FGR_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FGR_MOUSE
• UniProt AC: P14234
• Protein Name: Tyrosine-protein kinase Fgr
• Gene Name: Fgr
• Organism: Mus musculus (Mouse).
• 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
• 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. [PubMed: 11672534 Required for normal ITGB1 and ITGB2 signaling, normal cell spreading and adhesion in neutrophils and macrophages]
• Protein Sequence: MGCVFCKKLEPASKEDVGLEGDFRSQTAEERYFPDPTQGRTSSVFPQPTSPAFLNTGNMRSISGTGVTIFVALYDYEARTGDDLTFTKGEKFHILNNTEYDWWEARSLSSGHRGYVPSNYVAPVDSIQAEEWYFGKISRKDAERQLLSSGNPQGAFLIRESETTKGAYSLSIRDWDQNRGDHIKHYKIRKLDTGGYYITTRAQFDSIQDLVRHYMEVNDGLCYLLTAPCTTTKPQTLGLAKDAWEIDRNSIALERRLGTGCFGDVWLGTWNCSTKVAVKTLKPGTMSPKAFLEEAQIMKLLRHDKLVQLYAVVSEEPIYIVTEFMCYGSLLDFLKDREGQNLMLPHLVDMAAQVAEGMAYMERMNYIHRDLRAANILVGEYLICKIADFGLARLIEDNEYNPQQGTKFPIKWTAPEAALFGRFTVKSDVWSFGILLTELITKGRVPYPGMNNREVLEQVEHGYHMPCPPGCPASLYEVMEQAWRLDPEERPTFEYLQSFLEDYFTSTEPQYQPGDQT

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Myristoylation	------MGCVFCKKL ------CCCEECCCC	19.12	15561106
3	S-palmitoylation	-----MGCVFCKKLE -----CCCEECCCCC	1.73	15561106
6	S-palmitoylation	--MGCVFCKKLEPAS --CCCEECCCCCCCC	1.57	15561106
13	Phosphorylation	CKKLEPASKEDVGLE CCCCCCCCHHHCCCC	47.49	19144319
25	Phosphorylation	GLEGDFRSQTAEERY CCCCCCCCCCCHHHC	31.69	29176673
27	Phosphorylation	EGDFRSQTAEERYFP CCCCCCCCCHHHCCC	36.96	29176673
32	Phosphorylation	SQTAEERYFPDPTQG CCCCHHHCCCCCCCC	23.81	-
41	Phosphorylation	PDPTQGRTSSVFPQP CCCCCCCCCCCCCCC	31.98	25367039
42	Phosphorylation	DPTQGRTSSVFPQPT CCCCCCCCCCCCCCC	24.12	24719451
43	Phosphorylation	PTQGRTSSVFPQPTS CCCCCCCCCCCCCCC	27.45	29472430
49	Phosphorylation	SSVFPQPTSPAFLNT CCCCCCCCCCCCCCC	41.94	26026062
50	Phosphorylation	SVFPQPTSPAFLNTG CCCCCCCCCCCCCCC	22.40	27180971
56	Phosphorylation	TSPAFLNTGNMRSIS CCCCCCCCCCCEEEC	31.89	30635358
74	Phosphorylation	VTIFVALYDYEARTG EEEEEEEEEEECCCC	13.52	-
98	Phosphorylation	KFHILNNTEYDWWEA EEEEECCCCCCCEEE	34.54	25367039
100	Phosphorylation	HILNNTEYDWWEARS EEECCCCCCCEEEEC	18.15	26026062
133	Phosphorylation	SIQAEEWYFGKISRK CCCCHHHHCEECCHH	13.01	25367039
165	Ubiquitination	IRESETTKGAYSLSI EEECCCCCCEEEEEE	49.30	27667366
168	Phosphorylation	SETTKGAYSLSIRDW CCCCCCEEEEEEEEC	20.86	25521595
169	Phosphorylation	ETTKGAYSLSIRDWD CCCCCEEEEEEEECC	18.33	23737553
171	Phosphorylation	TKGAYSLSIRDWDQN CCCEEEEEEEECCCC	15.05	25367039
193	Phosphorylation	YKIRKLDTGGYYITT EEEEECCCCCEEEEE	42.83	17242355
196	Phosphorylation	RKLDTGGYYITTRAQ EECCCCCEEEEEHHH	7.95	21082442
197	Phosphorylation	KLDTGGYYITTRAQF ECCCCCEEEEEHHHH	8.61	25195567
199	Phosphorylation	DTGGYYITTRAQFDS CCCCEEEEEHHHHHC	8.29	22817900
206	Phosphorylation	TTRAQFDSIQDLVRH EEHHHHHCHHHHHHH	24.36	22817900
223	Phosphorylation	EVNDGLCYLLTAPCT HHCCCEEEEEECCCC	15.13	25367039
250	Phosphorylation	AWEIDRNSIALERRL CEECCCCHHHHHHHH	15.33	24719451
319	Phosphorylation	VVSEEPIYIVTEFMC EECCCCEEEEEEECH	10.47	22817900
400	Phosphorylation	RLIEDNEYNPQQGTK HHHHCCCCCCCCCCC	38.10	19144319
406	Phosphorylation	EYNPQQGTKFPIKWT CCCCCCCCCCCCEEE	25.77	25367039
492	Phosphorylation	LDPEERPTFEYLQSF CCHHHCCHHHHHHHH	35.01	20531401
495	Phosphorylation	EERPTFEYLQSFLED HHCCHHHHHHHHHHH	13.07	20531401
498	Phosphorylation	PTFEYLQSFLEDYFT CHHHHHHHHHHHHHC	29.24	20531401
503	Phosphorylation	LQSFLEDYFTSTEPQ HHHHHHHHHCCCCCC	10.20	20531401
505	Phosphorylation	SFLEDYFTSTEPQYQ HHHHHHHCCCCCCCC	28.63	20531401
506	Phosphorylation	FLEDYFTSTEPQYQP HHHHHHCCCCCCCCC	22.37	20531401
507	Phosphorylation	LEDYFTSTEPQYQPG HHHHHCCCCCCCCCC	48.94	20531401
511	Phosphorylation	FTSTEPQYQPGDQT- HCCCCCCCCCCCCC-	27.65	20531401
517	Phosphorylation	QYQPGDQT------- CCCCCCCC-------	45.37	20531401

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
511	Y	Phosphorylation	Kinase	SRC	P05480	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FGR_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of FGR_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CBL_MOUSE	Cbl	physical	7517397

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND TYR-400, AND MASSSPECTROMETRY.
PubMed: 19144319