UniProtKB - P05230 (FGF1_HUMAN)
Fibroblast growth factor 1
FGF1
Functioni
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 33 | Heparin2 Publications | 1 |
GO - Molecular functioni
- fibroblast growth factor receptor binding Source: UniProtKB
- growth factor activity Source: UniProtKB
- heparin binding Source: UniProtKB
- Hsp70 protein binding Source: Ensembl
- integrin binding Source: UniProtKB
- S100 protein binding Source: UniProtKB
GO - Biological processi
- activation of MAPK activity Source: UniProtKB
- activation of protein kinase B activity Source: UniProtKB
- anatomical structure morphogenesis Source: ProtInc
- angiogenesis Source: UniProtKB-KW
- animal organ morphogenesis Source: GO_Central
- branch elongation involved in ureteric bud branching Source: UniProtKB
- cell differentiation Source: GO_Central
- cellular response to heat Source: UniProtKB
- fibroblast growth factor receptor signaling pathway Source: UniProtKB
- lung development Source: GO_Central
- MAPK cascade Source: Reactome
- mesonephric epithelium development Source: UniProtKB
- multicellular organism development Source: ProtInc
- organ induction Source: Ensembl
- positive regulation of angiogenesis Source: UniProtKB
- positive regulation of cell division Source: UniProtKB
- positive regulation of cell migration Source: UniProtKB
- positive regulation of cell population proliferation Source: UniProtKB
- positive regulation of cholesterol biosynthetic process Source: BHF-UCL
- positive regulation of endothelial cell migration Source: UniProtKB
- positive regulation of epithelial cell proliferation Source: GO_Central
- positive regulation of gene expression Source: GO_Central
- positive regulation of hepatocyte proliferation Source: Ensembl
- positive regulation of intracellular signal transduction Source: BHF-UCL
- positive regulation of MAP kinase activity Source: UniProtKB
- positive regulation of protein kinase B signaling Source: Reactome
- positive regulation of protein phosphorylation Source: GO_Central
- positive regulation of sprouting angiogenesis Source: UniProtKB
- positive regulation of transcription by RNA polymerase II Source: BHF-UCL
- regulation of cell migration Source: GO_Central
- regulation of endothelial cell chemotaxis to fibroblast growth factor Source: UniProtKB
- regulation of endothelial tube morphogenesis Source: UniProtKB
- signal transduction Source: ProtInc
- wound healing Source: UniProtKB
Keywordsi
Molecular function | Developmental protein, Growth factor, Heparin-binding, Mitogen |
Biological process | Angiogenesis, Differentiation |
Enzyme and pathway databases
PathwayCommonsi | P05230 |
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 |
SignaLinki | P05230 |
SIGNORi | P05230 |
Names & Taxonomyi
Protein namesi | Recommended name: Fibroblast growth factor 1Short 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 |
Gene namesi | Name:FGF1 Synonyms:FGFA |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:3665, FGF1 |
MIMi | 131220, gene |
neXtProti | NX_P05230 |
VEuPathDBi | HostDB:ENSG00000113578.17 |
Subcellular locationi
Nucleus
Cytosol
Extracellular region or secreted
Other locations
Note: Lacks a cleavable signal sequence. Within the cytoplasm, it is transported to the cell membrane and then secreted by a non-classical pathway that requires Cu2+ ions and S100A13. Secreted in a complex with SYT1 (By similarity). Binding of exogenous FGF1 to FGFR facilitates endocytosis followed by translocation of FGF1 across endosomal membrane into the cytosol. Nuclear import from the cytosol requires the classical nuclear import machinery, involving proteins KPNA1 and KPNB1, as well as LRRC59.By similarity
Cytosol
- cytosol Source: UniProtKB
Extracellular region or secreted
- extracellular matrix Source: Ensembl
- extracellular region Source: UniProtKB
- extracellular space Source: UniProtKB
Nucleus
- nucleolus Source: Ensembl
- nucleoplasm Source: HPA
- nucleus Source: GO_Central
Other locations
- cell cortex Source: UniProtKB-SubCell
- cytoplasm Source: GO_Central
Keywords - Cellular componenti
Cytoplasm, Nucleus, SecretedPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 24 – 27 | KKPK → AAPA: Loss of nuclear import leading to loss of phosphorylation by PKC/PRKCD. 1 Publication | 4 | |
Mutagenesisi | 33 | N → A: No effect on integrin-binding. 1 Publication | 1 | |
Mutagenesisi | 50 | R → 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 Publications | 1 | |
Mutagenesisi | 102 | E → 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 Publication | 1 | |
Mutagenesisi | 109 | Y → 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 Publication | 1 | |
Mutagenesisi | 110 | N → 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 Publication | 1 | |
Mutagenesisi | 114 | S → A: Decrease in LRRC59-binding. 1 Publication | 1 | |
Mutagenesisi | 127 | K → 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 Publication | 1 | |
Mutagenesisi | 128 | K → 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 Publication | 1 | |
Mutagenesisi | 131 | S → A: Decrease in LRRC59-binding. 1 Publication | 1 | |
Mutagenesisi | 131 | S → E: Decrease in LRRC59-binding. 1 Publication | 1 | |
Mutagenesisi | 133 | K → A: Loss of LRRC59-binding. 1 Publication | 1 | |
Mutagenesisi | 133 | K → 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 Publications | 1 | |
Mutagenesisi | 133 | K → R: No effect on LRRC59-binding. 1 Publication | 1 | |
Mutagenesisi | 134 | R → 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 Publication | 1 |
Organism-specific databases
DisGeNETi | 2246 |
OpenTargetsi | ENSG00000113578 |
PharmGKBi | PA28105 |
Miscellaneous databases
Pharosi | P05230, Tchem |
Chemistry databases
ChEMBLi | CHEMBL2120 |
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
BioMutai | FGF1 |
DMDMi | 122737 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedBy similarity | |||
PropeptideiPRO_0000008907 | 2 – 15 | Add BLAST | 14 | |
ChainiPRO_0000008908 | 16 – 155 | Fibroblast growth factor 1Add BLAST | 140 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
EPDi | P05230 |
MassIVEi | P05230 |
MaxQBi | P05230 |
PaxDbi | P05230 |
PeptideAtlasi | P05230 |
PRIDEi | P05230 |
ProteomicsDBi | 51826 [P05230-1] 51827 [P05230-2] |
TopDownProteomicsi | P05230-1 [P05230-1] |
PTM databases
iPTMneti | P05230 |
PhosphoSitePlusi | P05230 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSG00000113578, Expressed in metanephric glomerulus and 189 other tissues |
ExpressionAtlasi | P05230, baseline and differential |
Genevisiblei | P05230, HS |
Organism-specific databases
HPAi | ENSG00000113578, Group enriched (brain, heart muscle, kidney) |
Interactioni
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 PublicationsBinary interactionsi
Hide detailsP05230
With | #Exp. | IntAct |
---|---|---|
FGFR1 [P11362] | 4 | EBI-698068,EBI-1028277 |
FGFR2 [P21802] | 2 | EBI-698068,EBI-1028658 |
FGFR3 [P22607] | 3 | EBI-698068,EBI-348399 |
VBP1 [P61758] | 3 | EBI-698068,EBI-357430 |
Isoform 1 [P05230-1]
With | #Exp. | IntAct |
---|---|---|
FGFR2 - isoform 1 [P21802-1] | 2 | EBI-15489950,EBI-15489960 |
Fibroblast growth factor 1 (PRO_0000008908)
With | #Exp. | IntAct |
---|---|---|
FGFR2 [P21802] | 5 | EBI-6880860,EBI-1028658 |
GO - Molecular functioni
- fibroblast growth factor receptor binding Source: UniProtKB
- growth factor activity Source: UniProtKB
- Hsp70 protein binding Source: Ensembl
- integrin binding Source: UniProtKB
- S100 protein binding Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 108537, 30 interactors |
CORUMi | P05230 |
DIPi | DIP-3787N |
IntActi | P05230, 17 interactors |
MINTi | P05230 |
STRINGi | 9606.ENSP00000480791 |
Chemistry databases
BindingDBi | P05230 |
Miscellaneous databases
RNActi | P05230, protein |
Structurei
Secondary structure
3D structure databases
BMRBi | P05230 |
SMRi | P05230 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P05230 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 127 – 143 | Heparin-bindingAdd BLAST | 17 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 24 – 27 | Nuclear localization signal | 4 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG3885, Eukaryota |
GeneTreei | ENSGT00940000160557 |
HOGENOMi | CLU_081609_5_1_1 |
InParanoidi | P05230 |
OMAi | KHADKNW |
OrthoDBi | 1157770at2759 |
PhylomeDBi | P05230 |
TreeFami | TF317805 |
Family and domain databases
CDDi | cd00058, FGF, 1 hit |
InterProi | View protein in InterPro IPR028210, FGF1 IPR002209, Fibroblast_GF_fam IPR008996, IL1/FGF |
PANTHERi | PTHR11486, PTHR11486, 1 hit PTHR11486:SF86, PTHR11486:SF86, 1 hit |
Pfami | View protein in Pfam PF00167, FGF, 1 hit |
PRINTSi | PR00263, HBGFFGF |
SMARTi | View protein in SMART SM00442, FGF, 1 hit |
SUPFAMi | SSF50353, SSF50353, 1 hit |
PROSITEi | View protein in PROSITE PS00247, HBGF_FGF, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
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
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketB5MCF4 | B5MCF4_HUMAN | Fibroblast growth factor 1 | FGF1 | 93 | Annotation score: | ||
C9JDC5 | C9JDC5_HUMAN | Fibroblast growth factor 1 | FGF1 | 58 | Annotation score: | ||
C9JUP6 | C9JUP6_HUMAN | Fibroblast growth factor 1 | FGF1 | 41 | Annotation score: |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_021357 | 21 | G → E1 PublicationCorresponds to variant dbSNP:rs17223632EnsemblClinVar. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_036536 | 57 – 60 | IQLQ → TDTK in isoform 2. 1 Publication | 4 | |
Alternative sequenceiVSP_036537 | 61 – 155 | Missing in isoform 2. 1 PublicationAdd BLAST | 95 |
Sequence databases
Genome annotation databases
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Web resourcesi
NIEHS-SNPs |
Sequence databases
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1AXM | X-ray | 3.00 | A/B/C/D/E/F | 21-155 | [»] | |
1DJS | X-ray | 2.40 | B | 21-155 | [»] | |
1DZC | NMR | - | A | 25-155 | [»] | |
1DZD | NMR | - | A | 29-155 | [»] | |
1E0O | X-ray | 2.80 | A/C | 16-155 | [»] | |
1EVT | X-ray | 2.80 | A/B | 22-155 | [»] | |
1HKN | X-ray | 2.00 | A/B/C/D/E/F | 17-155 | [»] | |
1JQZ | X-ray | 1.65 | A/B | 16-155 | [»] | |
1JT3 | X-ray | 1.95 | A/B | 16-155 | [»] | |
1JT4 | X-ray | 1.78 | A/B | 16-155 | [»] | |
1JT5 | X-ray | 1.85 | A/B | 16-155 | [»] | |
1JT7 | X-ray | 1.70 | A/B/C/D | 16-155 | [»] | |
1JTC | X-ray | 1.70 | A/B/C/D | 16-155 | [»] | |
1JY0 | X-ray | 1.70 | A/B | 16-155 | [»] | |
1K5U | X-ray | 2.00 | A/B/C | 16-154 | [»] | |
1K5V | X-ray | 2.10 | A/B | 16-154 | [»] | |
1M16 | X-ray | 1.70 | A/B | 16-155 | [»] | |
1NZK | X-ray | 1.95 | A/B/C/D | 16-152 | [»] | |
1P63 | X-ray | 1.60 | A/B | 16-155 | [»] | |
1PZZ | X-ray | 2.00 | A/B | 16-155 | [»] | |
1Q03 | X-ray | 2.05 | A/B | 16-152 | [»] | |
1Q04 | X-ray | 1.80 | A/B | 16-155 | [»] | |
1QCT | model | - | A/D | 24-153 | [»] | |
1RG8 | X-ray | 1.10 | A/B | 16-155 | [»] | |
1RML | NMR | - | A | 1-155 | [»] | |
1RY7 | X-ray | 3.20 | A | 1-155 | [»] | |
1YTO | X-ray | 2.10 | A/B/C/D | 16-155 | [»] | |
1Z2V | X-ray | 1.90 | A/B | 16-155 | [»] | |
1Z4S | X-ray | 2.60 | A/B/C/D | 16-155 | [»] | |
2AFG | X-ray | 2.00 | A/B/C/D | 16-155 | [»] | |
2AQZ | X-ray | 1.85 | A/B | 16-155 | [»] | |
2AXM | X-ray | 3.00 | A/B | 21-155 | [»] | |
2ERM | NMR | - | A | 17-155 | [»] | |
2HW9 | X-ray | 1.60 | A/B | 16-155 | [»] | |
2HWA | X-ray | 1.65 | A/B | 16-155 | [»] | |
2HWM | X-ray | 1.60 | A/B | 16-155 | [»] | |
2HZ9 | X-ray | 1.70 | A/B | 16-155 | [»] | |
2K43 | NMR | - | A | 23-155 | [»] | |
2K4A | NMR | - | B | 23-155 | [»] | |
2K8R | NMR | - | A | 23-155 | [»] | |
2KI4 | NMR | - | A/D | 23-155 | [»] | |
2KI6 | NMR | - | B/E | 23-155 | [»] | |
2NTD | X-ray | 2.52 | A/B/C/D | 16-155 | [»] | |
2Q9X | X-ray | 1.70 | A | 16-155 | [»] | |
2RQ9 | NMR | - | A | 22-155 | [»] | |
3B9U | X-ray | 1.55 | A | 16-155 | [»] | |
3BA4 | X-ray | 1.80 | A/B | 16-155 | [»] | |
3BA5 | X-ray | 1.75 | A/B | 16-155 | [»] | |
3BA7 | X-ray | 1.60 | A/B | 16-155 | [»] | |
3BAD | X-ray | 2.00 | A/B | 16-155 | [»] | |
3BAG | X-ray | 1.75 | A/B | 16-155 | [»] | |
3BAH | X-ray | 1.65 | A/B | 16-155 | [»] | |
3BAO | X-ray | 1.55 | A/B | 16-155 | [»] | |
3BAQ | X-ray | 1.80 | A/B | 16-155 | [»] | |
3BAU | X-ray | 1.60 | A/B | 16-155 | [»] | |
3BAV | X-ray | 1.62 | A/B | 16-155 | [»] | |
3BB2 | X-ray | 1.50 | A/B | 16-155 | [»] | |
3CQA | X-ray | 1.80 | A/B | 16-155 | [»] | |
3CRG | X-ray | 1.85 | A/B | 16-155 | [»] | |
3CRH | X-ray | 2.15 | A/B | 16-155 | [»] | |
3CRI | X-ray | 2.10 | A/B | 16-155 | [»] | |
3CU1 | X-ray | 2.60 | B/D | 22-152 | [»] | |
3FGM | X-ray | 1.95 | A/B | 16-155 | [»] | |
3FJ8 | X-ray | 2.00 | A/B | 16-155 | [»] | |
3FJ9 | X-ray | 1.90 | A/B | 16-155 | [»] | |
3FJA | X-ray | 1.95 | A/B | 16-155 | [»] | |
3FJB | X-ray | 2.00 | A/B | 16-155 | [»] | |
3FJC | X-ray | 2.00 | A/B | 16-155 | [»] | |
3FJD | X-ray | 1.90 | A/B | 16-155 | [»] | |
3FJE | X-ray | 2.10 | A/B | 16-155 | [»] | |
3FJF | X-ray | 1.90 | A/B | 16-155 | [»] | |
3FJH | X-ray | 1.90 | A/B | 16-155 | [»] | |
3FJI | X-ray | 2.55 | A/B/C/D | 16-155 | [»] | |
3FJJ | X-ray | 1.90 | A/B | 16-155 | [»] | |
3FJK | X-ray | 2.15 | A/B/C/D | 16-155 | [»] | |
3HOM | X-ray | 2.30 | A/B | 16-155 | [»] | |
3JUT | X-ray | 2.25 | A/B/C/D/E/F | 24-153 | [»] | |
3K1X | X-ray | 1.98 | A/B/C/D/E/F | 24-153 | [»] | |
3O3Q | X-ray | 1.60 | A/B/C/D | 16-155 | [»] | |
3OJ2 | X-ray | 2.20 | A/B | 1-155 | [»] | |
3OJM | X-ray | 2.10 | A | 1-155 | [»] | |
3OJV | X-ray | 2.60 | A/B | 21-155 | [»] | |
3UD7 | X-ray | 2.80 | A/B/C | 16-155 | [»] | |
3UD8 | X-ray | 2.37 | A/B/C | 16-155 | [»] | |
3UD9 | X-ray | 2.34 | A/B/C | 16-155 | [»] | |
3UDA | X-ray | 2.51 | A/B/C | 16-155 | [»] | |
4J23 | X-ray | 3.88 | B | 21-155 | [»] | |
4Q91 | X-ray | 1.80 | A/B | 16-155 | [»] | |
4Q9G | X-ray | 1.55 | A/B | 16-155 | [»] | |
4Q9P | X-ray | 1.80 | A/B | 16-155 | [»] | |
4QAL | X-ray | 1.50 | A/B | 16-155 | [»] | |
4QBC | X-ray | 1.52 | A/B | 16-155 | [»] | |
4QBV | X-ray | 1.50 | A/B | 16-155 | [»] | |
4QC4 | X-ray | 1.49 | A/B | 16-155 | [»] | |
4QO3 | X-ray | 2.05 | A/B | 16-155 | [»] | |
4XKI | X-ray | 2.00 | A/B | 16-155 | [»] | |
4YOL | X-ray | 1.97 | A/B | 16-155 | [»] | |
BMRBi | P05230 | |||||
SMRi | P05230 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 108537, 30 interactors |
CORUMi | P05230 |
DIPi | DIP-3787N |
IntActi | P05230, 17 interactors |
MINTi | P05230 |
STRINGi | 9606.ENSP00000480791 |
Chemistry databases
BindingDBi | P05230 |
ChEMBLi | CHEMBL2120 |
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 |
PTM databases
iPTMneti | P05230 |
PhosphoSitePlusi | P05230 |
Genetic variation databases
BioMutai | FGF1 |
DMDMi | 122737 |
Proteomic databases
EPDi | P05230 |
MassIVEi | P05230 |
MaxQBi | P05230 |
PaxDbi | P05230 |
PeptideAtlasi | P05230 |
PRIDEi | P05230 |
ProteomicsDBi | 51826 [P05230-1] 51827 [P05230-2] |
TopDownProteomicsi | P05230-1 [P05230-1] |
Protocols and materials databases
ABCDi | P05230, 1 sequenced antibody |
Antibodypediai | 1009, 736 antibodies |
DNASUi | 2246 |
Genome annotation databases
Organism-specific databases
CTDi | 2246 |
DisGeNETi | 2246 |
GeneCardsi | FGF1 |
HGNCi | HGNC:3665, FGF1 |
HPAi | ENSG00000113578, Group enriched (brain, heart muscle, kidney) |
MIMi | 131220, gene |
neXtProti | NX_P05230 |
OpenTargetsi | ENSG00000113578 |
PharmGKBi | PA28105 |
VEuPathDBi | HostDB:ENSG00000113578.17 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG3885, Eukaryota |
GeneTreei | ENSGT00940000160557 |
HOGENOMi | CLU_081609_5_1_1 |
InParanoidi | P05230 |
OMAi | KHADKNW |
OrthoDBi | 1157770at2759 |
PhylomeDBi | P05230 |
TreeFami | TF317805 |
Enzyme and pathway databases
PathwayCommonsi | P05230 |
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 |
SignaLinki | P05230 |
SIGNORi | P05230 |
Miscellaneous databases
BioGRID-ORCSi | 2246, 3 hits in 873 CRISPR screens |
ChiTaRSi | FGF1, human |
EvolutionaryTracei | P05230 |
GeneWikii | FGF1 |
GenomeRNAii | 2246 |
Pharosi | P05230, Tchem |
PROi | PR:P05230 |
RNActi | P05230, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000113578, Expressed in metanephric glomerulus and 189 other tissues |
ExpressionAtlasi | P05230, baseline and differential |
Genevisiblei | P05230, HS |
Family and domain databases
CDDi | cd00058, FGF, 1 hit |
InterProi | View protein in InterPro IPR028210, FGF1 IPR002209, Fibroblast_GF_fam IPR008996, IL1/FGF |
PANTHERi | PTHR11486, PTHR11486, 1 hit PTHR11486:SF86, PTHR11486:SF86, 1 hit |
Pfami | View protein in Pfam PF00167, FGF, 1 hit |
PRINTSi | PR00263, HBGFFGF |
SMARTi | View protein in SMART SM00442, FGF, 1 hit |
SUPFAMi | SSF50353, SSF50353, 1 hit |
PROSITEi | View protein in PROSITE PS00247, HBGF_FGF, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | FGF1_HUMAN | |
Accessioni | P05230Primary (citable) accession number: P05230 Secondary accession number(s): B2R5T0 Q16588 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 13, 1987 |
Last sequence update: | August 13, 1987 | |
Last modified: | February 10, 2021 | |
This is version 236 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human chromosome 5
Human chromosome 5: entries, gene names and cross-references to MIM