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Protein Page:
FGFR3 (mouse)
rdtyret
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
FGFR3 a receptor tyrosine kinase of the highly-conserved FGFR family that binds fibroblast growth factor (FGF). Mutations are associated with thanatophoric dysplasia (TD), craniosynostosis Adelaide type, many craniosynostotic syndromes and bone malformations. Three splice-variant isoforms have been described. Activating point mutations cause dwarfism, including achondroplasia, hypochrondroplasia and thanatophoric dysplasia, and facial and other morphogenetic disorders, including Crouzon syndrome, craniosynostosis Adelaide type, San Diego skeletal displasia and Muenke syndrome. Translocations t(4;14) involving the IgH region are common in multiple myeloma and frequently involve FGFR3. Activated FGFR3 found in 30% of bladder cancers and several cervical cancers, but not in other tumors. Two mutations found in colorectal cancer. Note: This description may include information from UniProtKB.
Protein type: EC 2.7.10.1; Protein kinase, TK; Kinase, protein; Membrane protein, integral; Protein kinase, tyrosine (receptor); TK group; FGFR family
Cellular Component: cell surface; cytoplasm; cytoplasmic vesicle; endoplasmic reticulum; Golgi apparatus; integral to membrane; integral to plasma membrane; internal side of plasma membrane; lysosome; membrane; nucleus; perinuclear region of cytoplasm; plasma membrane; transport vesicle
Molecular Function: ATP binding; fibroblast growth factor binding; fibroblast growth factor receptor activity; kinase activity; nucleotide binding; protein binding; protein kinase activity; protein-tyrosine kinase activity; transferase activity; transmembrane receptor protein tyrosine kinase activity
Biological Process: apoptosis; bone mineralization; cartilage development; cell differentiation; cell-cell signaling; digestive tract morphogenesis; fibroblast growth factor receptor signaling pathway; forebrain development; inner ear development; inner ear receptor cell differentiation; lens morphogenesis in camera-type eye; MAPKKK cascade; morphogenesis of an epithelium; myelination in the central nervous system; negative regulation of astrocyte differentiation; negative regulation of cell proliferation; negative regulation of developmental growth; negative regulation of epithelial cell proliferation; negative regulation of mitosis; negative regulation of smoothened signaling pathway; negative regulation of transcription from RNA polymerase II promoter; oligodendrocyte development; peptidyl-tyrosine phosphorylation; phosphorylation; positive regulation of bone mineralization; positive regulation of cell differentiation; positive regulation of cell proliferation; positive regulation of endothelial cell proliferation; positive regulation of MAPKKK cascade; positive regulation of neuron apoptosis; positive regulation of peptidyl-tyrosine phosphorylation; positive regulation of phosphoinositide 3-kinase activity; positive regulation of protein ubiquitination; positive regulation of tyrosine phosphorylation of Stat1 protein; positive regulation of tyrosine phosphorylation of Stat3 protein; protein amino acid autophosphorylation; protein amino acid phosphorylation; regulation of bone remodeling; regulation of ossification; regulation of osteoclast differentiation; response to axon injury; somatic stem cell maintenance; substantia nigra development
Reference #:  Q61851 (UniProtKB)
Alt. Names/Synonyms: FGFR-3; Fgfr3; Fibroblast growth factor receptor 3; HBGFR; Heparin-binding growth factor receptor; Mfr3; Sam3
Gene Symbols: Fgfr3
Molecular weight: 87,758 Da
Basal Isoelectric point: 5.89  Predict pI for various phosphorylation states
CST Pathways:  Angiogenesis  |  ESC Pluripotency and Differentiation  |  Tyrosine Kinases & Substrates
Select Structure to View Below

FGFR3

Protein Structure Not Found.


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Modification Sites and Domains  
Click here to view other types of protein modifications

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       mouse

 
0 1 S402 PPKKGLGSPTVHKVS
0 1 S418‑p FPLKRQVsLESNSSM
0 1 S424 VsLESNSSMNSNTPL
0 1 T429 NSSMNSNTPLVRIAR
0 10 S438‑p LVRIARLssGEGPVL
0 11 S439‑p VRIARLssGEGPVLA
0 1 K524 VSEMEMMKMIGKHKN
0 2 Y546‑p CTQGGPLyVLVEYAA
1 9 Y571 RRPPGMDYSFDACRL
0 1 S572 RPPGMDYSFDACRLP
0 12 Y593‑p KDLVSCAyQVARGME
0 2 Y601 QVARGMEYLASQKCI
0 1 K626 VTEDNVMKIADFGLA
1 47 Y641‑p RDVHNLDyyKKTTNG
1 18 Y642‑p DVHNLDyyKKTTNGR
2 3 Y719 ASCTHDLYMIMRECW
2 0 Y755 TVTSTDEYLDLSVPF
1 0 Y765 LSVPFEQYSPGGQDT
0 2 T772 YSPGGQDTPSSSSSG
0 2 S782 SSSSGDDSVFTHDLL
  human

► Hide Isoforms
 
S408‑p PPKKGLGsPTVHKIS
S424 FPLKRQVSLESNASM
S430 VSLESNASMSSNTPL
T435 NASMSSNTPLVRIAR
S444‑p LVRIARLssGEGPTL
S445‑p VRIARLssGEGPTLA
K530‑ac VSEMEMMkMIGKHKN
Y552 CTQGGPLYVLVEYAA
Y577‑p RRPPGLDysFDTCKP
S578‑p RPPGLDysFDTCKPP
Y599‑p KDLVSCAyQVARGME
Y607‑p QVARGMEyLASQKCI
K632‑ub VTEDNVMkIADFGLA
Y647‑p RDVHNLDyyKKTTNG
Y648‑p DVHNLDyyKKTTNGR
Y724‑p ANCTHDLyMIMRECW
Y760‑p TVTSTDEyLDLSAPF
Y770‑p LSAPFEQySPGGQDt
T777‑p ySPGGQDtPSSSSSG
S787‑p SSSSGDDsVFAHDLL
  FGFR3 iso3  
- gap
S312 YVTVLKVSLESNAsM
S318‑p VSLESNAsMSSNtPL
T323‑p NAsMSSNtPLVRIAR
S332 LVRIARLSSGEGPTL
S333 VRIARLSSGEGPTLA
K418 VSEMEMMKMIGKHKN
Y440 CTQGGPLYVLVEYAA
Y465 RRPPGLDYSFDTCKP
S466 RPPGLDYSFDTCKPP
Y487 KDLVSCAYQVARGME
Y495 QVARGMEYLASQKCI
K520 VTEDNVMKIADFGLA
Y535 RDVHNLDYYKKTTNG
Y536 DVHNLDYYKKTTNGR
Y612 ANCTHDLYMIMRECW
Y648 TVTSTDEYLDLSAPF
Y658 LSAPFEQYSPGGQDT
T665 YSPGGQDTPSSSSSG
S675 SSSSGDDSVFAHDLL
  rat

 
S402 PPKKGLGSPTVHKVS
S418 FPLKRQVSLESNSSM
S424 VSLESNSSMNSNTPL
T429 NSSMNSNTPLVRIAR
S438‑p LVRIARLssGEGPVL
S439‑p VRIARLssGEGPVLA
K524 VSEMEMMKMIGKHKN
Y546 CTQGGPLYVLVEYAA
Y571 RRPPGMDYSFDACRL
S572 RPPGMDYSFDACRLP
Y593 KDLVSCAYQVARGME
Y601 QVARGMEYLASQKCI
K626 VTEDNVMKIADFGLA
Y641‑p RDVHNLDyyKKTTNG
Y642‑p DVHNLDyyKKTTNGR
Y718 ANCTHDLYMIMRECW
Y754 TVTSTDEYLDLSVPF
Y764 LSVPFEQYSPGGQDT
T771 YSPGGQDTPSSSSSG
S781 SSSSGDDSVFTHDLL
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