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Protein

Fibroblast growth factor receptor 1

Gene

Fgfr1

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 embryonic development, cell proliferation, differentiation and migration. Required for normal mesoderm patterning and correct axial organization during embryonic development, normal skeletogenesis and normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. 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 IL17RD/SEF, and by FGFR1 ubiquitination, internalization and degradation (By similarity).By similarity6 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 sequential autophosphorylation on tyrosine residues (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei514 – 5141ATPPROSITE-ProRule annotation
Binding sitei568 – 5681ATPPROSITE-ProRule annotation
Active sitei623 – 6231Proton acceptorPROSITE-ProRule annotation
Binding sitei627 – 6271ATPPROSITE-ProRule annotation
Binding sitei641 – 6411ATPPROSITE-ProRule annotation
Sitei766 – 7661Mediates interaction with PLCG1 and SHBBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi484 – 4907ATPPROSITE-ProRule annotation
Nucleotide bindingi562 – 5643ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • angiogenesis Source: MGI
  • auditory receptor cell development Source: MGI
  • blood vessel morphogenesis Source: MGI
  • brain development Source: MGI
  • branching involved in salivary gland morphogenesis Source: MGI
  • cell maturation Source: MGI
  • chondrocyte differentiation Source: MGI
  • embryonic limb morphogenesis Source: MGI
  • fibroblast growth factor receptor signaling pathway Source: MGI
  • fibroblast growth factor receptor signaling pathway involved in orbitofrontal cortex development Source: UniProtKB
  • generation of neurons Source: MGI
  • inner ear morphogenesis Source: MGI
  • in utero embryonic development Source: MGI
  • lung-associated mesenchyme development Source: MGI
  • lung development Source: MGI
  • mesenchymal cell differentiation Source: MGI
  • midbrain development Source: MGI
  • middle ear morphogenesis Source: MGI
  • motogenic signaling involved in postnatal olfactory bulb interneuron migration Source: Ensembl
  • negative regulation of fibroblast growth factor production Source: MGI
  • negative regulation of gene expression Source: MGI
  • negative regulation of osteoblast differentiation Source: Ensembl
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • neuron projection development Source: Ensembl
  • orbitofrontal cortex development Source: UniProtKB
  • organ induction Source: MGI
  • outer ear morphogenesis Source: MGI
  • paraxial mesoderm development Source: MGI
  • peptidyl-tyrosine phosphorylation Source: UniProtKB
  • positive regulation of cardiac muscle cell proliferation Source: MGI
  • positive regulation of cell cycle Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of endothelial cell chemotaxis to fibroblast growth factor Source: MGI
  • positive regulation of MAPK cascade Source: MGI
  • positive regulation of MAP kinase activity Source: UniProtKB
  • positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway Source: MGI
  • positive regulation of mesenchymal cell proliferation Source: MGI
  • positive regulation of mitotic cell cycle DNA replication Source: MGI
  • positive regulation of neuron differentiation Source: UniProtKB
  • positive regulation of neuron projection development Source: MGI
  • positive regulation of parathyroid hormone secretion Source: MGI
  • positive regulation of phospholipase C activity Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling Source: MGI
  • regulation of cell proliferation Source: MGI
  • regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  • regulation of gene expression Source: MGI
  • regulation of lateral mesodermal cell fate specification Source: MGI
  • regulation of phosphorus metabolic process Source: MGI
  • regulation of sensory perception of pain Source: Ensembl
  • salivary gland morphogenesis Source: MGI
  • sensory perception of sound Source: MGI
  • stem cell population maintenance Source: Ensembl
  • ureteric bud development Source: MGI
  • vacuolar phosphate transport Source: MGI
  • vasculogenesis involved in coronary vascular morphogenesis Source: DFLAT
  • ventricular zone neuroblast division Source: UniProtKB
  • vitamin D3 metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Heparin-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiR-MMU-109704. PI3K Cascade.
R-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-190370. FGFR1b ligand binding and activation.
R-MMU-190373. FGFR1c ligand binding and activation.
R-MMU-190374. FGFR1c and Klotho ligand binding and activation.
R-MMU-445144. Signal transduction by L1.
R-MMU-5654219. Phospholipase C-mediated cascade: FGFR1.
R-MMU-5654687. Downstream signaling of activated FGFR1.
R-MMU-5654688. SHC-mediated cascade:FGFR1.
R-MMU-5654689. PI-3K cascade:FGFR1.
R-MMU-5654693. FRS-mediated FGFR1 signaling.
R-MMU-5654726. Negative regulation of FGFR1 signaling.
R-MMU-5673001. RAF/MAP kinase cascade.
R-MMU-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibroblast growth factor receptor 1 (EC:2.7.10.1By similarity)
Short name:
FGFR-1
Short name:
bFGF-R-1
Alternative name(s):
Basic fibroblast growth factor receptor 1
MFR
Proto-oncogene c-Fgr
CD_antigen: CD331
Gene namesi
Name:Fgfr1
Synonyms:Flg
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:95522. Fgfr1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 376355ExtracellularSequence analysisAdd
BLAST
Transmembranei377 – 39721HelicalSequence analysisAdd
BLAST
Topological domaini398 – 822425CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality around gastrulation, due to growth defects during early embryonic development and aberrant mesoderm patterning.2 Publications

Chemistry

ChEMBLiCHEMBL2111391.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 822801Fibroblast growth factor receptor 1PRO_0000016781Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi55 ↔ 101PROSITE-ProRule annotation
Glycosylationi77 – 771N-linked (GlcNAc...)Sequence analysis
Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence analysis
Disulfide bondi178 ↔ 230PROSITE-ProRule annotation
Glycosylationi227 – 2271N-linked (GlcNAc...)Sequence analysis
Glycosylationi240 – 2401N-linked (GlcNAc...)Sequence analysis
Glycosylationi264 – 2641N-linked (GlcNAc...)Sequence analysis
Disulfide bondi277 ↔ 341PROSITE-ProRule annotation
Glycosylationi296 – 2961N-linked (GlcNAc...)Sequence analysis
Glycosylationi317 – 3171N-linked (GlcNAc...)1 Publication
Glycosylationi330 – 3301N-linked (GlcNAc...)Sequence analysis
Modified residuei463 – 4631Phosphotyrosine; by autocatalysisBy similarity
Modified residuei583 – 5831Phosphotyrosine; by autocatalysisBy similarity
Modified residuei585 – 5851Phosphotyrosine; by autocatalysisBy similarity
Modified residuei653 – 6531Phosphotyrosine; by autocatalysisBy similarity
Modified residuei654 – 6541Phosphotyrosine; by autocatalysisBy similarity
Modified residuei730 – 7301Phosphotyrosine; by autocatalysisBy similarity
Modified residuei766 – 7661Phosphotyrosine; 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. Initial autophosphorylation at Tyr-653 increases the kinase activity by a factor of 50 to 100. After this, Tyr-583 becomes phosphorylated, followed by phosphorylation of Tyr-463, Tyr-766, Tyr-583 and Tyr-585. In a third stage, Tyr-654 is autophosphorylated, resulting in a further tenfold increase of kinase activity. 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 by NEDD4 after autophosphorylation, leading to internalization and lysosomal degradation. CBL is recruited to activated FGFR1 via FRS2 and GRB2, and mediates ubiquitination and subsequent degradation of FGFR1 (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.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP16092.
PaxDbiP16092.
PeptideAtlasiP16092.
PRIDEiP16092.

PTM databases

iPTMnetiP16092.
PhosphoSiteiP16092.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSMUSG00000031565.
CleanExiMM_FGFR1.
MM_FLG.
ExpressionAtlasiP16092. baseline and differential.
GenevisibleiP16092. MM.

Interactioni

Subunit structurei

Monomer. Homodimer after ligand binding. Interacts predominantly with FGF1 and FGF2, but can also interact with FGF3, FGF4, FGF5, FGF6, FGF8, FGF10, FGF19, FGF21, FGF22 and FGF23 (in vitro) (PubMed:10821861, PubMed:1309590, PubMed:17086194). 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, FGF21 and FGF23. Interacts (phosphorylated on Tyr-766) with PLCG1 (via SH2 domains). Interacts with FRS2. Interacts with RPS6KA1. Interacts (via C-terminus) with NEDD4 (via WW3 domain). Interacts with KL (PubMed:17086194). Interacts with SHB (via SH2 domain) (PubMed:12181353). Interacts with GRB10 (By similarity). Interacts with ANOS1; this interaction does not interfere with FGF2-binding to FGFR1, but prevents binding of heparin-bound FGF2 (By similarity). Interacts with SOX2 and SOX3 (PubMed:17728342). Interacts with FLRT1, FLRT2 and FLRT3 (PubMed:16872596). Found in a ternary complex with FGF1 and ITGAV:ITGB3 (By similarity).By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ncam1P135962EBI-7953898,EBI-916499From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199656. 7 interactions.
DIPiDIP-6033N.
IntActiP16092. 6 interactions.
MINTiMINT-2635590.
STRINGi10090.ENSMUSP00000081041.

Chemistry

BindingDBiP16092.

Structurei

Secondary structure

1
822
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi43 – 453Combined sources
Beta strandi51 – 544Combined sources
Beta strandi57 – 604Combined sources
Beta strandi63 – 686Combined sources
Beta strandi77 – 815Combined sources
Beta strandi83 – 908Combined sources
Helixi93 – 953Combined sources
Beta strandi96 – 10510Combined sources
Beta strandi108 – 11811Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CKNNMR-A25-119[»]
ProteinModelPortaliP16092.
SMRiP16092. Positions 25-119, 147-397, 420-801.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16092.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 11995Ig-like C2-type 1Add
BLAST
Domaini158 – 24689Ig-like C2-type 2Add
BLAST
Domaini255 – 357103Ig-like C2-type 3Add
BLAST
Domaini478 – 767290Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni160 – 17718Heparin-bindingAdd
BLAST

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

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118923.
HOGENOMiHOG000263410.
HOVERGENiHBG000345.
InParanoidiP16092.
KOiK04362.
PhylomeDBiP16092.
TreeFamiTF316307.

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. 2 hits.
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]

Sequences (6)i

Sequence statusi: Complete.

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

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P16092-1) [UniParc]FASTAAdd to basket
Also known as: FGFR1-IIIc, Long

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
MWGWKCLLFW AVLVTATLCT ARPAPTLPEQ AQPWGVPVEV ESLLVHPGDL
60 70 80 90 100
LQLRCRLRDD VQSINWLRDG VQLVESNRTR ITGEEVEVRD SIPADSGLYA
110 120 130 140 150
CVTSSPSGSD TTYFSVNVSD ALPSSEDDDD DDDSSSEEKE TDNTKPNRRP
160 170 180 190 200
VAPYWTSPEK MEKKLHAVPA AKTVKFKCPS SGTPNPTLRW LKNGKEFKPD
210 220 230 240 250
HRIGGYKVRY ATWSIIMDSV VPSDKGNYTC IVENEYGSIN HTYQLDVVER
260 270 280 290 300
SPHRPILQAG LPANKTVALG SNVEFMCKVY SDPQPHIQWL KHIEVNGSKI
310 320 330 340 350
GPDNLPYVQI LKTAGVNTTD KEMEVLHLRN VSFEDAGEYT CLAGNSIGLS
360 370 380 390 400
HHSAWLTVLE ALEERPAVMT SPLYLEIIIY CTGAFLISCM LGSVIIYKMK
410 420 430 440 450
SGTKKSDFHS QMAVHKLAKS IPLRRQVTVS ADSSASMNSG VLLVRPSRLS
460 470 480 490 500
SSGTPMLAGV SEYELPEDPR WELPRDRLVL GKPLGEGCFG QVVLAEAIGL
510 520 530 540 550
DKDKPNRVTK VAVKMLKSDA TEKDLSDLIS EMEMMKMIGK HKNIINLLGA
560 570 580 590 600
CTQDGPLYVI VEYASKGNLR EYLQARRPPG LEYCYNPSHN PEEQLSSKDL
610 620 630 640 650
VSCAYQVARG MEYLASKKCI HRDLAARNVL VTEDNVMKIA DFGLARDIHH
660 670 680 690 700
IDYYKKTTNG RLPVKWMAPE ALFDRIYTHQ SDVWSFGVLL WEIFTLGGSP
710 720 730 740 750
YPGVPVEELF KLLKEGHRMD KPSNCTNELY MMMRDCWHAV PSQRPTFKQL
760 770 780 790 800
VEDLDRIVAL TSNQEYLDLS IPLDQYSPSF PDTRSSTCSS GEDSVFSHEP
810 820
LPEEPCLPRH PTQLANSGLK RR
Length:822
Mass (Da):91,981
Last modified:May 1, 1991 - v2
Checksum:iD5A4695FA680926B
GO
Isoform 2 (identifier: P16092-2) [UniParc]FASTAAdd to basket
Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     31-119: Missing.

Show »
Length:733
Mass (Da):82,211
Checksum:i50E95FE644692528
GO
Isoform 3 (identifier: P16092-3) [UniParc]FASTAAdd to basket
Also known as: Variant

The sequence of this isoform differs from the canonical sequence as follows:
     30-30: Q → QGSSSWPLWVAAA
     148-149: Missing.

Show »
Length:832
Mass (Da):92,882
Checksum:iCD67254989FA0D33
GO
Isoform 4 (identifier: P16092-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     31-119: Missing.
     148-149: Missing.

Show »
Length:731
Mass (Da):81,899
Checksum:i2E88793289A97818
GO
Isoform 5 (identifier: P16092-5) [UniParc]FASTAAdd to basket
Also known as: FGFR1-IIIb

The sequence of this isoform differs from the canonical sequence as follows:
     31-119: Missing.
     148-149: Missing.
     313-323: TAGVNTTDKEM → HSGINSSDA
     327-336: HLRNVSFEDA → TLFNVTEAQS
     340-352: TCLAGNSIGLSHH → VCKVSNYIGEANQ
     359-360: LE → TRPVAK

Show »
Length:733
Mass (Da):82,067
Checksum:iC3B28DB146613C31
GO
Isoform 6 (identifier: P16092-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     148-149: Missing.

Show »
Length:820
Mass (Da):91,669
Checksum:i58319BDB3EEA9D34
GO

Sequence cautioni

The sequence AAB32845 differs from that shown.Proposes two coding sequences for the same mRNA.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti229 – 2291T → S in AAA37622 (PubMed:2161540).Curated
Sequence conflicti256 – 2583ILQ → HPS in AAA37290 (PubMed:1689490).Curated
Sequence conflicti256 – 2583ILQ → HPS in AAA37620 (PubMed:1708247).Curated
Sequence conflicti265 – 2651K → E in AAC52183 (PubMed:7897669).Curated
Sequence conflicti270 – 2701G → A in AAA37622 (PubMed:2161540).Curated
Sequence conflicti387 – 3871I → M in AAA37620 (PubMed:1708247).Curated
Sequence conflicti440 – 4401G → A in CAA36175 (PubMed:2161096).Curated
Sequence conflicti457 – 4571L → P in AAC52183 (PubMed:7897669).Curated
Sequence conflicti508 – 5081V → L in AAA37620 (PubMed:1708247).Curated
Sequence conflicti544 – 5441I → M in AAA37622 (PubMed:2161540).Curated
Sequence conflicti549 – 5491G → E in AAF05312 (PubMed:10821861).Curated
Sequence conflicti753 – 7531D → V in AAF05312 (PubMed:10821861).Curated
Sequence conflicti756 – 7561R → H in AAA37290 (PubMed:1689490).Curated
Sequence conflicti763 – 7631N → S in AAC52183 (PubMed:7897669).Curated
Sequence conflicti765 – 7651E → D in AAA37622 (PubMed:2161540).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei30 – 301Q → QGSSSWPLWVAAA in isoform 3. 1 PublicationVSP_002961
Alternative sequencei31 – 11989Missing in isoform 2, isoform 4 and isoform 5. 5 PublicationsVSP_002962Add
BLAST
Alternative sequencei148 – 1492Missing in isoform 3, isoform 4, isoform 5 and isoform 6. 4 PublicationsVSP_002963
Alternative sequencei313 – 32311TAGVNTTDKEM → HSGINSSDA in isoform 5. 1 PublicationVSP_041919Add
BLAST
Alternative sequencei327 – 33610HLRNVSFEDA → TLFNVTEAQS in isoform 5. 1 PublicationVSP_041920
Alternative sequencei340 – 35213TCLAG…GLSHH → VCKVSNYIGEANQ in isoform 5. 1 PublicationVSP_041921Add
BLAST
Alternative sequencei359 – 3602LE → TRPVAK in isoform 5. 1 PublicationVSP_041922

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28998 mRNA. Translation: AAA37290.1.
X51893 mRNA. Translation: CAA36175.1.
M65053 mRNA. Translation: AAA37620.1.
M33760 mRNA. Translation: AAA37622.1.
U23445 mRNA. Translation: AAC52183.1.
AF176552 mRNA. Translation: AAF05312.1.
AK028354 mRNA. Translation: BAC25899.1.
S74765 mRNA. Translation: AAB32845.1. Sequence problems.
AC160526 Genomic DNA. No translation available.
BC033447 mRNA. Translation: AAH33447.1.
CCDSiCCDS40304.1. [P16092-2]
CCDS52526.1. [P16092-1]
CCDS57614.1. [P16092-6]
PIRiA34849. TVMSFG.
B42057.
I49293.
JH0393.
RefSeqiNP_001073377.1. NM_001079908.2. [P16092-6]
NP_001073378.1. NM_001079909.2. [P16092-2]
NP_034336.2. NM_010206.3. [P16092-1]
XP_006509073.1. XM_006509010.2. [P16092-1]
XP_006509075.1. XM_006509012.1. [P16092-1]
XP_011240423.1. XM_011242121.1. [P16092-4]
UniGeneiMm.265716.

Genome annotation databases

EnsembliENSMUST00000084027; ENSMUSP00000081041; ENSMUSG00000031565. [P16092-1]
ENSMUST00000117179; ENSMUSP00000113909; ENSMUSG00000031565. [P16092-6]
ENSMUST00000119398; ENSMUSP00000113855; ENSMUSG00000031565. [P16092-2]
ENSMUST00000167764; ENSMUSP00000131343; ENSMUSG00000031565. [P16092-5]
ENSMUST00000178276; ENSMUSP00000137515; ENSMUSG00000031565. [P16092-5]
GeneIDi14182.
KEGGimmu:14182.
UCSCiuc009lfy.2. mouse. [P16092-1]
uc009lga.2. mouse. [P16092-2]
uc033jet.1. mouse. [P16092-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28998 mRNA. Translation: AAA37290.1.
X51893 mRNA. Translation: CAA36175.1.
M65053 mRNA. Translation: AAA37620.1.
M33760 mRNA. Translation: AAA37622.1.
U23445 mRNA. Translation: AAC52183.1.
AF176552 mRNA. Translation: AAF05312.1.
AK028354 mRNA. Translation: BAC25899.1.
S74765 mRNA. Translation: AAB32845.1. Sequence problems.
AC160526 Genomic DNA. No translation available.
BC033447 mRNA. Translation: AAH33447.1.
CCDSiCCDS40304.1. [P16092-2]
CCDS52526.1. [P16092-1]
CCDS57614.1. [P16092-6]
PIRiA34849. TVMSFG.
B42057.
I49293.
JH0393.
RefSeqiNP_001073377.1. NM_001079908.2. [P16092-6]
NP_001073378.1. NM_001079909.2. [P16092-2]
NP_034336.2. NM_010206.3. [P16092-1]
XP_006509073.1. XM_006509010.2. [P16092-1]
XP_006509075.1. XM_006509012.1. [P16092-1]
XP_011240423.1. XM_011242121.1. [P16092-4]
UniGeneiMm.265716.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CKNNMR-A25-119[»]
ProteinModelPortaliP16092.
SMRiP16092. Positions 25-119, 147-397, 420-801.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199656. 7 interactions.
DIPiDIP-6033N.
IntActiP16092. 6 interactions.
MINTiMINT-2635590.
STRINGi10090.ENSMUSP00000081041.

Chemistry

BindingDBiP16092.
ChEMBLiCHEMBL2111391.

PTM databases

iPTMnetiP16092.
PhosphoSiteiP16092.

Proteomic databases

MaxQBiP16092.
PaxDbiP16092.
PeptideAtlasiP16092.
PRIDEiP16092.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000084027; ENSMUSP00000081041; ENSMUSG00000031565. [P16092-1]
ENSMUST00000117179; ENSMUSP00000113909; ENSMUSG00000031565. [P16092-6]
ENSMUST00000119398; ENSMUSP00000113855; ENSMUSG00000031565. [P16092-2]
ENSMUST00000167764; ENSMUSP00000131343; ENSMUSG00000031565. [P16092-5]
ENSMUST00000178276; ENSMUSP00000137515; ENSMUSG00000031565. [P16092-5]
GeneIDi14182.
KEGGimmu:14182.
UCSCiuc009lfy.2. mouse. [P16092-1]
uc009lga.2. mouse. [P16092-2]
uc033jet.1. mouse. [P16092-4]

Organism-specific databases

CTDi2260.
MGIiMGI:95522. Fgfr1.

Phylogenomic databases

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118923.
HOGENOMiHOG000263410.
HOVERGENiHBG000345.
InParanoidiP16092.
KOiK04362.
PhylomeDBiP16092.
TreeFamiTF316307.

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiR-MMU-109704. PI3K Cascade.
R-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-190370. FGFR1b ligand binding and activation.
R-MMU-190373. FGFR1c ligand binding and activation.
R-MMU-190374. FGFR1c and Klotho ligand binding and activation.
R-MMU-445144. Signal transduction by L1.
R-MMU-5654219. Phospholipase C-mediated cascade: FGFR1.
R-MMU-5654687. Downstream signaling of activated FGFR1.
R-MMU-5654688. SHC-mediated cascade:FGFR1.
R-MMU-5654689. PI-3K cascade:FGFR1.
R-MMU-5654693. FRS-mediated FGFR1 signaling.
R-MMU-5654726. Negative regulation of FGFR1 signaling.
R-MMU-5673001. RAF/MAP kinase cascade.
R-MMU-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.

Miscellaneous databases

ChiTaRSiFgfr1. mouse.
EvolutionaryTraceiP16092.
PROiP16092.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031565.
CleanExiMM_FGFR1.
MM_FLG.
ExpressionAtlasiP16092. baseline and differential.
GenevisibleiP16092. MM.

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. 2 hits.
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_MOUSE
AccessioniPrimary (citable) accession number: P16092
Secondary accession number(s): E9Q2P4
, Q01736, Q60830, Q61562, Q80T10, Q8CFK8, Q9QZM7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: May 1, 1991
Last modified: September 7, 2016
This is version 186 of the entry and version 2 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.