Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 214 (22 Apr 2020)
Sequence version 2 (01 May 1991)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Fibroblast growth factor receptor 1

Gene

Fgfr1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei514ATPPROSITE-ProRule annotation1
Binding sitei568ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei623Proton acceptorPROSITE-ProRule annotation1
Binding sitei627ATPPROSITE-ProRule annotation1
Binding sitei641ATPPROSITE-ProRule annotation1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei766Mediates interaction with PLCG1 and SHBBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi484 – 490ATPPROSITE-ProRule annotation7
Nucleotide bindingi562 – 564ATPPROSITE-ProRule annotation3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHeparin-binding, Kinase, Receptor, Transferase, Tyrosine-protein kinase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.10.1 3474

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-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

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Fgfr1
Synonyms:Flg
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 8

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:95522 Fgfr1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini22 – 376ExtracellularSequence analysisAdd BLAST355
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei377 – 397HelicalSequence analysisAdd BLAST21
Topological domaini398 – 822CytoplasmicSequence analysisAdd BLAST425

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3960

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 21Sequence analysisAdd BLAST21
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001678122 – 822Fibroblast growth factor receptor 1Add BLAST801

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi55 ↔ 101PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi77N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi117N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi178 ↔ 230PROSITE-ProRule annotation
Glycosylationi227N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi240N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi264N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi277 ↔ 341PROSITE-ProRule annotation
Glycosylationi296N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi317N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi330N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P16092

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P16092

PeptideAtlas

More...
PeptideAtlasi
P16092

PRoteomics IDEntifications database

More...
PRIDEi
P16092

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
2314

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P16092

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P16092

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000031565 Expressed in decidua and 402 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P16092 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P16092 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
199656, 22 interactors

Database of interacting proteins

More...
DIPi
DIP-6033N

Protein interaction database and analysis system

More...
IntActi
P16092, 11 interactors

Molecular INTeraction database

More...
MINTi
P16092

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000081041

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P16092

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P16092 protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1822
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P16092

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P16092

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>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
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni160 – 177Heparin-bindingAdd BLAST18

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0200 Eukaryota
COG0515 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155860

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000288_74_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P16092

KEGG Orthology (KO)

More...
KOi
K04362

Identification of Orthologs from Complete Genome Data

More...
OMAi
KVRDHMW

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P16092

TreeFam database of animal gene trees

More...
TreeFami
TF316307

Family and domain databases

Conserved Domains Database

More...
CDDi
cd05098 PTKc_FGFR1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 3 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR028174 FGF_rcpt_1
IPR016248 FGF_rcpt_fam
IPR041159 FGFR_TM
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR013098 Ig_I-set
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR013151 Immunoglobulin
IPR011009 Kinase-like_dom_sf
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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF18123 FGFR3_TM, 1 hit
PF07679 I-set, 2 hits
PF00047 ig, 1 hit
PF07714 Pkinase_Tyr, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000628 FGFR, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00409 IG, 3 hits
SM00408 IGc2, 3 hits
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48726 SSF48726, 3 hits
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50835 IG_LIKE, 3 hits
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (6+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 6 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 6 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

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

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
J3QN85J3QN85_MOUSE
Fibroblast growth factor receptor
Fgfr1
833Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A1B0GSZ6A0A1B0GSZ6_MOUSE
Fibroblast growth factor receptor 1
Fgfr1
300Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
D3Z4V6D3Z4V6_MOUSE
Fibroblast growth factor receptor 1
Fgfr1
104Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A1B0GSQ7A0A1B0GSQ7_MOUSE
Fibroblast growth factor receptor 1
Fgfr1
86Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
D3YW77D3YW77_MOUSE
Fibroblast growth factor receptor 1
Fgfr1
50Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A1B0GSD9A0A1B0GSD9_MOUSE
Fibroblast growth factor receptor 1
Fgfr1
47Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>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
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS40304.1 [P16092-2]
CCDS52526.1 [P16092-1]
CCDS57614.1 [P16092-6]

Protein sequence database of the Protein Information Resource

More...
PIRi
A34849 TVMSFG
B42057
I49293
JH0393

NCBI Reference Sequences

More...
RefSeqi
NP_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
XP_006509075.1, XM_006509012.1
XP_011240423.1, XM_011242121.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000084027; ENSMUSP00000081041; ENSMUSG00000031565 [P16092-1]
ENSMUST00000117179; ENSMUSP00000113909; ENSMUSG00000031565 [P16092-6]
ENSMUST00000119398; ENSMUSP00000113855; ENSMUSG00000031565 [P16092-2]
ENSMUST00000167764; ENSMUSP00000131343; ENSMUSG00000031565 [P16092-5]
ENSMUST00000178276; ENSMUSP00000137515; ENSMUSG00000031565 [P16092-5]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
14182

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:14182

UCSC genome browser

More...
UCSCi
uc009lfy.2 mouse [P16092-1]
uc009lga.2 mouse [P16092-2]
uc033jet.1 mouse [P16092-4]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
XP_006509075.1, XM_006509012.1
XP_011240423.1, XM_011242121.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CKNNMR-A25-119[»]
SMRiP16092
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi199656, 22 interactors
DIPiDIP-6033N
IntActiP16092, 11 interactors
MINTiP16092
STRINGi10090.ENSMUSP00000081041

Chemistry databases

BindingDBiP16092
ChEMBLiCHEMBL3960

PTM databases

GlyConnecti2314
iPTMnetiP16092
PhosphoSitePlusiP16092

Proteomic databases

MaxQBiP16092
PaxDbiP16092
PeptideAtlasiP16092
PRIDEiP16092

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
11015 2306 antibodies

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

Comparative Toxicogenomics Database

More...
CTDi
2260
MGIiMGI:95522 Fgfr1

Phylogenomic databases

eggNOGiKOG0200 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000155860
HOGENOMiCLU_000288_74_1_1
InParanoidiP16092
KOiK04362
OMAiKVRDHMW
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

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Fgfr1 mouse
EvolutionaryTraceiP16092

Protein Ontology

More...
PROi
PR:P16092
RNActiP16092 protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000031565 Expressed in decidua and 402 other tissues
ExpressionAtlasiP16092 baseline and differential
GenevisibleiP16092 MM

Family and domain databases

CDDicd05098 PTKc_FGFR1, 1 hit
Gene3Di2.60.40.10, 3 hits
InterProiView protein in InterPro
IPR028174 FGF_rcpt_1
IPR016248 FGF_rcpt_fam
IPR041159 FGFR_TM
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR013098 Ig_I-set
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR013151 Immunoglobulin
IPR011009 Kinase-like_dom_sf
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
PfamiView protein in Pfam
PF18123 FGFR3_TM, 1 hit
PF07679 I-set, 2 hits
PF00047 ig, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PIRSFiPIRSF000628 FGFR, 1 hit
PRINTSiPR00109 TYRKINASE
SMARTiView protein in SMART
SM00409 IG, 3 hits
SM00408 IGc2, 3 hits
SM00219 TyrKc, 1 hit
SUPFAMiSSF48726 SSF48726, 3 hits
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50835 IG_LIKE, 3 hits
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFGFR1_MOUSE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P16092
Secondary accession number(s): E9Q2P4
, Q01736, Q60830, Q61562, Q80T10, Q8CFK8, Q9QZM7
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: May 1, 1991
Last modified: April 22, 2020
This is version 214 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  2. SIMILARITY comments
    Index of protein domains and families
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again