FGF1

Summary

FGF1 (fibroblast growth factor 1, HGNC:3665) is a protein-coding gene on chromosome 5q31.3, encoding Fibroblast growth factor 1 (P05230). Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration.

The protein encoded by this gene is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Multiple alternatively spliced variants encoding different isoforms have been described.

Source: NCBI Gene 2246 — RefSeq curated summary.

At a glance

• GWAS associations: 29
• Clinical variants (ClinVar): 21 total
• Druggable target: yes
• MANE Select transcript: NM_000800

Identifiers

Gene identifiers

Field	Value
HGNC ID	HGNC:3665
Approved symbol	FGF1
Name	fibroblast growth factor 1
Location	5q31.3
Locus type	gene with protein product
Status	Approved
Aliases	AFGF, ECGF, ECGFA, ECGFB, HBGF1, ECGF-beta, FGF-alpha, GLIO703
Ensembl gene	ENSG00000113578
Ensembl biotype	protein_coding
OMIM	131220
Entrez	2246

Gene structure

Transcript identifiers

Ensembl transcripts: 47 — 44 protein_coding, 2 retained_intron, 1 protein_coding_CDS_not_defined

ENST00000337706, ENST00000359370, ENST00000360966, ENST00000378046, ENST00000394496, ENST00000407758, ENST00000411960, ENST00000419524, ENST00000441680, ENST00000489937, ENST00000494344, ENST00000494579, ENST00000610990, ENST00000612258, ENST00000619447, ENST00000621536, ENST00000865998, ENST00000865999, ENST00000866000, ENST00000866001, ENST00000866002, ENST00000866003, ENST00000866004, ENST00000866005, ENST00000866006, ENST00000866007, ENST00000866008, ENST00000866009, ENST00000866010, ENST00000866011, ENST00000866012, ENST00000866013, ENST00000866014, ENST00000866015, ENST00000866016, ENST00000866017, ENST00000954582, ENST00000954583, ENST00000954584, ENST00000954585, ENST00000954586, ENST00000954587, ENST00000954588, ENST00000954589, ENST00000954590, ENST00000954591, ENST00000954592

RefSeq mRNA: 27 — MANE Select: NM_000800 NM_000800, NM_001144892, NM_001144934, NM_001144935, NM_001257205, NM_001257206, NM_001257207, NM_001257208, NM_001257209, NM_001257210, NM_001257211, NM_001257212, NM_001354951, NM_001354952, NM_001354953, NM_001354954, NM_001354955, NM_001354956, NM_001354957, NM_001354958, NM_001354959, NM_001354961, NM_001354962, NM_001354963, NM_001354964, NM_033136, NM_033137

CCDS: CCDS4275, CCDS4276

Canonical transcript exons

ENST00000337706 — 4 exons

Exon	Start	End
ENSE00001739928	142592178	142595484
ENSE00001902113	142685957	142686090
ENSE00003484867	142600702	142600805
ENSE00003530715	142613959	142614161

Expression profiles

Bgee: expression breadth ubiquitous, 228 present calls, max score 99.47.

FANTOM5 (CAGE): breadth broad, TPM avg 10.2126 / max 725.1782, expressed in 703 samples.

FANTOM5 promoters (14 alternative TSS)

Promoter ID	TPM avg	Samples expressed
63902	4.1956	183
63903	3.0320	147
63907	1.5899	195
63896	0.6376	316
63904	0.3033	114
63901	0.1089	65
63900	0.0987	42
63906	0.0680	46
63897	0.0515	13
63905	0.0470	29

Top tissues by expression

284 total, by Bgee expression score (0-100, higher = more expressed):

Tissue	Anatomy ID	Expression score	Quality
renal glomerulus	UBERON:0000074	99.47	gold quality
metanephric glomerulus	UBERON:0004736	99.37	gold quality
inferior vagus X ganglion	UBERON:0005363	99.34	gold quality
corpus callosum	UBERON:0002336	99.21	gold quality
cranial nerve II	UBERON:0000941	99.18	gold quality
lateral globus pallidus	UBERON:0002476	99.15	gold quality
globus pallidus	UBERON:0001875	99.11	gold quality
medial globus pallidus	UBERON:0002477	99.07	gold quality
medulla oblongata	UBERON:0001896	99.04	gold quality
inferior olivary complex	UBERON:0002127	98.98	gold quality
olfactory bulb	UBERON:0002264	98.97	gold quality
C1 segment of cervical spinal cord	UBERON:0006469	98.96	gold quality
subthalamic nucleus	UBERON:0001906	98.95	gold quality
trigeminal ganglion	UBERON:0001675	98.94	gold quality
substantia nigra pars reticulata	UBERON:0001966	98.88	gold quality
spinal cord	UBERON:0002240	98.87	gold quality
dorsal motor nucleus of vagus nerve	UBERON:0002870	98.86	gold quality
superior vestibular nucleus	UBERON:0007227	98.86	gold quality
substantia nigra	UBERON:0002038	98.82	gold quality
midbrain	UBERON:0001891	98.80	gold quality
middle frontal gyrus	UBERON:0002702	98.75	gold quality
substantia nigra pars compacta	UBERON:0001965	98.41	gold quality
ventral tegmental area	UBERON:0002691	98.41	gold quality
pons	UBERON:0000988	98.32	gold quality
putamen	UBERON:0001874	98.24	gold quality
dorsal root ganglion	UBERON:0000044	98.22	gold quality
amygdala	UBERON:0001876	98.19	gold quality
dorsal plus ventral thalamus	UBERON:0001897	98.02	gold quality
hypothalamus	UBERON:0001898	97.88	gold quality
Ammon’s horn	UBERON:0001954	97.75	gold quality

Single-cell (SCXA)

Detected in 2 experiment(s), a significant marker in 1.

Experiment	Marker?	Max mean expression
E-CURD-119	yes	31.67
E-ANND-3	no	3.35

Regulation

Is transcription factor: no

Upstream regulators (CollecTRI, top): ETS2, MYOD1, NFE2L2, NR1H3, PPARA, PPARG, RFX1, RFX2, RFX3, STAT3, ZHX2

miRNA regulators (miRDB)

132 targeting FGF1, top 30 by miRDB confidence (max_score; target_count = how many genes the miRNA targets in total — lower means more specific):

miRNA	Max score	Avg score	miRNA target_count
HSA-MIR-126-5P	100.00	72.71	3180
HSA-MIR-6740-5P	100.00	65.64	932
HSA-MIR-513B-5P	99.99	69.96	2150
HSA-MIR-485-3P	99.98	70.68	1585
HSA-MIR-539-3P	99.98	70.74	1616
HSA-MIR-12136	99.98	72.81	5713
HSA-MIR-302C-5P	99.97	72.56	3642
HSA-MIR-4487	99.96	64.58	1252
HSA-MIR-3143	99.93	71.96	3104
HSA-MIR-381-3P	99.93	71.87	2854
HSA-MIR-6835-3P	99.93	70.49	2904
HSA-MIR-300	99.92	71.76	2856
HSA-MIR-4731-5P	99.89	67.23	2537
HSA-MIR-153-5P	99.89	73.86	6317
HSA-MIR-4492	99.87	68.25	3611
HSA-MIR-579-3P	99.86	71.66	3628
HSA-MIR-664B-3P	99.84	71.65	3590
HSA-MIR-4799-5P	99.82	70.60	2663
HSA-MIR-7856-5P	99.75	69.99	2901
HSA-MIR-4699-3P	99.71	70.15	3142
HSA-MIR-4729	99.69	72.18	4233
HSA-MIR-5004-5P	99.68	66.63	1294
HSA-MIR-1251-3P	99.64	67.21	1408
HSA-MIR-4516	99.61	67.78	3390
HSA-MIR-6132	99.60	65.83	1554
HSA-MIR-6836-5P	99.60	65.62	1538
HSA-MIR-4328	99.57	71.06	4094
HSA-MIR-4762-5P	99.57	68.54	1424
HSA-MIR-5007-3P	99.51	68.14	1242
HSA-MIR-1224-5P	99.48	65.59	803

Literature-anchored findings (GeneRIF, showing 40)

• Alternative type I and I’ turn conformations in the beta8/beta9 beta-hairpin (PMID:11847269)
• possible role of fibroblast growth factors in expression of genes of the plasminogen activator system in breast fibroblasts (PMID:12008951)
• bFGF and aFGF may suppress endothelial-dependent monocyte recruitment and thus have an anti-inflammatory action during angiogenesis in chronic inflammation but inhibit the immunoinflammatory tumor defense mechanism (PMID:12057924)
• identification of rare partially unfolded states in equilibrium with the native conformation (PMID:12118009)
• Recombinant human FGF-1 binds to both the catalytic alpha-subunit and to the regulatory beta-subunit of CK2. A correlation between the mitogenic potential of FGF-1 mutants and their ability to bind to CK2 alpha was observed. (PMID:12145206)
• Maintenance of the human umbilical vein endothelial cell phenotype and differentiation into smooth muscle-like cells are reciprocally controlled by fibroblast growth factor-1 and activin A. (PMID:12417591)
• The mitogenic acitivity of AFGF was inhibited by the synthetic peptide Ac-ValTyrMetSerProPhe-NH2. (PMID:12440521)
• The conformational stability and dynamics of FGF1 have been measured on the basis of amide proton-exchange kinetics, monitored by two-dimensional NMR spectroscopy. (PMID:12484774)
• No associations of intracranial aneurysm and FGF1 were found. (PMID:12750963)
• According to phase of menstrual cycle, endometrial stromal cells from endometriosis patients in late proliferative phase had higher bFGF mRNA values and lower 1B FGF-antisense mRNA compared with controls (PMID:12788899)
• Binding studies demonstrated no high-affinity interaction of FGF-1 with fibrinogen or fibrin; unlike FGF-2, FGF-1 can support vascular endothelial cell growth only if continually present in soluble form. (PMID:12871334)
• An alternative core packing group, involving a set of five positions, has been introduced into human acidic FGF-1 (PMID:14627732)
• FGF1 transcriptionally induces membrane type-1 matrix metalloproteinase expression in a prostate carcinoma cell line. (PMID:14673954)
• Data show that mouse and human fibroblast growth factor 1 (FGF-1) internal ribosome entry sites show similar activity profiles, and have a conserved structural domain at both the nucleotide sequence and RNA structure levels. (PMID:15314170)
• Promoter polymorphism and genetic susceptibility for Alzheimer’s disease (PMID:15358178)
• 1.10-A atomic resolution X-ray structure of human fibroblast growth factor 1 (FGF-1), a member of the beta-trefoil superfold, has been determined (PMID:15382229)
• FGF-1 is a key human adipogenic factor, involved in fat tissue growth. (PMID:15561939)
• residues flanking the the beta4/beta5 and beta8/beta9 beta-hairpin turns of human acidic fibroblast growth factor are a primary structural determinant of the conformation within the turn (PMID:15632285)
• FGF-1 contains a second putative NLS (NLS2), which is located near the C-terminus. It is a bipartite NLS consisting of two clusters of lysines separated by a spacer of 10 amino acids. (PMID:15835896)
• FGF-1 regulates HO-1 expression through Nrf2 (PMID:15870071)
• A recombinant nonmitogenic form of aFGF (nhaFGF) was purified and the mitogenic activity of the purified nhaFGF was decreased dramatically comparable to that of the wild-type aFGF (haFGF). (PMID:15882952)
• Data indicate that after endocytosis, fibroblast growth factor receptor (FGFR)4 and its bound ligand, FGF1, are sorted mainly to the recycling compartment, whereas FGFR1-3 with ligand are sorted mainly to degradation in the lysosomes. (PMID:16091423)
• FGF1 dimerization upon heparin was favored over monomeric interactions even when a large excess of saccharide was present (PMID:16219767)
• FGF-1 might have both autocrine and paracrine functions in renal inflammation (PMID:16316338)
• A type I 4:6 turn at turn 1 of FGF-1 appears essential for efficient mitogenic function. (PMID:16355415)
• Data suggest that minor changes of local kynurenic acid concentration may modulate fibroblast growth factor-1 release, cell proliferation, and ultimately tissue damage in different pathological conditions. (PMID:16392031)
• Two molecules of suramin appear to bind simultaneously to one molecule of hFGF-1 with high affinity (PMID:16411766)
• Hsp90 is required for translocation of FGF-1 and FGF-2 across the endosomal membrane (PMID:16495214)
• FGF-1 can have an antifibrogenic role, inducing apoptosis of fibroblasts and inhibiting myofibroblast differentiation (PMID:16766579)
• analysis of heparan sulfate-related oligosaccharide binding to fibroblast growth factors 1 and 2 and their receptors (PMID:16807244)
• Can be efficiently expressed in Pichia pastoris. (PMID:17134911)
• Amplification of FGF-1 at 5q31 in ovarian cancer tissues leads to increased angiogenesis, and autocrine stimulation of cancer cells, which may result in poorer overall survival in patents with high-grade advanced stage serous ovarian cancer (PMID:17538174)
• Results describe the stabilization of human fibroblast growth factor-1 by targeting the N and C terminus beta-strand interactions. (PMID:17570396)
• FGF1 was scored as one of several lead candidate gene products to modulate the transdifferentiation process and is shown here to exert inhibitory effects on adipogenic commitment and differentiation. (PMID:17610236)
• FGF and PDGF have roles in cell proliferation and migration in osteoblastic cells (PMID:17852407)
• genetic variation within FGF1 cosegregates with elevated blood pressure in hypertensive families and that this association is likely to be mediated by upregulation of renal FGF1 expression. (PMID:17909102)
• FGF and FGFR may have a role in cleft lip and cleft palate (PMID:17963255)
• the induction of apoptosis through the inhibition of endogenous FGF signaling is caspase-9 pathway- dependent (PMID:18202770)
• The Asx-Pro-Asx-Gly type I beta-turn motif stability in FGF1. (PMID:18308335)
• integrin alphavbeta3 binding to FGF1 plays a role in FGF1 signaling (PMID:18441324)

Cross-species orthologs

2 orthologs

Organism	Symbol	Gene ID
mus_musculus	Fgf1	ENSMUSG00000036585
rattus_norvegicus	Fgf1	ENSRNOG00000087149

Paralogs (21): FGF10 (ENSG00000070193), FGF22 (ENSG00000070388), FGF4 (ENSG00000075388), FGF20 (ENSG00000078579), FGF14 (ENSG00000102466), FGF9 (ENSG00000102678), FGF21 (ENSG00000105550), FGF8 (ENSG00000107831), FGF6 (ENSG00000111241), FGF12 (ENSG00000114279), FGF23 (ENSG00000118972), FGF13 (ENSG00000129682), FGF5 (ENSG00000138675), FGF2 (ENSG00000138685), FGF7 (ENSG00000140285), FGF18 (ENSG00000156427), FGF17 (ENSG00000158815), FGF11 (ENSG00000161958), FGF19 (ENSG00000162344), FGF3 (ENSG00000186895), FGF16 (ENSG00000196468)

Protein

Protein identifiers

Fibroblast growth factor 1 — P05230 (reviewed: P05230)

Alternative names: Acidic fibroblast growth factor, Endothelial cell growth factor, Heparin-binding growth factor 1

All UniProt accessions (6): A0A7U3JVZ2, A8K147, B5MCF4, C9JDC5, C9JUP6, P05230

UniProt curated annotations — full annotation on UniProt →

Function. Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as a 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.

Subunit / interactions. 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 Cu(2+)-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.

Subcellular location. Secreted. Cytoplasm. Cell cortex. Cytosol. Nucleus.

Tissue specificity. Predominantly expressed in kidney and brain. Detected at much lower levels in heart and skeletal muscle.

Post-translational modifications. In the nucleus, phosphorylated by PKC/PRKCD.

Similarity. Belongs to the heparin-binding growth factors family.

Isoforms (2)

UniProt ID	Names	Canonical?
P05230-1	1	yes
P05230-2	2

RefSeq proteins (27): NP_000791, NP_001138364, NP_001138406, NP_001138407, NP_001244134, NP_001244135, NP_001244136, NP_001244137, NP_001244138, NP_001244139, NP_001244140, NP_001244141, NP_001341880, NP_001341881, NP_001341882, NP_001341883, NP_001341884, NP_001341885, NP_001341886, NP_001341887, NP_001341888, NP_001341890, NP_001341891, NP_001341892, NP_001341893, NP_149127, NP_149128 (=MANE)

Domains & families (InterPro)

ID	Name	Type
IPR002209	Fibroblast_GF_fam	Family
IPR008996	IL1/FGF	Homologous_superfamily

Pfam: PF00167

UniProt features (50 total): mutagenesis site 15, strand 14, turn 6, helix 5, splice variant 2, initiator methionine 1, propeptide 1, chain 1, region of interest 1, short sequence motif 1, binding site 1, modified residue 1, sequence variant 1

Structure

Experimental structures (PDB)

96 structures, top 30 by resolution.

PDB	Method	Resolution (Å)
1RG8	X-RAY DIFFRACTION	1.1
4QC4	X-RAY DIFFRACTION	1.49
4QBV	X-RAY DIFFRACTION	1.5
3BB2	X-RAY DIFFRACTION	1.5
4QAL	X-RAY DIFFRACTION	1.5
4QBC	X-RAY DIFFRACTION	1.52
3B9U	X-RAY DIFFRACTION	1.55
3BAO	X-RAY DIFFRACTION	1.55
4Q9G	X-RAY DIFFRACTION	1.55
1P63	X-RAY DIFFRACTION	1.6
2HW9	X-RAY DIFFRACTION	1.6
2HWM	X-RAY DIFFRACTION	1.6
3BA7	X-RAY DIFFRACTION	1.6
3BAU	X-RAY DIFFRACTION	1.6
3O3Q	X-RAY DIFFRACTION	1.6
3BAV	X-RAY DIFFRACTION	1.62
1JQZ	X-RAY DIFFRACTION	1.65
2HWA	X-RAY DIFFRACTION	1.65
3BAH	X-RAY DIFFRACTION	1.65
1JT7	X-RAY DIFFRACTION	1.7
1JTC	X-RAY DIFFRACTION	1.7
1JY0	X-RAY DIFFRACTION	1.7
1M16	X-RAY DIFFRACTION	1.7
2HZ9	X-RAY DIFFRACTION	1.7
2Q9X	X-RAY DIFFRACTION	1.7
3BA5	X-RAY DIFFRACTION	1.75
3BAG	X-RAY DIFFRACTION	1.75
1JT4	X-RAY DIFFRACTION	1.78
4Q91	X-RAY DIFFRACTION	1.8
1Q04	X-RAY DIFFRACTION	1.8

Predicted structure (AlphaFold)

Model	pLDDT	Fraction very-high
AF-P05230-F1	91.05	0.81

Functional residue map

Curated UniProt residues grouped by drug-discovery relevance — catalytic, ligand-binding, modification, and mutation-validated positions. Source: UniProtKB sequence features.

Ligand- & substrate-binding residues (1): 33

Post-translational modifications (1): 2

Mutagenesis-validated functional residues (15):

Position	Phenotype
24–27	loss of nuclear import leading to loss of phosphorylation by pkc/prkcd.
33	no effect on integrin-binding.
50	dominant-negative mutant. defective in integrin-binding and in ternary complex formation with integrin and fgfr1. no eff
102	no effect on integrin-binding. no effect on integrin- and heparin-binding, loss of fgfr1-binding, defective in inducing
109	no effect on integrin- and heparin-binding, loss of fgfr1-binding, defective in inducing fgf1 signaling, cell proliferat
110	no effect on integrin-binding. no effect on integrin- and heparin-binding, loss of fgfr1-binding, defective in inducing
114	decrease in lrrc59-binding.
127	reduced integrin-binding; when associated with e-128. defective in integrin-, heparin- and fgfr1-binding, and defective
128	reduced integrin-binding; when associated with e-127. defective in integrin-, heparin- and fgfr1-binding, and defective
131	decrease in lrrc59-binding.
133	loss of lrrc59-binding.
133	loss of csnk2a-, csnk2b- and lrrc59-binding. reduced integrin-binding; when associated with e-134. defective in integrin
133	no effect on lrrc59-binding.
134	reduced integrin-binding; when associated with e-133. defective in integrin-, heparin- and fgfr1-binding, and defective

Function

Pathways and Gene Ontology

Reactome pathways

40 pathways

ID	Pathway
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-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

MSigDB gene sets: 402 (showing top): GOBP_MORPHOGENESIS_OF_AN_EPITHELIUM, CREL_01, REACTOME_SIGNALING_BY_INSULIN_RECEPTOR, GOBP_REGULATION_OF_CELLULAR_RESPONSE_TO_GROWTH_FACTOR_STIMULUS, MODULE_516, GOBP_EPITHELIUM_DEVELOPMENT, GOBP_CELL_CHEMOTAXIS, GOBP_REGULATION_OF_PHOSPHORYLATION, KEGG_MAPK_SIGNALING_PATHWAY, GOBP_BRANCH_ELONGATION_OF_AN_EPITHELIUM, REACTOME_FGFR2C_LIGAND_BINDING_AND_ACTIVATION, REACTOME_SIGNALING_BY_FGFR, REACTOME_FGFR1_LIGAND_BINDING_AND_ACTIVATION, GOBP_POSITIVE_REGULATION_OF_VASCULATURE_DEVELOPMENT, GOBP_GROWTH

GO Biological Process (32): angiogenesis (GO:0001525), organ induction (GO:0001759), signal transduction (GO:0007165), positive regulation of cell population proliferation (GO:0008284), fibroblast growth factor receptor signaling pathway (GO:0008543), anatomical structure morphogenesis (GO:0009653), positive regulation of endothelial cell migration (GO:0010595), neurogenesis (GO:0022008), lung development (GO:0030324), regulation of cell migration (GO:0030334), positive regulation of cell migration (GO:0030335), activation of protein kinase B activity (GO:0032148), cellular response to heat (GO:0034605), wound healing (GO:0042060), positive regulation of MAP kinase activity (GO:0043406), positive regulation of MAPK cascade (GO:0043410), positive regulation of cholesterol biosynthetic process (GO:0045542), positive regulation of angiogenesis (GO:0045766), positive regulation of transcription by RNA polymerase II (GO:0045944), epithelial cell proliferation (GO:0050673), positive regulation of epithelial cell proliferation (GO:0050679), positive regulation of cell division (GO:0051781), branch elongation involved in ureteric bud branching (GO:0060681), positive regulation of ERK1 and ERK2 cascade (GO:0070374), mesonephric epithelium development (GO:0072163), regulation of endothelial tube morphogenesis (GO:1901509), positive regulation of intracellular signal transduction (GO:1902533), positive regulation of sprouting angiogenesis (GO:1903672), regulation of endothelial cell chemotaxis to fibroblast growth factor (GO:2000544), branching involved in ureteric bud morphogenesis (GO:0001658), cell differentiation (GO:0030154), regulation of morphogenesis of an epithelium (GO:1905330)

GO Molecular Function (6): fibroblast growth factor receptor binding (GO:0005104), integrin binding (GO:0005178), growth factor activity (GO:0008083), heparin binding (GO:0008201), S100 protein binding (GO:0044548), protein binding (GO:0005515)

GO Cellular Component (8): extracellular region (GO:0005576), obsolete extracellular space (GO:0005615), nucleus (GO:0005634), nucleoplasm (GO:0005654), cytoplasm (GO:0005737), cytosol (GO:0005829), cell cortex (GO:0005938), extracellular matrix (GO:0031012)

Reactome top-level categories

Rollup of top-15 pathways:

Category	Pathways
Downstream signaling of activated FGFR1	3
FGFR1 ligand binding and activation	2
FGFR3 ligand binding and activation	2
FGFR2 ligand binding and activation	2
IRS-mediated signalling	1
Intracellular signaling by second messengers	1
FGFR1 mutant receptor activation	1
FGFR3 mutant receptor activation	1
Signaling by FGFR4	1
FGFR2 mutant receptor activation	1
PI3K/AKT Signaling in Cancer	1
Downstream signaling of activated FGFR2	1
Downstream signaling of activated FGFR3	1
Downstream signaling of activated FGFR4	1
Signaling by FGFR1	1

GO top-level categories

Rollup of top GO terms by namespace:

Category	Terms
cellular anatomical structure	4
cell population proliferation	2
cell migration	2
cytoplasm	2
blood vessel morphogenesis	1
anatomical structure formation involved in morphogenesis	1
regulation of animal organ formation	1
specification of animal organ identity	1
developmental induction	1
positive regulation of animal organ morphogenesis	1
cell communication	1
cellular process	1
signaling	1
regulation of cellular process	1
cellular response to stimulus	1
regulation of cell population proliferation	1
positive regulation of cellular process	1
cell surface receptor protein tyrosine kinase signaling pathway	1
cellular response to fibroblast growth factor stimulus	1
developmental process	1
anatomical structure development	1
regulation of endothelial cell migration	1
positive regulation of cell migration	1
endothelial cell migration	1
nervous system development	1
cell differentiation	1
respiratory tube development	1
animal organ development	1
respiratory system development	1
regulation of cell motility	1
regulation of cell migration	1
positive regulation of cell motility	1
activation of protein kinase activity	1
response to heat	1
cellular response to stress	1
response to wounding	1
tissue regeneration	1
MAP kinase activity	1
regulation of MAP kinase activity	1
positive regulation of MAPK cascade	1

Protein interactions and networks

STRING

2785 interactions, top by confidence (×1000):

Protein A	Protein B	Partner UniProt	Score
FGF1	FGFR1	P11362	998
FGF1	FGFR2	P18443	997
FGF1	FGFR3	P22607	995
FGF1	FGFR4	P22455	994
FGF1	FGFBP1	Q14512	991
FGF1	FIBP	O43427	934
FGF1	FGF2	P09038	931
FGF1	FGF13	Q92913	925
FGF1	FGF17	O60258	922
FGF1	S100A13	Q99584	922
FGF1	HSPG2	P98160	845
FGF1	EGF	P01133	839
FGF1	IGF1	P01343	826
FGF1	FLT1	P16057	817
FGF1	TGFB1	P01137	808
FGF1	NGF	P01138	808

IntAct

37 interactions, top by confidence:

A	B	Type	Score
FGFR1	FGF1	psi-mi:“MI:0407”(direct interaction)	0.840
FGF1	FGFR1	psi-mi:“MI:0407”(direct interaction)	0.840
FGFR1	FGF1	psi-mi:“MI:2364”(proximity)	0.840
FGFR2	FGF1	psi-mi:“MI:0407”(direct interaction)	0.670
FGF1	FGFR2	psi-mi:“MI:2364”(proximity)	0.670
FGF1	VBP1	psi-mi:“MI:0915”(physical association)	0.560
	FGF1	psi-mi:“MI:0407”(direct interaction)	0.560
FGF1	FGFR3	psi-mi:“MI:0407”(direct interaction)	0.560
HSPG2	FGF1	psi-mi:“MI:0915”(physical association)	0.560
	FGF1	psi-mi:“MI:0407”(direct interaction)	0.540
	FGF1	psi-mi:“MI:0915”(physical association)	0.540
CLDN10	ATE1	psi-mi:“MI:0914”(association)	0.530
FGF1	SDC4	psi-mi:“MI:0914”(association)	0.530
CD44	PDPK1	psi-mi:“MI:0914”(association)	0.530
FGFR4	FGF1	psi-mi:“MI:2364”(proximity)	0.480
FGFR2	FGF1	psi-mi:“MI:0407”(direct interaction)	0.440
FGF1	FGFR3	psi-mi:“MI:0407”(direct interaction)	0.440
FGF1	FGF1	psi-mi:“MI:0407”(direct interaction)	0.440
FGF1	SRPK1	psi-mi:“MI:0217”(phosphorylation reaction)	0.440
TRPV2	FGF1	psi-mi:“MI:0915”(physical association)	0.370
RPL7L1	MAGEB2	psi-mi:“MI:0914”(association)	0.350
FGF1	KDM1A	psi-mi:“MI:0914”(association)	0.350

BioGRID (104): GSE1 (Affinity Capture-MS), EGFLAM (Affinity Capture-MS), RCOR1 (Affinity Capture-MS), RCOR3 (Affinity Capture-MS), KDM1A (Affinity Capture-MS), GPC6 (Affinity Capture-MS), GPC1 (Affinity Capture-MS), TGFBR3 (Affinity Capture-MS), SDC4 (Affinity Capture-MS), HMG20A (Affinity Capture-MS), SDC2 (Affinity Capture-MS), FGF1 (Affinity Capture-MS), FGFR1 (Co-localization), FGFR4 (Co-localization), FGF1 (Co-localization)

ESM2 similar proteins: A6P7H6, O35622, O57341, O60258, O76093, O88182, O89101, P03968, P03969, P05230, P12226, P19596, P20002, P20003, P21781, P34004, P36363, P37237, P41444, P48798, P48800, P48808, P55075, P61148, P61149, P61150, P61328, P61329, P63075, P63076, P70377, P70379, P79150, Q02195, Q0VCA0, Q5D0X0, Q5NVQ3, Q5RAY8, Q5RDS9, Q6GLR6

Diamond homologs: A0MTF4, A6P7H6, M3X9S6, O15520, O35565, O43320, O54769, P03968, P03969, P05230, P05524, P08620, P09038, P10767, P11403, P11487, P12034, P12226, P13109, P15655, P15656, P19596, P20002, P20003, P21658, P21781, P31371, P34004, P36363, P36364, P36386, P48798, P48799, P48800, P48801, P48802, P48803, P48804, P48805, P48806

SIGNOR signaling

7 interactions.

A	Effect	B	Mechanism
FGF1	up-regulates	FGFR4	binding
FGF1	up-regulates	FGFR3	binding
FGF1	“up-regulates activity”	FGFR1	binding
PRKCD	“up-regulates quantity”	FGF1	phosphorylation
FGF1	up-regulates	FGFR2	binding
FGF1	up-regulates	FGFR1	binding
“pazopanib hydrochloride”	“down-regulates activity”	FGF1	“chemical inhibition”

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 21 IntAct physical interaction partners (hypergeometric vs the genome-wide background, BH-FDR, gene-set size 15–500, ranked by fold). A functional readout of the neighbourhood — distinct from this gene’s own memberships above, and biased toward well-studied / hub proteins, so read it as themes rather than proof.

Reactome pathways:

Pathway	Partners	Fold	FDR
PIP3 activates AKT signaling	6	26.7×	8e-06

GO biological processes:

GO term	Partners	Fold	FDR
cell migration	6	19.4×	5e-05

Disease & clinical

Clinical variants and AI predictions

ClinVar

21 variants total. Per-class counts are floors (≥ shown; pagination cap):

Classification	Count (floor)
Pathogenic	0
Likely pathogenic	0
Uncertain significance	15
Likely benign	0
Benign	1

Top pathogenic / likely-pathogenic (0)

SpliceAI

762 predictions. Top by Δscore:

Variant	Effect	Δscore
5:142600695:TACT:T	donor_loss	1.0000
5:142600696:ACT:A	donor_loss	1.0000
5:142600698:TTAC:T	donor_loss	1.0000
5:142600699:TACT:T	donor_loss	1.0000
5:142600700:A:AC	donor_gain	1.0000
5:142600701:C:CC	donor_gain	1.0000
5:142600701:CTGA:C	donor_gain	1.0000
5:142600701:CTGAG:C	donor_gain	1.0000
5:142600802:TGAA:T	acceptor_gain	1.0000
5:142600806:C:CC	acceptor_gain	1.0000
5:142613957:A:AC	donor_gain	1.0000
5:142613958:C:CC	donor_gain	1.0000
5:142613958:CTGTG:C	donor_gain	1.0000
5:142595482:CTG:C	acceptor_gain	0.9900
5:142600696:A:AC	donor_gain	0.9900
5:142600697:C:CC	donor_gain	0.9900
5:142600697:CTTA:C	donor_gain	0.9900
5:142600701:CT:C	donor_gain	0.9900
5:142600701:CTG:C	donor_gain	0.9900
5:142600801:CTGAA:C	acceptor_gain	0.9900
5:142600803:GAA:G	acceptor_gain	0.9900
5:142600804:AA:A	acceptor_gain	0.9900
5:142600805:AC:A	acceptor_loss	0.9900
5:142600807:T:A	acceptor_loss	0.9900
5:142614162:C:CC	acceptor_gain	0.9900
5:142595480:GTCTG:G	acceptor_gain	0.9800
5:142595483:TG:T	acceptor_gain	0.9800
5:142595485:C:CC	acceptor_gain	0.9800
5:142613958:CT:C	donor_gain	0.9800
5:142614157:CAAGA:C	acceptor_gain	0.9800

AlphaMissense

0 scored. Top likely-pathogenic:

dbSNP variants (sampled 300 via entrez): RS1000033172 (5:142616532 G>A,C), RS1000048145 (5:142602377 A>C), RS1000078835 (5:142602685 G>A), RS1000111556 (5:142624030 C>T), RS1000156285 (5:142655486 T>C), RS1000183584 (5:142639230 T>A), RS1000211929 (5:142600258 G>T), RS1000228099 (5:142624253 G>A,C,T), RS1000243605 (5:142666956 G>C), RS1000254036 (5:142639629 T>C), RS1000298833 (5:142679395 C>T), RS1000320771 (5:142594283 C>G), RS1000325030 (5:142665034 T>C), RS1000369424 (5:142677577 G>A), RS1000408422 (5:142633250 T>C)

Disease associations

OMIM: gene MIM:131220 | disease phenotypes:

GenCC curated gene-disease

Mondo (0):

Orphanet (0):

HPO phenotypes

0 total (0 of 0 shown, HPO-id order):

GWAS associations

29 associations (top):

Study	Trait	p-value
GCST000960_7	Cardiac hypertrophy	8.000000e-07
GCST005667_33	Central corneal thickness	5.000000e-09
GCST006218_16	Erosive tooth wear (severe vs non-severe)	6.000000e-08
GCST006218_18	Erosive tooth wear (severe vs non-severe)	3.000000e-08
GCST006218_93	Erosive tooth wear (severe vs non-severe)	7.000000e-06
GCST006226_18	Erosive tooth wear (severe vs none or mild)	5.000000e-06
GCST008050_12	Waist-hip ratio	4.000000e-07
GCST008050_2	Waist-hip ratio	1.000000e-09
GCST008758_53	Pre-treatment viral load in HIV-1 infection	5.000000e-16
GCST010866_108	Coronary artery disease	2.000000e-11
GCST90000654_37	Central corneal thickness	7.000000e-12
GCST90013407_179	Liver enzyme levels (gamma-glutamyl transferase)	2.000000e-10
GCST90020024_922	A body shape index	2.000000e-08
GCST90020024_923	A body shape index	3.000000e-08
GCST90020024_924	A body shape index	1.000000e-13
GCST90020025_684	Waist-to-hip ratio adjusted for BMI	1.000000e-10
GCST90020025_685	Waist-to-hip ratio adjusted for BMI	9.000000e-17
GCST90020025_686	Waist-to-hip ratio adjusted for BMI	5.000000e-10
GCST90020025_687	Waist-to-hip ratio adjusted for BMI	4.000000e-23
GCST90020026_299	Hip index	2.000000e-10
GCST90020026_300	Hip index	5.000000e-09
GCST90020026_301	Hip index	7.000000e-10
GCST90020027_688	Waist-hip index	5.000000e-11
GCST90020027_689	Waist-hip index	4.000000e-17
GCST90020027_690	Waist-hip index	4.000000e-10
GCST90020027_691	Waist-hip index	4.000000e-23
GCST90020029_1279	Waist circumference adjusted for body mass index	2.000000e-08
GCST90020029_1280	Waist circumference adjusted for body mass index	5.000000e-09
GCST90020029_1281	Waist circumference adjusted for body mass index	2.000000e-14

EFO canonical traits (8, from GWAS)

EFO ID	Trait name
EFO:0002503	cardiac hypertrophy
EFO:0005213	central corneal thickness
EFO:0004343	waist-hip ratio
EFO:0010125	viral load
EFO:0004532	serum gamma-glutamyl transferase measurement
EFO:0007789	BMI-adjusted waist circumference
EFO:0007788	BMI-adjusted waist-hip ratio
EFO:0008039	BMI-adjusted hip circumference

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (3): CHEMBL2120 (SINGLE PROTEIN), CHEMBL4630720 (PROTEIN COMPLEX), CHEMBL4802036 (PROTEIN COMPLEX)

PharmGKB: 1 entry (VIP=true, CPIC=false)

Binding affinities (BindingDB)

11 measured of 11 human assays (11 total across all organisms); most potent 11 below. Values come from heterogeneous assays and are not directly comparable.

Ligand	Measure	Value
Linked sulfated tetracyclitol, 12	KD	0.4 nM
Linked sulfated tetracyclitol, 3	KD	7.2 nM
Linked sulfated tetracyclitol, 7	KD	8 nM
Linked sulfated tetracyclitol, 2	KD	20.7 nM
Linked sulfated tetracyclitol, 4	KD	25.4 nM
Linked sulfated tetracyclitol, 5	KD	29.8 nM
Linked sulfated tetracyclitol, 6	KD	39 nM
Linked sulfated tetracyclitol, 8	KD	40.4 nM
Linked sulfated tetracyclitol, 10	KD	115 nM
Linked sulfated tetracyclitol, 9	KD	119 nM
Linked sulfated tetracyclitol, 11	KD	187 nM

ChEMBL bioactivities

53 potent at pChembl≥5 of 68 total, top 50 by pChembl (potency: 10 = 0.1 nM, 6 = 1 µM).

pChembl	Type	Value	Unit	Molecule
9.92	Kd	0.12	nM	CHEMBL382044
9.84	Kd	0.144	nM	CHEMBL198643
9.62	Kd	0.24	nM	CHEMBL2059243
9.41	Kd	0.39	nM	CHEMBL262707
9.36	Kd	0.44	nM	CHEMBL2059242
9.22	Kd	0.6	nM	CHEMBL2059241
9.18	Kd	0.66	nM	CHEMBL265885
8.90	Kd	1.25	nM	CHEMBL2059502
8.31	Kd	4.94	nM	CHEMBL2059504
8.11	Kd	7.8	nM	CHEMBL2303816
8.10	Kd	8	nM	CHEMBL2059499
8.01	Kd	9.7	nM	CHEMBL2059500
7.84	Kd	14.3	nM	CHEMBL2059498
7.80	Kd	16	nM	CHEMBL2059247
7.73	Kd	18.5	nM	CHEMBL2059245
7.65	Kd	22.6	nM	CHEMBL2059246
7.61	Kd	24.8	nM	CHEMBL2059503
7.49	Kd	32.2	nM	CHEMBL2059505
7.30	Kd	50	nM	CHEMBL2374307
7.00	Kd	100	nM	CHEMBL604568
6.93	Kd	118	nM	CHEMBL602113
6.92	Kd	120	nM	CHEMBL590011
6.89	Kd	130	nM	CHEMBL2303817
6.80	Kd	160	nM	CHEMBL603122
6.80	Kd	160	nM	CHEMBL604368
6.79	Kd	161	nM	CHEMBL604366
6.72	Kd	190	nM	CHEMBL602307
6.72	Kd	190	nM	CHEMBL604570
6.70	Kd	200	nM	CHEMBL590012
6.68	Kd	210	nM	CHEMBL590010
6.62	IC50	240	nM	CHEMBL258321
6.62	Kd	240	nM	MUPARFOSTAT SODIUM
6.62	Kd	240	nM	CHEMBL589773
6.57	Kd	270	nM	CHEMBL2059244
6.55	Kd	280	nM	CHEMBL602114
6.44	Kd	360	nM	CHEMBL604569
6.27	Kd	540	nM	CHEMBL2093120
6.25	Kd	560	nM	CHEMBL2059506
6.21	Kd	610	nM	CHEMBL2059510
6.13	Kd	740	nM	CHEMBL3144211
6.10	Kd	790	nM	CHEMBL2029015
6.08	Kd	840	nM	CHEMBL2059507
6.06	Kd	870	nM	CHEMBL2059509
5.94	Kd	1150	nM	CHEMBL2303818
5.92	Kd	1200	nM	CHEMBL2029141
5.64	Kd	2300	nM	CHEMBL590013
5.44	Kd	3600	nM	CHEMBL2059508
5.32	Kd	4840	nM	CHEMBL3215304
5.22	Kd	6000	nM	CHEMBL604367
5.20	Kd	6360	nM	CHEMBL3215309

PubChem BioAssay actives

62 with measured affinity, of 158 total; 50 most potent distinct compounds. Largely complementary to BindingDB; screening values are coarse (µM, 4 dp), so sub-nM hits tie at the floor.

Compound	Assay	Type	Value	Unit
(2R,3S,4S,5S,6R)-2-[(2R,3S,4S,5R,6R)-2-[(2R,3S,4S,5R,6R)-2-[(2R,3S,4S,5R,6R)-2-[(2S,3S,4S,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-2-phenylmethoxyoxan-3-yl]oxy-3,5-dihydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-3,5-dihydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-3,5-dihydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol	256832: Binding affinity for FGF1 by BIAcore solution affinity assay	kd	0.0001	uM
(2R,3S,4S,5S,6R)-2-[(2R,3S,4S,5R,6R)-2-[(2R,3S,4S,5R,6R)-2-[(2R,3S,4S,5R,6R)-2-[(2S,3S,4S,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-2-octoxyoxan-3-yl]oxy-3,5-dihydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-3,5-dihydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-3,5-dihydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol	256832: Binding affinity for FGF1 by BIAcore solution affinity assay	kd	0.0001	uM
hexadecasodium;[(2R,3S,4S,5R,6R)-2-[(2R,3S,4S,5R,6R)-2-[(2R,3S,4S,5R,6R)-2-[(2R,3S,4S,5R,6R)-2-[(2S,3S,4R,5R,6R)-2-[3-[4-[[(3S,5S,8R,9S,10S,13R,14S,17R)-10,13-dimethyl-17-[(2R)-6-methylheptan-2-yl]-2,3,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-3-yl]oxymethyl]triazol-1-yl]propoxy]-4,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-3-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl] sulfate	672589: Binding affinity to FGF-1 by surface plasmon resonance assay	kd	0.0002	uM
6-[5-[(3aS,4S,6aR)-2-oxo-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl]pentanoylamino]-N-[(2S,3S,4S,5S,6R)-3-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5R,6R)-3,5-dihydroxy-6-(hydroxymethyl)-4-[(2R,3S,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-3,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-3,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]hexanamide	256832: Binding affinity for FGF1 by BIAcore solution affinity assay	kd	0.0004	uM
tridecasodium;[(2R,3R,4R,5S,6S)-5-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5R,6R)-3,5-disulfonatooxy-6-(sulfonatooxymethyl)-4-[(2R,3S,4S,5R,6R)-3,4,5-trisulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxy-6-[3-(octadecanoylamino)propoxy]-3,4-disulfonatooxyoxan-2-yl]methyl sulfate	672589: Binding affinity to FGF-1 by surface plasmon resonance assay	kd	0.0004	uM
[(1R,2R,6R)-5-[bis[[bis[(1S,4R,5R,6R)-4,5,6-trisulfonatooxycyclohex-2-en-1-yl]amino]methyl]amino]-2,6-disulfonatooxycyclohex-3-en-1-yl] sulfate	1799619: Binding Assay from Article 10.1002/cbic.200500089: “An experimental and molecular-modeling study of the binding of linked sulfated tetracyclitols to FGF-1 and FGF-2.”	kd	0.0004	uM
tridecasodium;[(2R,3S,4S,5R,6R)-2-[(2R,3S,4S,5R,6R)-2-[(2R,3S,4S,5R,6R)-2-[(2S,3S,4R,5R,6R)-2-[[(3S,5S,8R,9S,10S,13R,14S,17R)-10,13-dimethyl-17-[(2R)-6-methylheptan-2-yl]-2,3,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-3-yl]oxy]-4,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-3-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl] sulfate	672589: Binding affinity to FGF-1 by surface plasmon resonance assay	kd	0.0006	uM
N-[(2S,3S,4S,5S,6R)-3-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5R,6R)-3,5-dihydroxy-6-(hydroxymethyl)-4-[(2R,3S,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-3,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-3,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]-2-phenoxyacetamide	256832: Binding affinity for FGF1 by BIAcore solution affinity assay	kd	0.0007	uM
tetradecasodium;[(2R,3R,4S,5R,6R)-2-[(2R,3R,4S,5R,6R)-6-[(2R,3R,4S,5R,6R)-6-[(2R,3R,4S,5R,6R)-6-[[(4R)-4-[(3S,5S,8R,9S,10S,12S,13R,14S,17R)-12-acetyloxy-10,13-dimethyl-3-sulfonatooxy-2,3,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-17-yl]pentanoyl]amino]-4,5-disulfonatooxy-2-(sulfonatooxymethyl)oxan-3-yl]oxy-4,5-disulfonatooxy-2-(sulfonatooxymethyl)oxan-3-yl]oxy-4,5-disulfonatooxy-2-(sulfonatooxymethyl)oxan-3-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl] sulfate	672589: Binding affinity to FGF-1 by surface plasmon resonance assay	kd	0.0013	uM
tridecasodium;[(2R,3R,4S,5R,6R)-3-[(2R,3R,4S,5R,6R)-5-[(2R,3R,4S,5R,6R)-3,4-disulfonatooxy-6-(sulfonatooxymethyl)-5-[(2R,3R,4S,5R,6R)-3,4,5-trisulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-3,4-disulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxy-6-[3-(octadecanoylamino)propoxy]-4,5-disulfonatooxyoxan-2-yl]methyl sulfate	672589: Binding affinity to FGF-1 by surface plasmon resonance assay	kd	0.0049	uM
[(1R,2S,5R,6R)-2-[3-[bis[(1S,4R,5R,6R)-4,5,6-trisulfonatooxycyclohex-2-en-1-yl]amino]propyl-[(1S,4R,5R,6R)-4,5,6-trisulfonatooxycyclohex-2-en-1-yl]amino]-5,6-disulfonatooxycyclohex-3-en-1-yl] sulfate	1799619: Binding Assay from Article 10.1002/cbic.200500089: “An experimental and molecular-modeling study of the binding of linked sulfated tetracyclitols to FGF-1 and FGF-2.”	kd	0.0072	uM
(2S,3R,4R,5R)-5-sulfooxy-2-(sulfooxymethyl)-6-[(2R,3R,4R,5R,6S)-2,4,5-trisulfooxy-6-(sulfooxymethyl)oxan-3-yl]oxy-4-[(2R,3R,4S,5R,6S)-3,4,5-trisulfooxy-6-(sulfooxymethyl)oxan-2-yl]oxyoxane-3-sulfonic acid	73456: Dissociation constant for Fibroblast growth factor 1	kd	0.0078	uM
tridecasodium;[(2R,3R,4S,5R,6R)-2-[(2R,3R,4S,5R,6R)-6-[(2R,3R,4S,5R,6R)-6-[(2R,3R,4S,5R,6R)-6-[[(3S,5S,8R,9S,10S,13R,14S,17R)-10,13-dimethyl-17-[(2R)-6-methylheptan-2-yl]-2,3,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-3-yl]oxy]-4,5-disulfonatooxy-2-(sulfonatooxymethyl)oxan-3-yl]oxy-4,5-disulfonatooxy-2-(sulfonatooxymethyl)oxan-3-yl]oxy-4,5-disulfonatooxy-2-(sulfonatooxymethyl)oxan-3-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl] sulfate	672589: Binding affinity to FGF-1 by surface plasmon resonance assay	kd	0.0080	uM
[(1R,2S,5R,6R)-2-[7-[bis[(1S,4R,5R,6R)-4,5,6-trisulfonatooxycyclohex-2-en-1-yl]amino]heptyl-[(1S,4R,5R,6R)-4,5,6-trisulfonatooxycyclohex-2-en-1-yl]amino]-5,6-disulfonatooxycyclohex-3-en-1-yl] sulfate	1799619: Binding Assay from Article 10.1002/cbic.200500089: “An experimental and molecular-modeling study of the binding of linked sulfated tetracyclitols to FGF-1 and FGF-2.”	kd	0.0080	uM
tridecasodium;[(2R,3R,4S,5R,6R)-2-[(2R,3R,4S,5R,6R)-6-[(2R,3R,4S,5R,6R)-6-[(2R,3R,4S,5R,6R)-6-[4-[[(3S,5S,8R,9S,10S,13R,14S,17R)-10,13-dimethyl-17-[(2R)-6-methylheptan-2-yl]-2,3,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-3-yl]oxymethyl]triazol-1-yl]-4,5-disulfonatooxy-2-(sulfonatooxymethyl)oxan-3-yl]oxy-4,5-disulfonatooxy-2-(sulfonatooxymethyl)oxan-3-yl]oxy-4,5-disulfonatooxy-2-(sulfonatooxymethyl)oxan-3-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl] sulfate	672589: Binding affinity to FGF-1 by surface plasmon resonance assay	kd	0.0097	uM
decasodium;[(2R,3S,4S,5R,6R)-2-[(2R,3S,4S,5R,6R)-2-[(2S,3S,4S,5R,6R)-2-[3-[4-[[(3S,5S,8R,9S,10S,13R,14S,17R)-10,13-dimethyl-17-[(2R)-6-methylheptan-2-yl]-2,3,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-3-yl]oxymethyl]triazol-1-yl]propoxy]-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl] sulfate	672589: Binding affinity to FGF-1 by surface plasmon resonance assay	kd	0.0143	uM
decasodium;[(2R,3S,4S,5R,6R)-2-[(2R,3S,4S,5R,6R)-2-[(2S,3S,4S,5R,6R)-2-[[(3S,5S,8R,9S,10S,13R,14S,17R)-10,13-dimethyl-17-[(2R)-6-methylheptan-2-yl]-2,3,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-3-yl]oxy]-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl] sulfate	672589: Binding affinity to FGF-1 by surface plasmon resonance assay	kd	0.0160	uM
decasodium;[(2R,3S,4S,5R,6R)-2-[(2R,3S,4S,5R,6R)-2-[(2S,3S,4R,5R,6R)-2-[[(3S,5S,8R,9S,10S,13R,14S,17R)-10,13-dimethyl-17-[(2R)-6-methylheptan-2-yl]-2,3,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-3-yl]oxy]-4,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-3-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl] sulfate	672589: Binding affinity to FGF-1 by surface plasmon resonance assay	kd	0.0185	uM
[(1R,2S,5R,6R)-2-[2-[bis[(1S,4R,5R,6R)-4,5,6-trisulfonatooxycyclohex-2-en-1-yl]amino]ethyl-[(1S,4R,5R,6R)-4,5,6-trisulfonatooxycyclohex-2-en-1-yl]amino]-5,6-disulfonatooxycyclohex-3-en-1-yl] sulfate	1799619: Binding Assay from Article 10.1002/cbic.200500089: “An experimental and molecular-modeling study of the binding of linked sulfated tetracyclitols to FGF-1 and FGF-2.”	kd	0.0207	uM
decasodium;[(2R,3S,4S,5R,6R)-2-[(2R,3S,4S,5R,6R)-2-[(2S,3S,4R,5R,6R)-2-[3-[4-[[(3S,5S,8R,9S,10S,13R,14S,17R)-10,13-dimethyl-17-[(2R)-6-methylheptan-2-yl]-2,3,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-3-yl]oxymethyl]triazol-1-yl]propoxy]-4,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-3-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl] sulfate	672589: Binding affinity to FGF-1 by surface plasmon resonance assay	kd	0.0226	uM
decasodium;[(2R,3R,4S,5R,6R)-2-[(2R,3R,4S,5R,6R)-6-[(2R,3R,4S,5R,6R)-6-[[(3S,5S,8R,9S,10S,13R,14S,17R)-10,13-dimethyl-17-[(2R)-6-methylheptan-2-yl]-2,3,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-3-yl]oxy]-4,5-disulfonatooxy-2-(sulfonatooxymethyl)oxan-3-yl]oxy-4,5-disulfonatooxy-2-(sulfonatooxymethyl)oxan-3-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl] sulfate	672589: Binding affinity to FGF-1 by surface plasmon resonance assay	kd	0.0248	uM
[(1R,2S,5R,6R)-2-[4-[bis[(1S,4R,5R,6R)-4,5,6-trisulfonatooxycyclohex-2-en-1-yl]amino]butyl-[(1S,4R,5R,6R)-4,5,6-trisulfonatooxycyclohex-2-en-1-yl]amino]-5,6-disulfonatooxycyclohex-3-en-1-yl] sulfate	1799619: Binding Assay from Article 10.1002/cbic.200500089: “An experimental and molecular-modeling study of the binding of linked sulfated tetracyclitols to FGF-1 and FGF-2.”	kd	0.0254	uM
[(1R,2S,5R,6R)-2-[5-[bis[(1S,4R,5R,6R)-4,5,6-trisulfonatooxycyclohex-2-en-1-yl]amino]pentyl-[(1S,4R,5R,6R)-4,5,6-trisulfonatooxycyclohex-2-en-1-yl]amino]-5,6-disulfonatooxycyclohex-3-en-1-yl] sulfate	1799619: Binding Assay from Article 10.1002/cbic.200500089: “An experimental and molecular-modeling study of the binding of linked sulfated tetracyclitols to FGF-1 and FGF-2.”	kd	0.0298	uM
decasodium;[(2R,3R,4S,5R,6R)-3-[(2R,3R,4S,5R,6R)-3,4-disulfonatooxy-6-(sulfonatooxymethyl)-5-[(2R,3R,4S,5R,6R)-3,4,5-trisulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-6-[3-(octadecanoylamino)propoxy]-4,5-disulfonatooxyoxan-2-yl]methyl sulfate	672589: Binding affinity to FGF-1 by surface plasmon resonance assay	kd	0.0322	uM
[(1R,2S,5R,6R)-2-[6-[bis[(1S,4R,5R,6R)-4,5,6-trisulfonatooxycyclohex-2-en-1-yl]amino]hexyl-[(1S,4R,5R,6R)-4,5,6-trisulfonatooxycyclohex-2-en-1-yl]amino]-5,6-disulfonatooxycyclohex-3-en-1-yl] sulfate	1799619: Binding Assay from Article 10.1002/cbic.200500089: “An experimental and molecular-modeling study of the binding of linked sulfated tetracyclitols to FGF-1 and FGF-2.”	kd	0.0390	uM
[(1R,2S,5R,6R)-2-[8-[bis[(1S,4R,5R,6R)-4,5,6-trisulfonatooxycyclohex-2-en-1-yl]amino]octyl-[(1S,4R,5R,6R)-4,5,6-trisulfonatooxycyclohex-2-en-1-yl]amino]-5,6-disulfonatooxycyclohex-3-en-1-yl] sulfate	1799619: Binding Assay from Article 10.1002/cbic.200500089: “An experimental and molecular-modeling study of the binding of linked sulfated tetracyclitols to FGF-1 and FGF-2.”	kd	0.0404	uM
decasodium;[(2R,3R,4S,5R,6R)-2-[(2R,3R,4S,5R,6R)-6-[(2R,3R,4S,5R,6R)-6-[4-[[(3S,5S,8R,9S,10S,13R,14S,17R)-10,13-dimethyl-17-[(2R)-6-methylheptan-2-yl]-2,3,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-3-yl]oxymethyl]triazol-1-yl]-4,5-disulfonatooxy-2-(sulfonatooxymethyl)oxan-3-yl]oxy-4,5-disulfonatooxy-2-(sulfonatooxymethyl)oxan-3-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl] sulfate	672589: Binding affinity to FGF-1 by surface plasmon resonance assay	kd	0.0500	uM
hexadecasodium;[(2R,3R,4R,5S,6S)-5-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5R,6R)-3,5-disulfonatooxy-6-(sulfonatooxymethyl)-4-[(2R,3S,4S,5R,6R)-3,4,5-trisulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxy-6-[3-(4-phenyltriazol-1-yl)propoxy]-3,4-disulfonatooxyoxan-2-yl]methyl sulfate	459627: Binding affinity to FGF1 by surface plasmon-based solution affinity assay	kd	0.1000	uM
[(1R,2S,5R,6R)-2-[10-[bis[(1S,4R,5R,6R)-4,5,6-trisulfonatooxycyclohex-2-en-1-yl]amino]decyl-[(1S,4R,5R,6R)-4,5,6-trisulfonatooxycyclohex-2-en-1-yl]amino]-5,6-disulfonatooxycyclohex-3-en-1-yl] sulfate	1799619: Binding Assay from Article 10.1002/cbic.200500089: “An experimental and molecular-modeling study of the binding of linked sulfated tetracyclitols to FGF-1 and FGF-2.”	kd	0.1150	uM
tridecasodium;[(2R,3R,4R,5S,6S)-5-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5R,6R)-3,5-disulfonatooxy-6-(sulfonatooxymethyl)-4-[(2R,3S,4S,5R,6R)-3,4,5-trisulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxy-6-octoxy-3,4-disulfonatooxyoxan-2-yl]methyl sulfate	459627: Binding affinity to FGF1 by surface plasmon-based solution affinity assay	kd	0.1180	uM
[(1R,2S,5R,6R)-2-[9-[bis[(1S,4R,5R,6R)-4,5,6-trisulfonatooxycyclohex-2-en-1-yl]amino]nonyl-[(1S,4R,5R,6R)-4,5,6-trisulfonatooxycyclohex-2-en-1-yl]amino]-5,6-disulfonatooxycyclohex-3-en-1-yl] sulfate	1799619: Binding Assay from Article 10.1002/cbic.200500089: “An experimental and molecular-modeling study of the binding of linked sulfated tetracyclitols to FGF-1 and FGF-2.”	kd	0.1190	uM
hexadecasodium;[(2R,3R,4R,5S,6S)-5-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5R,6R)-3,5-disulfonatooxy-6-(sulfonatooxymethyl)-4-[(2R,3S,4S,5R,6R)-3,4,5-trisulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxy-6-[8-(4-naphthalen-1-yltriazol-1-yl)octoxy]-3,4-disulfonatooxyoxan-2-yl]methyl sulfate	459627: Binding affinity to FGF1 by surface plasmon-based solution affinity assay	kd	0.1200	uM
[(2S,3S,4S,5R,6R)-2,4,6-trisulfooxy-5-[(2R,3R,4S,5R,6S)-3,4,5-trisulfooxy-6-(sulfooxymethyl)oxan-2-yl]oxyoxan-3-yl]methanesulfonic acid	73456: Dissociation constant for Fibroblast growth factor 1	kd	0.1300	uM
hexadecasodium;[(2R,3R,4R,5S,6S)-5-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5R,6R)-3,5-disulfonatooxy-6-(sulfonatooxymethyl)-4-[(2R,3S,4S,5R,6R)-3,4,5-trisulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxy-6-phenylmethoxy-3,4-disulfonatooxyoxan-2-yl]methyl sulfate	459627: Binding affinity to FGF1 by surface plasmon-based solution affinity assay	kd	0.1600	uM
hexadecasodium;[(2R,3R,4R,5S,6S)-5-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5R,6R)-3,5-disulfonatooxy-6-(sulfonatooxymethyl)-4-[(2R,3S,4S,5R,6R)-3,4,5-trisulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxy-6-[8-(4-phenyltriazol-1-yl)octoxy]-3,4-disulfonatooxyoxan-2-yl]methyl sulfate	459627: Binding affinity to FGF1 by surface plasmon-based solution affinity assay	kd	0.1600	uM
hexadecasodium;[(2R,3R,4R,5S,6S)-5-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5R,6R)-3,5-disulfonatooxy-6-(sulfonatooxymethyl)-4-[(2R,3S,4S,5R,6R)-3,4,5-trisulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxy-6-octoxy-3,4-disulfonatooxyoxan-2-yl]methyl sulfate	459627: Binding affinity to FGF1 by surface plasmon-based solution affinity assay	kd	0.1610	uM
[(1R,2S,5R,6R)-2-[4-[bis[(1S,4R,5R,6R)-4,5,6-trisulfonatooxycyclohex-2-en-1-yl]amino]-N-[(1S,4R,5R,6R)-4,5,6-trisulfonatooxycyclohex-2-en-1-yl]anilino]-5,6-disulfonatooxycyclohex-3-en-1-yl] sulfate	1799619: Binding Assay from Article 10.1002/cbic.200500089: “An experimental and molecular-modeling study of the binding of linked sulfated tetracyclitols to FGF-1 and FGF-2.”	kd	0.1870	uM
hexadecasodium;[(2R,3R,4R,5S,6S)-5-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5R,6R)-3,5-disulfonatooxy-6-(sulfonatooxymethyl)-4-[(2R,3S,4S,5R,6R)-3,4,5-trisulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxy-6-[12-(4-naphthalen-1-yltriazol-1-yl)dodecoxy]-3,4-disulfonatooxyoxan-2-yl]methyl sulfate	459627: Binding affinity to FGF1 by surface plasmon-based solution affinity assay	kd	0.1900	uM
tridecasodium;[(2R,3R,4R,5S,6S)-5-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5R,6R)-3,5-disulfonatooxy-6-(sulfonatooxymethyl)-4-[(2R,3S,4S,5R,6R)-3,4,5-trisulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxy-6-[8-(4-naphthalen-1-yltriazol-1-yl)octoxy]-3,4-disulfonatooxyoxan-2-yl]methyl sulfate	459627: Binding affinity to FGF1 by surface plasmon-based solution affinity assay	kd	0.1900	uM
tridecasodium;[(2R,3S,4S,5R,6R)-2-[(2R,3S,4S,5R,6R)-2-[(2R,3S,4S,5R,6R)-2-[(2S,3S,4R,5R,6R)-2-[8-[[5-(dimethylamino)naphthalen-1-yl]sulfonylamino]octoxy]-4,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-3-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl] sulfate	459627: Binding affinity to FGF1 by surface plasmon-based solution affinity assay	kd	0.2000	uM
tridecasodium;[(2R,3S,4S,5R,6R)-2-[(2R,3S,4S,5R,6R)-2-[(2R,3S,4S,5R,6R)-2-[(2S,3S,4R,5R,6R)-2-[(4-butylphenyl)methoxy]-4,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-3-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl] sulfate	459627: Binding affinity to FGF1 by surface plasmon-based solution affinity assay	kd	0.2100	uM
(2S,3R,4S,5S,6S)-3-[(2S,3S,4S,5S)-3-amino-4,5-dihydroxyoxan-2-yl]oxy-6-[(2S,3R,4S,5S,6S)-5-amino-4-hydroxy-2-(hydroxymethyl)-6-[(2S,3R,4S,5S,6S)-4,5,6-trihydroxy-2-propoxycarbonyloxan-3-yl]oxyoxan-3-yl]oxy-4,5-dihydroxyoxane-2-carboxylic acid	321419: Binding affinity at FGF1	ic50	0.2400	uM
tridecasodium;[(2R,3R,4R,5S,6S)-5-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5R,6R)-3,5-disulfonatooxy-6-(sulfonatooxymethyl)-4-[(2R,3S,4S,5R,6R)-3,4,5-trisulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxy-6-phenylmethoxy-3,4-disulfonatooxyoxan-2-yl]methyl sulfate	459627: Binding affinity to FGF1 by surface plasmon-based solution affinity assay	kd	0.2400	uM
heptasodium;[(2R,3S,4S,5R,6R)-2-[(2S,3S,4R,5R,6R)-2-[[(3S,5S,8R,9S,10S,13R,14S,17R)-10,13-dimethyl-17-[(2R)-6-methylheptan-2-yl]-2,3,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-3-yl]oxy]-4,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-3-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl] sulfate	672589: Binding affinity to FGF-1 by surface plasmon resonance assay	kd	0.2700	uM
tridecasodium;[(2R,3R,4R,5S,6S)-5-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5R,6R)-3,5-disulfonatooxy-6-(sulfonatooxymethyl)-4-[(2R,3S,4S,5R,6R)-3,4,5-trisulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxy-6-[8-(4-phenyltriazol-1-yl)octoxy]-3,4-disulfonatooxyoxan-2-yl]methyl sulfate	459627: Binding affinity to FGF1 by surface plasmon-based solution affinity assay	kd	0.2800	uM
tridecasodium;[(2R,3R,4R,5S,6S)-5-[(2R,3S,4S,5R,6R)-4-[(2R,3S,4S,5R,6R)-3,5-disulfonatooxy-6-(sulfonatooxymethyl)-4-[(2R,3S,4S,5R,6R)-3,4,5-trisulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-2-yl]oxy-6-[3-(4-phenyltriazol-1-yl)propoxy]-3,4-disulfonatooxyoxan-2-yl]methyl sulfate	459627: Binding affinity to FGF1 by surface plasmon-based solution affinity assay	kd	0.3600	uM
[(2S,3S,4R,5S,6R)-3,5-disulfooxy-2-(sulfooxymethyl)-6-[(2S,3R,4S,5S)-4,5,6-trisulfooxy-2-(sulfooxymethyl)oxan-3-yl]oxyoxan-4-yl] hydrogen sulfate	73456: Dissociation constant for Fibroblast growth factor 1	kd	0.5400	uM
heptasodium;[(2R,3R,4S,5R,6R)-2-[(2R,3R,4S,5R,6R)-6-[[(3S,5S,8R,9S,10S,13R,14S,17R)-10,13-dimethyl-17-[(2R)-6-methylheptan-2-yl]-2,3,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-3-yl]oxy]-4,5-disulfonatooxy-2-(sulfonatooxymethyl)oxan-3-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl] sulfate	672589: Binding affinity to FGF-1 by surface plasmon resonance assay	kd	0.5600	uM
heptasodium;[(2S,3R,4S,5S,6R)-2-[(2R,3R,4S,5R,6R)-6-[4-[[(3S,5S,8R,9S,10S,13R,14S,17R)-10,13-dimethyl-17-[(2R)-6-methylheptan-2-yl]-2,3,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-3-yl]oxymethyl]triazol-1-yl]-4,5-disulfonatooxy-2-(sulfonatooxymethyl)oxan-3-yl]oxy-3,5-disulfonatooxy-6-(sulfonatooxymethyl)oxan-4-yl] sulfate	672589: Binding affinity to FGF-1 by surface plasmon resonance assay	kd	0.6100	uM
[(2R,3S,4S,5R,6R)-2-[(2S,3S,4R,5R)-3,4-disulfooxy-2,5-bis(sulfooxymethyl)oxolan-2-yl]oxy-6-(sulfomethyl)-4,5-disulfooxyoxan-3-yl]methanesulfonic acid	73456: Dissociation constant for Fibroblast growth factor 1	kd	0.7400	uM

CTD chemical–gene interactions

86 total (human), top 30 by PubMed support.

Chemical	Actions (top 5)	PubMed papers
Particulate Matter	decreases expression, increases abundance, decreases methylation, increases expression	4
bisphenol A	decreases expression	2
Air Pollutants	increases abundance, decreases methylation, increases expression, decreases expression	2
Benzo(a)pyrene	affects methylation	2
Nickel	decreases expression	2
Valproic Acid	affects cotreatment, increases expression, decreases expression	2
Aflatoxin B1	affects methylation, increases methylation	2
Cadmium Chloride	increases expression	2
afuresertib	decreases expression	1
2-methoxy-6-undecyl-1,4-benzoquinone	decreases expression	1
4-oxoretinoic acid	decreases expression	1
steviol	increases expression	1
stevioside	increases expression	1
ethyl-p-hydroxybenzoate	increases expression	1
sulforaphane	decreases expression	1
sodium arsenite	decreases expression	1
butyraldehyde	increases expression	1
tetrathiomolybdate	decreases secretion	1
rebaudioside A	increases expression	1
benzo(e)pyrene	increases methylation	1
aflatoxin B2	increases methylation	1
cupric chloride	affects binding, decreases reaction, increases oxidation	1
nickel sulfate	decreases expression	1
puerarin	increases expression	1
epigallocatechin gallate	decreases expression	1
amlexanox	affects binding, decreases secretion, increases stability, decreases reaction, increases oxidation	1
evodiamine	increases expression	1
arsenic disulfide	decreases expression, increases methylation	1
perfluorooctane sulfonic acid	decreases expression	1
CGP 52608	affects binding, increases reaction	1

ChEMBL screening assays

15 unique, capped per target: 15 binding

Representative assays (with source publication via chembl_document):

Assay ID	Type	Description	Source paper
CHEMBL1072346	Binding	Binding affinity to FGF1 by surface plasmon-based solution affinity assay	Synthesis and biological evaluation of polysulfated oligosaccharide glycosides as inhibitors of angiogenesis and tumor growth. — J Med Chem

Cellosaurus cell lines

3 cell lines: 3 embryonic stem cell

First 10 cell lines (id-ordered, not curated):

Cellosaurus	Name	Category	Sex
CVCL_A1S0	SEES3-1V human FGF1, clone1	Embryonic stem cell	Male
CVCL_A1S1	SEES3-1V human FGF1, clone2	Embryonic stem cell	Male
CVCL_A1S2	SEES3-1V human FGF1, clone3	Embryonic stem cell	Male

Clinical trials (associated diseases)

0 trials via MONDO — disease-level, not drug-specific.