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Tyrosine-protein kinase Fgr (EC 2.7.10.2) (Gardner-Rasheed feline sarcoma viral (v-fgr) oncogene homolog) (Proto-oncogene c-Fgr) (p55-Fgr) (p58-Fgr) (p58c-Fgr)

 FGR_HUMAN               Reviewed;         529 AA.
P09769; D3DPL7; Q9UIQ3;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 2.
27-SEP-2017, entry version 194.
RecName: Full=Tyrosine-protein kinase Fgr;
EC=2.7.10.2;
AltName: Full=Gardner-Rasheed feline sarcoma viral (v-fgr) oncogene homolog;
AltName: Full=Proto-oncogene c-Fgr;
AltName: Full=p55-Fgr;
AltName: Full=p58-Fgr;
AltName: Full=p58c-Fgr;
Name=FGR; Synonyms=SRC2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3275868; DOI=10.1128/MCB.8.1.259;
Katamine S., Notario V., Rao C.D., Miki T., Cheah M.S.C.,
Tronick S.R., Robbins K.C.;
"Primary structure of the human fgr proto-oncogene product p55c-fgr.";
Mol. Cell. Biol. 8:259-266(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-177 AND 524-529.
PubMed=2852026; DOI=10.1038/bjc.1988.294;
Brickell P.M., Patel M.;
"Structure and expression of c-fgr protooncogene mRNA in Epstein-Barr
virus converted cell lines.";
Br. J. Cancer 58:704-709(1988).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-143.
PubMed=3330776;
Inoue K., Ikawa S., Semba K., Sukegawa J., Yamamoto T., Toyoshima K.;
"Isolation and sequencing of cDNA clones homologous to the v-fgr
oncogene from a human B lymphocyte cell line, IM-9.";
Oncogene 1:301-304(1987).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-142.
PubMed=1690869;
Patel M., Leevers S.J., Brickell P.M.;
"Structure of the complete human c-fgr proto-oncogene and
identification of multiple transcriptional start sites.";
Oncogene 5:201-206(1990).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 111-416.
PubMed=3023853; DOI=10.1128/MCB.6.2.511;
Nishizawa M., Semba K., Yoshida M.C., Yamamoto T., Sasaki M.,
Toyoshima K.;
"Structure, expression, and chromosomal location of the human c-fgr
gene.";
Mol. Cell. Biol. 6:511-517(1986).
[9]
CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, AND TISSUE SPECIFICITY.
PubMed=2181286; DOI=10.1128/MCB.10.4.1789;
Inoue K., Yamamoto T., Toyoshima K.;
"Specific expression of human c-fgr in natural immunity effector
cells.";
Mol. Cell. Biol. 10:1789-1792(1990).
[10]
FUNCTION AS PROTO-ONCOGENE, ROLE IN DISEASE, CATALYTIC ACTIVITY, AND
MUTAGENESIS OF TYR-523.
PubMed=1737799;
Sartor O., Moriuchi R., Sameshima J.H., Severino M., Gutkind J.S.,
Robbins K.C.;
"Diverse biologic properties imparted by the c-fgr proto-oncogene.";
J. Biol. Chem. 267:3460-3465(1992).
[11]
INTERACTION WITH FCGR2A AND/OR FCGR2B, CATALYTIC ACTIVITY, ENZYME
REGULATION, AUTOPHOSPHORYLATION, AND TISSUE SPECIFICITY.
PubMed=8327512; DOI=10.1073/pnas.90.13.6305;
Hamada F., Aoki M., Akiyama T., Toyoshima K.;
"Association of immunoglobulin G Fc receptor II with Src-like protein-
tyrosine kinase Fgr in neutrophils.";
Proc. Natl. Acad. Sci. U.S.A. 90:6305-6309(1993).
[12]
PHOSPHORYLATION, AND FUNCTION IN INTEGRIN SIGNALING.
PubMed=7519620; DOI=10.1083/jcb.126.4.1111;
Berton G., Fumagalli L., Laudanna C., Sorio C.;
"Beta 2 integrin-dependent protein tyrosine phosphorylation and
activation of the FGR protein tyrosine kinase in human neutrophils.";
J. Cell Biol. 126:1111-1121(1994).
[13]
SUBCELLULAR LOCATION AT THE CYTOSKELETON, AND ENZYME REGULATION.
PubMed=8603737; DOI=10.1016/0014-5793(96)00029-4;
Yan S.R., Fumagalli L., Berton G.;
"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.";
FEBS Lett. 380:198-203(1996).
[14]
FUNCTION IN ACTIVATION OF PIK3R1, PHOSPHORYLATION, AND INTERACTION
WITH ITGB2 AND PIK3R1.
PubMed=10739672; DOI=10.1006/excr.2000.4816;
Axelsson L., Hellberg C., Melander F., Smith D., Zheng L.,
Andersson T.;
"Clustering of beta(2)-integrins on human neutrophils activates dual
signaling pathways to PtdIns 3-kinase.";
Exp. Cell Res. 256:257-263(2000).
[15]
ENZYME REGULATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=11078731; DOI=10.1074/jbc.M006571200;
Sergeant S., Waite K.A., Heravi J., McPhail L.C.;
"Phosphatidic acid regulates tyrosine phosphorylating activity in
human neutrophils: enhancement of Fgr activity.";
J. Biol. Chem. 276:4737-4746(2001).
[16]
UBIQUITINATION, AND INTERACTION WITH CBL.
PubMed=12435267; DOI=10.1042/BJ20021201;
Melander F., Andersson T., Dib K.;
"Fgr but not Syk tyrosine kinase is a target for beta 2 integrin-
induced c-Cbl-mediated ubiquitination in adherent human neutrophils.";
Biochem. J. 370:687-694(2003).
[17]
FUNCTION IN PHOSPHORYLATION OF FASLG, AND INTERACTION WITH FASLG.
PubMed=17164290; DOI=10.1242/jcs.03315;
Zuccato E., Blott E.J., Holt O., Sigismund S., Shaw M., Bossi G.,
Griffiths G.M.;
"Sorting of Fas ligand to secretory lysosomes is regulated by mono-
ubiquitylation and phosphorylation.";
J. Cell Sci. 120:191-199(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-34; TYR-412 AND TYR-523,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[19]
VARIANTS [LARGE SCALE ANALYSIS] ILE-110 AND ARG-130.
PubMed=17344846; DOI=10.1038/nature05610;
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- 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, 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.
{ECO:0000269|PubMed:10739672, ECO:0000269|PubMed:17164290,
ECO:0000269|PubMed:1737799, ECO:0000269|PubMed:7519620}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:1737799,
ECO:0000269|PubMed:2181286, ECO:0000269|PubMed:8327512}.
-!- ENZYME REGULATION: 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. {ECO:0000269|PubMed:11078731,
ECO:0000269|PubMed:8327512, ECO:0000269|PubMed:8603737}.
-!- SUBUNIT: 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).
{ECO:0000250}.
-!- INTERACTION:
P09917:ALOX5; NbExp=2; IntAct=EBI-1383732, EBI-79934;
P10275:AR; NbExp=3; IntAct=EBI-1383732, EBI-608057;
P00533:EGFR; NbExp=2; IntAct=EBI-1383732, EBI-297353;
P04626:ERBB2; NbExp=3; IntAct=EBI-1383732, EBI-641062;
P08238:HSP90AB1; NbExp=2; IntAct=EBI-1383732, EBI-352572;
P10721:KIT; NbExp=2; IntAct=EBI-1383732, EBI-1379503;
P08581:MET; NbExp=2; IntAct=EBI-1383732, EBI-1039152;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
{ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane;
Peripheral membrane protein; Cytoplasmic side. Cell projection,
ruffle membrane. Cytoplasm, cytosol. Cytoplasm, cytoskeleton.
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}.
-!- TISSUE SPECIFICITY: Detected in neutrophils, monocytes and natural
killer cells (at protein level). Detected in monocytes and large
lymphocytes. {ECO:0000269|PubMed:11078731,
ECO:0000269|PubMed:2181286, ECO:0000269|PubMed:8327512}.
-!- PTM: Ubiquitinated. Becomes ubiquitinated in response to ITGB2
signaling; this does not lead to degradation.
{ECO:0000269|PubMed:12435267}.
-!- PTM: 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. {ECO:0000269|PubMed:10739672,
ECO:0000269|PubMed:7519620}.
-!- DISEASE: Note=Mutations that cause aberrant kinase activation can
confer oncogene activity and promote aberrant cell proliferation.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. SRC subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; M19722; AAA52451.1; -; mRNA.
EMBL; AL031729; CAB62998.1; -; Genomic_DNA.
EMBL; CH471059; EAX07748.1; -; Genomic_DNA.
EMBL; CH471059; EAX07749.1; -; Genomic_DNA.
EMBL; CH471059; EAX07750.1; -; Genomic_DNA.
EMBL; BC064382; AAH64382.1; -; mRNA.
EMBL; X52207; CAA36457.2; -; Genomic_DNA.
EMBL; X52208; CAA36457.2; JOINED; Genomic_DNA.
EMBL; M12724; AAA52762.1; -; Genomic_DNA.
EMBL; M12719; AAA52762.1; JOINED; Genomic_DNA.
EMBL; M12720; AAA52762.1; JOINED; Genomic_DNA.
EMBL; M12721; AAA52762.1; JOINED; Genomic_DNA.
EMBL; M12722; AAA52762.1; JOINED; Genomic_DNA.
EMBL; M12723; AAA52762.1; JOINED; Genomic_DNA.
CCDS; CCDS305.1; -.
PIR; A27676; TVHUFR.
RefSeq; NP_001036194.1; NM_001042729.1.
RefSeq; NP_001036212.1; NM_001042747.1.
RefSeq; NP_005239.1; NM_005248.2.
RefSeq; XP_006710515.1; XM_006710452.2.
RefSeq; XP_011539312.1; XM_011541010.1.
UniGene; Hs.1422; -.
ProteinModelPortal; P09769; -.
SMR; P09769; -.
BioGrid; 108559; 24.
DIP; DIP-1049N; -.
ELM; P09769; -.
IntAct; P09769; 14.
MINT; MINT-1209880; -.
STRING; 9606.ENSP00000363115; -.
BindingDB; P09769; -.
ChEMBL; CHEMBL4454; -.
GuidetoPHARMACOLOGY; 2024; -.
iPTMnet; P09769; -.
PhosphoSitePlus; P09769; -.
SwissPalm; P09769; -.
BioMuta; FGR; -.
DMDM; 125358; -.
MaxQB; P09769; -.
PaxDb; P09769; -.
PeptideAtlas; P09769; -.
PRIDE; P09769; -.
DNASU; 2268; -.
Ensembl; ENST00000374003; ENSP00000363115; ENSG00000000938.
Ensembl; ENST00000374004; ENSP00000363116; ENSG00000000938.
Ensembl; ENST00000374005; ENSP00000363117; ENSG00000000938.
Ensembl; ENST00000399173; ENSP00000382126; ENSG00000000938.
GeneID; 2268; -.
KEGG; hsa:2268; -.
UCSC; uc001boj.4; human.
CTD; 2268; -.
DisGeNET; 2268; -.
EuPathDB; HostDB:ENSG00000000938.12; -.
GeneCards; FGR; -.
HGNC; HGNC:3697; FGR.
HPA; HPA002024; -.
MIM; 164940; gene.
neXtProt; NX_P09769; -.
OpenTargets; ENSG00000000938; -.
PharmGKB; PA28135; -.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118938; -.
HOGENOM; HOG000233858; -.
HOVERGEN; HBG008761; -.
InParanoid; P09769; -.
KO; K08891; -.
OMA; IRDWDQT; -.
OrthoDB; EOG091G0D46; -.
PhylomeDB; P09769; -.
TreeFam; TF351634; -.
Reactome; R-HSA-2029481; FCGR activation.
Reactome; R-HSA-432142; Platelet sensitization by LDL.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SignaLink; P09769; -.
SIGNOR; P09769; -.
ChiTaRS; FGR; human.
GeneWiki; FGR_(gene); -.
GenomeRNAi; 2268; -.
PRO; PR:P09769; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000000938; -.
CleanEx; HS_FGR; -.
ExpressionAtlas; P09769; baseline and differential.
Genevisible; P09769; HS.
GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
GO; GO:0016235; C:aggresome; IDA:HPA.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
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:HPA.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0034988; F:Fc-gamma receptor I complex binding; IDA:UniProtKB.
GO; GO:0034987; F:immunoglobulin receptor binding; ISS:UniProtKB.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0002768; P:immune response-regulating cell surface receptor signaling pathway; TAS:UniProtKB.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
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; ISS:UniProtKB.
GO; GO:0050715; P:positive regulation of cytokine secretion; ISS:UniProtKB.
GO; GO:0043306; P:positive regulation of mast cell degranulation; ISS:UniProtKB.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
GO; GO:0045088; P:regulation of innate immune response; ISS:UniProtKB.
GO; GO:0050764; P:regulation of phagocytosis; ISS:UniProtKB.
GO; GO:0045859; P:regulation of protein kinase activity; ISS:UniProtKB.
GO; GO:0009615; P:response to virus; TAS:ProtInc.
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.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
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;
Polymorphism; Proto-oncogene; Reference proteome; SH2 domain;
SH3 domain; Transferase; Tyrosine-protein kinase; Ubl conjugation.
INIT_MET 1 1 Removed.
CHAIN 2 529 Tyrosine-protein kinase Fgr.
/FTId=PRO_0000088091.
DOMAIN 77 138 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 144 241 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 263 516 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 269 277 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 382 382 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 291 291 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 34 34 Phosphotyrosine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 208 208 Phosphotyrosine.
{ECO:0000250|UniProtKB:P14234}.
MOD_RES 218 218 Phosphoserine.
{ECO:0000250|UniProtKB:P14234}.
MOD_RES 412 412 Phosphotyrosine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 523 523 Phosphotyrosine; by SRC.
{ECO:0000244|PubMed:19369195}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000250}.
LIPID 3 3 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 6 6 S-palmitoyl cysteine. {ECO:0000250}.
VARIANT 110 110 T -> I (in dbSNP:rs34597831).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041700.
VARIANT 130 130 S -> R (in dbSNP:rs35334091).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041701.
MUTAGEN 523 523 Y->F: Strongly increased catalytic
activity. Functions as oncogene.
{ECO:0000269|PubMed:1737799}.
SEQUENCE 529 AA; 59479 MW; 6B8C1E08414E0F9C CRC64;
MGCVFCKKLE PVATAKEDAG LEGDFRSYGA ADHYGPDPTK ARPASSFAHI PNYSNFSSQA
INPGFLDSGT IRGVSGIGVT LFIALYDYEA RTEDDLTFTK GEKFHILNNT EGDWWEARSL
SSGKTGCIPS NYVAPVDSIQ AEEWYFGKIG RKDAERQLLS PGNPQGAFLI RESETTKGAY
SLSIRDWDQT RGDHVKHYKI RKLDMGGYYI TTRVQFNSVQ ELVQHYMEVN DGLCNLLIAP
CTIMKPQTLG LAKDAWEISR SSITLERRLG TGCFGDVWLG TWNGSTKVAV KTLKPGTMSP
KAFLEEAQVM KLLRHDKLVQ LYAVVSEEPI YIVTEFMCHG SLLDFLKNPE GQDLRLPQLV
DMAAQVAEGM AYMERMNYIH RDLRAANILV GERLACKIAD FGLARLIKDD EYNPCQGSKF
PIKWTAPEAA LFGRFTIKSD VWSFGILLTE LITKGRIPYP GMNKREVLEQ VEQGYHMPCP
PGCPASLYEA MEQTWRLDPE ERPTFEYLQS FLEDYFTSAE PQYQPGDQT


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