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Q03364

- FGFR2_XENLA

UniProt

Q03364 - FGFR2_XENLA

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Protein

Fibroblast growth factor receptor 2

Gene

fgfr2

Organism
Xenopus laevis (African clawed frog)
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, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, 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 (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 sitei507 – 5071ATPPROSITE-ProRule annotation
Binding sitei561 – 5611ATPPROSITE-ProRule annotation
Active sitei616 – 6161Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi477 – 4859ATPPROSITE-ProRule annotation
Nucleotide bindingi555 – 5573ATPPROSITE-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. embryonic cranial skeleton morphogenesis Source: InterPro
  3. positive regulation of cell proliferation 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. 6726.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibroblast growth factor receptor 2 (EC:2.7.10.1)
Short name:
FGFR-2
Gene namesi
Name:fgfr2
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-1018301. fgfr2.

Subcellular locationi

Cell membrane; Single-pass type I membrane protein. Golgi apparatus By similarity. Cytoplasmic vesicle By similarity
Note: Detected on osteoblast plasma membrane lipid rafts. After ligand binding, the activated receptor is rapidly internalized and degraded (By similarity).By similarity

GO - Cellular componenti

  1. cytoplasmic vesicle Source: UniProtKB-KW
  2. Golgi apparatus Source: UniProtKB-KW
  3. integral component of membrane Source: UniProtKB-KW
  4. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1414Add
BLAST
Chaini15 – 813799Fibroblast growth factor receptor 2PRO_0000016793Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi58 ↔ 103PROSITE-ProRule annotation
Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi115 – 1151N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi170 ↔ 221PROSITE-ProRule annotation
Glycosylationi231 – 2311N-linked (GlcNAc...)Sequence Analysis
Glycosylationi255 – 2551N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi268 ↔ 332PROSITE-ProRule annotation
Glycosylationi287 – 2871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi308 – 3081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence Analysis
Modified residuei456 – 4561Phosphotyrosine; by autocatalysisBy similarity
Modified residuei576 – 5761Phosphotyrosine; by autocatalysisBy similarity
Modified residuei646 – 6461Phosphotyrosine; by autocatalysisBy similarity
Modified residuei647 – 6471Phosphotyrosine; by autocatalysisBy similarity
Modified residuei759 – 7591Phosphotyrosine; 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
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

PRIDEiQ03364.

Expressioni

Tissue specificityi

Expressed in the anterior neural plate in early neurula stage embryos. Later in development, the protein is also expressed in the eye anlagen, midbrain-hindbrain boundary and otic vesicle.

Interactioni

Subunit structurei

Monomer. Homodimer after ligand binding (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ03364.
SMRiQ03364. Positions 141-353, 458-755.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 367350ExtracellularSequence AnalysisAdd
BLAST
Topological domaini389 – 813425CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei368 – 38821HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 11797Ig-like C2-type 1Add
BLAST
Domaini145 – 23793Ig-like C2-type 2Add
BLAST
Domaini246 – 348103Ig-like C2-type 3Add
BLAST
Domaini471 – 760290Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni152 – 16918Heparin-bindingBy similarityAdd
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

HOVERGENiHBG000345.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR028175. FGF_rcpt_2.
IPR016248. FGF_rcpt_fam.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
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]
PANTHERiPTHR24416:SF130. PTHR24416:SF130. 1 hit.
PfamiPF07679. I-set. 2 hits.
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.

Q03364-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLLALLAFL LVSRTIARPS YSMVDDTTPE PEEPPAKYQI SKADVFPVLP
60 70 80 90 100
GEPLDLRCPL ADGPLVTWTK DGAKLEVNNR TLIVRTYLQI KESTTRDSGL
110 120 130 140 150
YACSVLKNSH FFHVNVTEAS SSGDDEDDND GSEDFTNDNN NIRAPYWTNT
160 170 180 190 200
EKMEKKLHAV SAANTVKLRC PAREPHPSNE WLKNGKEFKQ EHRIGGYKVR
210 220 230 240 250
NQHWSLIMES VVPSDKGIYT CIVENEHGSI NHTYHLDVIE RSSHRPILQA
260 270 280 290 300
GLPANTTAVV GGDAEFVCKV YSDAQPHIRW VRYIEKNGSR FGVDGLPYFK
310 320 330 340 350
VLKAAGVNVT DEEIEVLYVR NVSFEDAGEY TCIAGNSIGI SQHSAWLTVH
360 370 380 390 400
PAPVNPLEDN PVPYYMEIGI YSTGIFIIFC MVVVCVVCRM RQGAKKKKNF
410 420 430 440 450
TGPPVHKLTK RIPLHRQVTV SADSSSSMNS TTPLVRITTR LLNSTDAMPL
460 470 480 490 500
ANVSEYELPH DPMWEFSRDK LTLGKPLGEG CFGQVVMAEA LGIDKERPKE
510 520 530 540 550
SVTVAVKMLK DNATEKDLAD LVSEMEMMKM IGKHKNIINL LGACTQGGTL
560 570 580 590 600
YVIVEYAAKG NLRQYLRARR PLEMEYSFDV TRVPDEQMTF KDLVSCTYQI
610 620 630 640 650
ARGMEYLASQ KCIHRDLAAR NVLVTENNVM KIADFGLARD VNNIDYYKKT
660 670 680 690 700
SNGRLPVKWM APEALFDRVY THQSDVWSFG VLMWEIFTLG GSPYPGIPVE
710 720 730 740 750
ELFKLLKEGH RMDKPANCTN ELYMMMRDCW HAIPSHRPTF KQLVEDLDRI
760 770 780 790 800
LTLTTNEEYL DLSAPLEQYS PSFPDSSCSA SSSSGDDSVF SPDPMPHDPC
810
LPKFQHVNGV VKT
Length:813
Mass (Da):91,340
Last modified:June 1, 1994 - v1
Checksum:i815436569892A565
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X65943 mRNA. Translation: CAA46758.1.
PIRiA49123.
UniGeneiXl.16135.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X65943 mRNA. Translation: CAA46758.1 .
PIRi A49123.
UniGenei Xl.16135.

3D structure databases

ProteinModelPortali Q03364.
SMRi Q03364. Positions 141-353, 458-755.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q03364.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

Xenbasei XB-GENE-1018301. fgfr2.

Phylogenomic databases

HOVERGENi HBG000345.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 6726.

Family and domain databases

Gene3Di 2.60.40.10. 3 hits.
InterProi IPR028175. FGF_rcpt_2.
IPR016248. FGF_rcpt_fam.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
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 ]
PANTHERi PTHR24416:SF130. PTHR24416:SF130. 1 hit.
Pfami PF07679. I-set. 2 hits.
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. "Spatially restricted expression of fibroblast growth factor receptor-2 during Xenopus development."
    Friesel R., Brown S.A.N.
    Development 116:1051-1058(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiFGFR2_XENLA
AccessioniPrimary (citable) accession number: Q03364
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 29, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3