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Protein Page:
FGFR3 (human)
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: Protein kinase, TK; Protein kinase, tyrosine (receptor); EC 2.7.10.1; Kinase, protein; Membrane protein, integral; TK group; FGFR family
Chromosomal Location of Human Ortholog: 4p16.3
Cellular Component: cell surface; endoplasmic reticulum; extracellular region; focal adhesion; Golgi apparatus; integral to plasma membrane; nucleus; plasma membrane; transport vesicle
Molecular Function: 1-phosphatidylinositol-3-kinase activity; ATP binding; fibroblast growth factor binding; fibroblast growth factor receptor activity; phosphatidylinositol-4,5-bisphosphate 3-kinase activity; protein binding; protein-tyrosine kinase activity; Ras guanyl-nucleotide exchange factor activity
Biological Process: bone mineralization; cell-cell signaling; chondrocyte differentiation; endochondral ossification; fibroblast growth factor receptor signaling pathway; JAK-STAT cascade; MAPKKK cascade; negative regulation of developmental growth; peptidyl-tyrosine phosphorylation; phosphoinositide phosphorylation; phosphoinositide-mediated signaling; positive regulation of cell proliferation; positive regulation of GTPase activity; positive regulation of MAPKKK cascade; positive regulation of phosphoinositide 3-kinase activity; positive regulation of tyrosine phosphorylation of Stat1 protein; positive regulation of tyrosine phosphorylation of Stat3 protein; protein amino acid autophosphorylation; regulation of phosphoinositide 3-kinase cascade; skeletal development
Disease: Achondroplasia; Achondroplasia, Severe, With Developmental Delay And Acanthosis Nigricans; Bladder Cancer; Camptodactyly, Tall Stature, And Hearing Loss Syndrome; Cervical Cancer; Colorectal Cancer; Crouzon Syndrome With Acanthosis Nigricans; Hypochondroplasia; Lacrimoauriculodentodigital Syndrome; Muenke Syndrome; Nevus, Epidermal; Testicular Germ Cell Tumor; Thanatophoric Dysplasia, Type I; Thanatophoric Dysplasia, Type Ii
Reference #:  P22607 (UniProtKB)
Alt. Names/Synonyms: ACH; achondroplasia, thanatophoric dwarfism; CD333; CEK2; FGFR-3; FGFR3; Fibroblast growth factor receptor 3; HSFGFR3EX; hydroxyaryl-protein kinase; JTK4; tyrosine kinase JTK4
Gene Symbols: FGFR3
Molecular weight: 87,710 Da
Basal Isoelectric point: 5.59  Predict pI for various phosphorylation states
CST Pathways:  Angiogenesis  |  ESC Pluripotency and Differentiation  |  Tyrosine Kinases & Substrates
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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FGFR3

Protein Structure Not Found.
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Sites Implicated In
cell growth, altered: Y577‑p, Y724‑p, Y760‑p, Y770‑p
transcription, altered: Y724‑p
enzymatic activity, induced: Y724‑p, Y760‑p
molecular association, regulation: Y724‑p, Y760‑p
phosphorylation: Y724‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

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.


       human

► Hide Isoforms
 
0 2 S408‑p PPKKGLGsPTVHKIS
0 2 S424‑p FPLKRQVsLESNASM
0 1 S430 VsLESNASMSSNTPL
0 1 T435 NASMSSNTPLVRIAR
0 10 S444‑p LVRIARLssGEGPtL
0 11 S445‑p VRIARLssGEGPtLA
0 1 T450‑p LssGEGPtLANVSEL
0 1 K530‑ac VSEMEMMkMIGKHKN
0 2 Y552 CTQGGPLYVLVEYAA
1 9 Y577‑p RRPPGLDysFDTCKP
0 2 S578‑p RPPGLDysFDTCKPP
0 12 Y599‑p KDLVSCAyQVARGME
0 2 Y607‑p QVARGMEyLASQKCI
0 1 K632‑ub VTEDNVMkIADFGLA
1 47 Y647‑p RDVHNLDyyKKTTNG
1 18 Y648‑p DVHNLDyyKKTTNGR
2 3 Y724‑p ANCTHDLyMIMRECW
2 0 Y760‑p TVTSTDEyLDLSAPF
1 0 Y770‑p LSAPFEQySPGGQDt
0 2 T777‑p ySPGGQDtPSSSSSG
0 2 S787‑p SSSSGDDsVFAHDLL
  FGFR3 iso3  
- gap
S312 YVTVLKVSLESNAsM
S318‑p VSLESNAsMSSNtPL
T323‑p NAsMSSNtPLVRIAR
S332 LVRIARLSSGEGPTL
S333 VRIARLSSGEGPTLA
T338 LSSGEGPTLANVSEL
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
  mouse

 
S402‑p PPKKGLGsPTVHKVS
S418‑p FPLKRQVsLESNSSM
S424 VsLESNSSMNSNTPL
T429 NSSMNSNTPLVRIAR
S438‑p LVRIARLssGEGPVL
S439‑p VRIARLssGEGPVLA
V444 LssGEGPVLANVSEL
K524 VSEMEMMKMIGKHKN
Y546‑p CTQGGPLyVLVEYAA
Y571 RRPPGMDYSFDACRL
S572 RPPGMDYSFDACRLP
Y593‑p KDLVSCAyQVARGME
Y601 QVARGMEYLASQKCI
K626 VTEDNVMKIADFGLA
Y641‑p RDVHNLDyyKKTTNG
Y642‑p DVHNLDyyKKTTNGR
Y719 ASCTHDLYMIMRECW
Y755 TVTSTDEYLDLSVPF
Y765 LSVPFEQYSPGGQDT
T772 YSPGGQDTPSSSSSG
S782 SSSSGDDSVFTHDLL
  rat

 
S402 PPKKGLGSPTVHKVS
S418 FPLKRQVSLESNSSM
S424 VSLESNSSMNSNTPL
T429 NSSMNSNTPLVRIAR
S438‑p LVRIARLssGEGPVL
S439‑p VRIARLssGEGPVLA
V444 LssGEGPVLANVSEL
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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