dbPTM

FGFR1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FGFR1_MOUSE
UniProt AC	P16092
Protein Name	Fibroblast growth factor receptor 1
Gene Name	Fgfr1
Organism	Mus musculus (Mouse).
Sequence Length	822
Subcellular Localization	Cell membrane Single-pass type I membrane protein. Nucleus. Cytoplasm, cytosol. Cytoplasmic vesicle. After ligand binding, both receptor and ligand are rapidly internalized. Can translocate to the nucleus after internalization, or by translocation f
Protein Description	Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of embryonic development, cell proliferation, differentiation and migration. Required for normal mesoderm patterning and correct axial organization during embryonic development, normal skeletogenesis and normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. Phosphorylates PLCG1, FRS2, GAB1 and SHB. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes phosphorylation of SHC1, STAT1 and PTPN11/SHP2. In the nucleus, enhances RPS6KA1 and CREB1 activity and contributes to the regulation of transcription. FGFR1 signaling is down-regulated by IL17RD/SEF, and by FGFR1 ubiquitination, internalization and degradation (By similarity)..
Protein Sequence	MWGWKCLLFWAVLVTATLCTARPAPTLPEQAQPWGVPVEVESLLVHPGDLLQLRCRLRDDVQSINWLRDGVQLVESNRTRITGEEVEVRDSIPADSGLYACVTSSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRRPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMLGSVIIYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVSADSSASMNSGVLLVRPSRLSSSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSIPLDQYSPSFPDTRSSTCSSGEDSVFSHEPLPEEPCLPRHPTQLANSGLKRR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
76	Phosphorylation	DGVQLVESNRTRITG HCEEEEECCCCEECC	24.92	-
77	N-linked_Glycosylation	GVQLVESNRTRITGE CEEEEECCCCEECCC	35.52	-
117	N-linked_Glycosylation	DTTYFSVNVSDALPS CCEEEEEEHHHCCCC	26.78	-
180	Phosphorylation	TVKFKCPSSGTPNPT EEEEECCCCCCCCCC	51.36	-
198 (in isoform 3)	Ubiquitination	-	51.10	22790023
198	Ubiquitination	LKNGKEFKPDHRIGG HHCCCCCCCCCCCCC	51.10	22790023
208 (in isoform 3)	Ubiquitination	-	4.21	-
227	N-linked_Glycosylation	VVPSDKGNYTCIVEN CCCCCCCCEEEEEEC	34.38	-
240	N-linked_Glycosylation	ENEYGSINHTYQLDV ECCCCCEEEEEEEEE	24.12	-
264	N-linked_Glycosylation	LQAGLPANKTVALGS CCCCCCCCCEEECCC	38.29	-
296	N-linked_Glycosylation	WLKHIEVNGSKIGPD EEEEEEECCCCCCCC	35.91	-
317	N-linked_Glycosylation	ILKTAGVNTTDKEME EEECCCCCCCCCCEE	36.02	19349973
330	N-linked_Glycosylation	MEVLHLRNVSFEDAG EEEEEECCCCHHHCC	39.90	-
410	Phosphorylation	TKKSDFHSQMAVHKL CCCHHHHHHHHHHHH	22.96	25338131
447	Phosphorylation	GVLLVRPSRLSSSGT CEEEEEHHHCCCCCC	34.98	25338131
450	Phosphorylation	LVRPSRLSSSGTPML EEEHHHCCCCCCCCC	22.73	26370283
451	Phosphorylation	VRPSRLSSSGTPMLA EEHHHCCCCCCCCCC	37.06	26370283
452	Phosphorylation	RPSRLSSSGTPMLAG EHHHCCCCCCCCCCC	43.22	25338131
454	Phosphorylation	SRLSSSGTPMLAGVS HHCCCCCCCCCCCCC	13.89	25338131
463	Phosphorylation	MLAGVSEYELPEDPR CCCCCCCCCCCCCCC	18.43	-
583	Phosphorylation	RRPPGLEYCYNPSHN HCCCCCCCCCCCCCC	12.79	27717184
585	Phosphorylation	PPGLEYCYNPSHNPE CCCCCCCCCCCCCHH	29.25	27717184
605	Phosphorylation	KDLVSCAYQVARGME HHHHHHHHHHHHHHH	14.09	-
613	Phosphorylation	QVARGMEYLASKKCI HHHHHHHHHHCCCCC	9.93	-
653	Phosphorylation	RDIHHIDYYKKTTNG CCCCCCEEEECCCCC	19.31	26824392
654	Phosphorylation	DIHHIDYYKKTTNGR CCCCCEEEECCCCCC	11.40	20116462
730	Phosphorylation	SNCTNELYMMMRDCW CCCHHHHHHHHHHHH	4.10	-
766	Phosphorylation	ALTSNQEYLDLSIPL HCCCCCCEECEECCH	8.85	12181353
777	Phosphorylation	SIPLDQYSPSFPDTR ECCHHHCCCCCCCCC	14.40	25338131
785	Phosphorylation	PSFPDTRSSTCSSGE CCCCCCCCCCCCCCC	31.90	26160508
786	Phosphorylation	SFPDTRSSTCSSGED CCCCCCCCCCCCCCC	30.09	25293948
787	Phosphorylation	FPDTRSSTCSSGEDS CCCCCCCCCCCCCCC	20.04	26160508
789	Phosphorylation	DTRSSTCSSGEDSVF CCCCCCCCCCCCCCC	41.27	26160508
790	Phosphorylation	TRSSTCSSGEDSVFS CCCCCCCCCCCCCCC	48.63	26160508
794	Phosphorylation	TCSSGEDSVFSHEPL CCCCCCCCCCCCCCC	22.28	26160508
817	Phosphorylation	HPTQLANSGLKRR-- CHHHHHHCCCCCC--	39.64	28066266

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
-	K	Ubiquitination	E3 ubiquitin ligase	Cbl	P22682	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FGFR1_MOUSE !!

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 FGFR1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FRS2_MOUSE	Frs2	physical	15513912
VIGLN_HUMAN	HDLBP	physical	26496610
MAP2_HUMAN	METAP2	physical	26496610
HOMEZ_HUMAN	HOMEZ	physical	26496610

Drug and Disease Associations

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

Regulatory Network of FGFR1_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-317, AND MASSSPECTROMETRY.	19349973 [Abstract]