dbPTM

FGR_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FGR_RAT
UniProt AC	Q6P6U0
Protein Name	Tyrosine-protein kinase Fgr
Gene Name	Fgr
Organism	Rattus norvegicus (Rat).
Sequence Length	517
Subcellular Localization	Cell membrane Lipid-anchor Cytoplasmic side . Cell membrane Peripheral membrane protein Cytoplasmic side. Cell projection, ruffle membrane. Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Mitochondrion inner membrane. Mitochondrion intermembrane space.
Protein 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. 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..
Protein Sequence	MGCVFCKKLEPAPKEDVGLEGDFRSQGAEERYYPDPTQGRSSSISPQPISPAFLNVGNIRSVSGTGVTIFVALYDYEARTGDDLTFTKGEKFHILNNTEYDWWEARSLSSGRTGYVPSNYVAPVDSIQAEEWYFGKISRKDAERQLLSDGNPQGAFLIRESETTKGAYSLSIRDWDQNRGDHIKHYKIRKLDMGGYYITTRAQFESVQDLVRHYMEVNDGLCYLLTAPCMVMKPQTLGLAKDAWEIDRNSIALDRRLGTGCFGDVWLGTWNCSTKVAVKTLKPGTMSPKAFLEEAQIMKLLRHDKLVQLYAVVSEEPIYIVTEFMCYGSLLDFLKDRKGHNLMLPNLVDMAAQVAEGMAYMERMNYIHRDLRAANILVGEHLICKIADFGLARLIVDDEYNPQQGTKFPIKWTAPEAALFGRFTVKSDVWSFGILLTELITKGRVPYPGMNNREVLEQVEHGYHMPCPPGCPVSLYEVMEQTWRLDPEERPTFEYLQSFLEDYFTSTEPQYQPGDQT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Myristoylation	------MGCVFCKKL ------CCCEECCCC	19.12	-
3	S-palmitoylation	-----MGCVFCKKLE -----CCCEECCCCC	1.73	-
6	S-palmitoylation	--MGCVFCKKLEPAP --CCCEECCCCCCCC	1.57	-
32	Phosphorylation	SQGAEERYYPDPTQG CCCCHHHCCCCCCCC	23.72	-
41	Phosphorylation	PDPTQGRSSSISPQP CCCCCCCCCCCCCCC	34.95	22673903
42	Phosphorylation	DPTQGRSSSISPQPI CCCCCCCCCCCCCCC	30.26	22673903
43	Phosphorylation	PTQGRSSSISPQPIS CCCCCCCCCCCCCCC	28.47	29779826
45	Phosphorylation	QGRSSSISPQPISPA CCCCCCCCCCCCCCC	21.30	22673903
50	Phosphorylation	SISPQPISPAFLNVG CCCCCCCCCCEEEEC	19.50	22673903
88	Ubiquitination	GDDLTFTKGEKFHIL CCCCEECCCCEEEEC	61.96	-
168	Phosphorylation	SETTKGAYSLSIRDW CCCCCCEEEEEEEEC	20.86	22673903
169	Phosphorylation	ETTKGAYSLSIRDWD CCCCCEEEEEEEECC	18.33	22673903
196	Phosphorylation	RKLDMGGYYITTRAQ EEECCCCEEEEEHHH	5.98	30181290
197	Phosphorylation	KLDMGGYYITTRAQF EECCCCEEEEEHHHH	8.61	30181290
199	Phosphorylation	DMGGYYITTRAQFES CCCCEEEEEHHHHHC	8.29	30181290
206	Phosphorylation	TTRAQFESVQDLVRH EEHHHHHCHHHHHHH	26.77	30181290
400	Phosphorylation	RLIVDDEYNPQQGTK EEEECCCCCCCCCCC	38.85	27097102
511	Phosphorylation	FTSTEPQYQPGDQT- HCCCCCCCCCCCCC-	27.65	7515063

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
400	Y	Phosphorylation	Kinase	FGR	Q6P6U0	PSP
511	Y	Phosphorylation	Kinase	CSK	P32577	PSP
511	Y	Phosphorylation	Kinase	FGR	Q6P6U0	PSP
511	Y	Phosphorylation	Kinase	SRC	Q9WUD9	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FGR_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of FGR_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
SYUA_HUMAN	SNCA	physical	11744621

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of FGR_RAT

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Regulation of c-Fgr protein kinase by c-Src kinase (CSK) and bypolycationic effectors."; Ruzzene M., James P., Brunati A.M., Donella-Deana A., Pinna L.A.; J. Biol. Chem. 269:15885-15891(1994). Cited for: PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY, PHOSPHORYLATION ATTYR-400 AND TYR-511, MASS SPECTROMETRY, AND ENZYME REGULATION.	7515063 [Abstract]