Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-01030
Entry Name
UniProt Accession
Theoretical PI
5.23
Molecular Weight
58866.65
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Tyrosine-protein kinase Fgr
Protein Synonyms/Alias
2.7.10.2; Proto-oncogene c-Fgr; p55-Fgr;
Gene Name
Fgr
Gene Synonyms/Alias
Created Date
01-JAN-1990
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
3
Canonical
*****MGCVFCKKLE
[1]
S-Palmitoylation
6
Canonical
**MGCVFCKKLEPAS
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Predicted from GPS-Lipid
Functional Description
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.
Sequence Annotation
Domain: 65 126 SH3.
Domain: 132 229 SH2.
Domain: 251 504 Protein kinase.
Nucleotide-binding: 257 265 ATP.
Active site: 370 370 Proton acceptor.
Binding site: 279 279 ATP.
Modified residue: 13 13 Phosphoserine.
Modified residue: 32 32 Phosphotyrosine.
Modified residue: 400 400 Phosphotyrosine; alternate.
Modified residue: 400 400 Phosphotyrosine; by autocatalysis;alternate.
Modified residue: 511 511 Phosphotyrosine; by SRC.
Protein Length
517 AA.
Protein Sequence
(Canonical)
MGCVFCKKLE PASKEDVGLE GDFRSQTAEE RYFPDPTQGR TSSVFPQPTS PAFLNTGNMR  60
SISGTGVTIF VALYDYEART GDDLTFTKGE KFHILNNTEY DWWEARSLSS GHRGYVPSNY  120
VAPVDSIQAE EWYFGKISRK DAERQLLSSG NPQGAFLIRE SETTKGAYSL SIRDWDQNRG  180
DHIKHYKIRK LDTGGYYITT RAQFDSIQDL VRHYMEVNDG LCYLLTAPCT TTKPQTLGLA  240
KDAWEIDRNS IALERRLGTG CFGDVWLGTW NCSTKVAVKT LKPGTMSPKA FLEEAQIMKL  300
LRHDKLVQLY AVVSEEPIYI VTEFMCYGSL LDFLKDREGQ NLMLPHLVDM AAQVAEGMAY  360
MERMNYIHRD LRAANILVGE YLICKIADFG LARLIEDNEY NPQQGTKFPI KWTAPEAALF  420
GRFTVKSDVW SFGILLTELI TKGRVPYPGM NNREVLEQVE HGYHMPCPPG CPASLYEVME  480
QAWRLDPEER PTFEYLQSFL EDYFTSTEPQ YQPGDQT                           517
FASTA
(Canonical)
>LipidDB-10090-01030|P14234
MGCVFCKKLEPASKEDVGLEGDFRSQTAEERYFPDPTQGRTSSVFPQPTSPAFLNTGNMR
SISGTGVTIFVALYDYEARTGDDLTFTKGEKFHILNNTEYDWWEARSLSSGHRGYVPSNY
VAPVDSIQAEEWYFGKISRKDAERQLLSSGNPQGAFLIRESETTKGAYSLSIRDWDQNRG
DHIKHYKIRKLDTGGYYITTRAQFDSIQDLVRHYMEVNDGLCYLLTAPCTTTKPQTLGLA
KDAWEIDRNSIALERRLGTGCFGDVWLGTWNCSTKVAVKTLKPGTMSPKAFLEEAQIMKL
LRHDKLVQLYAVVSEEPIYIVTEFMCYGSLLDFLKDREGQNLMLPHLVDMAAQVAEGMAY
MERMNYIHRDLRAANILVGEYLICKIADFGLARLIEDNEYNPQQGTKFPIKWTAPEAALF
GRFTVKSDVWSFGILLTELITKGRVPYPGMNNREVLEQVEHGYHMPCPPGCPASLYEVME
QAWRLDPEERPTFEYLQSFLEDYFTSTEPQYQPGDQT
Gene Ontology
GO:0042995; C:cell projection; IEA:UniProtKB-KW
GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW
GO:0005829; C:cytosol; IEA:Ensembl
GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl
GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0034987; F:immunoglobulin receptor binding; IDA:UniProtKB
GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:UniProtKB
GO:0001784; F:phosphotyrosine binding; IDA:UniProtKB
GO:0019901; F:protein kinase binding; IDA:UniProtKB
GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB
GO:0045087; P:innate immune response; IEA:UniProtKB-KW
GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB
GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB
GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB
GO:0050715; P:positive regulation of cytokine secretion; IDA:UniProtKB
GO:0043306; P:positive regulation of mast cell degranulation; IDA:UniProtKB
GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IEA:Ensembl
GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl
GO:0046777; P:protein autophosphorylation; IEA:Ensembl
GO:0032956; P:regulation of actin cytoskeleton organization; TAS:UniProtKB
GO:0008360; P:regulation of cell shape; IMP:UniProtKB
GO:0045088; P:regulation of innate immune response; IMP:UniProtKB
GO:0050764; P:regulation of phagocytosis; IMP:UniProtKB
GO:0045859; P:regulation of protein kinase activity; IDA:UniProtKB
Interpro
InterPro; IPR028459; FGR
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
Pfam; PF07714; Pkinase_Tyr;
Pfam; PF00017; SH2;
Pfam; PF00018; SH3_1;
SMART
SMART; SM00252; SH2;
SMART; SM00326; SH3;
SMART; SM00219; TyrKc;
PROSITE
PROSITE; PS00107; PROTEIN_KINASE_ATP;
PROSITE; PS50011; PROTEIN_KINASE_DOM;
PROSITE; PS00109; PROTEIN_KINASE_TYR;
PROSITE; PS50001; SH2;
PROSITE; PS50002; SH3;
PRINTS
PRINTS; PR00401; SH2DOMAIN;
PRINTS; PR00452; SH3DOMAIN;
PRINTS; PR00109; TYRKINASE;