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UniProtKB - P05230 (FGF1_HUMAN)

Entry version 240 (23 Feb 2022)
Sequence version 1 (13 Aug 1987)
Previous versions | rss
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Protein

Fibroblast growth factor 1

Gene

FGF1

Organism
Homo sapiens (Human)
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 (PubMed:18441324, PubMed:20422052).

Can induce angiogenesis (PubMed:23469107).

6 Publications

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 sitei33Heparin2 Publications1

<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

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P05230

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-109704, PI3K Cascade
R-HSA-1257604, PIP3 activates AKT signaling
R-HSA-1839122, Signaling by activated point mutants of FGFR1
R-HSA-1839130, Signaling by activated point mutants of FGFR3
R-HSA-190322, FGFR4 ligand binding and activation
R-HSA-190370, FGFR1b ligand binding and activation
R-HSA-190371, FGFR3b ligand binding and activation
R-HSA-190372, FGFR3c ligand binding and activation
R-HSA-190373, FGFR1c ligand binding and activation
R-HSA-190375, FGFR2c ligand binding and activation
R-HSA-190377, FGFR2b ligand binding and activation
R-HSA-2033514, FGFR3 mutant receptor activation
R-HSA-2033519, Activated point mutants of FGFR2
R-HSA-2219530, Constitutive Signaling by Aberrant PI3K in Cancer
R-HSA-5654219, Phospholipase C-mediated cascade: FGFR1
R-HSA-5654221, Phospholipase C-mediated cascade, FGFR2
R-HSA-5654227, Phospholipase C-mediated cascade, FGFR3
R-HSA-5654228, Phospholipase C-mediated cascade, FGFR4
R-HSA-5654687, Downstream signaling of activated FGFR1
R-HSA-5654688, SHC-mediated cascade:FGFR1
R-HSA-5654689, PI-3K cascade:FGFR1
R-HSA-5654693, FRS-mediated FGFR1 signaling
R-HSA-5654695, PI-3K cascade:FGFR2
R-HSA-5654699, SHC-mediated cascade:FGFR2
R-HSA-5654700, FRS-mediated FGFR2 signaling
R-HSA-5654704, SHC-mediated cascade:FGFR3
R-HSA-5654706, FRS-mediated FGFR3 signaling
R-HSA-5654710, PI-3K cascade:FGFR3
R-HSA-5654712, FRS-mediated FGFR4 signaling
R-HSA-5654719, SHC-mediated cascade:FGFR4
R-HSA-5654720, PI-3K cascade:FGFR4
R-HSA-5654726, Negative regulation of FGFR1 signaling
R-HSA-5654727, Negative regulation of FGFR2 signaling
R-HSA-5654732, Negative regulation of FGFR3 signaling
R-HSA-5654733, Negative regulation of FGFR4 signaling
R-HSA-5655253, Signaling by FGFR2 in disease
R-HSA-5655302, Signaling by FGFR1 in disease
R-HSA-5673001, RAF/MAP kinase cascade
R-HSA-6811558, PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-HSA-8851708, Signaling by FGFR2 IIIa TM
R-HSA-8853338, Signaling by FGFR3 point mutants in cancer

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P05230

SIGNOR Signaling Network Open Resource

More...SIGNORi		P05230

<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
Endothelial cell growth factor
Short name:
ECGF
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: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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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
  • UP000005640 <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 5

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:3665, FGF1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		131220, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P05230

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000113578

<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 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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi24 – 27KKPK → AAPA: Loss of nuclear import leading to loss of phosphorylation by PKC/PRKCD. 1 Publication4
Mutagenesisi33N → A: No effect on integrin-binding. 1 Publication1
Mutagenesisi50R → E: Dominant-negative mutant. Defective in integrin-binding and in ternary complex formation with integrin and FGFR1. No effect on heparin- and FGFR1-binding. Defective in inducing FGF1 signaling, cell proliferation and cell migration. Defective in inducing angiogenesis, and suppression of angiogenesis in different in vitro and in vivo angiogenesis models. 3 Publications1
Mutagenesisi102E → A: No effect on integrin-binding. No effect on integrin- and heparin-binding, loss of FGFR1-binding, defective in inducing FGF1 signaling, cell proliferation and cell migration; when associated with A-109 and A-110. 1 Publication1
Mutagenesisi109Y → A: No effect on integrin- and heparin-binding, loss of FGFR1-binding, defective in inducing FGF1 signaling, cell proliferation and cell migration; when associated with A-102 and A-110. 1 Publication1
Mutagenesisi110N → A: No effect on integrin-binding. No effect on integrin- and heparin-binding, loss of FGFR1-binding, defective in inducing FGF1 signaling, cell proliferation and cell migration; when associated with A-102 and A-109. 1 Publication1
Mutagenesisi114S → A: Decrease in LRRC59-binding. 1 Publication1
Mutagenesisi127K → E: Reduced integrin-binding; when associated with E-128. Defective in integrin-, heparin- and FGFR1-binding, and defective in inducing FGF1 signaling, cell proliferation and cell migration; when associated with E-128; E-133 and E-134. 1 Publication1
Mutagenesisi128K → E: Reduced integrin-binding; when associated with E-127. Defective in integrin-, heparin- and FGFR1-binding, and defective in inducing FGF1 signaling, cell proliferation and cell migration; when associated with E-127; E-133 and E-134. 1 Publication1
Mutagenesisi131S → A: Decrease in LRRC59-binding. 1 Publication1
Mutagenesisi131S → E: Decrease in LRRC59-binding. 1 Publication1
Mutagenesisi133K → A: Loss of LRRC59-binding. 1 Publication1
Mutagenesisi133K → E: Loss of CSNK2A-, CSNK2B- and LRRC59-binding. Reduced integrin-binding; when associated with E-134. Defective in integrin-, heparin- and FGFR1-binding, and defective in inducing FGF1 signaling, cell proliferation and cell migration; when associated with E-128; E-133 and E-134. 2 Publications1
Mutagenesisi133K → R: No effect on LRRC59-binding. 1 Publication1
Mutagenesisi134R → E: Reduced integrin-binding; when associated with E-133. Defective in integrin-, heparin- and FGFR1-binding, and defective in inducing FGF1 signaling, cell proliferation and cell migration; when associated with E-127; E-128 and E-133. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		2246

Open Targets

More...OpenTargetsi		ENSG00000113578

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA28105

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P05230, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2120

Drug and drug target database

More...DrugBanki		DB08238, 5-aminonaphthalene-2-sulfonic acid
DB01025, Amlexanox
DB10770, Foreskin fibroblast (neonatal)
DB10772, Foreskin keratinocyte (neonatal)
DB01942, Formic acid
DB01109, Heparin
DB03959, N,O6-Disulfo-Glucosamine
DB04409, Naphthalene Trisulfonate
DB02264, O2-Sulfo-Glucuronic Acid
DB06589, Pazopanib
DB00686, Pentosan polysulfate
DB01901, Sucrosofate

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		FGF1

Domain mapping of disease mutations (DMDM)

More...DMDMi		122737

<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_00000089072 – 15Add 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_000000890816 – 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.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P05230

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P05230

MaxQB - The MaxQuant DataBase

More...MaxQBi		P05230

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

More...PaxDbi		P05230

PeptideAtlas

More...PeptideAtlasi		P05230

PRoteomics IDEntifications database

More...PRIDEi		P05230

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		51826 [P05230-1]
51827 [P05230-2]

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P05230-1 [P05230-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P05230

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

More...PhosphoSitePlusi		P05230

<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

Predominantly expressed in kidney and brain. Detected at much lower levels in heart and skeletal muscle.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000113578, Expressed in metanephric glomerulus and 189 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P05230, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P05230, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000113578, Tissue enhanced (brain, choroid plexus)

<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.

Interacts with LRRC59.

Interacts with CSNKA, CSNKB and FIBP. 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 (PubMed:20422052).

13 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		108537, 40 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P05230

Database of interacting proteins

More...DIPi		DIP-3787N

Protein interaction database and analysis system

More...IntActi		P05230, 18 interactors

Molecular INTeraction database

More...MINTi		P05230

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000480791

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P05230

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P05230, 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

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

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		P05230

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

More...SMRi		P05230

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		P05230

<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-bindingAdd BLAST17

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi24 – 27Nuclear localization signal4

<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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_081609_5_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P05230

Identification of Orthologs from Complete Genome Data

More...OMAi		YQDSSWY

Database of Orthologous Groups

More...OrthoDBi		1157770at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P05230

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>Sequences (2+)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 2 <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 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P05230-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><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.

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MAEGEITTFT ALTEKFNLPP GNYKKPKLLY CSNGGHFLRI LPDGTVDGTR 
        60         70         80         90        100
DRSDQHIQLQ LSAESVGEVY IKSTETGQYL AMDTDGLLYG SQTPNEECLF 
       110        120        130        140        150
LERLEENHYN TYISKKHAEK NWFVGLKKNG SCKRGPRTHY GQKAILFLPL 

PVSSD
Length:155
Mass (Da):17,460
Last modified:August 13, 1987 - 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:iF586E8BFB09F1580
GO
Isoform 2 (identifier: P05230-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     57-60: IQLQ → TDTK
     61-155: Missing.

Show »
Length:60
Mass (Da):6,698
Checksum:iB53E08C406484714
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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B5MCF4B5MCF4_HUMAN
Fibroblast growth factor 1
FGF1
93Annotation 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>
C9JDC5C9JDC5_HUMAN
Fibroblast growth factor 1
FGF1
58Annotation 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>
C9JUP6C9JUP6_HUMAN
Fibroblast growth factor 1
FGF1
41Annotation 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>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_02135721G → E1 PublicationCorresponds to variant dbSNP:rs17223632EnsemblClinVar.1

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_03653657 – 60IQLQ → TDTK in isoform 2. 1 Publication4
Alternative sequenceiVSP_03653761 – 155Missing in isoform 2. 1 PublicationAdd BLAST95

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
M13361 mRNA Translation: AAA79245.1
M30492, M30490, M30491 Genomic DNA Translation: AAA52446.1
M23087, M23086 Genomic DNA Translation: AAA52638.1
X51943 mRNA Translation: CAA36206.1
X65778 mRNA Translation: CAA46661.1
S67291 mRNA Translation: AAB29057.2
S67292 mRNA Translation: AAB29058.1
AY601819 Genomic DNA Translation: AAS99352.1
AC005370 Genomic DNA No translation available.
AK312301 mRNA Translation: BAG35227.1
CH471062 Genomic DNA Translation: EAW61881.1
CH471062 Genomic DNA Translation: EAW61882.1
CH471062 Genomic DNA Translation: EAW61885.1
BC032697 mRNA Translation: AAH32697.1
M60515 mRNA Translation: AAA51672.1
M60516 mRNA Translation: AAA51673.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS4275.1 [P05230-1]
CCDS4276.1 [P05230-2]

Protein sequence database of the Protein Information Resource

More...PIRi		A33665
JH0708

NCBI Reference Sequences

More...RefSeqi		NP_000791.1, NM_000800.4 [P05230-1]
NP_001138364.1, NM_001144892.2 [P05230-1]
NP_001138406.1, NM_001144934.1 [P05230-1]
NP_001138407.1, NM_001144935.1 [P05230-1]
NP_001244134.1, NM_001257205.1 [P05230-1]
NP_001244136.1, NM_001257207.1 [P05230-1]
NP_001244137.1, NM_001257208.1 [P05230-1]
NP_001244138.1, NM_001257209.1 [P05230-1]
NP_001244139.1, NM_001257210.1 [P05230-1]
NP_149127.1, NM_033136.3 [P05230-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000337706; ENSP00000338548; ENSG00000113578
ENST00000359370; ENSP00000352329; ENSG00000113578
ENST00000360966; ENSP00000354231; ENSG00000113578 [P05230-2]
ENST00000378046; ENSP00000367285; ENSG00000113578
ENST00000419524; ENSP00000396195; ENSG00000113578
ENST00000441680; ENSP00000404742; ENSG00000113578
ENST00000610990; ENSP00000481868; ENSG00000113578
ENST00000612258; ENSP00000479024; ENSG00000113578
ENST00000619447; ENSP00000480980; ENSG00000113578
ENST00000621536; ENSP00000480791; ENSG00000113578

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2246

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:2246

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...MANE-Selecti		ENST00000337706.7; ENSP00000338548.2; NM_000800.5; NP_000791.1

UCSC genome browser

More...UCSCi		uc003lmm.5, human [P05230-1]

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13361 mRNA Translation: AAA79245.1
M30492, M30490, M30491 Genomic DNA Translation: AAA52446.1
M23087, M23086 Genomic DNA Translation: AAA52638.1
X51943 mRNA Translation: CAA36206.1
X65778 mRNA Translation: CAA46661.1
S67291 mRNA Translation: AAB29057.2
S67292 mRNA Translation: AAB29058.1
AY601819 Genomic DNA Translation: AAS99352.1
AC005370 Genomic DNA No translation available.
AK312301 mRNA Translation: BAG35227.1
CH471062 Genomic DNA Translation: EAW61881.1
CH471062 Genomic DNA Translation: EAW61882.1
CH471062 Genomic DNA Translation: EAW61885.1
BC032697 mRNA Translation: AAH32697.1
M60515 mRNA Translation: AAA51672.1
M60516 mRNA Translation: AAA51673.1
CCDSiCCDS4275.1 [P05230-1]
CCDS4276.1 [P05230-2]
PIRiA33665
JH0708
RefSeqiNP_000791.1, NM_000800.4 [P05230-1]
NP_001138364.1, NM_001144892.2 [P05230-1]
NP_001138406.1, NM_001144934.1 [P05230-1]
NP_001138407.1, NM_001144935.1 [P05230-1]
NP_001244134.1, NM_001257205.1 [P05230-1]
NP_001244136.1, NM_001257207.1 [P05230-1]
NP_001244137.1, NM_001257208.1 [P05230-1]
NP_001244138.1, NM_001257209.1 [P05230-1]
NP_001244139.1, NM_001257210.1 [P05230-1]
NP_149127.1, NM_033136.3 [P05230-2]

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
1AXMX-ray3.00A/B/C/D/E/F21-155[»]
1DJSX-ray2.40B21-155[»]
1DZCNMR-A25-155[»]
1DZDNMR-A29-155[»]
1E0OX-ray2.80A/C16-155[»]
1EVTX-ray2.80A/B22-155[»]
1HKNX-ray2.00A/B/C/D/E/F17-155[»]
1JQZX-ray1.65A/B16-155[»]
1JT3X-ray1.95A/B16-155[»]
1JT4X-ray1.78A/B16-155[»]
1JT5X-ray1.85A/B16-155[»]
1JT7X-ray1.70A/B/C/D16-155[»]
1JTCX-ray1.70A/B/C/D16-155[»]
1JY0X-ray1.70A/B16-155[»]
1K5UX-ray2.00A/B/C16-154[»]
1K5VX-ray2.10A/B16-154[»]
1M16X-ray1.70A/B16-155[»]
1NZKX-ray1.95A/B/C/D16-152[»]
1P63X-ray1.60A/B16-155[»]
1PZZX-ray2.00A/B16-155[»]
1Q03X-ray2.05A/B16-152[»]
1Q04X-ray1.80A/B16-155[»]
1RG8X-ray1.10A/B16-155[»]
1RMLNMR-A1-155[»]
1RY7X-ray3.20A1-155[»]
1YTOX-ray2.10A/B/C/D16-155[»]
1Z2VX-ray1.90A/B16-155[»]
1Z4SX-ray2.60A/B/C/D16-155[»]
2AFGX-ray2.00A/B/C/D16-155[»]
2AQZX-ray1.85A/B16-155[»]
2AXMX-ray3.00A/B21-155[»]
2ERMNMR-A17-155[»]
2HW9X-ray1.60A/B16-155[»]
2HWAX-ray1.65A/B16-155[»]
2HWMX-ray1.60A/B16-155[»]
2HZ9X-ray1.70A/B16-155[»]
2K43NMR-A23-155[»]
2K4ANMR-B23-155[»]
2K8RNMR-A23-155[»]
2KI4NMR-A/D23-155[»]
2KI6NMR-B/E23-155[»]
2NTDX-ray2.52A/B/C/D16-155[»]
2Q9XX-ray1.70A16-155[»]
2RQ9NMR-A22-155[»]
3B9UX-ray1.55A16-155[»]
3BA4X-ray1.80A/B16-155[»]
3BA5X-ray1.75A/B16-155[»]
3BA7X-ray1.60A/B16-155[»]
3BADX-ray2.00A/B16-155[»]
3BAGX-ray1.75A/B16-155[»]
3BAHX-ray1.65A/B16-155[»]
3BAOX-ray1.55A/B16-155[»]
3BAQX-ray1.80A/B16-155[»]
3BAUX-ray1.60A/B16-155[»]
3BAVX-ray1.62A/B16-155[»]
3BB2X-ray1.50A/B16-155[»]
3CQAX-ray1.80A/B16-155[»]
3CRGX-ray1.85A/B16-155[»]
3CRHX-ray2.15A/B16-155[»]
3CRIX-ray2.10A/B16-155[»]
3CU1X-ray2.60B/D22-152[»]
3FGMX-ray1.95A/B16-155[»]
3FJ8X-ray2.00A/B16-155[»]
3FJ9X-ray1.90A/B16-155[»]
3FJAX-ray1.95A/B16-155[»]
3FJBX-ray2.00A/B16-155[»]
3FJCX-ray2.00A/B16-155[»]
3FJDX-ray1.90A/B16-155[»]
3FJEX-ray2.10A/B16-155[»]
3FJFX-ray1.90A/B16-155[»]
3FJHX-ray1.90A/B16-155[»]
3FJIX-ray2.55A/B/C/D16-155[»]
3FJJX-ray1.90A/B16-155[»]
3FJKX-ray2.15A/B/C/D16-155[»]
3HOMX-ray2.30A/B16-155[»]
3JUTX-ray2.25A/B/C/D/E/F24-153[»]
3K1XX-ray1.98A/B/C/D/E/F24-153[»]
3O3QX-ray1.60A/B/C/D16-155[»]
3OJ2X-ray2.20A/B1-155[»]
3OJMX-ray2.10A1-155[»]
3OJVX-ray2.60A/B21-155[»]
3UD7X-ray2.80A/B/C16-155[»]
3UD8X-ray2.37A/B/C16-155[»]
3UD9X-ray2.34A/B/C16-155[»]
3UDAX-ray2.51A/B/C16-155[»]
4J23X-ray3.88B21-155[»]
4Q91X-ray1.80A/B16-155[»]
4Q9GX-ray1.55A/B16-155[»]
4Q9PX-ray1.80A/B16-155[»]
4QALX-ray1.50A/B16-155[»]
4QBCX-ray1.52A/B16-155[»]
4QBVX-ray1.50A/B16-155[»]
4QC4X-ray1.49A/B16-155[»]
4QO3X-ray2.05A/B16-155[»]
4XKIX-ray2.00A/B16-155[»]
4YOLX-ray1.97A/B16-155[»]
BMRBiP05230
SMRiP05230
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi108537, 40 interactors
CORUMiP05230
DIPiDIP-3787N
IntActiP05230, 18 interactors
MINTiP05230
STRINGi9606.ENSP00000480791

Chemistry databases

BindingDBiP05230
ChEMBLiCHEMBL2120
DrugBankiDB08238, 5-aminonaphthalene-2-sulfonic acid
DB01025, Amlexanox
DB10770, Foreskin fibroblast (neonatal)
DB10772, Foreskin keratinocyte (neonatal)
DB01942, Formic acid
DB01109, Heparin
DB03959, N,O6-Disulfo-Glucosamine
DB04409, Naphthalene Trisulfonate
DB02264, O2-Sulfo-Glucuronic Acid
DB06589, Pazopanib
DB00686, Pentosan polysulfate
DB01901, Sucrosofate

PTM databases

iPTMnetiP05230
PhosphoSitePlusiP05230

Genetic variation databases

BioMutaiFGF1
DMDMi122737

Proteomic databases

EPDiP05230
MassIVEiP05230
MaxQBiP05230
PaxDbiP05230
PeptideAtlasiP05230
PRIDEiP05230
ProteomicsDBi51826 [P05230-1]
51827 [P05230-2]
TopDownProteomicsiP05230-1 [P05230-1]

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		P05230, 1 sequenced antibody

Antibodypedia a portal for validated antibodies

More...Antibodypediai		1009, 773 antibodies from 44 providers

The DNASU plasmid repository

More...DNASUi		2246

Genome annotation databases

EnsembliENST00000337706; ENSP00000338548; ENSG00000113578
ENST00000359370; ENSP00000352329; ENSG00000113578
ENST00000360966; ENSP00000354231; ENSG00000113578 [P05230-2]
ENST00000378046; ENSP00000367285; ENSG00000113578
ENST00000419524; ENSP00000396195; ENSG00000113578
ENST00000441680; ENSP00000404742; ENSG00000113578
ENST00000610990; ENSP00000481868; ENSG00000113578
ENST00000612258; ENSP00000479024; ENSG00000113578
ENST00000619447; ENSP00000480980; ENSG00000113578
ENST00000621536; ENSP00000480791; ENSG00000113578
GeneIDi2246
KEGGihsa:2246
MANE-SelectiENST00000337706.7; ENSP00000338548.2; NM_000800.5; NP_000791.1
UCSCiuc003lmm.5, human [P05230-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2246
DisGeNETi2246

GeneCards: human genes, protein and diseases

More...GeneCardsi		FGF1
HGNCiHGNC:3665, FGF1
HPAiENSG00000113578, Tissue enhanced (brain, choroid plexus)
MIMi131220, gene
neXtProtiNX_P05230
OpenTargetsiENSG00000113578
PharmGKBiPA28105
VEuPathDBiHostDB:ENSG00000113578

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3885, Eukaryota
GeneTreeiENSGT00940000160557
HOGENOMiCLU_081609_5_1_1
InParanoidiP05230
OMAiYQDSSWY
OrthoDBi1157770at2759
PhylomeDBiP05230
TreeFamiTF317805

Enzyme and pathway databases

PathwayCommonsiP05230
ReactomeiR-HSA-109704, PI3K Cascade
R-HSA-1257604, PIP3 activates AKT signaling
R-HSA-1839122, Signaling by activated point mutants of FGFR1
R-HSA-1839130, Signaling by activated point mutants of FGFR3
R-HSA-190322, FGFR4 ligand binding and activation
R-HSA-190370, FGFR1b ligand binding and activation
R-HSA-190371, FGFR3b ligand binding and activation
R-HSA-190372, FGFR3c ligand binding and activation
R-HSA-190373, FGFR1c ligand binding and activation
R-HSA-190375, FGFR2c ligand binding and activation
R-HSA-190377, FGFR2b ligand binding and activation
R-HSA-2033514, FGFR3 mutant receptor activation
R-HSA-2033519, Activated point mutants of FGFR2
R-HSA-2219530, Constitutive Signaling by Aberrant PI3K in Cancer
R-HSA-5654219, Phospholipase C-mediated cascade: FGFR1
R-HSA-5654221, Phospholipase C-mediated cascade, FGFR2
R-HSA-5654227, Phospholipase C-mediated cascade, FGFR3
R-HSA-5654228, Phospholipase C-mediated cascade, FGFR4
R-HSA-5654687, Downstream signaling of activated FGFR1
R-HSA-5654688, SHC-mediated cascade:FGFR1
R-HSA-5654689, PI-3K cascade:FGFR1
R-HSA-5654693, FRS-mediated FGFR1 signaling
R-HSA-5654695, PI-3K cascade:FGFR2
R-HSA-5654699, SHC-mediated cascade:FGFR2
R-HSA-5654700, FRS-mediated FGFR2 signaling
R-HSA-5654704, SHC-mediated cascade:FGFR3
R-HSA-5654706, FRS-mediated FGFR3 signaling
R-HSA-5654710, PI-3K cascade:FGFR3
R-HSA-5654712, FRS-mediated FGFR4 signaling
R-HSA-5654719, SHC-mediated cascade:FGFR4
R-HSA-5654720, PI-3K cascade:FGFR4
R-HSA-5654726, Negative regulation of FGFR1 signaling
R-HSA-5654727, Negative regulation of FGFR2 signaling
R-HSA-5654732, Negative regulation of FGFR3 signaling
R-HSA-5654733, Negative regulation of FGFR4 signaling
R-HSA-5655253, Signaling by FGFR2 in disease
R-HSA-5655302, Signaling by FGFR1 in disease
R-HSA-5673001, RAF/MAP kinase cascade
R-HSA-6811558, PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-HSA-8851708, Signaling by FGFR2 IIIa TM
R-HSA-8853338, Signaling by FGFR3 point mutants in cancer
SignaLinkiP05230
SIGNORiP05230

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		2246, 8 hits in 1036 CRISPR screens

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

More...ChiTaRSi		FGF1, human
EvolutionaryTraceiP05230

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		FGF1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		2246
PharosiP05230, Tchem

Protein Ontology

More...PROi		PR:P05230
RNActiP05230, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000113578, Expressed in metanephric glomerulus and 189 other tissues
ExpressionAtlasiP05230, baseline and differential
GenevisibleiP05230, HS

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_HUMAN
<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: P05230
Secondary accession number(s): B2R5T0
, D3DQF2, P07502, Q16588
<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: August 13, 1987
Last sequence update: August 13, 1987
Last modified: February 23, 2022
This is version 240 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families
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