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P18460 (FGFR3_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibroblast growth factor receptor 3

Short name=FGFR-3
EC=2.7.10.1
Alternative name(s):
Tyrosine kinase receptor CEK2
Gene names
Name:FGFR3
Synonyms:CEK2
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length806 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. 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 By similarity.

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Enzyme regulation

Present in an inactive conformation in the absence of bound ligand. Ligand binding leads to dimerization and activation by autophosphorylation on tyrosine residues By similarity.

Subunit structure

Monomer. Homodimer after ligand binding By similarity.

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity.

Domain

The second and third Ig-like domains directly interact with fibroblast growth factors (FGF) and heparan sulfate proteoglycans By similarity.

Post-translational modification

Autophosphorylated. Binding of FGF family members together with heparan sulfate proteoglycan or heparin promotes receptor dimerization and autophosphorylation on tyrosine residues. Autophosphorylation occurs in trans between the two FGFR molecules present in the dimer By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.

Contains 3 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 806787Fibroblast growth factor receptor 3
PRO_0000016790

Regions

Topological domain20 – 364345Extracellular Potential
Transmembrane365 – 38925Helical; Potential
Topological domain390 – 806417Cytoplasmic Potential
Domain24 – 124101Ig-like C2-type 1
Domain150 – 23889Ig-like C2-type 2
Domain247 – 349103Ig-like C2-type 3
Domain466 – 755290Protein kinase
Nucleotide binding472 – 4809ATP By similarity
Compositional bias131 – 14111Asp/Glu-rich (highly acidic)

Sites

Active site6111Proton acceptor By similarity
Binding site5021ATP By similarity

Amino acid modifications

Modified residue6411Phosphotyrosine; by autocatalysis By similarity
Modified residue6421Phosphotyrosine; by autocatalysis By similarity
Modified residue7181Phosphotyrosine; by autocatalysis By similarity
Modified residue7541Phosphotyrosine; by autocatalysis By similarity
Glycosylation831N-linked (GlcNAc...) Potential
Glycosylation961N-linked (GlcNAc...) Potential
Glycosylation1181N-linked (GlcNAc...) Potential
Glycosylation2191N-linked (GlcNAc...) Potential
Glycosylation2561N-linked (GlcNAc...) Potential
Glycosylation2881N-linked (GlcNAc...) Potential
Glycosylation3091N-linked (GlcNAc...) Potential
Glycosylation3221N-linked (GlcNAc...) Potential
Disulfide bond61 ↔ 107 By similarity
Disulfide bond170 ↔ 222 By similarity
Disulfide bond269 ↔ 333 By similarity

Sequences

Sequence LengthMass (Da)Tools
P18460 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: B38B3C6D5F2314B6

FASTA80689,730
        10         20         30         40         50         60 
MRAAWGSVWC LCLAAAVGAL PAARRRGAER SGGQAAEYLR SETAFLEELV FGSGDTIELS 

        70         80         90        100        110        120 
CNTQSSSVSV FWFKDGIGIA PSNRTHIGQK LLKIINVSYD DSGLYSCKPR HSNEVLGNFT 

       130        140        150        160        170        180 
VRVTDSPSSG DDEDDDDESE DTGVPFWTRP DKMEKKLLAV PAANTVRFRC PAGGNPTPTI 

       190        200        210        220        230        240 
YWLKNGKEFK GEHRIGGIKL RHQQWSLVME SVVPSDRGNY TCVVENKYGN IRHTYQLDVL 

       250        260        270        280        290        300 
ERSPHRPILQ AGLPANQTVV VGSNVEFHCK VYSDAQPHIQ WLKHVEVNGS KYGPDGTPYV 

       310        320        330        340        350        360 
TVLKTAGVNT TDKELEILYL RNVTFEDAGE YTCLAGNSIG FSHHSAWLTV LPAEELMEMD 

       370        380        390        400        410        420 
DSGSVYAGIL SYGTGLVLFI LVLVIVIICR MKMPNKKAMN TTTVQKVSKF PLKRQQVSLE 

       430        440        450        460        470        480 
SNSSMNSNTP LVRITRLSSS DGPMLANVSE LELPPDPKWE LARSRLTLGK PLGEGCFGQV 

       490        500        510        520        530        540 
VMAEAIGIDK DKPNKAITVA VKMLKDDATD KDLSDLVSEM EMMKMIGKHK NIINLLGACT 

       550        560        570        580        590        600 
QDGPLYVLVE YASKGNLREY LRARRPPGMD YSFDTCKLPE EQLTFKDLVS CAYQVARGME 

       610        620        630        640        650        660 
YLASQKCIHR DLAARNVLVT EDNVMKIADF GLARDVHNID YYKKTTNGRL PVKWMAPEAL 

       670        680        690        700        710        720 
FDRVYTHQSD VWSFGVLLWE IFTLGGSPYP GIPVEELFKL LKEGHRMDKP ANCTHDLYMI 

       730        740        750        760        770        780 
MRECWHAVPS QRPTFKQLVE DLDRVLTMTS TDEYLDLSVP FEQYSPAGQD THSTCSSGDD 

       790        800 
SVFAHDLLPD EPCLPKHVPC NGVIRT 

« Hide

References

[1]"A distinctive family of embryonic protein-tyrosine kinase receptors."
Pasquale E.B.
Proc. Natl. Acad. Sci. U.S.A. 87:5812-5816(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M35195 mRNA. Translation: AAA48664.1.
PIRA35963.
RefSeqNP_990840.2. NM_205509.2.
UniGeneGga.14066.

3D structure databases

ProteinModelPortalP18460.
SMRP18460. Positions 145-355, 453-750.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000001710.

Proteomic databases

PaxDbP18460.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396515.
KEGGgga:396515.

Organism-specific databases

CTD2261.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000263410.
HOVERGENHBG000345.
InParanoidP18460.
KOK05094.
PhylomeDBP18460.

Enzyme and pathway databases

BRENDA2.7.10.1. 1306.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
InterProIPR028176. FGF_rcpt_3.
IPR016248. FGF_rcpt_fam.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PANTHERPTHR24416:SF128. PTHR24416:SF128. 1 hit.
PfamPF07679. I-set. 2 hits.
PF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFPIRSF000628. FGFR. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50835. IG_LIKE. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20816552.
PROP18460.

Entry information

Entry nameFGFR3_CHICK
AccessionPrimary (citable) accession number: P18460
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: April 16, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families