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Protein

Fibroblast growth factor receptor 1

Gene

FGFR1

Organism
Pleurodeles waltl (Iberian ribbed newt)
Status
Reviewed-Annotation score: 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 embryonic development, cell proliferation, differentiation and migration. Required for normal mesoderm patterning and normal skeletogenesis. Phosphorylates PLCG1, FRS2, GAB1 and SHB. 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. Promotes phosphorylation of SHC1, STAT1 and PTPN11/SHP2. In the nucleus, enhances RPS6KA1 and CREB1 activity and contributes to the regulation of transcription. FGFR1 signaling is down-regulated by ubiquitination, internalization and degradation (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 sequential autophosphorylation on tyrosine residues (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei510 – 5101ATPPROSITE-ProRule annotation
Binding sitei564 – 5641ATPPROSITE-ProRule annotation
Active sitei619 – 6191Proton acceptorPROSITE-ProRule annotation
Binding sitei623 – 6231ATPPROSITE-ProRule annotation
Binding sitei637 – 6371ATPPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi480 – 4867ATPPROSITE-ProRule annotation
Nucleotide bindingi558 – 5603ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fibroblast growth factor receptor 1 (EC:2.7.10.1)
Short name:
FGFR-1
Alternative name(s):
PFR1
Gene namesi
Name:FGFR1
OrganismiPleurodeles waltl (Iberian ribbed newt)
Taxonomic identifieri8319 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaCaudataSalamandroideaSalamandridaePleurodelinaePleurodeles

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 374351ExtracellularSequence analysisAdd
BLAST
Transmembranei375 – 39521HelicalSequence analysisAdd
BLAST
Topological domaini396 – 816421CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 816793Fibroblast growth factor receptor 1PRO_0000249216Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 100PROSITE-ProRule annotation
Glycosylationi76 – 761N-linked (GlcNAc...)Sequence analysis
Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence analysis
Disulfide bondi176 ↔ 228PROSITE-ProRule annotation
Glycosylationi238 – 2381N-linked (GlcNAc...)Sequence analysis
Glycosylationi262 – 2621N-linked (GlcNAc...)Sequence analysis
Disulfide bondi275 ↔ 339PROSITE-ProRule annotation
Glycosylationi294 – 2941N-linked (GlcNAc...)Sequence analysis
Glycosylationi315 – 3151N-linked (GlcNAc...)Sequence analysis
Glycosylationi328 – 3281N-linked (GlcNAc...)Sequence analysis
Modified residuei459 – 4591Phosphotyrosine; by autocatalysisBy similarity
Modified residuei579 – 5791Phosphotyrosine; by autocatalysisBy similarity
Modified residuei581 – 5811Phosphotyrosine; by autocatalysisBy similarity
Modified residuei649 – 6491Phosphotyrosine; by autocatalysisBy similarity
Modified residuei650 – 6501Phosphotyrosine; by autocatalysisBy similarity
Modified residuei726 – 7261Phosphotyrosine; by autocatalysisBy similarity
Modified residuei762 – 7621Phosphotyrosine; 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 and proceeds in a highly ordered manner. Phosphotyrosine residues provide docking sites for interacting proteins and so are crucial for FGFR1 function and its regulation (By similarity).By similarity
Ubiquitinated. FGFR1 is rapidly ubiquitinated after autophosphorylation, leading to internalization and degradation (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

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ91285.

Expressioni

Developmental stagei

Maternally derived transcript whose level of expression remains constant during early developmental stages or early gastrula. At tail-bud stage, transcripts are localized primarily to the neural and mesodermal tissues.1 Publication

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ91285.
SMRiQ91285. Positions 32-123, 148-357, 460-761.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 11894Ig-like C2-type 1Add
BLAST
Domaini156 – 24489Ig-like C2-type 2Add
BLAST
Domaini253 – 355103Ig-like C2-type 3Add
BLAST
Domaini474 – 763290Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi126 – 1316Poly-Asp
Compositional biasi429 – 4357Poly-Ser

Domaini

The second and third Ig-like domains directly interact with fibroblast growth factors (FGF) and heparan sulfate proteoglycans. Isoforms lacking the first Ig-like domain have higher affinity for fibroblast growth factors (FGF) and heparan sulfate proteoglycans than isoforms with all three Ig-like domains (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

HOVERGENiHBG000345.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR028174. FGF_rcpt_1.
IPR016248. FGF_rcpt_fam.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
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:SF131. PTHR24416:SF131. 1 hit.
PfamiPF07679. I-set. 1 hit.
PF00047. ig. 1 hit.
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]

Sequencei

Sequence statusi: Complete.

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

Q91285-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSWRHLVFW AMLVMATLSA ARPAPTLPEQ VSPKAKVEVE SYSAHHGDLL
60 70 80 90 100
QLRCRLRDDV HSINWEKDGV QLAETNRTRI TGAEVEVRDA VQEDSGLYAC
110 120 130 140 150
MTHRPSGTET TFFAVNVSDR IPSVEDDDDD DEKSSSEEKE AENSKPNPVA
160 170 180 190 200
PFWAHPEKME KKLHAVPAAK TVKFRCPAGG TPSPTLRWLK NGKEFKPDHR
210 220 230 240 250
IGGYKVRYQT WSIIMDSVVP SDKGPYTCLV ENNYGSINHT YQLDVVERSP
260 270 280 290 300
HRPILQAGLP ANQTVPVGSN VDFVCKVYSD PQPHIQWLKH VTVNGSKYGS
310 320 330 340 350
DGLPLVQVLK AAGVNTTDKE MEVLHLRNVS FEDAWEYTCL AGNSIGISHH
360 370 380 390 400
SAWLTVVEAI SENPVIMTSP LYLEIIIYCT GAFLISCMLV TVIIYKMKNT
410 420 430 440 450
TKKTDFNSQP AVHKLAKSFP LQRQVSADSS SSMSSGVMLV RPSRLSSSGS
460 470 480 490 500
PMLTGVSEYE LPEDPRWEFS RDRLILGKPL GEGCFGQVVM GEAIGLDKEK
510 520 530 540 550
PNRVTKVAVK MLKSDATEKD LSDLISEMEM MKMIGKHKNI INLLGACTQD
560 570 580 590 600
GPLYVIVEYA SKGNLREYLR ARRPPGMEYC YNPIHVSKDM LSFKDLVSCA
610 620 630 640 650
YQVARGMEYL ASKKCIHRDL AARNVLVTED SVMKIADFGL ARDIHHIDYY
660 670 680 690 700
KKTTNGRLPV KWMAPEALFD RIYTHQSDVW SFGVLLWEIF TLGGSPYPGV
710 720 730 740 750
PVEELFKLLK EGHRMDKPGN CTNELYMMMR DCWHAVPSQR PTFKQLVEDL
760 770 780 790 800
DRIVAMTSNQ EYLDLSMPVD QYSPGFPDTR SSTCSSGEDS VFSHDPLPDE
810
PCLPKYQHAN GGLKKR
Length:816
Mass (Da):91,548
Last modified:November 1, 1996 - v1
Checksum:i91A7E16EE25256A6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59380 mRNA. Translation: CAA42023.1.
PIRiA49151.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59380 mRNA. Translation: CAA42023.1.
PIRiA49151.

3D structure databases

ProteinModelPortaliQ91285.
SMRiQ91285. Positions 32-123, 148-357, 460-761.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ91285.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG000345.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR028174. FGF_rcpt_1.
IPR016248. FGF_rcpt_fam.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
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:SF131. PTHR24416:SF131. 1 hit.
PfamiPF07679. I-set. 1 hit.
PF00047. ig. 1 hit.
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 nameiFGFR1_PLEWA
AccessioniPrimary (citable) accession number: Q91285
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 95 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

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.