FGFR3_HUMAN - dbPTM
FGFR3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FGFR3_HUMAN
UniProt AC P22607
Protein Name Fibroblast growth factor receptor 3
Gene Name FGFR3
Organism Homo sapiens (Human).
Sequence Length 806
Subcellular Localization Isoform 1: Cell membrane
Single-pass type I membrane protein. Cytoplasmic vesicle. Endoplasmic reticulum. The activated receptor is rapidly internalized and degraded. Detected in intracellular vesicles after internalization of the autophosphorylated
Protein Description Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation and apoptosis. Plays an essential role in the regulation of chondrocyte differentiation, proliferation and apoptosis, and is required for normal skeleton development. Regulates both osteogenesis and postnatal bone mineralization by osteoblasts. Promotes apoptosis in chondrocytes, but can also promote cancer cell proliferation. Required for normal development of the inner ear. Phosphorylates PLCG1, CBL and FRS2. 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. Plays a role in the regulation of vitamin D metabolism. Mutations that lead to constitutive kinase activation or impair normal FGFR3 maturation, internalization and degradation lead to aberrant signaling. Over-expressed or constitutively activated FGFR3 promotes activation of PTPN11/SHP2, STAT1, STAT5A and STAT5B. Secreted isoform 3 retains its capacity to bind FGF1 and FGF2 and hence may interfere with FGF signaling..
Protein Sequence MGAPACALALCVAVAIVAGASSESLGTEQRVVGRAAEVPGPEPGQQEQLVFGSGDAVELSCPPPGGGPMGPTVWVKDGTGLVPSERVLVGPQRLQVLNASHEDSGAYSCRQRLTQRVLCHFSVRVTDAPSSGDDEDGEDEAEDTGVDTGAPYWTRPERMDKKLLAVPAANTVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDVLERSPHRPILQAGLPANQTAVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKVGPDGTPYVTVLKTAGANTTDKELEVLSLHNVTFEDAGEYTCLAGNSIGFSHHSAWLVVLPAEEELVEADEAGSVYAGILSYGVGFFLFILVVAAVTLCRLRSPPKKGLGSPTVHKISRFPLKRQVSLESNASMSSNTPLVRIARLSSGEGPTLANVSELELPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTSTDEYLDLSAPFEQYSPGGQDTPSSSSSGDDSVFAHDLLPPAPPSSGGSRT
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
84PhosphorylationDGTGLVPSERVLVGP
CCCCCCCCCEEEECC		30.4730301811
98N-linked_GlycosylationPQRLQVLNASHEDSG
CCEEEEECCCCCCCC		40.31UniProtKB CARBOHYD
183O-linked_GlycosylationCPAAGNPTPSISWLK
CCCCCCCCCCCEECC		33.40OGP
185PhosphorylationAAGNPTPSISWLKNG
CCCCCCCCCEECCCC		31.5628188228
225N-linked_GlycosylationVVPSDRGNYTCVVEN
ECCCCCCCEEEEEEC		29.81UniProtKB CARBOHYD
236PhosphorylationVVENKFGSIRQTYTL
EEECCCCCEEEEEEE		20.1024719451
262N-linked_GlycosylationLQAGLPANQTAVLGS
CCCCCCCCCEEECCC		37.48UniProtKB CARBOHYD
294N-linked_GlycosylationWLKHVEVNGSKVGPD
EEEEEEECCEEECCC		35.20UniProtKB CARBOHYD
311 (in isoform 2)Phosphorylation-26.6029978859
314 (in isoform 2)Phosphorylation-14.0329978859
315N-linked_GlycosylationVLKTAGANTTDKELE
EEECCCCCCCCCCEE		42.46UniProtKB CARBOHYD
316 (in isoform 2)Phosphorylation-35.5229978859
328N-linked_GlycosylationLEVLSLHNVTFEDAG
EEEEEECCCCCCCCC		39.56UniProtKB CARBOHYD
338PhosphorylationFEDAGEYTCLAGNSI
CCCCCCEEECCCCEE		9.2018669648
408PhosphorylationPPKKGLGSPTVHKIS
CCCCCCCCCCCCCCC		23.5725849741
410PhosphorylationKKGLGSPTVHKISRF
CCCCCCCCCCCCCCC		36.6228985074
413UbiquitinationLGSPTVHKISRFPLK
CCCCCCCCCCCCCCC		37.73-
424PhosphorylationFPLKRQVSLESNASM
CCCCCCEECCCCCCC		20.3420639409
427PhosphorylationKRQVSLESNASMSSN
CCCEECCCCCCCCCC		42.8820639409
430PhosphorylationVSLESNASMSSNTPL
EECCCCCCCCCCCCC		24.3721406692
432PhosphorylationLESNASMSSNTPLVR
CCCCCCCCCCCCCEE		20.2421406692
433PhosphorylationESNASMSSNTPLVRI
CCCCCCCCCCCCEEE		35.7621406692
435PhosphorylationNASMSSNTPLVRIAR
CCCCCCCCCCEEEEE		21.6821406692
444PhosphorylationLVRIARLSSGEGPTL
CEEEEECCCCCCCCC		30.6426503892
445PhosphorylationVRIARLSSGEGPTLA
EEEEECCCCCCCCCC		45.5122617229
450PhosphorylationLSSGEGPTLANVSEL
CCCCCCCCCCCCCCC		49.7326503892
455PhosphorylationGPTLANVSELELPAD
CCCCCCCCCCCCCCC		35.9525072903
508UbiquitinationKPVTVAVKMLKDDAT
CCEEEEEEEHHCCCC		28.8616410555
515PhosphorylationKMLKDDATDKDLSDL
EEHHCCCCCCCHHHH		51.0526074081
520PhosphorylationDATDKDLSDLVSEME
CCCCCCHHHHHHHHH		38.7526074081
524PhosphorylationKDLSDLVSEMEMMKM
CCHHHHHHHHHHHHH		38.2226074081
530AcetylationVSEMEMMKMIGKHKN
HHHHHHHHHHHCCCC		26.5112437665
577PhosphorylationRRPPGLDYSFDTCKP
CCCCCCCCCCCCCCC		19.1119901323
578PhosphorylationRPPGLDYSFDTCKPP
CCCCCCCCCCCCCCC		19.1319901323
596PhosphorylationLTFKDLVSCAYQVAR
CCHHHHHHHHHHHHH		10.59-
599PhosphorylationKDLVSCAYQVARGME
HHHHHHHHHHHHHHH		14.0912601080
607PhosphorylationQVARGMEYLASQKCI
HHHHHHHHHHHCCCH		9.93-
632UbiquitinationVTEDNVMKIADFGLA
ECCCCEEHHHHHHCC		30.38-
647PhosphorylationRDVHNLDYYKKTTNG
CCCCCCCCCCCCCCC		21.9827259358
648PhosphorylationDVHNLDYYKKTTNGR
CCCCCCCCCCCCCCC		12.9929262532
724PhosphorylationANCTHDLYMIMRECW
CCCCHHHHHHHHHHH		7.2229262532
760PhosphorylationTVTSTDEYLDLSAPF
EECCCCHHCCCCCCC		14.3417145761
770PhosphorylationLSAPFEQYSPGGQDT
CCCCCCCCCCCCCCC		15.0511294897
771PhosphorylationSAPFEQYSPGGQDTP
CCCCCCCCCCCCCCC		19.4324275569
777PhosphorylationYSPGGQDTPSSSSSG
CCCCCCCCCCCCCCC		19.7224275569
779PhosphorylationPGGQDTPSSSSSGDD
CCCCCCCCCCCCCCC		44.9724275569
780PhosphorylationGGQDTPSSSSSGDDS
CCCCCCCCCCCCCCC		35.1324275569
787PhosphorylationSSSSGDDSVFAHDLL
CCCCCCCCEECCCCC		24.7124275569
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
577YPhosphorylationKinaseFGFR3P22607
PhosphoELM
599YPhosphorylationKinaseFGFR1P16092
PSP
647YPhosphorylationKinaseFGFR3P22607
PSP
648YPhosphorylationKinaseFGFR3P22607
PSP
724YPhosphorylationKinaseFGFR3P22607
PSP
760YPhosphorylationKinaseFGFR3P22607
PhosphoELM
770YPhosphorylationKinaseFGFR3P22607
PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseCBLP22681
PMID:18485666
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FGFR3_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 FGFR3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMG7_HUMANSMG7physical
16169070
BORA_HUMANBORAphysical
16169070
CCD17_HUMANCCDC17physical
16169070
HBAZ_HUMANHBZphysical
16169070
HNRPL_HUMANHNRNPLphysical
16169070
NDUS6_HUMANNDUFS6physical
16169070
GOLI_HUMANRNF130physical
16169070
ATF3_HUMANATF3physical
16169070
ARAP1_HUMANARAP1physical
16169070
SCG1_HUMANCHGBphysical
16169070
CATK_HUMANCTSKphysical
16169070
RADIL_HUMANRADILphysical
16169070
TF3C1_HUMANGTF3C1physical
16169070
K2C8_HUMANKRT8physical
16169070
DPOA2_HUMANPOLA2physical
16169070
CE126_HUMANKIAA1377physical
16169070
RL8_HUMANRPL8physical
16169070
ADT3_HUMANSLC25A6physical
16169070
SH2B1_MOUSESh2b1physical
11827956
FGF9_HUMANFGF9physical
8576175
FGF1_HUMANFGF1physical
8576175
GRB2_HUMANGRB2physical
9045692
FGF9_HUMANFGF9physical
10574949
FGF8_HUMANFGF8physical
10574949
FGF1_HUMANFGF1physical
10574949
HS90A_HUMANHSP90AA1physical
21487019
HS90B_HUMANHSP90AB1physical
21487019
HSP7C_HUMANHSPA8physical
21487019
CDC37_HUMANCDC37physical
21487019
HSP74_HUMANHSPA4physical
21487019
FGFR3_HUMANFGFR3physical
11294897
FGFR3_HUMANFGFR3physical
10918587
GRB2_HUMANGRB2physical
26344197
ILKAP_HUMANILKAPphysical
26344197
VHL_HUMANVHLgenetic
28319113
FNTA_HUMANFNTAgenetic
28319113
EPHA4_HUMANEPHA4physical
16365308
KALM_HUMANKAL1physical
19696444
Drug and Disease Associations
Kegg Disease
H00010 Multiple myeloma
H00022 Bladder cancer
H00458 Craniosynostosis, including: Pfeiffer syndrome; Apert syndrome; Crouzon syndrome; Jackson-Weiss synd
H00505 FGFR3-related short limb skeletal dysplasias, including: Achondroplasia; Hypochondroplasia; Thanatop
H00642 Lacrimo-auriculo-dento-digital syndrome (LADD); Levy-Hollister syndrome
H00997 CATSHL syndrome
OMIM Disease
100800Achondroplasia (ACH)
612247Crouzon syndrome with acanthosis nigricans (CAN)
187600Thanatophoric dysplasia 1 (TD1)
187601Thanatophoric dysplasia 2 (TD2)
146000Hypochondroplasia (HCH)
109800Bladder cancer (BLC)
603956Cervical cancer (CERCA)
610474Camptodactyly tall stature and hearing loss syndrome (CATSHL syndrome)
254500Multiple myeloma (MM)
149730Lacrimo-auriculo-dento-digital syndrome (LADDS)
162900Keratinocytic non-epidermolytic nevus (KNEN)
602849Muenke syndrome (MNKS)
182000Keratosis, seborrheic (KERSEB)
273300Testicular germ cell tumor (TGCT)
Kegg Drug
D08907 Dovitinib lactate (USAN)
D09919 Lenvatinib (USAN/INN)
D09920 Lenvatinib mesilate (JAN); Lenvatinib mesylate (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FGFR3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A novel interaction between fibroblast growth factor receptor 3 andthe p85 subunit of phosphoinositide 3-kinase: activation-dependentregulation of ERK by p85 in multiple myeloma cells.";
Salazar L., Kashiwada T., Krejci P., Muchowski P., Donoghue D.,Wilcox W.R., Thompson L.M.;
Hum. Mol. Genet. 18:1951-1961(2009).
Cited for: FUNCTION, INTERACTION WITH PIK3R1 AND PLCG1, AND PHOSPHORYLATION ATTYR-760.
"Identification of tyrosine residues in constitutively activatedfibroblast growth factor receptor 3 involved in mitogenesis, Statactivation, and phosphatidylinositol 3-kinase activation.";
Hart K.C., Robertson S.C., Donoghue D.J.;
Mol. Biol. Cell 12:931-942(2001).
Cited for: FUNCTION IN STIMULATION OF CELL PROLIFERATION; PHOSPHORYLATION OFPIK3R1; PTPN11/SHP2; STAT1; STAT3 AND MAP KINASES, PHOSPHORYLATION ATTYR-724, MUTAGENESIS OF TYR-577; TYR-724; TYR-760 AND TYR-770, ANDCHARACTERIZATION OF VARIANT GLU-650.

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