6B8C1E08414E0F9C
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti110 – 1101T → I.1 Publication
    Corresponds to variant rs34597831 [ dbSNP | Ensembl ].
    VAR_041700
    Natural varianti130 – 1301S → R.1 Publication
    Corresponds to variant rs35334091 [ dbSNP | Ensembl ].
    VAR_041701

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19722 mRNA. Translation: AAA52451.1.
    AL031729 Genomic DNA. Translation: CAB62998.1.
    CH471059 Genomic DNA. Translation: EAX07748.1.
    CH471059 Genomic DNA. Translation: EAX07749.1.
    CH471059 Genomic DNA. Translation: EAX07750.1.
    BC064382 mRNA. Translation: AAH64382.1.
    X52207, X52208 Genomic DNA. Translation: CAA36457.2.
    M12724
    , M12719, M12720, M12721, M12722, M12723 Genomic DNA. Translation: AAA52762.1.
    CCDSiCCDS305.1.
    PIRiA27676. TVHUFR.
    RefSeqiNP_001036194.1. NM_001042729.1.
    NP_001036212.1. NM_001042747.1.
    NP_005239.1. NM_005248.2.
    XP_006710515.1. XM_006710452.1.
    UniGeneiHs.1422.

    Genome annotation databases

    EnsembliENST00000374003; ENSP00000363115; ENSG00000000938.
    ENST00000374004; ENSP00000363116; ENSG00000000938.
    ENST00000374005; ENSP00000363117; ENSG00000000938.
    ENST00000399173; ENSP00000382126; ENSG00000000938.
    GeneIDi2268.
    KEGGihsa:2268.
    UCSCiuc001boj.3. human.

    Polymorphism databases

    DMDMi125358.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19722 mRNA. Translation: AAA52451.1 .
    AL031729 Genomic DNA. Translation: CAB62998.1 .
    CH471059 Genomic DNA. Translation: EAX07748.1 .
    CH471059 Genomic DNA. Translation: EAX07749.1 .
    CH471059 Genomic DNA. Translation: EAX07750.1 .
    BC064382 mRNA. Translation: AAH64382.1 .
    X52207 , X52208 Genomic DNA. Translation: CAA36457.2 .
    M12724
    , M12719 , M12720 , M12721 , M12722 , M12723 Genomic DNA. Translation: AAA52762.1 .
    CCDSi CCDS305.1.
    PIRi A27676. TVHUFR.
    RefSeqi NP_001036194.1. NM_001042729.1.
    NP_001036212.1. NM_001042747.1.
    NP_005239.1. NM_005248.2.
    XP_006710515.1. XM_006710452.1.
    UniGenei Hs.1422.

    3D structure databases

    ProteinModelPortali P09769.
    SMRi P09769. Positions 78-527.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108559. 20 interactions.
    DIPi DIP-1049N.
    IntActi P09769. 12 interactions.
    MINTi MINT-1209880.
    STRINGi 9606.ENSP00000363115.

    Chemistry

    BindingDBi P09769.
    ChEMBLi CHEMBL4454.
    GuidetoPHARMACOLOGYi 2024.

    PTM databases

    PhosphoSitei P09769.

    Polymorphism databases

    DMDMi 125358.

    Proteomic databases

    PaxDbi P09769.
    PRIDEi P09769.

    Protocols and materials databases

    DNASUi 2268.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374003 ; ENSP00000363115 ; ENSG00000000938 .
    ENST00000374004 ; ENSP00000363116 ; ENSG00000000938 .
    ENST00000374005 ; ENSP00000363117 ; ENSG00000000938 .
    ENST00000399173 ; ENSP00000382126 ; ENSG00000000938 .
    GeneIDi 2268.
    KEGGi hsa:2268.
    UCSCi uc001boj.3. human.

    Organism-specific databases

    CTDi 2268.
    GeneCardsi GC01M027938.
    HGNCi HGNC:3697. FGR.
    HPAi CAB018959.
    HPA002024.
    MIMi 164940. gene.
    neXtProti NX_P09769.
    PharmGKBi PA28135.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233858.
    HOVERGENi HBG008761.
    InParanoidi P09769.
    KOi K08891.
    OMAi TWNGSTK.
    OrthoDBi EOG7GTT2V.
    PhylomeDBi P09769.
    TreeFami TF351634.

    Enzyme and pathway databases

    Reactomei REACT_160274. FCGR activation.
    REACT_23879. Platelet sensitization by LDL.
    SignaLinki P09769.

    Miscellaneous databases

    ChiTaRSi FGR. human.
    GeneWikii FGR_(gene).
    GenomeRNAii 2268.
    NextBioi 9223.
    PROi P09769.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09769.
    Bgeei P09769.
    CleanExi HS_FGR.
    Genevestigatori P09769.

    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. "Primary structure of the human fgr proto-oncogene product p55c-fgr."
      Katamine S., Notario V., Rao C.D., Miki T., Cheah M.S.C., Tronick S.R., Robbins K.C.
      Mol. Cell. Biol. 8:259-266(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Brain.
    5. "Structure and expression of c-fgr protooncogene mRNA in Epstein-Barr virus converted cell lines."
      Brickell P.M., Patel M.
      Br. J. Cancer 58:704-709(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-177 AND 524-529.
    6. "Isolation and sequencing of cDNA clones homologous to the v-fgr oncogene from a human B lymphocyte cell line, IM-9."
      Inoue K., Ikawa S., Semba K., Sukegawa J., Yamamoto T., Toyoshima K.
      Oncogene 1:301-304(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-143.
    7. "Structure of the complete human c-fgr proto-oncogene and identification of multiple transcriptional start sites."
      Patel M., Leevers S.J., Brickell P.M.
      Oncogene 5:201-206(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-142.
    8. "Structure, expression, and chromosomal location of the human c-fgr gene."
      Nishizawa M., Semba K., Yoshida M.C., Yamamoto T., Sasaki M., Toyoshima K.
      Mol. Cell. Biol. 6:511-517(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 111-416.
    9. "Specific expression of human c-fgr in natural immunity effector cells."
      Inoue K., Yamamoto T., Toyoshima K.
      Mol. Cell. Biol. 10:1789-1792(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
    10. "Diverse biologic properties imparted by the c-fgr proto-oncogene."
      Sartor O., Moriuchi R., Sameshima J.H., Severino M., Gutkind J.S., Robbins K.C.
      J. Biol. Chem. 267:3460-3465(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS PROTO-ONCOGENE, ROLE IN DISEASE, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-523.
    11. "Association of immunoglobulin G Fc receptor II with Src-like protein-tyrosine kinase Fgr in neutrophils."
      Hamada F., Aoki M., Akiyama T., Toyoshima K.
      Proc. Natl. Acad. Sci. U.S.A. 90:6305-6309(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FCGR2A AND/OR FCGR2B, CATALYTIC ACTIVITY, ENZYME REGULATION, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
    12. "Beta 2 integrin-dependent protein tyrosine phosphorylation and activation of the FGR protein tyrosine kinase in human neutrophils."
      Berton G., Fumagalli L., Laudanna C., Sorio C.
      J. Cell Biol. 126:1111-1121(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, FUNCTION IN INTEGRIN SIGNALING.
    13. "Activation of SRC family kinases in human neutrophils. Evidence that p58C-FGR and p53/56LYN redistributed to a Triton X-100-insoluble cytoskeletal fraction, also enriched in the caveolar protein caveolin, display an enhanced kinase activity."
      Yan S.R., Fumagalli L., Berton G.
      FEBS Lett. 380:198-203(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION AT THE CYTOSKELETON, ENZYME REGULATION.
    14. "Clustering of beta(2)-integrins on human neutrophils activates dual signaling pathways to PtdIns 3-kinase."
      Axelsson L., Hellberg C., Melander F., Smith D., Zheng L., Andersson T.
      Exp. Cell Res. 256:257-263(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ACTIVATION OF PIK3R1, PHOSPHORYLATION, INTERACTION WITH ITGB2 AND PIK3R1.
    15. "Phosphatidic acid regulates tyrosine phosphorylating activity in human neutrophils: enhancement of Fgr activity."
      Sergeant S., Waite K.A., Heravi J., McPhail L.C.
      J. Biol. Chem. 276:4737-4746(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    16. "Fgr but not Syk tyrosine kinase is a target for beta 2 integrin-induced c-Cbl-mediated ubiquitination in adherent human neutrophils."
      Melander F., Andersson T., Dib K.
      Biochem. J. 370:687-694(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH CBL.
    17. "Sorting of Fas ligand to secretory lysosomes is regulated by mono-ubiquitylation and phosphorylation."
      Zuccato E., Blott E.J., Holt O., Sigismund S., Shaw M., Bossi G., Griffiths G.M.
      J. Cell Sci. 120:191-199(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF FASLG, INTERACTION WITH FASLG.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-34; TYR-412 AND TYR-523, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-110 AND ARG-130.

    Entry informationi

    Entry nameiFGR_HUMAN
    AccessioniPrimary (citable) accession number: P09769
    Secondary accession number(s): D3DPL7, Q9UIQ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 164 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3