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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)DescriptionActionsGraphical viewLength
Binding sitei514ATPPROSITE-ProRule annotation1
Binding sitei568ATPPROSITE-ProRule annotation1
Active sitei623Proton acceptorPROSITE-ProRule annotation1
Binding sitei627ATPPROSITE-ProRule annotation1
Binding sitei641ATPPROSITE-ProRule annotation1
Sitei766Mediates interaction with PLCG1 and SHBBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi484 – 490ATPPROSITE-ProRule annotation7
Nucleotide bindingi562 – 564ATPPROSITE-ProRule annotation3

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
  • negative regulation of fibroblast growth factor production Source: MGI
  • negative regulation of gene expression Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • 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
  • salivary gland morphogenesis Source: MGI
  • sensory perception of sound Source: MGI
  • 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)DescriptionActionsGraphical viewLength
Topological domaini22 – 376ExtracellularSequence analysisAdd BLAST355
Transmembranei377 – 397HelicalSequence analysisAdd BLAST21
Topological domaini398 – 822CytoplasmicSequence analysisAdd BLAST425

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 databases

ChEMBLiCHEMBL3960.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000001678122 – 822Fibroblast growth factor receptor 1Add BLAST801

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi55 ↔ 101PROSITE-ProRule annotation
Glycosylationi77N-linked (GlcNAc...)Sequence analysis1
Glycosylationi117N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi178 ↔ 230PROSITE-ProRule annotation
Glycosylationi227N-linked (GlcNAc...)Sequence analysis1
Glycosylationi240N-linked (GlcNAc...)Sequence analysis1
Glycosylationi264N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi277 ↔ 341PROSITE-ProRule annotation
Glycosylationi296N-linked (GlcNAc...)Sequence analysis1
Glycosylationi317N-linked (GlcNAc...)1 Publication1
Glycosylationi330N-linked (GlcNAc...)Sequence analysis1
Modified residuei463Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei583Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei585Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei653Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei654Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei730Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei766Phosphotyrosine; by autocatalysisBy 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 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.
PhosphoSitePlusiP16092.

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 interactors.
DIPiDIP-6033N.
IntActiP16092. 6 interactors.
MINTiMINT-2635590.
STRINGi10090.ENSMUSP00000081041.

Chemistry databases

BindingDBiP16092.

Structurei

Secondary structure

1822
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi43 – 45Combined sources3
Beta strandi51 – 54Combined sources4
Beta strandi57 – 60Combined sources4
Beta strandi63 – 68Combined sources6
Beta strandi77 – 81Combined sources5
Beta strandi83 – 90Combined sources8
Helixi93 – 95Combined sources3
Beta strandi96 – 105Combined sources10
Beta strandi108 – 118Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CKNNMR-A25-119[»]
ProteinModelPortaliP16092.
SMRiP16092.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16092.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 119Ig-like C2-type 1Add BLAST95
Domaini158 – 246Ig-like C2-type 2Add BLAST89
Domaini255 – 357Ig-like C2-type 3Add BLAST103
Domaini478 – 767Protein kinasePROSITE-ProRule annotationAdd BLAST290

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni160 – 177Heparin-bindingAdd BLAST18

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)DescriptionActionsGraphical viewLength
Sequence conflicti229T → S in AAA37622 (PubMed:2161540).Curated1
Sequence conflicti256 – 258ILQ → HPS in AAA37290 (PubMed:1689490).Curated3
Sequence conflicti256 – 258ILQ → HPS in AAA37620 (PubMed:1708247).Curated3
Sequence conflicti265K → E in AAC52183 (PubMed:7897669).Curated1
Sequence conflicti270G → A in AAA37622 (PubMed:2161540).Curated1
Sequence conflicti387I → M in AAA37620 (PubMed:1708247).Curated1
Sequence conflicti440G → A in CAA36175 (PubMed:2161096).Curated1
Sequence conflicti457L → P in AAC52183 (PubMed:7897669).Curated1
Sequence conflicti508V → L in AAA37620 (PubMed:1708247).Curated1
Sequence conflicti544I → M in AAA37622 (PubMed:2161540).Curated1
Sequence conflicti549G → E in AAF05312 (PubMed:10821861).Curated1
Sequence conflicti753D → V in AAF05312 (PubMed:10821861).Curated1
Sequence conflicti756R → H in AAA37290 (PubMed:1689490).Curated1
Sequence conflicti763N → S in AAC52183 (PubMed:7897669).Curated1
Sequence conflicti765E → D in AAA37622 (PubMed:2161540).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00296130Q → QGSSSWPLWVAAA in isoform 3. 1 Publication1
Alternative sequenceiVSP_00296231 – 119Missing in isoform 2, isoform 4 and isoform 5. 5 PublicationsAdd BLAST89
Alternative sequenceiVSP_002963148 – 149Missing in isoform 3, isoform 4, isoform 5 and isoform 6. 4 Publications2
Alternative sequenceiVSP_041919313 – 323TAGVNTTDKEM → HSGINSSDA in isoform 5. 1 PublicationAdd BLAST11
Alternative sequenceiVSP_041920327 – 336HLRNVSFEDA → TLFNVTEAQS in isoform 5. 1 Publication10
Alternative sequenceiVSP_041921340 – 352TCLAG…GLSHH → VCKVSNYIGEANQ in isoform 5. 1 PublicationAdd BLAST13
Alternative sequenceiVSP_041922359 – 360LE → TRPVAK in isoform 5. 1 Publication2

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CKNNMR-A25-119[»]
ProteinModelPortaliP16092.
SMRiP16092.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP16092.
ChEMBLiCHEMBL3960.

PTM databases

iPTMnetiP16092.
PhosphoSitePlusiP16092.

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: November 2, 2016
This is version 188 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.