Q61851 (FGFR3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fibroblast growth factor receptor 3
Short name=FGFR-3
EC=2.7.10.1

Alternative name(s):
Heparin-binding growth factor receptor
CD_antigen=CD333

Gene names

Name:	Fgfr3
Synonyms:	Mfr3, Sam3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	801 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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. 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 STAT1, STAT5A and STAT5B. Plays a role in postnatal lung development. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.10
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. Ref.8
Subunit structure	Monomer. Homodimer after ligand binding. Interacts with FGF1, FGF2, FGF4, FGF6; FGF8, FGF9, FGF10, FGF17, FGF18, FGF19, FGF20 and FGF23 (in vitro). Interacts with KLB. Affinity for fibroblast growth factors (FGFs) is increased by heparan sulfate glycosaminoglycans that function as coreceptors. Likewise, KLB increases the affinity for FGF19 and FGF21. Interacts with PIK3R1, PLCG1, SOCS1 and SOCS3 By similarity. Ref.5
Subcellular location	Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle By similarity. Endoplasmic reticulum By similarity. Note: The activated receptor is rapidly internalized and degraded. Detected in intracellular vesicles after internalization of the autophosphorylated receptor By similarity.
Tissue specificity	In embryo, expressed in heart, lung, kidney, skin, head and liver but not in muscle. In adult, highest levels in brain. Also expressed in liver, lung, kidney, testis, ovary and uterus. Very low levels in heart, thymus, spleen and muscle.
Developmental stage	Expressed in embryos from mid-gestation and in adult.
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. Phosphorylation at Tyr-719 is essential for stimulation of cell proliferation and activation of PIK3R1, STAT1 and MAP kinase signaling. Phosphorylation at Tyr-755 is required for interaction with PIK3R1 and PLCG1 By similarity. Ref.8 Ubiquitinated. Is rapidly ubiquitinated after ligand binding and autophosphorylation, leading to receptor internalization and degradation. Subject to both proteasomal and lysosomal degradation By similarity. Ref.8 N-glycosylated in the endoplasmic reticulum. The N-glycan chains undergo further maturation to an Endo H-resistant form in the Golgi apparatus By similarity.
Disruption phenotype	Mice exhibit defects in their skeleton, including kyphosis, scoliosis, crooked tails and curvature and overgrowth of long bones and vertebrae. This bone dysplasia is due to defects in the regulation of chondrocyte proliferation and differentiation in the cartilaginous growth plate. Mice also display inner ear defects including failure of pillar cell differentiation and tunnel of Corti formation, resulting in profound deafness. Mice lacking both FGFR3 and FGFR4 display pronounced dwarfism, and while their lungs appear normal at birth, they are completely blocked in alveogenesis and do not form secondary septae to delimit alveoli. These mice also show elevated serum levels of 1,25-dihydroxyvitamin D3 and reduced serum phosphorus levels. Ref.4 Ref.6 Ref.7 Ref.10
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.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cell membrane Cytoplasmic vesicle Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	MAPK cascade Inferred from direct assay Ref.8. Source: MGI alveolar secondary septum development Inferred from genetic interaction Ref.7. Source: MGI apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW axonogenesis involved in innervation Inferred from mutant phenotype PubMed 17557302. Source: MGI bone maturation Inferred from mutant phenotype PubMed 20582225. Source: BHF-UCL bone morphogenesis Inferred from mutant phenotype PubMed 19407216. Source: MGI cartilage development Inferred from mutant phenotype PubMed 15781473. Source: MGI central nervous system myelination Inferred from mutant phenotype PubMed 12574417. Source: MGI cochlea development Inferred from mutant phenotype PubMed 17557302. Source: MGI digestive tract morphogenesis Inferred from mutant phenotype PubMed 19407216. Source: MGI epithelial cell fate commitment Inferred from mutant phenotype PubMed 19407216. Source: MGI inner ear receptor cell differentiation Inferred from mutant phenotype PubMed 17117437. Source: MGI lens fiber cell development Inferred from genetic interaction PubMed 18455718. Source: MGI lens morphogenesis in camera-type eye Inferred from mutant phenotype PubMed 11290300. Source: MGI morphogenesis of an epithelium Inferred from mutant phenotype PubMed 17117437. Source: MGI negative regulation of apoptotic process Inferred from mutant phenotype PubMed 12574417. Source: MGI negative regulation of astrocyte differentiation Inferred from mutant phenotype PubMed 12574417. Source: MGI negative regulation of developmental growth Inferred from mutant phenotype PubMed 20582225. Source: BHF-UCL negative regulation of epithelial cell proliferation Inferred from mutant phenotype PubMed 11290300PubMed 17192470. Source: MGI negative regulation of mitosis Inferred from genetic interaction PubMed 18455718. Source: MGI negative regulation of smoothened signaling pathway Inferred from mutant phenotype PubMed 9811582. Source: MGI negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 9811582. Source: MGI peptidyl-tyrosine phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of ERK1 and ERK2 cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway Inferred from genetic interaction PubMed 18187602. Source: MGI positive regulation of apoptotic process Inferred from mutant phenotype PubMed 15708559. Source: MGI positive regulation of canonical Wnt receptor signaling pathway Inferred from mutant phenotype PubMed 19407216. Source: MGI positive regulation of cell differentiation Inferred from mutant phenotype PubMed 12417662PubMed 17117437. Source: MGI positive regulation of endothelial cell proliferation Inferred from mutant phenotype PubMed 16291864. Source: MGI positive regulation of phosphatidylinositol 3-kinase activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of phospholipase activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of protein ubiquitination Inferred from direct assay Ref.8. Source: MGI positive regulation of tyrosine phosphorylation of Stat1 protein Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of tyrosine phosphorylation of Stat3 protein Inferred from sequence or structural similarity. Source: UniProtKB post-anal tail morphogenesis Inferred from mutant phenotype PubMed 20582225. Source: BHF-UCL protein autophosphorylation Inferred from sequence or structural similarity. Source: UniProtKB response to axon injury Inferred from mutant phenotype PubMed 16009496. Source: MGI somatic stem cell maintenance Inferred from mutant phenotype PubMed 19407216. Source: MGI substantia nigra development Inferred from mutant phenotype PubMed 17234579. Source: MGI
Cellular_component	cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB internal side of plasma membrane Inferred from direct assay Ref.8. Source: MGI lysosome Inferred from direct assay Ref.8. Source: MGI perinuclear region of cytoplasm Inferred from direct assay Ref.8. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW fibroblast growth factor binding Inferred from sequence or structural similarity. Source: UniProtKB fibroblast growth factor-activated receptor activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q61851-1)

Also known as: IIIc;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q61851-2)

Also known as: IIIb;

The sequence of this isoform differs from the canonical sequence as follows:
     305-352: TAGANTTDKE...HHSAWLVVLP → SWISENVEAD...FWLRVHGPQA

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 801	781	Fibroblast growth factor receptor 3		PRO_0000016786
Regions
	Topological domain	21 – 369	349	Extracellular Potential
	Transmembrane	370 – 390	21	Helical; Potential
	Topological domain	391 – 801	411	Cytoplasmic Potential
	Domain	22 – 124	103	Ig-like C2-type 1
	Domain	145 – 238	94	Ig-like C2-type 2
	Domain	247 – 349	103	Ig-like C2-type 3
	Domain	466 – 756	291	Protein kinase
	Nucleotide binding	472 – 480	9	ATP By similarity
Sites
	Active site	611	1	Proton acceptor By similarity
	Binding site	502	1	ATP By similarity
Amino acid modifications
	Modified residue	641	1	Phosphotyrosine; by autocatalysis Ref.9
	Modified residue	642	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	719	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	755	1	Phosphotyrosine; by autocatalysis By similarity
	Glycosylation	96	1	N-linked (GlcNAc...) Potential
	Glycosylation	219	1	N-linked (GlcNAc...) Potential
	Glycosylation	256	1	N-linked (GlcNAc...) Potential
	Glycosylation	288	1	N-linked (GlcNAc...) Potential
	Glycosylation	309	1	N-linked (GlcNAc...) Potential
	Glycosylation	322	1	N-linked (GlcNAc...) Potential
	Disulfide bond	59 ↔ 107		By similarity
	Disulfide bond	170 ↔ 222		By similarity
	Disulfide bond	269 ↔ 333		By similarity
Natural variations
	Alternative sequence	305 – 352	48	TAGAN…LVVLP → SWISENVEADARLRLANVSE RDGGEYLCRATNFIGVAEKA FWLRVHGPQA in isoform 2.		VSP_002990
Experimental info
	Mutagenesis	644	1	K → E: Constitutively activated kinase. Ref.8
	Sequence conflict	684	1	P → L in AAB25535. Ref.2
	Sequence conflict	687	1	Missing in AAB25535. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (IIIc) [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 68BC110212691705	FASTA	801	87,758
	10 20 30 40 50 60 MVVPACVLVF CVAVVAGATS EPPGPEQRVV RRAAEVPGPE PSQQEQVAFG SGDTVELSCH 70 80 90 100 110 120 PPGGAPTGPT VWAKDGTGLV ASHRILVGPQ RLQVLNASHE DAGVYSCQHR LTRRVLCHFS 130 140 150 160 170 180 VRVTDAPSSG DDEDGEDVAE DTGAPYWTRP ERMDKKLLAV PAANTVRFRC PAAGNPTPSI 190 200 210 220 230 240 SWLKNGKEFR GEHRIGGIKL RHQQWSLVME SVVPSDRGNY TCVVENKFGS IRQTYTLDVL 250 260 270 280 290 300 ERSPHRPILQ AGLPANQTAI LGSDVEFHCK VYSDAQPHIQ WLKHVEVNGS KVGPDGTPYV 310 320 330 340 350 360 TVLKTAGANT TDKELEVLSL HNVTFEDAGE YTCLAGNSIG FSHHSAWLVV LPAEEELMET 370 380 390 400 410 420 DEAGSVYAGV LSYGVVFFLF ILVVAAVILC RLRSPPKKGL GSPTVHKVSR FPLKRQVSLE 430 440 450 460 470 480 SNSSMNSNTP LVRIARLSSG EGPVLANVSE LELPADPKWE LSRTRLTLGK PLGEGCFGQV 490 500 510 520 530 540 VMAEAIGIDK DRTAKPVTVA VKMLKDDATD KDLSDLVSEM EMMKMIGKHK NIINLLGACT 550 560 570 580 590 600 QGGPLYVLVE YAAKGNLREF LRARRPPGMD YSFDACRLPE EQLTCKDLVS CAYQVARGME 610 620 630 640 650 660 YLASQKCIHR DLAARNVLVT EDNVMKIADF GLARDVHNLD YYKKTTNGRL PVKWMAPEAL 670 680 690 700 710 720 FDRVYTHQSD VWSFGVLLWE IFTPGGPSPY PGIPVEELFK LLKEGHRMDK PASCTHDLYM 730 740 750 760 770 780 IMRECWHAVP SQRPTFKQLV EDLDRILTVT STDEYLDLSV PFEQYSPGGQ DTPSSSSSGD 790 800 DSVFTHDLLP PGPPSNGGPR T
	Isoform 2 (IIIb) [UniParc]. Checksum: F45BCEDCB9795093	FASTA	803	88,246
	10 20 30 40 50 60 MVVPACVLVF CVAVVAGATS EPPGPEQRVV RRAAEVPGPE PSQQEQVAFG SGDTVELSCH 70 80 90 100 110 120 PPGGAPTGPT VWAKDGTGLV ASHRILVGPQ RLQVLNASHE DAGVYSCQHR LTRRVLCHFS 130 140 150 160 170 180 VRVTDAPSSG DDEDGEDVAE DTGAPYWTRP ERMDKKLLAV PAANTVRFRC PAAGNPTPSI 190 200 210 220 230 240 SWLKNGKEFR GEHRIGGIKL RHQQWSLVME SVVPSDRGNY TCVVENKFGS IRQTYTLDVL 250 260 270 280 290 300 ERSPHRPILQ AGLPANQTAI LGSDVEFHCK VYSDAQPHIQ WLKHVEVNGS KVGPDGTPYV 310 320 330 340 350 360 TVLKSWISEN VEADARLRLA NVSERDGGEY LCRATNFIGV AEKAFWLRVH GPQAAEEELM 370 380 390 400 410 420 ETDEAGSVYA GVLSYGVVFF LFILVVAAVI LCRLRSPPKK GLGSPTVHKV SRFPLKRQVS 430 440 450 460 470 480 LESNSSMNSN TPLVRIARLS SGEGPVLANV SELELPADPK WELSRTRLTL GKPLGEGCFG 490 500 510 520 530 540 QVVMAEAIGI DKDRTAKPVT VAVKMLKDDA TDKDLSDLVS EMEMMKMIGK HKNIINLLGA 550 560 570 580 590 600 CTQGGPLYVL VEYAAKGNLR EFLRARRPPG MDYSFDACRL PEEQLTCKDL VSCAYQVARG 610 620 630 640 650 660 MEYLASQKCI HRDLAARNVL VTEDNVMKIA DFGLARDVHN LDYYKKTTNG RLPVKWMAPE 670 680 690 700 710 720 ALFDRVYTHQ SDVWSFGVLL WEIFTPGGPS PYPGIPVEEL FKLLKEGHRM DKPASCTHDL 730 740 750 760 770 780 YMIMRECWHA VPSQRPTFKQ LVEDLDRILT VTSTDEYLDL SVPFEQYSPG GQDTPSSSSS 790 800 GDDSVFTHDL LPPGPPSNGG PRT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Ligand specificity and heparin dependence of fibroblast growth factor receptors 1 and 3." Ornitz D.M., Leder P. J. Biol. Chem. 267:16305-16311(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Isolation of the complementary DNA encoding a mouse heparin-binding growth factor receptor with the use of a unique kinase insert sequence." Katoh O., Hattori Y., Sasaki H., Sakamoto H., Fujimoto K., Fujii T., Sugimura T., Terada M. Cancer Res. 53:1136-1141(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[3]	"Fibroblast growth factor receptor (FGFR) 3. Alternative splicing in immunoglobulin-like domain III creates a receptor highly specific for acidic FGF/FGF-1." Chellaiah A.T., McEwen D.G., Werner S., Xu J., Ornitz D.M. J. Biol. Chem. 269:11620-11627(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 242-364 (ISOFORM 2).
[4]	"Fibroblast growth factor receptor 3 is a negative regulator of bone growth." Deng C., Wynshaw-Boris A., Zhou F., Kuo A., Leder P. Cell 84:911-921(1996) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[5]	"Receptor specificity of the fibroblast growth factor family." Ornitz D.M., Xu J., Colvin J.S., McEwen D.G., MacArthur C.A., Coulier F., Gao G., Goldfarb M. J. Biol. Chem. 271:15292-15297(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FGF1; FGF2; FGF4; FGF8 AND FGF9, FUNCTION IN CELL PROLIFERATION.
[6]	"Skeletal overgrowth and deafness in mice lacking fibroblast growth factor receptor 3." Colvin J.S., Bohne B.A., Harding G.W., McEwen D.G., Ornitz D.M. Nat. Genet. 12:390-397(1996) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[7]	"FGFR-3 and FGFR-4 function cooperatively to direct alveogenesis in the murine lung." Weinstein M., Xu X., Ohyama K., Deng C.X. Development 125:3615-3623(1998) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[8]	"Defective lysosomal targeting of activated fibroblast growth factor receptor 3 in achondroplasia." Cho J.Y., Guo C., Torello M., Lunstrum G.P., Iwata T., Deng C., Horton W.A. Proc. Natl. Acad. Sci. U.S.A. 101:609-614(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS FGF2 RECEPTOR AND IN PHOSPHORYLATION OF CBL, UBIQUITINATION, PHOSPHORYLATION, ENZYME REGULATION, MUTAGENESIS OF 644.
[9]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-641, MASS SPECTROMETRY. Tissue: Brain.
[10]	"Regulation of serum 1,25(OH)2Vitamin D3 levels by fibroblast growth factor 23 is mediated by FGF receptors 3 and 4." Gattineni J., Twombley K., Goetz R., Mohammadi M., Baum M. Am. J. Physiol. 301:F371-F377(2011) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION IN VITAMIN D METABOLISM.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M81342 mRNA. Translation: AAA39535.1. S56291 mRNA. Translation: AAB25535.1. L26492 Genomic DNA. Translation: AAA21490.2.
IPI	IPI00126264. IPI00223033.
PIR	A48991. I55363.
UniGene	Mm.6904.
3D structure databases
ProteinModelPortal	Q61851.
SMR	Q61851. Positions 17-363, 453-794.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6031N.
IntAct	Q61851. 1 interaction.
MINT	MINT-5181473.
PTM databases
PhosphoSite	Q61851.
Proteomic databases
PaxDb	Q61851.
PRIDE	Q61851.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
MGI	MGI:95524. Fgfr3.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000263410.
HOVERGEN	HBG000345.
OrthoDB	EOG48WC1F.
Enzyme and pathway databases
BRENDA	2.7.10.1. 3474.
Gene expression databases
CleanEx	MM_FGFR3.
Genevestigator	Q61851.
Family and domain databases
Gene3D	2.60.40.10. 3 hits.
InterPro	IPR007110. Ig-like_dom. IPR013783. Ig-like_fold. IPR013098. Ig_I-set. IPR003598. Ig_sub2. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001245. Ser-Thr/Tyr_kinase_cat_dom. IPR008266. Tyr_kinase_AS. IPR020635. Tyr_kinase_cat_dom. IPR016248. Tyr_kinase_fibroblast_GF_rcpt. [Graphical view]
Pfam	PF07679. I-set. 2 hits. PF07714. Pkinase_Tyr. 1 hit. [Graphical view]
PIRSF	PIRSF000628. FGFR. 1 hit.
PRINTS	PR00109. TYRKINASE.
SMART	SM00408. IGc2. 3 hits. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	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]
ProtoNet	Search...
Other
ChEMBL	CHEMBL4066.
ChiTaRS	FGFR3. mouse.
SOURCE	Search...

Entry information

Entry name

FGFR3_MOUSE

Accession

Primary (citable) accession number: Q61851
Secondary accession number(s): Q61564, Q63834

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 29, 2013
This is version 130 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program