FGR_MOUSE
ID FGR_MOUSE Reviewed; 517 AA.
AC P14234; Q61404; Q8BGM0;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Tyrosine-protein kinase Fgr;
DE EC=2.7.10.2;
DE AltName: Full=Proto-oncogene c-Fgr;
DE AltName: Full=p55-Fgr;
GN Name=Fgr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=DBA/2J;
RX PubMed=2674853;
RA Yi T.L., Willman C.L.;
RT "Cloning of the murine c-fgr proto-oncogene cDNA and induction of c-fgr
RT expression by proliferation and activation factors in normal bone marrow-
RT derived monocytic cells.";
RL Oncogene 4:1081-1087(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Monocytic leukemia;
RX PubMed=2179817;
RA King F.J., Cole M.D.;
RT "Molecular cloning and sequencing of the murine c-fgr gene.";
RL Oncogene 5:337-344(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION IN IMMUNITY TO LISTERIA INFECTION.
RX PubMed=8125254; DOI=10.1101/gad.8.4.387;
RA Lowell C.A., Soriano P., Varmus H.E.;
RT "Functional overlap in the src gene family: inactivation of hck and fgr
RT impairs natural immunity.";
RL Genes Dev. 8:387-398(1994).
RN [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION IN CELL ADHESION AND INTEGRIN SIGNALING.
RX PubMed=8666673; DOI=10.1083/jcb.133.4.895;
RA Lowell C.A., Fumagalli L., Berton G.;
RT "Deficiency of Src family kinases p59/61hck and p58c-fgr results in
RT defective adhesion-dependent neutrophil functions.";
RL J. Cell Biol. 133:895-910(1996).
RN [8]
RP FUNCTION IN ITGB1 SIGNALING, FUNCTION IN PHOSPHORYLATION OF CBL, AND
RP INTERACTION WITH CBL.
RX PubMed=9687507; DOI=10.1093/emboj/17.15.4391;
RA Meng F., Lowell C.A.;
RT "A beta 1 integrin signaling pathway involving Src-family kinases, Cbl and
RT PI-3 kinase is required for macrophage spreading and migration.";
RL EMBO J. 17:4391-4403(1998).
RN [9]
RP INTERACTION WITH SIRPA AND PTPNS1, MUTAGENESIS OF LYS-279, AND FUNCTION AS
RP NEGATIVE REGULATOR OF PHAGOCYTOSIS.
RX PubMed=10662797; DOI=10.1084/jem.191.3.515;
RA Gresham H.D., Dale B.M., Potter J.W., Chang P.W., Vines C.M., Lowell C.A.,
RA Lagenaur C.F., Willman C.L.;
RT "Negative regulation of phagocytosis in murine macrophages by the Src
RT kinase family member, Fgr.";
RL J. Exp. Med. 191:515-528(2000).
RN [10]
RP FUNCTION AS NEGATIVE REGULATOR OF SYK AND INTEGRIN SIGNALING, AND
RP INTERACTION WITH SYK.
RX PubMed=11672534; DOI=10.1016/s1074-7613(01)00221-7;
RA Vines C.M., Potter J.W., Xu Y., Geahlen R.L., Costello P.S.,
RA Tybulewicz V.L., Lowell C.A., Chang P.W., Gresham H.D., Willman C.L.;
RT "Inhibition of beta 2 integrin receptor and Syk kinase signaling in
RT monocytes by the Src family kinase Fgr.";
RL Immunity 15:507-519(2001).
RN [11]
RP FUNCTION IN REGULATION OF CELL MIGRATION; ACTIVATION OF RAC1 AND IN
RP PHOSPHORYLATION OF PIK3R1; PTK2/FAK1; VAV2; PTK2B/PYK2 AND CTTN, CATALYTIC
RP ACTIVITY, INTERACTION WITH PTK2/FAK1, MYRISTOYLATION AT GLY-2,
RP PALMITOYLATION AT CYS-3 AND CYS-6, MUTAGENESIS OF 1-MET--LYS-7, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15561106; DOI=10.1016/j.yexcr.2004.09.005;
RA Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L.,
RA Lowell C.A., Berton G.;
RT "The proto-oncogene Fgr regulates cell migration and this requires its
RT plasma membrane localization.";
RL Exp. Cell Res. 302:253-269(2005).
RN [12]
RP FUNCTION, INTERACTION WITH CLNK, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 102-TRP-TRP-103.
RX PubMed=16439675; DOI=10.1182/blood-2005-10-4102;
RA Sasanuma H., Tatsuno A., Hidano S., Ohshima K., Matsuzaki Y., Hayashi K.,
RA Lowell C.A., Kitamura D., Goitsuka R.;
RT "Dual function for the adaptor MIST in IFN-gamma production by NK and
RT CD4+NKT cells regulated by the Src kinase Fgr.";
RL Blood 107:3647-3655(2006).
RN [13]
RP INTERACTION WITH FLT3.
RX PubMed=16684964; DOI=10.1182/blood-2005-07-008896;
RA Heiss E., Masson K., Sundberg C., Pedersen M., Sun J., Bengtsson S.,
RA Ronnstrand L.;
RT "Identification of Y589 and Y599 in the juxtamembrane domain of Flt3 as
RT ligand-induced autophosphorylation sites involved in binding of Src family
RT kinases and the protein tyrosine phosphatase SHP2.";
RL Blood 108:1542-1550(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND TYR-400, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-196 AND SER-206, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [16]
RP FUNCTION IN REGULATION OF CELL MIGRATION, AND INTERACTION WITH ABL1; ITGB1
RP AND ITGB2.
RX PubMed=19903482; DOI=10.1016/j.febslet.2009.11.009;
RA Baruzzi A., Iacobucci I., Soverini S., Lowell C.A., Martinelli G.,
RA Berton G.;
RT "c-Abl and Src-family kinases cross-talk in regulation of myeloid cell
RT migration.";
RL FEBS Lett. 584:15-21(2010).
RN [17]
RP FUNCTION IN PHOSPHORYLATION OF SYK; MAST CELL DEGRANULATION AND RELEASE OF
RP CYTOKINES, AND INTERACTION WITH FCER1G.
RX PubMed=21746961; DOI=10.4049/jimmunol.1100296;
RA Lee J.H., Kim J.W., Kim do K., Kim H.S., Park H.J., Park D.K., Kim A.R.,
RA Kim B., Beaven M.A., Park K.L., Kim Y.M., Choi W.S.;
RT "The Src family kinase Fgr is critical for activation of mast cells and
RT IgE-mediated anaphylaxis in mice.";
RL J. Immunol. 187:1807-1815(2011).
CC -!- FUNCTION: Non-receptor tyrosine-protein kinase that transmits signals
CC from cell surface receptors devoid of kinase activity and contributes
CC to the regulation of immune responses, including neutrophil, monocyte,
CC macrophage and mast cell functions, cytoskeleton remodeling in response
CC to extracellular stimuli, phagocytosis, cell adhesion and migration.
CC Promotes mast cell degranulation, release of inflammatory cytokines and
CC IgE-mediated anaphylaxis. Acts downstream of receptors that bind the Fc
CC region of immunoglobulins, such as MS4A2/FCER1B, FCER1G and FCGR2. Acts
CC downstream of ITGB1 and ITGB2, and regulates actin cytoskeleton
CC reorganization, cell spreading and adhesion. Depending on the context,
CC activates or inhibits cellular responses. Functions as negative
CC regulator of ITGB2 signaling, phagocytosis and SYK activity in
CC monocytes (PubMed:11672534). Required for normal ITGB1 and ITGB2
CC signaling, normal cell spreading and adhesion in neutrophils and
CC macrophages (PubMed:8666673 and PubMed:9687507). Functions as positive
CC regulator of cell migration and regulates cytoskeleton reorganization
CC via RAC1 activation (PubMed:15561106). Phosphorylates SYK (in vitro)
CC and promotes SYK-dependent activation of AKT1 and MAP kinase signaling
CC (PubMed:21746961). Phosphorylates PLD2 in antigen-stimulated mast
CC cells, leading to PLD2 activation and the production of the signaling
CC molecules lysophosphatidic acid and diacylglycerol. Promotes activation
CC of PIK3R1. Phosphorylates FASLG, and thereby regulates its
CC ubiquitination and subsequent internalization. Phosphorylates ABL1.
CC Promotes phosphorylation of CBL, CTTN, PIK3R1, PTK2/FAK1, PTK2B/PYK2
CC and VAV2. Phosphorylates HCLS1 that has already been phosphorylated by
CC SYK, but not unphosphorylated HCLS1. Together with CLNK, it acts as a
CC negative regulator of natural killer cell-activating receptors and
CC inhibits interferon-gamma production (PubMed:16439675).
CC {ECO:0000269|PubMed:10662797, ECO:0000269|PubMed:11672534,
CC ECO:0000269|PubMed:15561106, ECO:0000269|PubMed:16439675,
CC ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:21746961,
CC ECO:0000269|PubMed:8125254, ECO:0000269|PubMed:8666673,
CC ECO:0000269|PubMed:9687507}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028,
CC ECO:0000269|PubMed:15561106};
CC -!- ACTIVITY REGULATION: Activated by autophosphorylation. Prior
CC phosphorylation at Tyr-511 by SRC inhibits ulterior autophosphorylation
CC at Tyr-400. Activated by phorbol myristate acetate, phosphatidic acid
CC and poly-Lys. Binding (via SH2 domain) of HCLS1 that is already
CC phosphorylated by SYK strongly increases kinase activity.
CC -!- SUBUNIT: Interacts with ITGB1, ITGB2, MS4A2/FCER1B, FCER1G and FCGR2.
CC Interacts (via SH2 domain) with SYK (tyrosine phosphorylated).
CC Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated).
CC Interacts with PTK2/FAK1. Interacts (via SH2 domain) with HCLS1
CC (tyrosine phosphorylated by SYK). Interacts with SIRPA and PTPNS1.
CC Interacts (not phosphorylated on tyrosine residues) with CBL; FGR
CC tyrosine phosphorylation promotes dissociation (By similarity).
CC Interacts with CLNK (PubMed:16439675). {ECO:0000250,
CC ECO:0000269|PubMed:16439675}.
CC -!- INTERACTION:
CC P14234; Q9QZE2: Clnk; NbExp=3; IntAct=EBI-7587024, EBI-8040679;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15561106};
CC Lipid-anchor {ECO:0000305|PubMed:15561106}; Cytoplasmic side
CC {ECO:0000305|PubMed:15561106}. Cell membrane
CC {ECO:0000269|PubMed:15561106}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15561106}; Cytoplasmic side
CC {ECO:0000269|PubMed:15561106}. Cell projection, ruffle membrane
CC {ECO:0000269|PubMed:15561106}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:15561106}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:15561106}. Mitochondrion inner membrane
CC {ECO:0000250}. Mitochondrion intermembrane space {ECO:0000250}.
CC Note=Detected in mitochondrial intermembrane space and at inner
CC membranes (By similarity). Colocalizes with actin fibers at membrane
CC ruffles. Detected at plasma membrane lipid rafts. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in natural killer cells (at protein
CC level). {ECO:0000269|PubMed:16439675}.
CC -!- PTM: Ubiquitinated. Becomes ubiquitinated in response to ITGB2
CC signaling; this does not lead to degradation (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated. Autophosphorylated on tyrosine residues. Becomes
CC phosphorylated in response to FCGR2 engagement, cell adhesion and
CC signaling by ITGB2. Prior phosphorylation at Tyr-511 by SRC inhibits
CC ulterior autophosphorylation at Tyr-400 (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice lacking both Fgr and
CC Hck are normal and fertile, but show increased susceptibility to
CC infection with Listeria monocytogenes. In addition, their
CC polymorphonuclear leukocytes show defects in cell spreading and
CC adhesion. {ECO:0000269|PubMed:8125254, ECO:0000269|PubMed:8666673}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; X16440; CAA34463.1; -; mRNA.
DR EMBL; X52191; CAA36437.1; -; mRNA.
DR EMBL; AK036438; BAC29429.1; -; mRNA.
DR EMBL; AK036476; BAC29445.1; -; mRNA.
DR EMBL; AK038141; BAC29939.1; -; mRNA.
DR EMBL; AK155902; BAE33493.1; -; mRNA.
DR EMBL; AL627184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466552; EDL30081.1; -; Genomic_DNA.
DR EMBL; CH466552; EDL30082.1; -; Genomic_DNA.
DR CCDS; CCDS18739.1; -.
DR PIR; A43807; A43807.
DR RefSeq; NP_034338.3; NM_010208.4.
DR RefSeq; XP_006538607.1; XM_006538544.3.
DR RefSeq; XP_006538608.1; XM_006538545.3.
DR AlphaFoldDB; P14234; -.
DR SMR; P14234; -.
DR BioGRID; 199663; 2.
DR CORUM; P14234; -.
DR IntAct; P14234; 3.
DR MINT; P14234; -.
DR STRING; 10090.ENSMUSP00000030693; -.
DR BindingDB; P14234; -.
DR ChEMBL; CHEMBL2034795; -.
DR iPTMnet; P14234; -.
DR PhosphoSitePlus; P14234; -.
DR SwissPalm; P14234; -.
DR jPOST; P14234; -.
DR MaxQB; P14234; -.
DR PaxDb; P14234; -.
DR PeptideAtlas; P14234; -.
DR PRIDE; P14234; -.
DR ProteomicsDB; 271590; -.
DR Antibodypedia; 711; 575 antibodies from 39 providers.
DR DNASU; 14191; -.
DR Ensembl; ENSMUST00000030693; ENSMUSP00000030693; ENSMUSG00000028874.
DR Ensembl; ENSMUST00000171223; ENSMUSP00000128411; ENSMUSG00000028874.
DR GeneID; 14191; -.
DR KEGG; mmu:14191; -.
DR UCSC; uc012dmj.1; mouse.
DR CTD; 2268; -.
DR MGI; MGI:95527; Fgr.
DR VEuPathDB; HostDB:ENSMUSG00000028874; -.
DR eggNOG; KOG0197; Eukaryota.
DR GeneTree; ENSGT00940000157554; -.
DR HOGENOM; CLU_000288_7_2_1; -.
DR InParanoid; P14234; -.
DR OMA; AQIPNYN; -.
DR OrthoDB; 539311at2759; -.
DR PhylomeDB; P14234; -.
DR TreeFam; TF351634; -.
DR BRENDA; 2.7.10.2; 3474.
DR Reactome; R-MMU-2029481; FCGR activation.
DR Reactome; R-MMU-432142; Platelet sensitization by LDL.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 14191; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Fgr; mouse.
DR PRO; PR:P14234; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P14234; protein.
DR Bgee; ENSMUSG00000028874; Expressed in granulocyte and 68 other tissues.
DR Genevisible; P14234; MM.
DR GO; GO:0016235; C:aggresome; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034988; F:Fc-gamma receptor I complex binding; ISO:MGI.
DR GO; GO:0034987; F:immunoglobulin receptor binding; IDA:UniProtKB.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0030282; P:bone mineralization; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0032815; P:negative regulation of natural killer cell activation; IMP:UniProtKB.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; IDA:UniProtKB.
DR GO; GO:0043306; P:positive regulation of mast cell degranulation; IDA:UniProtKB.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISO:MGI.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; TAS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR GO; GO:0045088; P:regulation of innate immune response; IMP:UniProtKB.
DR GO; GO:0050764; P:regulation of phagocytosis; IMP:UniProtKB.
DR GO; GO:0045859; P:regulation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd10367; SH2_Src_Fgr; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR035693; Fgr_SH2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW Immunity; Innate immunity; Kinase; Lipoprotein; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Myristate; Nucleotide-binding; Palmitate;
KW Phosphoprotein; Proto-oncogene; Reference proteome; SH2 domain; SH3 domain;
KW Transferase; Tyrosine-protein kinase; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..517
FT /note="Tyrosine-protein kinase Fgr"
FT /id="PRO_0000088092"
FT DOMAIN 65..126
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 132..229
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 251..504
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 102..103
FT /note="Interaction with CLNK"
FT /evidence="ECO:0000269|PubMed:16439675"
FT ACT_SITE 370
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 257..265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 279
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 32
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09769"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P6U0"
FT MOD_RES 196
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 400
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 511
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P09769"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000305|PubMed:15561106"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:15561106"
FT LIPID 6
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:15561106"
FT MUTAGEN 1..7
FT /note="Missing: Abolishes localization at the cell
FT membrane."
FT /evidence="ECO:0000269|PubMed:15561106"
FT MUTAGEN 102..103
FT /note="WW->AA: Loss of CLNK binding."
FT /evidence="ECO:0000269|PubMed:16439675"
FT MUTAGEN 279
FT /note="K->R: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:10662797"
FT CONFLICT 33
FT /note="F -> Y (in Ref. 1; CAA34463 and 2; CAA36437)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="T -> N (in Ref. 1; CAA34463)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="R -> Q (in Ref. 1; CAA34463)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 517 AA; 58867 MW; 87DF5B19BF3F4734 CRC64;
MGCVFCKKLE PASKEDVGLE GDFRSQTAEE RYFPDPTQGR TSSVFPQPTS PAFLNTGNMR
SISGTGVTIF VALYDYEART GDDLTFTKGE KFHILNNTEY DWWEARSLSS GHRGYVPSNY
VAPVDSIQAE EWYFGKISRK DAERQLLSSG NPQGAFLIRE SETTKGAYSL SIRDWDQNRG
DHIKHYKIRK LDTGGYYITT RAQFDSIQDL VRHYMEVNDG LCYLLTAPCT TTKPQTLGLA
KDAWEIDRNS IALERRLGTG CFGDVWLGTW NCSTKVAVKT LKPGTMSPKA FLEEAQIMKL
LRHDKLVQLY AVVSEEPIYI VTEFMCYGSL LDFLKDREGQ NLMLPHLVDM AAQVAEGMAY
MERMNYIHRD LRAANILVGE YLICKIADFG LARLIEDNEY NPQQGTKFPI KWTAPEAALF
GRFTVKSDVW SFGILLTELI TKGRVPYPGM NNREVLEQVE HGYHMPCPPG CPASLYEVME
QAWRLDPEER PTFEYLQSFL EDYFTSTEPQ YQPGDQT
