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Entry version 142 (16 Oct 2019)
Sequence version 2 (07 Jul 2009)
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Protein

Fibroblast growth factor receptor 1-A

Gene

fgfr1a

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
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 normal skeletogenesis. Phosphorylates PLCG1, FRS2, GAB1 and SHB. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol-1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes phosphorylation of SHC1, STAT1 and PTPN11/SHP2. In the nucleus, enhances RPS6KA1 and CREB1 activity and contributes to the regulation of transcription. FGFR1 signaling is down-regulated by ubiquitination, internalization and degradation (By similarity).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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_section">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_section">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 sitei501ATPPROSITE-ProRule annotation1
Binding sitei555ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei610Proton acceptorPROSITE-ProRule annotation1
Binding sitei614ATPPROSITE-ProRule annotation1
Binding sitei628ATPPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi471 – 477ATPPROSITE-ProRule annotation7
Nucleotide bindingi549 – 551ATPPROSITE-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 functionKinase, Receptor, Transferase, Tyrosine-protein kinase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-DRE-109704 PI3K Cascade
R-DRE-1257604 PIP3 activates AKT signaling
R-DRE-190370 FGFR1b ligand binding and activation
R-DRE-190373 FGFR1c ligand binding and activation
R-DRE-190374 FGFR1c and Klotho ligand binding and activation
R-DRE-5654219 Phospholipase C-mediated cascade: FGFR1
R-DRE-5654687 Downstream signaling of activated FGFR1
R-DRE-5654688 SHC-mediated cascade:FGFR1
R-DRE-5654689 PI-3K cascade:FGFR1
R-DRE-5654693 FRS-mediated FGFR1 signaling
R-DRE-5654726 Negative regulation of FGFR1 signaling
R-DRE-5673001 RAF/MAP kinase cascade
R-DRE-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_and_taxonomy_section">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-A (EC:2.7.10.1)
Short name:
FGFR-1-A
Short name:
bFGF-R-1-A
Alternative name(s):
Basic fibroblast growth factor receptor 1-A
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:fgfr1a
Synonyms:fgfr1
ORF Names:si:ch211-198o12.1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri7955 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000000437 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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

Zebrafish Information Network genome database

More...
ZFINi
ZDB-GENE-980526-255 fgfr1a

<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_location_section">'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 domaini27 – 363ExtracellularSequence analysisAdd BLAST337
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Transmembranei364 – 384HelicalSequence analysisAdd BLAST21
Topological domaini385 – 810CytoplasmicSequence analysisAdd BLAST426

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus

<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 – 26Sequence analysisAdd BLAST26
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000024920227 – 810Fibroblast growth factor receptor 1-AAdd BLAST784

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 bondi53 ↔ 99PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi107N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi113N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi167 ↔ 219PROSITE-ProRule annotation
Glycosylationi216N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi229N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi253N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi266 ↔ 330PROSITE-ProRule annotation
Glycosylationi285N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi306N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi319N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi358N-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 residuei450Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei570Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei572Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei640Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei641Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei717Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei753Phosphotyrosine; by autocatalysisBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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. Phosphotyrosine residues provide docking sites for interacting proteins and so are crucial for FGFR1 function and its regulation (By similarity).By similarity
Ubiquitinated. FGFR1 is rapidly ubiquitinated after autophosphorylation, leading to internalization and degradation (By similarity).By similarity
N-glycosylated in the endoplasmic reticulum. The N-glycan chains undergo further maturation to an Endo H-resistant form in the Golgi apparatus (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...
PaxDbi
Q90Z00

PRoteomics IDEntifications database

More...
PRIDEi
Q90Z00

<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

Initially expressed in adaxial mesoderm with transcripts distinctly localized to the anterior portion of each half-somite. Hereupon, also strongly expressed in the otic vesicles, branchial arches and the brain, especially at the midbrain-hindbrain boundary (MHB).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSDARG00000011027 Expressed in 85 organ(s), highest expression level in tail bud paraxial mesoderm

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q90Z00 baseline and differential

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer. Homodimer after ligand binding (By similarity).

Interacts with cnpy1.

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
Q90Z00, 2 interactors

Molecular INTeraction database

More...
MINTi
Q90Z00

STRING: functional protein association networks

More...
STRINGi
7955.ENSDARP00000069260

<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

3D structure databases

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

More...
SMRi
Q90Z00

Database of comparative protein structure models

More...
ModBasei
Search...

<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_and_domains_section">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>Domaini28 – 115Ig-like C2-type 1Add BLAST88
Domaini147 – 235Ig-like C2-type 2Add BLAST89
Domaini244 – 346Ig-like C2-type 3Add BLAST103
Domaini465 – 754Protein kinasePROSITE-ProRule annotationAdd BLAST290

<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

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q90Z00

KEGG Orthology (KO)

More...
KOi
K04362

Identification of Orthologs from Complete Genome Data

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OMAi
KVRDHMW

Database of Orthologous Groups

More...
OrthoDBi
220433at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q90Z00

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
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
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_length">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 (5+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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 5 <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.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 5 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: Q90Z00-1) [UniParc]FASTAAdd to basket

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
MKMMMIMKTT LLLISVLLTQ ALQSQGRPAI QDEAPAEPTS YTLDSGEKLE
60 70 80 90 100
LSCKAKEDTQ KVTWTKDLVP LVDGEHTRLR NDQMEIEKVE PTDSGLYACF
110 120 130 140 150
AQGLNSNHTE YFNISVTDEE DEVDSSSEEA KLSNDQNLPM APVWAQPDKM
160 170 180 190 200
EKKLHAVPAS KTVKFRCQAN GNPTPTLKWL KNGKEFKRDQ RIGGFKVREH
210 220 230 240 250
MWTIIMESVV PSDRGNYTCL VENRHGSINH TYQLDVVERS PHRPILQAGL
260 270 280 290 300
PANRTAVVGS DVEFECKVFS DPQPHIQWLK HIEVNGSRYG PDGLPYVRAL
310 320 330 340 350
KTAGVNTTDK EMEVLQIRNV SLEDAGEYTC LAGNSIGHSH HSAWLTVYKA
360 370 380 390 400
VPPTQLPNQT YLEVLIYCVG FFLICVMVGT AVLAKMHSSA KKSDFNSQLA
410 420 430 440 450
VHKLAKSIPL RRQVTVSVDS SSSMHSGGML VRPSRLSSSG SPMLSGVSEY
460 470 480 490 500
ELPQDPRWEV QRDRLVLGKP LGEGCFGQVM MAEAMGMDKE KPNRITKVAV
510 520 530 540 550
KMLKSDATEK DLSDLISEME MMKIIGKHKN IINLLGACTQ DGPLYVIVEF
560 570 580 590 600
AAKGNLREYL RVRRPPGMEY CYNPDQVPVE NMSIKDLVSC AYQVARGMEY
610 620 630 640 650
LASKKCIHRD LAARNVLVTE DNVMKIADFG LARDIHHIDY YKKTTNGRLP
660 670 680 690 700
VKWMAPEALF DRIYTHQSDV WSFGVLLWEI FTLGGSPYPG VPVEELFKLL
710 720 730 740 750
KEGHRMDRPS TCTHELYMMM RDCWHAVPSQ RPTFKQLVED LDRTLSMTSN
760 770 780 790 800
QEYLDLSVSL DQFSPNFPDT RSSTCSSGED SVFSHDAGAD EPCLPKFPPH
810
PNRGVAFKKR
Length:810
Mass (Da):91,041
Last modified:July 7, 2009 - 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:i20D0C8B8022893CD
GO
Isoform 2 (identifier: Q90Z00-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     414-415: Missing.

Show »
Length:808
Mass (Da):90,841
Checksum:i1D78853DA1AB9D9C
GO
Isoform 3 (identifier: Q90Z00-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     302-349: Missing.
     414-415: Missing.

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Length:760
Mass (Da):85,611
Checksum:iE5D282A4CDE184F3
GO
Isoform 4 (identifier: Q90Z00-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     302-415: Missing.

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Length:696
Mass (Da):78,556
Checksum:i7D41D8835390B35C
GO
Isoform 5 (identifier: Q90Z00-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     302-349: TAGVNTTDKE...HHSAWLTVYK → NSGVNSSDTQ...AWLTVVKHLQ
     414-415: Missing.

Show »
Length:809
Mass (Da):91,011
Checksum:i5BDD9A3BFBF8A6D1
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F1QWQ8F1QWQ8_DANRE
Fibroblast growth factor receptor 1...
fgfr1a
328Annotation 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 AAI62342 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAK64494 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAO45658 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAO45659 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAO45660 differs from that shown. Reason: Erroneous initiation.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 conflicti92T → A in AAK64494 (PubMed:15221377).Curated1
Sequence conflicti92T → A in AAO45658 (PubMed:15221377).Curated1
Sequence conflicti92T → A in AAO45659 (PubMed:15221377).Curated1
Sequence conflicti92T → A in AAO45660 (PubMed:15221377).Curated1
Sequence conflicti92T → A in AAI62342 (Ref. 3) Curated1
Sequence conflicti92T → A in CAM60064 (PubMed:18296487).Curated1
Sequence conflicti351V → I in CAM60064 (PubMed:18296487).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_037674302 – 415Missing in isoform 4. 1 PublicationAdd BLAST114
Alternative sequenceiVSP_037675302 – 349Missing in isoform 3. 1 PublicationAdd BLAST48
Alternative sequenceiVSP_037676302 – 349TAGVN…LTVYK → NSGVNSSDTQVLTLYNVTEE QSGEYICKVSNYIGQANQSA WLTVVKHLQ in isoform 5. 1 PublicationAdd BLAST48
Alternative sequenceiVSP_037677414 – 415Missing in isoform 2, isoform 3 and isoform 5. 1 Publication2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF389400 mRNA Translation: AAK64494.1 Different initiation.
AY197498 mRNA Translation: AAO45658.1 Different initiation.
AY197499 mRNA Translation: AAO45659.1 Different initiation.
AY197500 mRNA Translation: AAO45660.1 Different initiation.
AY197501 mRNA Translation: AAO45661.1
BX247873, CR376860 Genomic DNA Translation: CAK04365.2
BX247873, CR376860 Genomic DNA Translation: CAM13573.2
BX247873, CR376860 Genomic DNA Translation: CAM13574.1
CR376860, BX247873 Genomic DNA Translation: CAP19402.1
CR376860, BX247873 Genomic DNA Translation: CAP19403.1
CR376860, BX247873 Genomic DNA Translation: CAP19404.1
BC162342 mRNA Translation: AAI62342.1 Different initiation.
CU458752 mRNA Translation: CAM60064.1

NCBI Reference Sequences

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RefSeqi
NP_001296328.1, NM_001309399.1 [Q90Z00-2]
NP_001296329.1, NM_001309400.1 [Q90Z00-4]
NP_694494.2, NM_152962.3 [Q90Z00-1]
XP_009302579.1, XM_009304304.2 [Q90Z00-5]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSDART00000024882; ENSDARP00000013742; ENSDARG00000011027 [Q90Z00-5]
ENSDART00000135166; ENSDARP00000115638; ENSDARG00000011027 [Q90Z00-4]
ENSDART00000147742; ENSDARP00000116533; ENSDARG00000011027 [Q90Z00-2]
ENSDART00000167394; ENSDARP00000131679; ENSDARG00000011027 [Q90Z00-4]

Database of genes from NCBI RefSeq genomes

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GeneIDi
30705

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
dre:30705

Keywords - Coding sequence diversityi

Alternative splicing

<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
AF389400 mRNA Translation: AAK64494.1 Different initiation.
AY197498 mRNA Translation: AAO45658.1 Different initiation.
AY197499 mRNA Translation: AAO45659.1 Different initiation.
AY197500 mRNA Translation: AAO45660.1 Different initiation.
AY197501 mRNA Translation: AAO45661.1
BX247873, CR376860 Genomic DNA Translation: CAK04365.2
BX247873, CR376860 Genomic DNA Translation: CAM13573.2
BX247873, CR376860 Genomic DNA Translation: CAM13574.1
CR376860, BX247873 Genomic DNA Translation: CAP19402.1
CR376860, BX247873 Genomic DNA Translation: CAP19403.1
CR376860, BX247873 Genomic DNA Translation: CAP19404.1
BC162342 mRNA Translation: AAI62342.1 Different initiation.
CU458752 mRNA Translation: CAM60064.1
RefSeqiNP_001296328.1, NM_001309399.1 [Q90Z00-2]
NP_001296329.1, NM_001309400.1 [Q90Z00-4]
NP_694494.2, NM_152962.3 [Q90Z00-1]
XP_009302579.1, XM_009304304.2 [Q90Z00-5]

3D structure databases

SMRiQ90Z00
ModBaseiSearch...

Protein-protein interaction databases

IntActiQ90Z00, 2 interactors
MINTiQ90Z00
STRINGi7955.ENSDARP00000069260

Proteomic databases

PaxDbiQ90Z00
PRIDEiQ90Z00

Genome annotation databases

EnsembliENSDART00000024882; ENSDARP00000013742; ENSDARG00000011027 [Q90Z00-5]
ENSDART00000135166; ENSDARP00000115638; ENSDARG00000011027 [Q90Z00-4]
ENSDART00000147742; ENSDARP00000116533; ENSDARG00000011027 [Q90Z00-2]
ENSDART00000167394; ENSDARP00000131679; ENSDARG00000011027 [Q90Z00-4]
GeneIDi30705
KEGGidre:30705

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
30705
ZFINiZDB-GENE-980526-255 fgfr1a

Phylogenomic databases

eggNOGiKOG0200 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000155860
InParanoidiQ90Z00
KOiK04362
OMAiKVRDHMW
OrthoDBi220433at2759
PhylomeDBiQ90Z00
TreeFamiTF316307

Enzyme and pathway databases

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

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q90Z00

Gene expression databases

BgeeiENSDARG00000011027 Expressed in 85 organ(s), highest expression level in tail bud paraxial mesoderm
ExpressionAtlasiQ90Z00 baseline and differential

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
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
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

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiFGR1A_DANRE
<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: Q90Z00
Secondary accession number(s): A2BEU6
, A2BEU7, A4JYD6, B3DGB8, Q1LY25, Q800Y8, Q800Y9, Q800Z0, Q800Z1
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: July 7, 2009
Last modified: October 16, 2019
This is version 142 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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