FGR
entrez
2268
canonical
uniprot
P09769
canonical
ensembl
ENSG00000000938
resolver
ensp
ENSP00000363115
resolver
ensp
ENSP00000363116
resolver
ensp
ENSP00000363117
resolver
ensp
ENSP00000382126
resolver
ensp
ENSP00000529174
resolver
ensp
ENSP00000529175
resolver
ensp
ENSP00000529176
resolver
ensp
ENSP00000529177
resolver
ensp
ENSP00000529180
resolver
ensp
ENSP00000529181
resolver
ensp
ENSP00000529182
resolver
ensp
ENSP00000529183
resolver
ensp
ENSP00000529184
resolver
ensp
ENSP00000529186
resolver
ensp
ENSP00000529187
resolver
ensp
ENSP00000529188
resolver
ensp
ENSP00000529190
resolver
ensp
ENSP00000638181
resolver
ensp
ENSP00000638182
resolver
ensp
ENSP00000638184
resolver
ensp
ENSP00000638185
resolver
enst
ENST00000374003
resolver
enst
ENST00000374004
resolver
enst
ENST00000374005
resolver
enst
ENST00000399173
resolver
enst
ENST00000859115
resolver
enst
ENST00000859116
resolver
enst
ENST00000859117
resolver
enst
ENST00000859118
resolver
enst
ENST00000859121
resolver
enst
ENST00000859122
resolver
enst
ENST00000859123
resolver
enst
ENST00000859124
resolver
enst
ENST00000859125
resolver
enst
ENST00000859127
resolver
enst
ENST00000859128
resolver
enst
ENST00000859129
resolver
enst
ENST00000859131
resolver
enst
ENST00000968122
resolver
enst
ENST00000968123
resolver
enst
ENST00000968125
resolver
enst
ENST00000968126
resolver
genesymbol
FGR
resolver
genesymbol
c-fgr
resolver
genesymbol_syn
SRC2
resolver
hgnc
HGNC:3697
resolver
uniprot
D3DPL7
resolver
uniprot
P78453
resolver
uniprot
Q9UIQ3
resolver
uniprot_entry
FGR_HUMAN
resolver
uniprot_entry
P78453_HUMAN
resolver
uniprot_sec
D3DPL7
resolver
uniprot_sec
Q9UIQ3
resolver
activity_regulation
ACTIVITY 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}.
uniprot
proteins
amino_acid_sequence
MGCVFCKKLEPVATAKEDAGLEGDFRSYGAADHYGPDPTKARPASSFAHIPNYSNFSSQAINPGFLDSGTIRGVSGIGVTLFIALYDYEARTEDDLTFTKGEKFHILNNTEGDWWEARSLSSGKTGCIPSNYVAPVDSIQAEEWYFGKIGRKDAERQLLSPGNPQGAFLIRESETTKGAYSLSIRDWDQTRGDHVKHYKIRKLDMGGYYITTRVQFNSVQELVQHYMEVNDGLCNLLIAPCTIMKPQTLGLAKDAWEISRSSITLERRLGTGCFGDVWLGTWNGSTKVAVKTLKPGTMSPKAFLEEAQVMKLLRHDKLVQLYAVVSEEPIYIVTEFMCHGSLLDFLKNPEGQDLRLPQLVDMAAQVAEGMAYMERMNYIHRDLRAANILVGERLACKIADFGLARLIKDDEYNPCQGSKFPIKWTAPEAALFGRFTIKSDVWSFGILLTELITKGRIPYPGMNKREVLEQVEQGYHMPCPPGCPASLYEAMEQTWRLDPEERPTFEYLQSFLEDYFTSAEPQYQPGDQT
uniprot
proteins
disease_involvement
DISEASE: Note=Mutations that cause aberrant kinase activation can confer oncogene activity and promote aberrant cell proliferation.
uniprot
proteins
ec_number
2.7.10.2
uniprot
proteins
function
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 a 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 a 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. Together with CLNK, it acts as a negative regulator of natural killer cell-activating receptors and inhibits interferon-gamma production (By similarity). {ECO:0000250|UniProtKB:P14234, ECO:0000269|PubMed:10739672, ECO:0000269|PubMed:17164290, ECO:0000269|PubMed:1737799, ECO:0000269|PubMed:7519620}.
uniprot
proteins
mass_dalton
59479
uniprot
proteins
mutagenesis
MUTAGEN 523; /note="Y->F: Strongly increased catalytic activity. Functions as oncogene."; /evidence="ECO:0000269|PubMed:1737799
uniprot
proteins
post_translational_modification
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}.
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
SRC subfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
10739672
uniprot
proteins
pubmed
11078731
uniprot
proteins
pubmed
12435267
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
1690869
uniprot
proteins
pubmed
17164290
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
1737799
uniprot
proteins
pubmed
1847500
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
2181286
uniprot
proteins
pubmed
2852026
uniprot
proteins
pubmed
3023853
uniprot
proteins
pubmed
3275868
uniprot
proteins
pubmed
3330776
uniprot
proteins
pubmed
7519620
uniprot
proteins
pubmed
8327512
uniprot
proteins
pubmed
8603737
uniprot
proteins
sequence_length
529
uniprot
proteins
subcellular_location
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}.
uniprot
proteins