Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
We will be switching to the new UniProt website soon. Please explore and share your feedback. Take me to the new website.

UniProtKB - P61149 (FGF1_RAT)

Entry version 141 (23 Feb 2022)
Sequence version 1 (10 May 2004)
Previous versions | rss
Add a publicationFeedback
Protein

Fibroblast growth factor 1

Gene

Fgf1

Organism
Rattus norvegicus (Rat)
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

Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro. Acts as a ligand for FGFR1 and integrins. Binds to FGFR1 in the presence of heparin leading to FGFR1 dimerization and activation via sequential autophosphorylation on tyrosine residues which act as docking sites for interacting proteins, leading to the activation of several signaling cascades. Binds to integrin ITGAV:ITGB3. Its binding to integrin, subsequent ternary complex formation with integrin and FGFR1, and the recruitment of PTPN11 to the complex are essential for FGF1 signaling. Induces the phosphorylation and activation of FGFR1, FRS2, MAPK3/ERK1, MAPK1/ERK2 and AKT1. Can induce angiogenesis.

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 sitei33HeparinBy similarity1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionDevelopmental protein, Growth factor, Heparin-binding, Mitogen
Biological processAngiogenesis, Differentiation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-109704, PI3K Cascade
R-RNO-1257604, PIP3 activates AKT signaling
R-RNO-190322, FGFR4 ligand binding and activation
R-RNO-190370, FGFR1b ligand binding and activation
R-RNO-190371, FGFR3b ligand binding and activation
R-RNO-190372, FGFR3c ligand binding and activation
R-RNO-190373, FGFR1c ligand binding and activation
R-RNO-190375, FGFR2c ligand binding and activation
R-RNO-190377, FGFR2b ligand binding and activation
R-RNO-5654219, Phospholipase C-mediated cascade: FGFR1
R-RNO-5654221, Phospholipase C-mediated cascade, FGFR2
R-RNO-5654227, Phospholipase C-mediated cascade, FGFR3
R-RNO-5654228, Phospholipase C-mediated cascade, FGFR4
R-RNO-5654687, Downstream signaling of activated FGFR1
R-RNO-5654688, SHC-mediated cascade:FGFR1
R-RNO-5654689, PI-3K cascade:FGFR1
R-RNO-5654693, FRS-mediated FGFR1 signaling
R-RNO-5654695, PI-3K cascade:FGFR2
R-RNO-5654699, SHC-mediated cascade:FGFR2
R-RNO-5654700, FRS-mediated FGFR2 signaling
R-RNO-5654704, SHC-mediated cascade:FGFR3
R-RNO-5654706, FRS-mediated FGFR3 signaling
R-RNO-5654710, PI-3K cascade:FGFR3
R-RNO-5654712, FRS-mediated FGFR4 signaling
R-RNO-5654719, SHC-mediated cascade:FGFR4
R-RNO-5654720, PI-3K cascade:FGFR4
R-RNO-5654726, Negative regulation of FGFR1 signaling
R-RNO-5654727, Negative regulation of FGFR2 signaling
R-RNO-5654732, Negative regulation of FGFR3 signaling
R-RNO-5654733, Negative regulation of FGFR4 signaling
R-RNO-5673001, RAF/MAP kinase cascade
R-RNO-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 1
Short name:
FGF-1
Alternative name(s):
Acidic fibroblast growth factor
Short name:
aFGF
Heparin-binding growth factor 1
Short name:
HBGF-1
<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:Fgf1
Synonyms:Fgf-1, Fgfa
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<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
  • UP000002494 <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 18

Organism-specific databases

Rat genome database

More...RGDi		2605, Fgf1

<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

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_00000089162 – 15By similarityAdd BLAST14
<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_000000891716 – 155Fibroblast growth factor 1Add BLAST140

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei2N-acetylalanineBy 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

In the nucleus, phosphorylated by PKC/PRKCD.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

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

More...PaxDbi		P61149

PTM databases

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

More...PhosphoSitePlusi		P61149

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSRNOG00000013867, Expressed in heart and 19 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P61149, RN

<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.

Interacts with FGFR1, FGFR2, FGFR3 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors.

Found in a complex with FGFBP1, FGF1 and FGF2.

Interacts with FGFBP1.

Part of a Cu2+-dependent multiprotein aggregate containing FGF1, S100A13 and SYT1.

Interacts with SYT1.

Interacts with S100A13 (By similarity).

Interacts with LRRC59 (By similarity).

Interacts with CSNKA, CSNKB and FIBP (By similarity). While binding with LRRC59, CSNKA and FIBP seem mutually exclusive, CSNKB and FIBP may cooperatively interact with FGF1.

Forms a ternary complex with FGFR1 and ITGAV:ITGB3 and induces the recruitment of PTPN11 to the complex (By similarity).

By similarity

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		247356, 1 interactor

Protein interaction database and analysis system

More...IntActi		P61149, 2 interactors

Molecular INTeraction database

More...MINTi		P61149

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000018577

<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

1155
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		P61149

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

More...SMRi		P61149

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		P61149

<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

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>Regioni127 – 143Heparin-bindingBy similarityAdd BLAST17

<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 heparin-binding growth factors family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3885, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000160557

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P61149

Identification of Orthologs from Complete Genome Data

More...OMAi		SQNGGYH

Database of Orthologous Groups

More...OrthoDBi		1157770at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P61149

TreeFam database of animal gene trees

More...TreeFami		TF317805

Family and domain databases

Conserved Domains Database

More...CDDi		cd00058, FGF, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR028210, FGF1
IPR002209, Fibroblast_GF_fam
IPR008996, IL1/FGF

The PANTHER Classification System

More...PANTHERi		PTHR11486, PTHR11486, 1 hit
PTHR11486:SF86, PTHR11486:SF86, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00167, FGF, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00263, HBGFFGF

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00442, FGF, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50353, SSF50353, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00247, HBGF_FGF, 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>Sequencei

<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.

P61149-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAEGEITTFA ALTERFNLPL GNYKKPKLLY CSNGGHFLRI LPDGTVDGTR 
        60         70         80         90        100
DRSDQHIQLQ LSAESAGEVY IKGTETGQYL AMDTEGLLYG SQTPNEECLF 
       110        120        130        140        150
LERLEENHYN TYTSKKHAEK NWFVGLKKNG SCKRGPRTHY GQKAILFLPL 

PVSSD
Length:155
Mass (Da):17,418
Last modified:May 10, 2004 - v1
<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:i8880E4FF0FBA4161
GO

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
X14232 mRNA Translation: CAA32448.1

Protein sequence database of the Protein Information Resource

More...PIRi		S04147

NCBI Reference Sequences

More...RefSeqi		NP_036978.1, NM_012846.1
XP_006254712.1, XM_006254650.3
XP_006254713.1, XM_006254651.3
XP_006254714.1, XM_006254652.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000018577; ENSRNOP00000018577; ENSRNOG00000013867
ENSRNOT00000087408; ENSRNOP00000070685; ENSRNOG00000013867

Database of genes from NCBI RefSeq genomes

More...GeneIDi		25317

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:25317

UCSC genome browser

More...UCSCi		RGD:2605, rat

<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
X14232 mRNA Translation: CAA32448.1
PIRiS04147
RefSeqiNP_036978.1, NM_012846.1
XP_006254712.1, XM_006254650.3
XP_006254713.1, XM_006254651.3
XP_006254714.1, XM_006254652.3

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
2J3PX-ray1.40A/B22-155[»]
2UUSX-ray2.20A/B22-153[»]
BMRBiP61149
SMRiP61149
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi247356, 1 interactor
IntActiP61149, 2 interactors
MINTiP61149
STRINGi10116.ENSRNOP00000018577

PTM databases

PhosphoSitePlusiP61149

Proteomic databases

PaxDbiP61149

Genome annotation databases

EnsembliENSRNOT00000018577; ENSRNOP00000018577; ENSRNOG00000013867
ENSRNOT00000087408; ENSRNOP00000070685; ENSRNOG00000013867
GeneIDi25317
KEGGirno:25317
UCSCiRGD:2605, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2246
RGDi2605, Fgf1

Phylogenomic databases

eggNOGiKOG3885, Eukaryota
GeneTreeiENSGT00940000160557
InParanoidiP61149
OMAiSQNGGYH
OrthoDBi1157770at2759
PhylomeDBiP61149
TreeFamiTF317805

Enzyme and pathway databases

ReactomeiR-RNO-109704, PI3K Cascade
R-RNO-1257604, PIP3 activates AKT signaling
R-RNO-190322, FGFR4 ligand binding and activation
R-RNO-190370, FGFR1b ligand binding and activation
R-RNO-190371, FGFR3b ligand binding and activation
R-RNO-190372, FGFR3c ligand binding and activation
R-RNO-190373, FGFR1c ligand binding and activation
R-RNO-190375, FGFR2c ligand binding and activation
R-RNO-190377, FGFR2b ligand binding and activation
R-RNO-5654219, Phospholipase C-mediated cascade: FGFR1
R-RNO-5654221, Phospholipase C-mediated cascade, FGFR2
R-RNO-5654227, Phospholipase C-mediated cascade, FGFR3
R-RNO-5654228, Phospholipase C-mediated cascade, FGFR4
R-RNO-5654687, Downstream signaling of activated FGFR1
R-RNO-5654688, SHC-mediated cascade:FGFR1
R-RNO-5654689, PI-3K cascade:FGFR1
R-RNO-5654693, FRS-mediated FGFR1 signaling
R-RNO-5654695, PI-3K cascade:FGFR2
R-RNO-5654699, SHC-mediated cascade:FGFR2
R-RNO-5654700, FRS-mediated FGFR2 signaling
R-RNO-5654704, SHC-mediated cascade:FGFR3
R-RNO-5654706, FRS-mediated FGFR3 signaling
R-RNO-5654710, PI-3K cascade:FGFR3
R-RNO-5654712, FRS-mediated FGFR4 signaling
R-RNO-5654719, SHC-mediated cascade:FGFR4
R-RNO-5654720, PI-3K cascade:FGFR4
R-RNO-5654726, Negative regulation of FGFR1 signaling
R-RNO-5654727, Negative regulation of FGFR2 signaling
R-RNO-5654732, Negative regulation of FGFR3 signaling
R-RNO-5654733, Negative regulation of FGFR4 signaling
R-RNO-5673001, RAF/MAP kinase cascade
R-RNO-6811558, PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling

Miscellaneous databases

EvolutionaryTraceiP61149

Protein Ontology

More...PROi		PR:P61149

Gene expression databases

BgeeiENSRNOG00000013867, Expressed in heart and 19 other tissues
GenevisibleiP61149, RN

Family and domain databases

CDDicd00058, FGF, 1 hit
InterProiView protein in InterPro
IPR028210, FGF1
IPR002209, Fibroblast_GF_fam
IPR008996, IL1/FGF
PANTHERiPTHR11486, PTHR11486, 1 hit
PTHR11486:SF86, PTHR11486:SF86, 1 hit
PfamiView protein in Pfam
PF00167, FGF, 1 hit
PRINTSiPR00263, HBGFFGF
SMARTiView protein in SMART
SM00442, FGF, 1 hit
SUPFAMiSSF50353, SSF50353, 1 hit
PROSITEiView protein in PROSITE
PS00247, HBGF_FGF, 1 hit

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 nameiFGF1_RAT
<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: P61149
Secondary accession number(s): P10935
<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: May 10, 2004
Last sequence update: May 10, 2004
Last modified: February 23, 2022
This is version 141 of the entry and version 1 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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