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Protein

Fibroblast growth factor receptor 2

Gene

Fgfr2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, trophoblast function, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. 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. FGFR2 signaling is down-regulated by ubiquitination, internalization and degradation. Mutations that lead to constitutive kinase activation or impair normal FGFR2 maturation, internalization and degradation lead to aberrant signaling. Over-expressed FGFR2 promotes activation of STAT1.4 Publications

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)DescriptionActionsGraphical viewLength
Binding sitei517ATPPROSITE-ProRule annotation1
Binding sitei571ATPPROSITE-ProRule annotation1
Active sitei626Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi487 – 495ATPPROSITE-ProRule annotation9
Nucleotide bindingi565 – 567ATPPROSITE-ProRule annotation3

GO - Molecular functioni

GO - Biological processi

  • angiogenesis Source: MGI
  • animal organ morphogenesis Source: MGI
  • apoptotic process Source: UniProtKB-KW
  • axonogenesis Source: MGI
  • bone development Source: MGI
  • bone mineralization Source: MGI
  • bone morphogenesis Source: MGI
  • branch elongation involved in salivary gland morphogenesis Source: MGI
  • branching involved in labyrinthine layer morphogenesis Source: MGI
  • branching involved in prostate gland morphogenesis Source: MGI
  • branching involved in salivary gland morphogenesis Source: MGI
  • branching morphogenesis of a nerve Source: MGI
  • bud elongation involved in lung branching Source: MGI
  • cell-cell signaling Source: MGI
  • cell fate commitment Source: MGI
  • coronal suture morphogenesis Source: MGI
  • digestive tract development Source: MGI
  • embryonic cranial skeleton morphogenesis Source: MGI
  • embryonic digestive tract morphogenesis Source: MGI
  • embryonic organ development Source: MGI
  • embryonic organ morphogenesis Source: MGI
  • embryonic pattern specification Source: MGI
  • endodermal digestive tract morphogenesis Source: MGI
  • epidermis morphogenesis Source: MGI
  • epithelial cell differentiation Source: MGI
  • epithelial cell proliferation Source: MGI
  • epithelial cell proliferation involved in salivary gland morphogenesis Source: MGI
  • epithelial tube branching involved in lung morphogenesis Source: MGI
  • fibroblast growth factor receptor signaling pathway Source: MGI
  • fibroblast growth factor receptor signaling pathway involved in hemopoiesis Source: UniProtKB
  • fibroblast growth factor receptor signaling pathway involved in mammary gland specification Source: MGI
  • fibroblast growth factor receptor signaling pathway involved in negative regulation of apoptotic process in bone marrow Source: UniProtKB
  • fibroblast growth factor receptor signaling pathway involved in orbitofrontal cortex development Source: UniProtKB
  • fibroblast growth factor receptor signaling pathway involved in positive regulation of cell proliferation in bone marrow Source: UniProtKB
  • gland morphogenesis Source: MGI
  • hair follicle morphogenesis Source: MGI
  • inner ear morphogenesis Source: MGI
  • in utero embryonic development Source: MGI
  • lacrimal gland development Source: MGI
  • lateral sprouting from an epithelium Source: MGI
  • lens fiber cell development Source: MGI
  • limb bud formation Source: MGI
  • lung alveolus development Source: MGI
  • lung-associated mesenchyme development Source: MGI
  • lung development Source: MGI
  • lung lobe morphogenesis Source: MGI
  • mammary gland bud formation Source: MGI
  • membranous septum morphogenesis Source: MGI
  • mesenchymal cell differentiation Source: MGI
  • mesenchymal cell differentiation involved in lung development Source: MGI
  • mesenchymal cell proliferation involved in lung development Source: MGI
  • midbrain development Source: MGI
  • morphogenesis of embryonic epithelium Source: MGI
  • multicellular organism growth Source: MGI
  • negative regulation of cell proliferation Source: MGI
  • negative regulation of mitotic nuclear division Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • neuromuscular junction development Source: MGI
  • odontogenesis Source: MGI
  • orbitofrontal cortex development Source: UniProtKB
  • organ growth Source: MGI
  • otic vesicle formation Source: ParkinsonsUK-UCL
  • outflow tract septum morphogenesis Source: MGI
  • peptidyl-tyrosine phosphorylation Source: MGI
  • positive regulation of canonical Wnt signaling pathway Source: MGI
  • positive regulation of cardiac muscle cell proliferation Source: MGI
  • positive regulation of cell cycle Source: UniProtKB
  • positive regulation of cell division Source: MGI
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of epithelial cell proliferation Source: MGI
  • positive regulation of epithelial cell proliferation involved in lung morphogenesis Source: MGI
  • positive regulation of ERK1 and ERK2 cascade Source: MGI
  • positive regulation of gene expression Source: MGI
  • positive regulation of MAPK cascade Source: MGI
  • positive regulation of mesenchymal cell proliferation Source: MGI
  • positive regulation of phospholipase activity Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of Wnt signaling pathway Source: MGI
  • post-embryonic development Source: MGI
  • prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis Source: MGI
  • prostate epithelial cord elongation Source: MGI
  • prostate gland morphogenesis Source: MGI
  • protein autophosphorylation Source: MGI
  • pyramidal neuron development Source: UniProtKB
  • regulation of branching involved in prostate gland morphogenesis Source: MGI
  • regulation of cell fate commitment Source: MGI
  • regulation of cell proliferation Source: MGI
  • regulation of epithelial cell proliferation Source: MGI
  • regulation of ERK1 and ERK2 cascade Source: MGI
  • regulation of fibroblast growth factor receptor signaling pathway Source: MGI
  • regulation of morphogenesis of a branching structure Source: MGI
  • regulation of multicellular organism growth Source: MGI
  • regulation of smoothened signaling pathway Source: MGI
  • regulation of smooth muscle cell differentiation Source: MGI
  • reproductive structure development Source: MGI
  • squamous basal epithelial stem cell differentiation involved in prostate gland acinus development Source: MGI
  • synaptic vesicle transport Source: MGI
  • ureteric bud development Source: MGI
  • vasculogenesis involved in coronary vascular morphogenesis Source: DFLAT
  • ventricular cardiac muscle tissue morphogenesis Source: MGI
  • ventricular zone neuroblast division Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

ATP-binding, Heparin-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibroblast growth factor receptor 2 (EC:2.7.10.1)
Short name:
FGFR-2
Alternative name(s):
Keratinocyte growth factor receptor
Short name:
KGFR
CD_antigen: CD332
Gene namesi
Name:Fgfr2
Synonyms:Bek, Ect1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:95523. Fgfr2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini22 – 377ExtracellularSequence analysisAdd BLAST356
Transmembranei378 – 398HelicalSequence analysisAdd BLAST21
Topological domaini399 – 821CytoplasmicSequence analysisAdd BLAST423

GO - Cellular componenti

  • cell cortex Source: MGI
  • cell surface Source: MGI
  • cytoplasm Source: MGI
  • cytoplasmic, membrane-bounded vesicle Source: UniProtKB-SubCell
  • excitatory synapse Source: UniProtKB
  • extracellular region Source: MGI
  • Golgi apparatus Source: UniProtKB-SubCell
  • integral component of plasma membrane Source: MGI
  • intracellular membrane-bounded organelle Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality shortly after implantation, due to trophoblast defects, absence of a functional placenta, failure of limb bud formation, plus defects in lung branching and heart development.4 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi769Y → F: Abolishes phosphorylation of FRS2 and activation of MAP kinases. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Chemistry databases

ChEMBLiCHEMBL2111391.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Add BLAST21
ChainiPRO_000001678422 – 821Fibroblast growth factor receptor 2Add BLAST800

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi62 ↔ 107PROSITE-ProRule annotation
Glycosylationi83N-linked (GlcNAc...)Sequence analysis1
Glycosylationi123N-linked (GlcNAc...)Sequence analysis1
Glycosylationi147N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi179 ↔ 231PROSITE-ProRule annotation
Glycosylationi228N-linked (GlcNAc...)Sequence analysis1
Glycosylationi241N-linked (GlcNAc...)Sequence analysis1
Glycosylationi265N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi278 ↔ 342PROSITE-ProRule annotation
Glycosylationi297N-linked (GlcNAc...)Sequence analysis1
Glycosylationi318N-linked (GlcNAc...)Sequence analysis1
Glycosylationi331N-linked (GlcNAc...)Sequence analysis1
Modified residuei466Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei586Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei588Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei656Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei657Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei769Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei780PhosphoserineBy similarity1

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
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).By similarity
Ubiquitinated. FGFR2 is rapidly ubiquitinated after autophosphorylation, leading to internalization and degradation. Subject to degradation both in lysosomes and by the proteasome (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP21803.
PaxDbiP21803.
PRIDEiP21803.

PTM databases

iPTMnetiP21803.
PhosphoSitePlusiP21803.

Expressioni

Gene expression databases

CleanExiMM_FGFR2.

Interactioni

Subunit structurei

Monomer. Homodimer after ligand binding. Interacts predominantly with FGF1 and FGF2, but can also interact with FGF3, FGF4, FGF6, FGF7, FGF8, FGF9, FGF10, FGF17, FGF18 and FGF22 (in vitro) (PubMed:8663044). Ligand specificity is determined by tissue-specific expression of isoforms, and differences in the third Ig-like domain are crucial for ligand specificity. 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 PLCG1 (PubMed:15629145). Interacts with GRB2 and PAK4 (By similarity). Interacts with FLRT2 (PubMed:21765038).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ncam1P135952EBI-6286942,EBI-774943

GO - Molecular functioni

  • fibroblast growth factor binding Source: MGI
  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

BioGridi199657. 2 interactors.
DIPiDIP-6038N.
IntActiP21803. 2 interactors.
STRINGi10090.ENSMUSP00000112430.

Structurei

Secondary structure

1821
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi48 – 52Combined sources5
Beta strandi58 – 61Combined sources4
Beta strandi69 – 74Combined sources6
Beta strandi77 – 79Combined sources3
Beta strandi83 – 88Combined sources6
Beta strandi91 – 94Combined sources4
Helixi99 – 101Combined sources3
Beta strandi103 – 110Combined sources8
Beta strandi115 – 124Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4HWUX-ray2.90A/B45-127[»]
ProteinModelPortaliP21803.
SMRiP21803.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 125Ig-like C2-type 1Add BLAST101
Domaini154 – 247Ig-like C2-type 2Add BLAST94
Domaini256 – 358Ig-like C2-type 3Add BLAST103
Domaini481 – 770Protein kinasePROSITE-ProRule annotationAdd BLAST290

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni161 – 178Heparin-bindingBy similarityAdd BLAST18

Domaini

The second and third Ig-like domains directly interact with fibroblast growth factors (FGF) and heparan sulfate proteoglycans. Alternative splicing events affecting the third Ig-like domain are crucial for ligand selectivity (By similarity).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

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000263410.
HOVERGENiHBG000345.
InParanoidiP21803.
KOiK05093.
PhylomeDBiP21803.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR016248. FGF_rcpt_fam.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
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]
PfamiPF07679. I-set. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000628. FGFR. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
SSF56112. 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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: P21803-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MVSWGRFICL VLVTMATLSL ARPSFSLVED TTLEPEEPPT KYQISQPEAY
60 70 80 90 100
VVAPGESLEL QCMLKDAAVI SWTKDGVHLG PNNRTVLIGE YLQIKGATPR
110 120 130 140 150
DSGLYACTAA RTVDSETWIF MVNVTDAISS GDDEDDTDSS EDVVSENRSN
160 170 180 190 200
QRAPYWTNTE KMEKRLHACP AANTVKFRCP AGGNPTSTMR WLKNGKEFKQ
210 220 230 240 250
EHRIGGYKVR NQHWSLIMES VVPSDKGNYT CLVENEYGSI NHTYHLDVVE
260 270 280 290 300
RSPHRPILQA GLPANASTVV GGDVEFVCKV YSDAQPHIQW IKHVEKNGSK
310 320 330 340 350
NGPDGLPYLK VLKAAGVNTT DKEIEVLYIR NVTFEDAGEY TCLAGNSIGI
360 370 380 390 400
SFHSAWLTVL PAPVREKEIT ASPDYLEIAI YCIGVFLIAC MVVTVIFCRM
410 420 430 440 450
KTTTKKPDFS SQPAVHKLTK RIPLRRQVTV SAESSSSMNS NTPLVRITTR
460 470 480 490 500
LSSTADTPML AGVSEYELPE DPKWEFPRDK LTLGKPLGEG CFGQVVMAEA
510 520 530 540 550
VGIDKDKPKE AVTVAVKMLK DDATEKDLSD LVSEMEMMKM IGKHKNIINL
560 570 580 590 600
LGACTQDGPL YVIVEYASKG NLREYLRARR PPGMEYSYDI NRVPEEQMTF
610 620 630 640 650
KDLVSCTYQL ARGMEYLASQ KCIHRDLAAR NVLVTENNVM KIADFGLARD
660 670 680 690 700
INNIDYYKKT TNGRLPVKWM APEALFDRVY THQSDVWSFG VLMWEIFTLG
710 720 730 740 750
GSPYPGIPVE ELFKLLKEGH RMDKPTNCTN ELYMMMRDCW HAVPSQRPTF
760 770 780 790 800
KQLVEDLDRI LTLTTNEEYL DLTQPLEQYS PSYPDTSSSC SSGDDSVFSP
810 820
DPMPYEPCLP QYPHINGSVK T
Length:821
Mass (Da):91,984
Last modified:November 1, 1997 - v4
Checksum:iFCDB28ADD61F4414
GO
Isoform Short (identifier: P21803-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     37-37: E → G
     38-152: Missing.
     314-361: AAGVNTTDKE...FHSAWLTVLP → HSGINSSNAE...AWLTVLPKQQ

Show »
Length:707
Mass (Da):79,531
Checksum:iE57F5804B12F667C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti53A → V in CAA39083 (PubMed:1711190).Curated1
Sequence conflicti55 – 56GE → RG in CAA39083 (PubMed:1711190).Curated2
Sequence conflicti90E → R in CAA39083 (PubMed:1711190).Curated1
Sequence conflicti119I → Y in CAA39083 (PubMed:1711190).Curated1
Sequence conflicti142 – 143DV → R in CAA39083 (PubMed:1711190).Curated2
Sequence conflicti169C → V in CAA39083 (PubMed:1711190).Curated1
Sequence conflicti169C → V in AAA39377 (PubMed:1846048).Curated1
Sequence conflicti187S → P in CAA39083 (PubMed:1711190).Curated1
Sequence conflicti187S → P in AAA39377 (PubMed:1846048).Curated1
Sequence conflicti214W → R in CAA39083 (PubMed:1711190).Curated1
Sequence conflicti229Y → I in CAA39083 (PubMed:1711190).Curated1
Sequence conflicti275E → R in CAA39083 (PubMed:1711190).Curated1
Sequence conflicti301N → Y in CAA39083 (PubMed:1711190).Curated1
Sequence conflicti301N → Y in AAA39377 (PubMed:1846048).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00298537E → G in isoform Short. 1 Publication1
Alternative sequenceiVSP_00298638 – 152Missing in isoform Short. 1 PublicationAdd BLAST115
Alternative sequenceiVSP_002987314 – 361AAGVN…LTVLP → HSGINSSNAEVLALFNVTEM DAGEYICKVSNYIGQANQSA WLTVLPKQQ in isoform Short. 1 PublicationAdd BLAST48

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55441 mRNA. Translation: CAA39083.1.
M63503 mRNA. Translation: AAA39377.1.
M86441 mRNA. Translation: AAA37286.1.
Y16152 Genomic DNA. Translation: CAA76098.1.
Y16167 Genomic DNA. Translation: CAA76099.1.
M23362 mRNA. Translation: AAA37285.1.
PIRiA38429.
A44142. TVMSBK.
S17295.
RefSeqiNP_034337.2. NM_010207.2.
NP_963895.2. NM_201601.2.
UniGeneiMm.16340.

Genome annotation databases

GeneIDi14183.
KEGGimmu:14183.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55441 mRNA. Translation: CAA39083.1.
M63503 mRNA. Translation: AAA39377.1.
M86441 mRNA. Translation: AAA37286.1.
Y16152 Genomic DNA. Translation: CAA76098.1.
Y16167 Genomic DNA. Translation: CAA76099.1.
M23362 mRNA. Translation: AAA37285.1.
PIRiA38429.
A44142. TVMSBK.
S17295.
RefSeqiNP_034337.2. NM_010207.2.
NP_963895.2. NM_201601.2.
UniGeneiMm.16340.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4HWUX-ray2.90A/B45-127[»]
ProteinModelPortaliP21803.
SMRiP21803.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199657. 2 interactors.
DIPiDIP-6038N.
IntActiP21803. 2 interactors.
STRINGi10090.ENSMUSP00000112430.

Chemistry databases

ChEMBLiCHEMBL2111391.

PTM databases

iPTMnetiP21803.
PhosphoSitePlusiP21803.

Proteomic databases

MaxQBiP21803.
PaxDbiP21803.
PRIDEiP21803.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi14183.
KEGGimmu:14183.

Organism-specific databases

CTDi2263.
MGIiMGI:95523. Fgfr2.

Phylogenomic databases

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000263410.
HOVERGENiHBG000345.
InParanoidiP21803.
KOiK05093.
PhylomeDBiP21803.

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.

Miscellaneous databases

ChiTaRSiFgfr2. mouse.
PROiP21803.
SOURCEiSearch...

Gene expression databases

CleanExiMM_FGFR2.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR016248. FGF_rcpt_fam.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
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]
PfamiPF07679. I-set. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000628. FGFR. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
SSF56112. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiFGFR2_MOUSE
AccessioniPrimary (citable) accession number: P21803
Secondary accession number(s): O55141, Q00389, Q61342
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 168 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.