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

 FGR_RAT                 Reviewed;         517 AA.
Q6P6U0; Q63206;
19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
23-MAY-2018, entry version 126.
RecName: Full=Tyrosine-protein kinase Fgr;
EC=2.7.10.2;
AltName: Full=Proto-oncogene c-Fgr;
AltName: Full=p55-Fgr;
Name=Fgr;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Fischer 344; TISSUE=Leukemia;
Yue C.C., Labash J.D., Jaye M.;
"Nucleotide and deduced amino acid sequence of rat FGR.";
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
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).
[4]
PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY, PHOSPHORYLATION AT
TYR-400 AND TYR-511, IDENTIFICATION BY MASS SPECTROMETRY, AND ENZYME
REGULATION.
PubMed=7515063;
Ruzzene M., James P., Brunati A.M., Donella-Deana A., Pinna L.A.;
"Regulation of c-Fgr protein kinase by c-Src kinase (CSK) and by
polycationic effectors.";
J. Biol. Chem. 269:15885-15891(1994).
[5]
FUNCTION IN PHOSPHORYLATION OF HCLS1.
PubMed=8611520; DOI=10.1021/bi9528614;
Ruzzene M., Brunati A.M., Marin O., Donella-Deana A., Pinna L.A.;
"SH2 domains mediate the sequential phosphorylation of HS1 protein by
p72syk and Src-related protein tyrosine kinases.";
Biochemistry 35:5327-5332(1996).
[6]
FUNCTION IN PHOSPHORYLATION OF HCLS1, AUTOPHOSPHORYLATION, AND ENZYME
REGULATION.
PubMed=9183008; DOI=10.1111/j.1432-1033.1997.t01-1-00701.x;
Ruzzene M., Brunati A.M., Donella-Deana A., Marin O., Pinna L.A.;
"Specific stimulation of c-Fgr kinase by tyrosine-phosphorylated
(poly)peptides--possible implication in the sequential mode of protein
phosphorylation.";
Eur. J. Biochem. 245:701-707(1997).
[7]
CATALYTIC ACTIVITY, FUNCTION IN PHOSPHORYLATION OF HCLS1, INTERACTION
WITH HCLS1, AND AUTOPHOSPHORYLATION.
PubMed=10066823; DOI=10.1074/jbc.274.11.7557;
Brunati A.M., Donella-Deana A., James P., Quadroni M., Contri A.,
Marin O., Pinna L.A.;
"Molecular features underlying the sequential phosphorylation of HS1
protein and its association with c-Fgr protein-tyrosine kinase.";
J. Biol. Chem. 274:7557-7564(1999).
[8]
FUNCTION IN PHOSPHORYLATION OF PLD2 AND MAST CELL ACTIVATION, AND
INTERACTION WITH PLD2.
PubMed=15282299; DOI=10.1128/MCB.24.16.6980-6992.2004;
Choi W.S., Hiragun T., Lee J.H., Kim Y.M., Kim H.P., Chahdi A.,
Her E., Han J.W., Beaven M.A.;
"Activation of RBL-2H3 mast cells is dependent on tyrosine
phosphorylation of phospholipase D2 by Fyn and Fgr.";
Mol. Cell. Biol. 24:6980-6992(2004).
[9]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=18247338; DOI=10.1002/jcb.21670;
Tibaldi E., Brunati A.M., Massimino M.L., Stringaro A., Colone M.,
Agostinelli E., Arancia G., Toninello A.;
"Src-Tyrosine kinases are major agents in mitochondrial tyrosine
phosphorylation.";
J. Cell. Biochem. 104:840-849(2008).
[10]
FUNCTION IN MAST CELL DEGRANULATION AND PHOSPHORYLATION OF SYK,
INTERACTION WITH MS4A2/FCER1B, AND SUBCELLULAR LOCATION ON PLASMA
MEMBRANE LIPID RAFTS.
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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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. 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 (By similarity).
Phosphorylates HCLS1 that has already been phosphorylated by SYK,
but not unphosphorylated HCLS1. {ECO:0000250,
ECO:0000269|PubMed:10066823, ECO:0000269|PubMed:15282299,
ECO:0000269|PubMed:21746961, ECO:0000269|PubMed:8611520,
ECO:0000269|PubMed:9183008}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:10066823,
ECO:0000269|PubMed:7515063}.
-!- ENZYME 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. {ECO:0000269|PubMed:7515063,
ECO:0000269|PubMed:9183008}.
-!- SUBUNIT: Interacts with ITGB1, ITGB2, MS4A2/FCER1B 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}.
-!- 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 {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.
Cytoplasm, cytoskeleton {ECO:0000250}. Mitochondrion inner
membrane. Mitochondrion intermembrane space. Note=Colocalizes with
actin fibers at membrane ruffles (By similarity). Detected at
plasma membrane lipid rafts. Detected in mitochondrial
intermembrane space and at inner membranes. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in brain cortex (at protein level).
{ECO:0000269|PubMed:18247338}.
-!- 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 (By similarity). Prior
phosphorylation at Tyr-511 by SRC inhibits ulterior
autophosphorylation at Tyr-400. {ECO:0000250,
ECO:0000269|PubMed:7515063}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. SRC subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; X57018; CAA40337.1; -; mRNA.
EMBL; CH473968; EDL80655.1; -; Genomic_DNA.
EMBL; CH473968; EDL80656.1; -; Genomic_DNA.
EMBL; CH473968; EDL80657.1; -; Genomic_DNA.
EMBL; BC062025; AAH62025.1; -; mRNA.
PIR; S24547; S24547.
RefSeq; NP_077059.2; NM_024145.2.
RefSeq; XP_006239141.1; XM_006239079.3.
RefSeq; XP_006239142.1; XM_006239080.3.
RefSeq; XP_006239143.1; XM_006239081.3.
RefSeq; XP_006239144.1; XM_006239082.3.
UniGene; Rn.11309; -.
ProteinModelPortal; Q6P6U0; -.
SMR; Q6P6U0; -.
BioGrid; 249398; 2.
IntAct; Q6P6U0; 1.
MINT; Q6P6U0; -.
STRING; 10116.ENSRNOP00000013779; -.
BindingDB; Q6P6U0; -.
ChEMBL; CHEMBL4362; -.
iPTMnet; Q6P6U0; -.
PhosphoSitePlus; Q6P6U0; -.
PaxDb; Q6P6U0; -.
PRIDE; Q6P6U0; -.
Ensembl; ENSRNOT00000013778; ENSRNOP00000013779; ENSRNOG00000009912.
Ensembl; ENSRNOT00000085674; ENSRNOP00000075272; ENSRNOG00000009912.
GeneID; 79113; -.
KEGG; rno:79113; -.
UCSC; RGD:621319; rat.
CTD; 2268; -.
RGD; 621319; Fgr.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118938; -.
HOGENOM; HOG000233858; -.
HOVERGEN; HBG008761; -.
InParanoid; Q6P6U0; -.
KO; K08891; -.
OMA; QTWRLDP; -.
PhylomeDB; Q6P6U0; -.
TreeFam; TF351634; -.
Reactome; R-RNO-2029481; FCGR activation.
Reactome; R-RNO-432142; Platelet sensitization by LDL.
Reactome; R-RNO-6798695; Neutrophil degranulation.
PRO; PR:Q6P6U0; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000009912; -.
Genevisible; Q6P6U0; RN.
GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
GO; GO:0016235; C:aggresome; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IDA:RGD.
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:RGD.
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; IEA:Ensembl.
GO; GO:0034987; F:immunoglobulin receptor binding; ISS:UniProtKB.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0001784; F:phosphotyrosine residue binding; ISS:UniProtKB.
GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:RGD.
GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
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:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS: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; IEA:Ensembl.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
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: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; Direct protein sequencing; Immunity;
Innate immunity; Kinase; Lipoprotein; Membrane; Mitochondrion;
Mitochondrion inner membrane; Myristate; Nucleotide-binding;
Palmitate; Phosphoprotein; Proto-oncogene; Reference proteome;
SH3 domain; Transferase; Tyrosine-protein kinase; Ubl conjugation.
INIT_MET 1 1 Removed.
CHAIN 2 517 Tyrosine-protein kinase Fgr.
/FTId=PRO_0000413581.
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 32 32 Phosphotyrosine.
{ECO:0000250|UniProtKB:P09769}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 196 196 Phosphotyrosine.
{ECO:0000250|UniProtKB:P14234}.
MOD_RES 206 206 Phosphoserine.
{ECO:0000250|UniProtKB:P14234}.
MOD_RES 400 400 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:7515063}.
MOD_RES 511 511 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:7515063}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000250}.
LIPID 3 3 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 6 6 S-palmitoyl cysteine. {ECO:0000250}.
CONFLICT 313 313 V -> A (in Ref. 1; CAA40337).
{ECO:0000305}.
SEQUENCE 517 AA; 58821 MW; 0D960BBBCAF2911B CRC64;
MGCVFCKKLE PAPKEDVGLE GDFRSQGAEE RYYPDPTQGR SSSISPQPIS PAFLNVGNIR
SVSGTGVTIF VALYDYEART GDDLTFTKGE KFHILNNTEY DWWEARSLSS GRTGYVPSNY
VAPVDSIQAE EWYFGKISRK DAERQLLSDG NPQGAFLIRE SETTKGAYSL SIRDWDQNRG
DHIKHYKIRK LDMGGYYITT RAQFESVQDL VRHYMEVNDG LCYLLTAPCM VMKPQTLGLA
KDAWEIDRNS IALDRRLGTG CFGDVWLGTW NCSTKVAVKT LKPGTMSPKA FLEEAQIMKL
LRHDKLVQLY AVVSEEPIYI VTEFMCYGSL LDFLKDRKGH NLMLPNLVDM AAQVAEGMAY
MERMNYIHRD LRAANILVGE HLICKIADFG LARLIVDDEY NPQQGTKFPI KWTAPEAALF
GRFTVKSDVW SFGILLTELI TKGRVPYPGM NNREVLEQVE HGYHMPCPPG CPVSLYEVME
QTWRLDPEER PTFEYLQSFL EDYFTSTEPQ YQPGDQT


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San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




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