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P18460

- FGFR3_CHICK

UniProt

P18460 - FGFR3_CHICK

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Protein

Fibroblast growth factor receptor 3

Gene

FGFR3

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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.By similarity

Catalytic activityi

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

Enzyme regulationi

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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei502 – 5021ATPPROSITE-ProRule annotation
Active sitei611 – 6111Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi472 – 4809ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. fibroblast growth factor-activated receptor activity Source: InterPro

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. positive regulation of cell proliferation Source: InterPro
  3. skeletal system development Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 1306.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibroblast growth factor receptor 3 (EC:2.7.10.1)
Short name:
FGFR-3
Alternative name(s):
Tyrosine kinase receptor CEK2
Gene namesi
Name:FGFR3
Synonyms:CEK2
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 806787Fibroblast growth factor receptor 3PRO_0000016790Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi61 ↔ 107PROSITE-ProRule annotation
Glycosylationi83 – 831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi96 – 961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi118 – 1181N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi170 ↔ 222PROSITE-ProRule annotation
Glycosylationi219 – 2191N-linked (GlcNAc...)Sequence Analysis
Glycosylationi256 – 2561N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi269 ↔ 333PROSITE-ProRule annotation
Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi309 – 3091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi322 – 3221N-linked (GlcNAc...)Sequence Analysis
Modified residuei641 – 6411Phosphotyrosine; by autocatalysisBy similarity
Modified residuei642 – 6421Phosphotyrosine; by autocatalysisBy similarity
Modified residuei718 – 7181Phosphotyrosine; by autocatalysisBy similarity
Modified residuei754 – 7541Phosphotyrosine; by autocatalysisBy similarity

Post-translational modificationi

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.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP18460.

Interactioni

Subunit structurei

Monomer. Homodimer after ligand binding By similarity.By similarity

Protein-protein interaction databases

STRINGi9031.ENSGALP00000001710.

Structurei

3D structure databases

ProteinModelPortaliP18460.
SMRiP18460. Positions 145-355, 453-750.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 364345ExtracellularSequence AnalysisAdd
BLAST
Topological domaini390 – 806417CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei365 – 38925HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 124101Ig-like C2-type 1Add
BLAST
Domaini150 – 23889Ig-like C2-type 2Add
BLAST
Domaini247 – 349103Ig-like C2-type 3Add
BLAST
Domaini466 – 755290Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi131 – 14111Asp/Glu-rich (highly acidic)Add
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000263410.
HOVERGENiHBG000345.
InParanoidiP18460.
KOiK05094.
PhylomeDBiP18460.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR028176. 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]
PANTHERiPTHR24416:SF128. PTHR24416:SF128. 1 hit.
PfamiPF07679. I-set. 2 hits.
PF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000628. FGFR. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50835. IG_LIKE. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P18460-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRAAWGSVWC LCLAAAVGAL PAARRRGAER SGGQAAEYLR SETAFLEELV
60 70 80 90 100
FGSGDTIELS CNTQSSSVSV FWFKDGIGIA PSNRTHIGQK LLKIINVSYD
110 120 130 140 150
DSGLYSCKPR HSNEVLGNFT VRVTDSPSSG DDEDDDDESE DTGVPFWTRP
160 170 180 190 200
DKMEKKLLAV PAANTVRFRC PAGGNPTPTI YWLKNGKEFK GEHRIGGIKL
210 220 230 240 250
RHQQWSLVME SVVPSDRGNY TCVVENKYGN IRHTYQLDVL ERSPHRPILQ
260 270 280 290 300
AGLPANQTVV VGSNVEFHCK VYSDAQPHIQ WLKHVEVNGS KYGPDGTPYV
310 320 330 340 350
TVLKTAGVNT TDKELEILYL RNVTFEDAGE YTCLAGNSIG FSHHSAWLTV
360 370 380 390 400
LPAEELMEMD DSGSVYAGIL SYGTGLVLFI LVLVIVIICR MKMPNKKAMN
410 420 430 440 450
TTTVQKVSKF PLKRQQVSLE SNSSMNSNTP LVRITRLSSS DGPMLANVSE
460 470 480 490 500
LELPPDPKWE LARSRLTLGK PLGEGCFGQV VMAEAIGIDK DKPNKAITVA
510 520 530 540 550
VKMLKDDATD KDLSDLVSEM EMMKMIGKHK NIINLLGACT QDGPLYVLVE
560 570 580 590 600
YASKGNLREY LRARRPPGMD YSFDTCKLPE EQLTFKDLVS CAYQVARGME
610 620 630 640 650
YLASQKCIHR DLAARNVLVT EDNVMKIADF GLARDVHNID YYKKTTNGRL
660 670 680 690 700
PVKWMAPEAL FDRVYTHQSD VWSFGVLLWE IFTLGGSPYP GIPVEELFKL
710 720 730 740 750
LKEGHRMDKP ANCTHDLYMI MRECWHAVPS QRPTFKQLVE DLDRVLTMTS
760 770 780 790 800
TDEYLDLSVP FEQYSPAGQD THSTCSSGDD SVFAHDLLPD EPCLPKHVPC

NGVIRT
Length:806
Mass (Da):89,730
Last modified:November 1, 1990 - v1
Checksum:iB38B3C6D5F2314B6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M35195 mRNA. Translation: AAA48664.1.
PIRiA35963.
RefSeqiNP_990840.2. NM_205509.2.
UniGeneiGga.14066.

Genome annotation databases

GeneIDi396515.
KEGGigga:396515.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M35195 mRNA. Translation: AAA48664.1 .
PIRi A35963.
RefSeqi NP_990840.2. NM_205509.2.
UniGenei Gga.14066.

3D structure databases

ProteinModelPortali P18460.
SMRi P18460. Positions 145-355, 453-750.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9031.ENSGALP00000001710.

Proteomic databases

PaxDbi P18460.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 396515.
KEGGi gga:396515.

Organism-specific databases

CTDi 2261.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000263410.
HOVERGENi HBG000345.
InParanoidi P18460.
KOi K05094.
PhylomeDBi P18460.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 1306.

Miscellaneous databases

NextBioi 20816552.
PROi P18460.

Family and domain databases

Gene3Di 2.60.40.10. 3 hits.
InterProi IPR028176. 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 ]
PANTHERi PTHR24416:SF128. PTHR24416:SF128. 1 hit.
Pfami PF07679. I-set. 2 hits.
PF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
PIRSFi PIRSF000628. FGFR. 1 hit.
PRINTSi PR00109. TYRKINASE.
SMARTi SM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50835. IG_LIKE. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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].

Entry informationi

Entry nameiFGFR3_CHICK
AccessioniPrimary (citable) accession number: P18460
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: October 29, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3