FGFR1_HUMAN - dbPTM
FGFR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FGFR1_HUMAN
UniProt AC P11362
Protein Name Fibroblast growth factor receptor 1
Gene Name FGFR1
Organism Homo sapiens (Human).
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..
Protein Sequence MWSWKCLLFWAVLVTATLCTARPSPTLPEQAQPWGAPVEVESFLVHPGDLLQLRCRLRDDVQSINWLRDGVQLAESNRTRITGEEVEVQDSVPADSGLYACVTSSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVSADSSASMNSGVLLVRPSRLSSSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQYSPSFPDTRSSTCSSGEDSVFSHEPLPEEPCLPRHPAQLANGGLKRR
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 Orthologous
Protein Cluster
55 (in isoform 14)Phosphorylation-6.9924719451
55 (in isoform 18)Phosphorylation-6.9924719451
63 (in isoform 14)Phosphorylation-20.1024719451
63 (in isoform 18)Phosphorylation-20.1024719451
65 (in isoform 14)Phosphorylation-36.6624719451
65 (in isoform 18)Phosphorylation-36.6624719451
77N-linked_GlycosylationGVQLAESNRTRITGE
CCHHHHHCCCCCCCC		40.63UniProtKB CARBOHYD
91PhosphorylationEEVEVQDSVPADSGL
CEEEEECCCCCCCCE		16.95-
117N-linked_GlycosylationDTTYFSVNVSDALPS
CCEEEEEEHHHCCCC		26.78UniProtKB CARBOHYD
144 (in isoform 7)Phosphorylation-51.1724719451
147 (in isoform 19)Phosphorylation-55.2124719451
152 (in isoform 7)Phosphorylation-5.8924719451
154PhosphorylationNRMPVAPYWTSPEKM
CCCCCCCCCCCHHHH		16.1612601080
154 (in isoform 7)Phosphorylation-16.1624719451
155 (in isoform 19)Phosphorylation-6.8524719451
157 (in isoform 19)Phosphorylation-19.5424719451
164AcetylationSPEKMEKKLHAVPAA
CHHHHHHHHHCCCCC		32.0020167786
172AcetylationLHAVPAAKTVKFKCP
HHCCCCCCEEEEECC		56.8320167786
177PhosphorylationAAKTVKFKCPSSGTP
CCCEEEEECCCCCCC		39.2524719451
177 (in isoform 21)Phosphorylation-39.2524719451
185PhosphorylationCPSSGTPNPTLRWLK
CCCCCCCCCCCHHHH		41.8624719451
185 (in isoform 21)Phosphorylation-41.8624719451
187PhosphorylationSSGTPNPTLRWLKNG
CCCCCCCCCHHHHCC		35.2824719451
187 (in isoform 21)Phosphorylation-35.2824719451
210PhosphorylationIGGYKVRYATWSIIM
CCCEEEEEEEEEEEE		16.0322210691
219PhosphorylationTWSIIMDSVVPSDKG
EEEEEECCCCCCCCC		13.9722210691
223PhosphorylationIMDSVVPSDKGNYTC
EECCCCCCCCCCEEE		40.1022210691
227N-linked_GlycosylationVVPSDKGNYTCIVEN
CCCCCCCCEEEEEEC		34.38UniProtKB CARBOHYD
228PhosphorylationVPSDKGNYTCIVENE
CCCCCCCEEEEEECC		16.2024260401
237 (in isoform 18)Phosphorylation-18.8330243723
238 (in isoform 18)Phosphorylation-21.2230243723
239 (in isoform 16)Phosphorylation-3.6830243723
240 (in isoform 16)Phosphorylation-24.1230243723
240 (in isoform 18)Phosphorylation-24.1230243723
240N-linked_GlycosylationENEYGSINHTYQLDV
ECCCCCEEEEEEEEE		24.12UniProtKB CARBOHYD
242 (in isoform 16)Phosphorylation-14.4230243723
264N-linked_GlycosylationLQAGLPANKTVALGS
CCCCCCCCCEEECCC		38.29UniProtKB CARBOHYD
280PhosphorylationVEFMCKVYSDPQPHI
EEEEEEECCCCCCCE		7.8912601080
296N-linked_GlycosylationWLKHIEVNGSKIGPD
EEEEEEECCCCCCCC		35.9116335952
307PhosphorylationIGPDNLPYVQILKTA
CCCCCCCCEEEEECC		14.2512601080
317N-linked_GlycosylationILKTAGVNTTDKEME
EEECCCCCCCCCCEE		36.02UniProtKB CARBOHYD
330N-linked_GlycosylationMEVLHLRNVSFEDAG
EEEEEECCCCHHHCC		39.90UniProtKB CARBOHYD
403PhosphorylationVYKMKSGTKKSDFHS
EEECCCCCCCCHHHH		42.25-
410PhosphorylationTKKSDFHSQMAVHKL
CCCCHHHHHHHHHHH		22.96-
416UbiquitinationHSQMAVHKLAKSIPL
HHHHHHHHHHHCCCC		43.47-
420PhosphorylationAVHKLAKSIPLRRQV
HHHHHHHCCCCCCEE		24.6724719451
428PhosphorylationIPLRRQVTVSADSSA
CCCCCEEEEECCCCC		10.6223090842
430PhosphorylationLRRQVTVSADSSASM
CCCEEEEECCCCCCC		19.5923090842
433PhosphorylationQVTVSADSSASMNSG
EEEEECCCCCCCCCC		27.7623090842
434PhosphorylationVTVSADSSASMNSGV
EEEECCCCCCCCCCE		25.5523090842
436PhosphorylationVSADSSASMNSGVLL
EECCCCCCCCCCEEE		22.0523090842
439PhosphorylationDSSASMNSGVLLVRP
CCCCCCCCCEEEEEH		22.95-
447PhosphorylationGVLLVRPSRLSSSGT
CEEEEEHHHCCCCCC		34.9827732954
450PhosphorylationLVRPSRLSSSGTPML
EEEHHHCCCCCCCCC		22.7328857561
451PhosphorylationVRPSRLSSSGTPMLA
EEHHHCCCCCCCCCC		37.0628857561
452PhosphorylationRPSRLSSSGTPMLAG
EHHHCCCCCCCCCCC		43.2228857561
454PhosphorylationSRLSSSGTPMLAGVS
HHCCCCCCCCCCCCC		13.8927732954
463PhosphorylationMLAGVSEYELPEDPR
CCCCCCCCCCCCCCC		18.4312601080
481PhosphorylationPRDRLVLGKPLGEGC
CCCCEECCCCCCCCH		23.2727642862
482PhosphorylationRDRLVLGKPLGEGCF
CCCEECCCCCCCCHH		32.6724719451
482UbiquitinationRDRLVLGKPLGEGCF
CCCEECCCCCCCCHH		32.67-
494PhosphorylationGCFGQVVLAEAIGLD
CHHHHHHHHHHHCCC		3.6127642862
510UbiquitinationDKPNRVTKVAVKMLK
CCCCCHHHHHHHHHH		25.91-
572PhosphorylationSKGNLREYLQARRPP
CCCCHHHHHHHHCCC		9.55-
583PhosphorylationRRPPGLEYCYNPSHN
HCCCCCCCCCCCCCC		12.7919224897
585PhosphorylationPPGLEYCYNPSHNPE
CCCCCCCCCCCCCHH		29.2519224897
588PhosphorylationLEYCYNPSHNPEEQL
CCCCCCCCCCHHHHC		32.0528152594
602PhosphorylationLSSKDLVSCAYQVAR
CCHHHHHHHHHHHHH		10.59-
605PhosphorylationKDLVSCAYQVARGME
HHHHHHHHHHHHHHH		14.0912601080
613PhosphorylationQVARGMEYLASKKCI
HHHHHHHHHHCCCCC		9.93-
614PhosphorylationVARGMEYLASKKCIH
HHHHHHHHHCCCCCC		2.5027642862
616PhosphorylationRGMEYLASKKCIHRD
HHHHHHHCCCCCCHH		30.0127642862
638UbiquitinationVTEDNVMKIADFGLA
ECCCCEEHHHHHHCC		30.38-
653PhosphorylationRDIHHIDYYKKTTNG
CCCCCCEEEECCCCC		19.3121945579
654PhosphorylationDIHHIDYYKKTTNGR
CCCCCEEEECCCCCC		11.4021945579
655UbiquitinationIHHIDYYKKTTNGRL
CCCCEEEECCCCCCC		37.10-
677PhosphorylationEALFDRIYTHQSDVW
HHHHHHHHCCHHHHH		10.088622701
684PhosphorylationYTHQSDVWSFGVLLW
HCCHHHHHHHHHHHH		7.9224719451
701PhosphorylationFTLGGSPYPGVPVEE
HHCCCCCCCCCCHHH		17.8311459840
730PhosphorylationSNCTNELYMMMRDCW
CCCHHHHHHHHHHHH		4.1012601080
748UbiquitinationPSQRPTFKQLVEDLD
CCCCCCHHHHHHHHH		45.24-
766PhosphorylationALTSNQEYLDLSMPL
HCCCCHHHCCCCCCH		8.8510652257
776PhosphorylationLSMPLDQYSPSFPDT
CCCCHHHCCCCCCCC		23.4025884760
777PhosphorylationSMPLDQYSPSFPDTR
CCCHHHCCCCCCCCC		14.4018411303
779PhosphorylationPLDQYSPSFPDTRSS
CHHHCCCCCCCCCCC		43.39-
785PhosphorylationPSFPDTRSSTCSSGE
CCCCCCCCCCCCCCC		31.9027732954
786PhosphorylationSFPDTRSSTCSSGED
CCCCCCCCCCCCCCC		30.0927732954
787PhosphorylationFPDTRSSTCSSGEDS
CCCCCCCCCCCCCCC		20.0427732954
789PhosphorylationDTRSSTCSSGEDSVF
CCCCCCCCCCCCCCC		41.2727732954
790PhosphorylationTRSSTCSSGEDSVFS
CCCCCCCCCCCCCCC		48.6327732954
794PhosphorylationTCSSGEDSVFSHEPL
CCCCCCCCCCCCCCC		22.2827732954
797PhosphorylationSGEDSVFSHEPLPEE
CCCCCCCCCCCCCCC		25.4527732954
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
154YPhosphorylationKinaseFGFR1P11362
PSP
280YPhosphorylationKinaseFGFR1P11362
PhosphoELM
307YPhosphorylationKinaseFGFR1P11362
PhosphoELM
463YPhosphorylationKinaseFGFR1P16092
PSP
463YPhosphorylationKinaseFGFR1P11362
PSP
583YPhosphorylationKinaseFGFR1P11362
PSP
583YPhosphorylationKinaseFGFR1P16092
PSP
585YPhosphorylationKinaseFGFR1P11362
PSP
585YPhosphorylationKinaseFGFR1P16092
PSP
605YPhosphorylationKinaseFGFR1P16092
PSP
605YPhosphorylationKinaseFGFR1P11362
PhosphoELM
653YPhosphorylationKinaseBMXP51813
GPS
653YPhosphorylationKinaseFGFR1P11362
PSP
653YPhosphorylationKinaseFGFR1P16092
PSP
654YPhosphorylationKinaseBMXP51813
GPS
654YPhosphorylationKinaseFGFR1P16092
PSP
654YPhosphorylationKinaseFGFR1P11362
PSP
730YPhosphorylationKinaseFGFR1P11362
PSP
766YPhosphorylationKinaseFGFR1P11362
PSP
777SPhosphorylationKinaseMAPK1P28482
GPS
777SPhosphorylationKinaseMAPK3P27361
GPS
777SPhosphorylationKinaseMAPK14Q16539
GPS
779SPhosphorylationKinasePRKCEQ02156
GPS
789SPhosphorylationKinaseRPS6KA3P51812
GPS
-KUbiquitinationE3 ubiquitin ligaseCBLP22681
PMID:17944804
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:21765395
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FGFR1_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FPPS_HUMANFDPSphysical
12020352
FRS3_HUMANFRS3physical
9660748
FGFR1_HUMANFGFR1physical
11030354
FGF1_HUMANFGF1physical
8576175
FRS2_HUMANFRS2physical
11877385
FRS2_HUMANFRS2physical
10629055
PLCG1_HUMANPLCG1physical
9660748
FRS2_HUMANFRS2physical
9660748
FGF2_HUMANFGF2physical
10950949
FRS2_HUMANFRS2physical
11090629
BNIP2_HUMANBNIP2physical
10551883
IMB1_HUMANKPNB1physical
11257130
CBP_HUMANCREBBPphysical
15929978
STAT3_HUMANSTAT3physical
20388777
JAK2_HUMANJAK2physical
20388777
SRC_HUMANSRCphysical
20388777
NEDD4_HUMANNEDD4physical
21765395
FGF23_HUMANFGF23physical
22393163
PTK6_HUMANPTK6physical
22974441
ITK_HUMANITKphysical
22974441
NCK1_HUMANNCK1physical
22974441
VAV_HUMANVAV1physical
22974441
ERBB3_HUMANERBB3physical
16273093
FGFR1_HUMANFGFR1physical
10918587
FGFR1_HUMANFGFR1physical
8622701
KS6A3_HUMANRPS6KA3physical
24141780
NEDD4_HUMANNEDD4physical
25292214
CTNB1_HUMANCTNNB1physical
25241761
CADH1_HUMANCDH1physical
25241761
FGF8_HUMANFGF8physical
25241761
SOS1_HUMANSOS1physical
25241761
CBP_HUMANCREBBPphysical
25241761
P85A_HUMANPIK3R1physical
25241761
PLCG1_HUMANPLCG1physical
25241761
FGF1_HUMANFGF1physical
18199118
FGF2_HUMANFGF2physical
18199118
FGF3_HUMANFGF3physical
18199118
FGF5_HUMANFGF5physical
18199118
FGF6_HUMANFGF6physical
18199118
FGF8_HUMANFGF8physical
18199118
FGF9_HUMANFGF9physical
18199118
FGF10_HUMANFGF10physical
18199118
FGF17_HUMANFGF17physical
18199118
KS6A1_HUMANRPS6KA1physical
15117958
SLAP1_HUMANSLAphysical
15117958
P85A_HUMANPIK3R1physical
15117958
P85B_HUMANPIK3R2physical
15117958
PLCG1_HUMANPLCG1physical
15117958
3BP2_HUMANSH3BP2physical
15117958
NCK2_HUMANNCK2physical
15117958
TNS2_HUMANTENC1physical
15117958
RTN1_HUMANRTN1physical
15117958
RTN3_HUMANRTN3physical
15117958
EPHA4_HUMANEPHA4physical
18790757
YES_HUMANYES1physical
16631103
FGFR1_HUMANFGFR1physical
19224897
ACK1_HUMANTNK2physical
25945695
AKT1_HUMANAKT1physical
25945695
5HT1A_HUMANHTR1Aphysical
22035699
FGF2_HUMANFGF2physical
15548653
KALM_HUMANKAL1physical
15548653
FRS2_HUMANFRS2physical
10464310
FGFR1_HUMANFGFR1physical
10464310
CRK_HUMANCRKphysical
10464310
EPHA4_HUMANEPHA4physical
16365308
KALM_HUMANKAL1physical
19696444
FGF2_HUMANFGF2physical
19696444
FGFR1_HUMANFGFR1physical
8321198
PLCG1_HUMANPLCG1physical
8321198
P85A_HUMANPIK3R1physical
8321198
RASA1_HUMANRASA1physical
8321198
Drug and Disease Associations
Kegg Disease
H00255 Hypogonadotropic hypogonadism, including: Kallmann syndrome (KAL); Fertile eunuch syndrome (FEUNS)
H00443 Osteoglophonic dysplasia (OD); Osteoglophonic dwarfism (OGD)
H00458 Craniosynostosis, including: Pfeiffer syndrome; Apert syndrome; Crouzon syndrome; Jackson-Weiss synd
H00516 Isolated orofacial clefts, including: Cleft lip with or without cleft palate; Cleft palate
H01207 Trigonocephaly
OMIM Disease
101600Pfeiffer syndrome (PS)
147950Hypogonadotropic hypogonadism 2 with or without anosmia (HH2)
166250Osteoglophonic dysplasia (OGD)
615465Hartsfield syndrome (HRTFDS)
190440Trigonocephaly 1 (TRIGNO1)
Kegg Drug
D08878 Brivanib alaninate (JAN/USAN/INN)
D08907 Dovitinib lactate (USAN)
D09589 Brivanib (USAN)
D09919 Lenvatinib (USAN/INN)
D09920 Lenvatinib mesilate (JAN); Lenvatinib mesylate (USAN)
D10137 Regorafenib hydrate (JAN); Stivarga (TN)
D10138 Regorafenib (USAN/INN)
D10396 Nintedanib esylate (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FGFR1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-296, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"The selectivity of receptor tyrosine kinase signaling is controlledby a secondary SH2 domain binding site.";
Bae J.H., Lew E.D., Yuzawa S., Tome F., Lax I., Schlessinger J.;
Cell 138:514-524(2009).
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 458-774 IN COMPLEX WITH PLCG1AND ATP ANALOG, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,AUTOPHOSPHORYLATION, AND PHOSPHORYLATION AT TYR-653; TYR-654 ANDTYR-766.
"The precise sequence of FGF receptor autophosphorylation iskinetically driven and is disrupted by oncogenic mutations.";
Lew E.D., Furdui C.M., Anderson K.S., Schlessinger J.;
Sci. Signal. 2:RA6-RA6(2009).
Cited for: FUNCTION AS PROTO-ONCOGENE, ACTIVE SITE, MUTAGENESIS OF ASN-546 ANDASP-623, CATALYTIC ACTIVITY, PHOSPHORYLATION AT TYR-463; TYR-653;TYR-654; TYR-583; TYR-585 AND TYR-730, MASS SPECTROMETRY, AND ENZYMEREGULATION.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-653, AND MASSSPECTROMETRY.
"Autophosphorylation of FGFR1 kinase is mediated by a sequential andprecisely ordered reaction.";
Furdui C.M., Lew E.D., Schlessinger J., Anderson K.S.;
Mol. Cell 21:711-717(2006).
Cited for: PHOSPHORYLATION AT TYR-463; TYR-653; TYR-654; TYR-583 AND TYR-585, ANDMASS SPECTROMETRY.
"Identification of six novel autophosphorylation sites on fibroblastgrowth factor receptor 1 and elucidation of their importance inreceptor activation and signal transduction.";
Mohammadi M., Dikic I., Sorokin A., Burgess W.H., Jaye M.,Schlessinger J.;
Mol. Cell. Biol. 16:977-989(1996).
Cited for: PHOSPHORYLATION AT TYR-463; TYR-583; TYR-585; TYR-653; TYR-654 ANDTYR-730, CATALYTIC ACTIVITY, ENZYME REGULATION, FUNCTION INPHOSPHORYLATION OF PLCG1 AND SHC1; ACTIVATION OF MAP KINASES ANDREGULATION OF CELL PROLIFERATION AND DIFFERENTIATION, AND MUTAGENESISOF TYR-653 AND TYR-654.

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