Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00539
Entry Name
UniProt Accession
Theoretical PI
5.41
Molecular Weight
59478.62
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Tyrosine-protein kinase Fgr
Protein Synonyms/Alias
2.7.10.2; Gardner-Rasheed feline sarcoma viral (v-fgr) oncogene homolog; Proto-oncogene c-Fgr; p55-Fgr; p58-Fgr; p58c-Fgr;
Gene Name
FGR
Gene Synonyms/Alias
SRC2;
Created Date
01-JUL-1989
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGCVFCKKL
[1]
N-Myristoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Baker SJ, Cosenza SC, Reddy EP. The role of v-Fgr myristoylation and the Gagdomain in membrane binding and cellular transformation. Virology. 1998 Sep15;249(1):1-11.[PMID:9740771]
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, 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.
Sequence Annotation
Domain: 77 138 SH3.
Domain: 144 241 SH2.
Domain: 263 516 Protein kinase.
Nucleotide-binding: 269 277 ATP.
Active site: 382 382 Proton acceptor.
Binding site: 291 291 ATP.
Modified residue: 34 34 Phosphotyrosine.
Modified residue: 412 412 Phosphotyrosine.
Modified residue: 523 523 Phosphotyrosine; by SRC.
Protein Length
529 AA.
Protein Sequence
(Canonical)
MGCVFCKKLE PVATAKEDAG LEGDFRSYGA ADHYGPDPTK ARPASSFAHI PNYSNFSSQA  60
INPGFLDSGT IRGVSGIGVT LFIALYDYEA RTEDDLTFTK GEKFHILNNT EGDWWEARSL  120
SSGKTGCIPS NYVAPVDSIQ AEEWYFGKIG RKDAERQLLS PGNPQGAFLI RESETTKGAY  180
SLSIRDWDQT RGDHVKHYKI RKLDMGGYYI TTRVQFNSVQ ELVQHYMEVN DGLCNLLIAP  240
CTIMKPQTLG LAKDAWEISR SSITLERRLG TGCFGDVWLG TWNGSTKVAV KTLKPGTMSP  300
KAFLEEAQVM KLLRHDKLVQ LYAVVSEEPI YIVTEFMCHG SLLDFLKNPE GQDLRLPQLV  360
DMAAQVAEGM AYMERMNYIH RDLRAANILV GERLACKIAD FGLARLIKDD EYNPCQGSKF  420
PIKWTAPEAA LFGRFTIKSD VWSFGILLTE LITKGRIPYP GMNKREVLEQ VEQGYHMPCP  480
PGCPASLYEA MEQTWRLDPE ERPTFEYLQS FLEDYFTSAE PQYQPGDQT              529
FASTA
(Canonical)
>LipidDB-9606-00539|P09769
MGCVFCKKLEPVATAKEDAGLEGDFRSYGAADHYGPDPTKARPASSFAHIPNYSNFSSQA
INPGFLDSGTIRGVSGIGVTLFIALYDYEARTEDDLTFTKGEKFHILNNTEGDWWEARSL
SSGKTGCIPSNYVAPVDSIQAEEWYFGKIGRKDAERQLLSPGNPQGAFLIRESETTKGAY
SLSIRDWDQTRGDHVKHYKIRKLDMGGYYITTRVQFNSVQELVQHYMEVNDGLCNLLIAP
CTIMKPQTLGLAKDAWEISRSSITLERRLGTGCFGDVWLGTWNGSTKVAVKTLKPGTMSP
KAFLEEAQVMKLLRHDKLVQLYAVVSEEPIYIVTEFMCHGSLLDFLKNPEGQDLRLPQLV
DMAAQVAEGMAYMERMNYIHRDLRAANILVGERLACKIADFGLARLIKDDEYNPCQGSKF
PIKWTAPEAALFGRFTIKSDVWSFGILLTELITKGRIPYPGMNKREVLEQVEQGYHMPCP
PGCPASLYEAMEQTWRLDPEERPTFEYLQSFLEDYFTSAEPQYQPGDQT
Gene Ontology
GO:0015629; C:actin cytoskeleton; IEA:Ensembl
GO:0005829; C:cytosol; TAS:Reactome
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW
GO:0005886; C:plasma membrane; ISS:UniProtKB
GO:0032587; C:ruffle membrane; IEA:Ensembl
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0034988; F:Fc-gamma receptor I complex binding; IDA:UniProtKB
GO:0034987; F:immunoglobulin receptor binding; ISS:UniProtKB
GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:UniProtKB
GO:0001784; F:phosphotyrosine binding; ISS:UniProtKB
GO:0019901; F:protein kinase binding; ISS:UniProtKB
GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB
GO:0007596; P:blood coagulation; TAS:Reactome
GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB
GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome
GO:0002768; P:immune response-regulating cell surface receptor signaling pathway; TAS:UniProtKB
GO:0045087; P:innate immune response; TAS:Reactome
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; ISS:UniProtKB
GO:0050715; P:positive regulation of cytokine secretion; ISS:UniProtKB
GO:0043306; P:positive regulation of mast cell degranulation; ISS:UniProtKB
GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:UniProtKB
GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:UniProtKB
GO:0046777; P:protein autophosphorylation; IDA:UniProtKB
GO:0006468; P:protein phosphorylation; TAS:ProtInc
GO:0008360; P:regulation of cell shape; ISS:UniProtKB
GO:0045088; P:regulation of innate immune response; ISS:UniProtKB
GO:0050764; P:regulation of phagocytosis; ISS:UniProtKB
GO:0045859; P:regulation of protein kinase activity; ISS:UniProtKB
GO:0009615; P:response to virus; TAS:ProtInc
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;