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Tyrosine-protein kinase Fgr (EC 2.7.10.2) (Proto-oncogene c-Fgr) (p55-Fgr)

 FGR_MOUSE               Reviewed;         517 AA.
P14234; Q61404; Q8BGM0;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
12-SEP-2018, entry version 179.
RecName: Full=Tyrosine-protein kinase Fgr;
EC=2.7.10.2;
AltName: Full=Proto-oncogene c-Fgr;
AltName: Full=p55-Fgr;
Name=Fgr;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=DBA/2J;
PubMed=2674853;
Yi T.L., Willman C.L.;
"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.";
Oncogene 4:1081-1087(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Monocytic leukemia;
PubMed=2179817;
King F.J., Cole M.D.;
"Molecular cloning and sequencing of the murine c-fgr gene.";
Oncogene 5:337-344(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
DISRUPTION PHENOTYPE, AND FUNCTION IN IMMUNITY TO LISTERIA INFECTION.
PubMed=8125254; DOI=10.1101/gad.8.4.387;
Lowell C.A., Soriano P., Varmus H.E.;
"Functional overlap in the src gene family: inactivation of hck and
fgr impairs natural immunity.";
Genes Dev. 8:387-398(1994).
[7]
DISRUPTION PHENOTYPE, AND FUNCTION IN CELL ADHESION AND INTEGRIN
SIGNALING.
PubMed=8666673; DOI=10.1083/jcb.133.4.895;
Lowell C.A., Fumagalli L., Berton G.;
"Deficiency of Src family kinases p59/61hck and p58c-fgr results in
defective adhesion-dependent neutrophil functions.";
J. Cell Biol. 133:895-910(1996).
[8]
FUNCTION IN ITGB1 SIGNALING, FUNCTION IN PHOSPHORYLATION OF CBL, AND
INTERACTION WITH CBL.
PubMed=9687507; DOI=10.1093/emboj/17.15.4391;
Meng F., Lowell C.A.;
"A beta 1 integrin signaling pathway involving Src-family kinases, Cbl
and PI-3 kinase is required for macrophage spreading and migration.";
EMBO J. 17:4391-4403(1998).
[9]
INTERACTION WITH SIRPA AND PTPNS1, MUTAGENESIS OF LYS-279, AND
FUNCTION AS NEGATIVE REGULATOR OF PHAGOCYTOSIS.
PubMed=10662797; DOI=10.1084/jem.191.3.515;
Gresham H.D., Dale B.M., Potter J.W., Chang P.W., Vines C.M.,
Lowell C.A., Lagenaur C.F., Willman C.L.;
"Negative regulation of phagocytosis in murine macrophages by the Src
kinase family member, Fgr.";
J. Exp. Med. 191:515-528(2000).
[10]
FUNCTION AS NEGATIVE REGULATOR OF SYK AND INTEGRIN SIGNALING, AND
INTERACTION WITH SYK.
PubMed=11672534; DOI=10.1016/S1074-7613(01)00221-7;
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.;
"Inhibition of beta 2 integrin receptor and Syk kinase signaling in
monocytes by the Src family kinase Fgr.";
Immunity 15:507-519(2001).
[11]
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 AT
GLY-2, PALMITOYLATION AT CYS-3 AND CYS-6, MUTAGENESIS OF 1-MET--LYS-7,
AND SUBCELLULAR LOCATION.
PubMed=15561106; DOI=10.1016/j.yexcr.2004.09.005;
Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L.,
Lowell C.A., Berton G.;
"The proto-oncogene Fgr regulates cell migration and this requires its
plasma membrane localization.";
Exp. Cell Res. 302:253-269(2005).
[12]
INTERACTION WITH FLT3.
PubMed=16684964; DOI=10.1182/blood-2005-07-008896;
Heiss E., Masson K., Sundberg C., Pedersen M., Sun J., Bengtsson S.,
Ronnstrand L.;
"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.";
Blood 108:1542-1550(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND TYR-400, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-196 AND SER-206, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[15]
FUNCTION IN REGULATION OF CELL MIGRATION, AND INTERACTION WITH ABL1;
ITGB1 AND ITGB2.
PubMed=19903482; DOI=10.1016/j.febslet.2009.11.009;
Baruzzi A., Iacobucci I., Soverini S., Lowell C.A., Martinelli G.,
Berton G.;
"c-Abl and Src-family kinases cross-talk in regulation of myeloid cell
migration.";
FEBS Lett. 584:15-21(2010).
[16]
FUNCTION IN PHOSPHORYLATION OF SYK; MAST CELL DEGRANULATION AND
RELEASE OF CYTOKINES, AND INTERACTION WITH FCER1G.
PubMed=21746961; DOI=10.4049/jimmunol.1100296;
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.;
"The Src family kinase Fgr is critical for activation of mast cells
and IgE-mediated anaphylaxis in mice.";
J. Immunol. 187:1807-1815(2011).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:10662797, ECO:0000269|PubMed:11672534,
ECO:0000269|PubMed:15561106, ECO:0000269|PubMed:19903482,
ECO:0000269|PubMed:21746961, ECO:0000269|PubMed:8125254,
ECO:0000269|PubMed:8666673, ECO:0000269|PubMed:9687507}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:15561106}.
-!- ACTIVITY REGULATION: 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.
-!- SUBUNIT: 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). {ECO:0000250}.
-!- INTERACTION:
Q9QZE2:Clnk; NbExp=3; IntAct=EBI-7587024, EBI-8040679;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15561106};
Lipid-anchor {ECO:0000305|PubMed:15561106}; Cytoplasmic side
{ECO:0000305|PubMed:15561106}. Cell membrane
{ECO:0000269|PubMed:15561106}; Peripheral membrane protein
{ECO:0000269|PubMed:15561106}; Cytoplasmic side
{ECO:0000269|PubMed:15561106}. Cell projection, ruffle membrane
{ECO:0000269|PubMed:15561106}. Cytoplasm, cytosol
{ECO:0000269|PubMed:15561106}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:15561106}. Mitochondrion inner membrane
{ECO:0000250}. Mitochondrion intermembrane space {ECO:0000250}.
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.
{ECO:0000250}.
-!- PTM: Ubiquitinated. Becomes ubiquitinated in response to ITGB2
signaling; this does not lead to degradation (By similarity).
{ECO:0000250}.
-!- PTM: 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). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: 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. {ECO:0000269|PubMed:8125254,
ECO:0000269|PubMed:8666673}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. SRC subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; X16440; CAA34463.1; -; mRNA.
EMBL; X52191; CAA36437.1; -; mRNA.
EMBL; AK036438; BAC29429.1; -; mRNA.
EMBL; AK036476; BAC29445.1; -; mRNA.
EMBL; AK038141; BAC29939.1; -; mRNA.
EMBL; AK155902; BAE33493.1; -; mRNA.
EMBL; AL627184; CAM14378.1; -; Genomic_DNA.
EMBL; CH466552; EDL30081.1; -; Genomic_DNA.
EMBL; CH466552; EDL30082.1; -; Genomic_DNA.
CCDS; CCDS18739.1; -.
PIR; A43807; A43807.
RefSeq; NP_034338.3; NM_010208.4.
RefSeq; XP_006538607.1; XM_006538544.3.
RefSeq; XP_006538608.1; XM_006538545.3.
UniGene; Mm.271665; -.
ProteinModelPortal; P14234; -.
SMR; P14234; -.
BioGrid; 199663; 2.
CORUM; P14234; -.
IntAct; P14234; 3.
MINT; P14234; -.
STRING; 10090.ENSMUSP00000030693; -.
BindingDB; P14234; -.
ChEMBL; CHEMBL2034795; -.
iPTMnet; P14234; -.
PhosphoSitePlus; P14234; -.
SwissPalm; P14234; -.
MaxQB; P14234; -.
PaxDb; P14234; -.
PeptideAtlas; P14234; -.
PRIDE; P14234; -.
Ensembl; ENSMUST00000030693; ENSMUSP00000030693; ENSMUSG00000028874.
Ensembl; ENSMUST00000171223; ENSMUSP00000128411; ENSMUSG00000028874.
GeneID; 14191; -.
KEGG; mmu:14191; -.
UCSC; uc012dmj.1; mouse.
CTD; 2268; -.
MGI; MGI:95527; Fgr.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118938; -.
HOGENOM; HOG000233858; -.
HOVERGEN; HBG008761; -.
InParanoid; P14234; -.
KO; K08891; -.
OMA; QTWRLDP; -.
OrthoDB; EOG091G0D46; -.
TreeFam; TF351634; -.
BRENDA; 2.7.10.2; 3474.
Reactome; R-MMU-2029481; FCGR activation.
Reactome; R-MMU-432142; Platelet sensitization by LDL.
Reactome; R-MMU-6798695; Neutrophil degranulation.
PRO; PR:P14234; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028874; Expressed in 73 organ(s), highest expression level in blood.
Genevisible; P14234; MM.
GO; GO:0016235; C:aggresome; ISO:MGI.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0034988; F:Fc-gamma receptor I complex binding; ISO:MGI.
GO; GO:0034987; F:immunoglobulin receptor binding; IDA:UniProtKB.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0001784; F:phosphotyrosine residue binding; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; ISO:MGI.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
GO; GO:0050715; P:positive regulation of cytokine secretion; IDA:UniProtKB.
GO; GO:0043306; P:positive regulation of mast cell degranulation; IDA:UniProtKB.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISO:MGI.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; TAS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
GO; GO:0045088; P:regulation of innate immune response; IMP:UniProtKB.
GO; GO:0050764; P:regulation of phagocytosis; IMP:UniProtKB.
GO; GO:0045859; P:regulation of protein kinase activity; IDA:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
CDD; cd10367; SH2_Src_Fgr; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR035693; Fgr_SH2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00452; SH3DOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Cell projection; Complete proteome;
Cytoplasm; Cytoskeleton; Immunity; Innate immunity; Kinase;
Lipoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane;
Myristate; Nucleotide-binding; Palmitate; Phosphoprotein;
Proto-oncogene; Reference proteome; SH2 domain; SH3 domain;
Transferase; Tyrosine-protein kinase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000305}.
CHAIN 2 517 Tyrosine-protein kinase Fgr.
/FTId=PRO_0000088092.
DOMAIN 65 126 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 132 229 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 251 504 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 257 265 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 370 370 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 279 279 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 32 32 Phosphotyrosine.
{ECO:0000250|UniProtKB:P09769}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000250|UniProtKB:Q6P6U0}.
MOD_RES 196 196 Phosphotyrosine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 206 206 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 400 400 Phosphotyrosine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 511 511 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P09769}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000305|PubMed:15561106}.
LIPID 3 3 S-palmitoyl cysteine.
{ECO:0000305|PubMed:15561106}.
LIPID 6 6 S-palmitoyl cysteine.
{ECO:0000305|PubMed:15561106}.
MUTAGEN 1 7 Missing: Abolishes localization at the
cell membrane.
{ECO:0000269|PubMed:15561106}.
MUTAGEN 279 279 K->R: Loss of kinase activity.
{ECO:0000269|PubMed:10662797}.
CONFLICT 33 33 F -> Y (in Ref. 1; CAA34463 and 2;
CAA36437). {ECO:0000305}.
CONFLICT 41 41 T -> N (in Ref. 1; CAA34463).
{ECO:0000305}.
CONFLICT 212 212 R -> Q (in Ref. 1; CAA34463).
{ECO:0000305}.
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


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