FGF1

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 key	Position(s)	DescriptionActions	Graphical view	Length
Binding siteⁱ	33	Heparin2 Publications		1

GO - Molecular functionⁱ

1-phosphatidylinositol-3-kinase activity Source: Reactome
fibroblast growth factor receptor binding
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 18441324
growth factor activity
Source: UniProtKB
Inferred from direct assayⁱ
- 20145243
heparin binding
Source: UniProtKB
Inferred from direct assayⁱ
- 20145243
Hsp70 protein binding Source: Ensembl
integrin binding
Source: UniProtKB
Inferred from direct assayⁱ
- 18441324
phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: Reactome
protein tyrosine kinase activity Source: Reactome
Ras guanyl-nucleotide exchange factor activity Source: Reactome
S100 protein binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 11432880

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

activation of MAPK activity
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 18441324
activation of protein kinase B activity
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 18441324
anatomical structure morphogenesis
Source: ProtInc
Traceable author statementⁱ
- 1693186
angiogenesis Source: UniProtKB-KW
branch elongation involved in ureteric bud branching
Source: UniProtKB
Inferred from direct assayⁱ
- 11731227
cell differentiation Source: UniProtKB-KW
cell proliferation Source: Ensembl
cellular response to heat
Source: UniProtKB
Inferred from direct assayⁱ
- 12746488
fibroblast growth factor receptor signaling pathway
Source: UniProtKB
Inferred from direct assayⁱ
- 20145243
lung development Source: Ensembl
MAPK cascade Source: Reactome
mesonephric epithelium development
Source: UniProtKB
Inferred from direct assayⁱ
- 11731227
multicellular organism development
Source: ProtInc
Traceable author statementⁱ
- 10903182
organ induction Source: Ensembl
positive regulation of angiogenesis
Source: UniProtKB
Inferred from direct assayⁱ
- 20145243
positive regulation of cell division
Source: UniProtKB
Inferred from direct assayⁱ
- 20145243
positive regulation of cell migration
Source: UniProtKB
Inferred from direct assayⁱ
- 20145243
positive regulation of cell proliferation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 18441324
- 23469107
positive regulation of cholesterol biosynthetic process
Source: BHF-UCL
Inferred from direct assayⁱ
- 19229075
positive regulation of endothelial cell migration
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 23469107
positive regulation of epithelial cell proliferation Source: Ensembl
positive regulation of intracellular signal transduction
Source: BHF-UCL
Inferred from direct assayⁱ
- 19229075
positive regulation of MAP kinase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 16756958
positive regulation of protein kinase B signaling Source: Reactome
positive regulation of sprouting angiogenesis
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 23469107
positive regulation of transcription by RNA polymerase II
Source: BHF-UCL
Inferred from direct assayⁱ
- 19229075
regulation of endothelial cell chemotaxis to fibroblast growth factor
Source: UniProtKB
Inferred from direct assayⁱ
- 16756958
regulation of endothelial tube morphogenesis
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 23469107
signal transduction
Source: ProtInc
Non-traceable author statementⁱ
- 3778488

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Developmental protein, Growth factor, Heparin-binding, Mitogen
Biological process	Angiogenesis, Differentiation

Enzyme and pathway databases

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 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
Gene namesⁱ	Name:FGF1 Synonyms:FGFA
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 5

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000113578.17
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:3665 FGF1
MIMⁱ	131220 gene
neXtProtⁱ	NX_P05230

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus, Secreted

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	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

DisGeNET More...DisGeNETⁱ	2246
Open Targets More...OpenTargetsⁱ	ENSG00000113578
PharmGKBⁱ	PA28105

Chemistry databases

ChEMBLⁱ	CHEMBL2120
Drug and drug target database More...DrugBankⁱ	DB08238 5-AMINO-NAPHTALENE-2-MONOSULFONATE DB01025 Amlexanox DB01942 Formic Acid DB04409 Naphthalene Trisulfonate DB02264 O2-Sulfo-Glucuronic Acid DB06589 Pazopanib DB00686 Pentosan Polysulfate DB01901 Sucrosofate

Polymorphism and mutation databases

BioMutaⁱ	FGF1
DMDMⁱ	122737

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	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

In the nucleus, phosphorylated by PKC/PRKCD.1 Publication

Keywords - PTMⁱ

Acetylation, Phosphoprotein

Proteomic databases

EPDⁱ	P05230
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P05230
PaxDbⁱ	P05230
PeptideAtlas More...PeptideAtlasⁱ	P05230
PRIDEⁱ	P05230
ProteomicsDBⁱ	51826 51827 [P05230-2]
TopDownProteomicsⁱ	P05230-1 [P05230-1]

PTM databases

iPTMnetⁱ	P05230
PhosphoSitePlusⁱ	P05230

Expressionⁱ

Tissue specificityⁱ

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

Gene expression databases

Bgeeⁱ	ENSG00000113578 Expressed in 171 organ(s), highest expression level in metanephric glomerulus
CleanExⁱ	HS_FGF1
ExpressionAtlasⁱ	P05230 baseline and differential
Genevisibleⁱ	P05230 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB017519 HPA003265

HPAⁱ

CAB017519
HPA003265

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 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
FGFR1	P11362	3	EBI-698068,EBI-1028277
FGFR2	P21802	2	EBI-698068,EBI-1028658
FGFR2	P21802-1	2	EBI-15489950,EBI-15489960
FGFR3	P22607	3	EBI-698068,EBI-348399

GO - Molecular functionⁱ

fibroblast growth factor receptor binding
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 18441324
growth factor activity
Source: UniProtKB
Inferred from direct assayⁱ
- 20145243
Hsp70 protein binding Source: Ensembl
integrin binding
Source: UniProtKB
Inferred from direct assayⁱ
- 18441324
Ras guanyl-nucleotide exchange factor activity Source: Reactome
S100 protein binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 11432880

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	108537, 27 interactors
Database of interacting proteins More...DIPⁱ	DIP-3787N
IntActⁱ	P05230, 8 interactors
Molecular INTeraction database More...MINTⁱ	P05230
STRINGⁱ	9606.ENSP00000338548

Chemistry databases

BindingDBⁱ

P05230

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Turnⁱ	11 – 13	Combined sources	3
Beta strandⁱ	23 – 25	Combined sources	3
Beta strandⁱ	27 – 31	Combined sources	5
Turnⁱ	32 – 35	Combined sources	4
Beta strandⁱ	36 – 40	Combined sources	5
Turnⁱ	42 – 44	Combined sources	3
Beta strandⁱ	46 – 49	Combined sources	4
Helixⁱ	55 – 57	Combined sources	3
Beta strandⁱ	59 – 65	Combined sources	7
Beta strandⁱ	68 – 73	Combined sources	6
Turnⁱ	74 – 76	Combined sources	3
Beta strandⁱ	79 – 82	Combined sources	4
Beta strandⁱ	84 – 86	Combined sources	3
Beta strandⁱ	88 – 93	Combined sources	6
Helixⁱ	96 – 98	Combined sources	3
Beta strandⁱ	100 – 105	Combined sources	6
Turnⁱ	106 – 108	Combined sources	3
Beta strandⁱ	109 – 115	Combined sources	7
Helixⁱ	118 – 120	Combined sources	3
Beta strandⁱ	123 – 126	Combined sources	4
Beta strandⁱ	130 – 132	Combined sources	3
Helixⁱ	135 – 137	Combined sources	3
Turnⁱ	138 – 141	Combined sources	4
Helixⁱ	143 – 145	Combined sources	3
Beta strandⁱ	147 – 151	Combined sources	5

Show more details

3D structure databases

ProteinModelPortalⁱ	P05230
SMRⁱ	P05230
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P05230

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

Belongs to the heparin-binding growth factors family.Curated

Phylogenomic databases

eggNOGⁱ	KOG3885 Eukaryota ENOG4111IPH LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00730000110923
HOGENOMⁱ	HOG000236341
HOVERGENⁱ	HBG007580
InParanoidⁱ	P05230
KEGG Orthology (KO) More...KOⁱ	K18496
OMAⁱ	LGPRTHY
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0NAY
PhylomeDBⁱ	P05230
TreeFamⁱ	TF317805

Family and domain databases

Conserved Domains Database More...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
Pfam protein domain database More...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

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show all Align All

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

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
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

Checksum:ⁱF586E8BFB09F1580

GO

Isoform 2 (identifier: P05230-2) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MAEGEITTFT ALTEKFNLPP GNYKKPKLLY CSNGGHFLRI LPDGTVDGTR 
        60
DRSDQHTDTK

Show »

Length:60

Mass (Da):6,698

Checksum:ⁱB53E08C406484714

GO

Computationally mapped potential isoform sequencesⁱ

There are 3 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

B5MCF4	B5MCF4_HUMAN	Fibroblast growth factor 1 Fibroblast growth factor 1 (Acidic fibroblast growth factor) (Heparin-binding growth factor 1)	FGF1	93	Annotation score:
C9JDC5	C9JDC5_HUMAN	Fibroblast growth factor 1 Fibroblast growth factor 1 (Acidic fibroblast growth factor) (Heparin-binding growth factor 1)	FGF1	58	Annotation score:
C9JUP6	C9JUP6_HUMAN	Fibroblast growth factor 1 Fibroblast growth factor 1 (Acidic fibroblast growth factor) (Heparin-binding 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:rs17223632Ensembl.		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

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS4275.1 [P05230-1] CCDS4276.1 [P05230-2]
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]
UniGeneⁱ	Hs.483635

Genome annotation databases

Ensemblⁱ	ENST00000337706; ENSP00000338548; ENSG00000113578 [P05230-1] ENST00000359370; ENSP00000352329; ENSG00000113578 [P05230-1] ENST00000360966; ENSP00000354231; ENSG00000113578 [P05230-2] ENST00000378046; ENSP00000367285; ENSG00000113578 [P05230-1] ENST00000419524; ENSP00000396195; ENSG00000113578 [P05230-1] ENST00000441680; ENSP00000404742; ENSG00000113578 [P05230-1] ENST00000610990; ENSP00000481868; ENSG00000113578 [P05230-1] ENST00000612258; ENSP00000479024; ENSG00000113578 [P05230-1] ENST00000619447; ENSP00000480980; ENSG00000113578 [P05230-1] ENST00000621536; ENSP00000480791; ENSG00000113578 [P05230-1]
GeneIDⁱ	2246
KEGGⁱ	hsa:2246
UCSC genome browser More...UCSCⁱ	uc003lmm.5 human [P05230-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P05230	Fibroblast growth factor 1		PONAB		155	UniRef100_P05230
Fibroblast growth factor 1		HUMAN		64
Multifunctional fusion protein		PANTR		155
Multifunctional fusion protein		RHIRO		155
Multifunctional fusion protein		COLAP		155
+21
P05230-2	Fibroblast growth factor 1		PANTR		60	UniRef100_A0A2I3SM57
Fibroblast growth factor 1		COLAP		61
Fibroblast growth factor 1		MACMU		60
Fibroblast growth factor 1		PONAB		60
Fibroblast growth factor 1		CERAT		60
+9

Protein	Similar proteins		Species	Score	Length	Source
P05230	Fibroblast growth factor 1		PONAB		155	UniRef90_P05230
Fibroblast growth factor 1		HUMAN		64
Multifunctional fusion protein		PANTR		155
Multifunctional fusion protein		RHIRO		155
Multifunctional fusion protein		COLAP		155
+30
P05230-2	Fibroblast growth factor 1		PANTR		60	UniRef90_A0A2I3SM57
Fibroblast growth factor 1		COLAP		61
Fibroblast growth factor 1		MACMU		60
Fibroblast growth factor 1		PONAB		60
Fibroblast growth factor 1		CERAT		60
+9

Protein	Similar proteins		Species	Score	Length	Source
P05230	Fibroblast growth factor 1		PONAB		155	UniRef50_P05230
Fibroblast growth factor 1	)	BOVIN		155
Fibroblast growth factor 1		MESAU		155
Fibroblast growth factor 1 (Fragment)		PIG		152
Fibroblast growth factor 1		HUMAN		64
+201
P05230-2	Fibroblast growth factor 1		PANTR		60	UniRef50_A0A2I3SM57
Fibroblast growth factor 1		COLAP		61
Fibroblast growth factor 1		MACMU		60
Fibroblast growth factor 1		PONAB		60
Fibroblast growth factor 1		CERAT		60
+14

Cross-referencesⁱ

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
CCDSⁱ	CCDS4275.1 [P05230-1] CCDS4276.1 [P05230-2]
PIRⁱ	A33665 JH0708
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]
UniGeneⁱ	Hs.483635

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 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	[»]
ProteinModelPortalⁱ	P05230
SMRⁱ	P05230
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	108537, 27 interactors
DIPⁱ	DIP-3787N
IntActⁱ	P05230, 8 interactors
MINTⁱ	P05230
STRINGⁱ	9606.ENSP00000338548

Chemistry databases

BindingDBⁱ	P05230
ChEMBLⁱ	CHEMBL2120
DrugBankⁱ	DB08238 5-AMINO-NAPHTALENE-2-MONOSULFONATE DB01025 Amlexanox DB01942 Formic Acid DB04409 Naphthalene Trisulfonate DB02264 O2-Sulfo-Glucuronic Acid DB06589 Pazopanib DB00686 Pentosan Polysulfate DB01901 Sucrosofate

PTM databases

iPTMnetⁱ	P05230
PhosphoSitePlusⁱ	P05230

Polymorphism and mutation databases

BioMutaⁱ	FGF1
DMDMⁱ	122737

Proteomic databases

EPDⁱ	P05230
MaxQBⁱ	P05230
PaxDbⁱ	P05230
PeptideAtlasⁱ	P05230
PRIDEⁱ	P05230
ProteomicsDBⁱ	51826 51827 [P05230-2]
TopDownProteomicsⁱ	P05230-1 [P05230-1]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	2246
Structural Biology Knowledgebase	Search...

Genome annotation databases

Organism-specific databases

CTDⁱ	2246
DisGeNETⁱ	2246
EuPathDBⁱ	HostDB:ENSG00000113578.17
GeneCardsⁱ	FGF1
HGNCⁱ	HGNC:3665 FGF1
HPAⁱ	CAB017519 HPA003265
MIMⁱ	131220 gene
neXtProtⁱ	NX_P05230
OpenTargetsⁱ	ENSG00000113578
PharmGKBⁱ	PA28105
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3885 Eukaryota ENOG4111IPH LUCA
GeneTreeⁱ	ENSGT00730000110923
HOGENOMⁱ	HOG000236341
HOVERGENⁱ	HBG007580
InParanoidⁱ	P05230
KOⁱ	K18496
OMAⁱ	LGPRTHY
OrthoDBⁱ	EOG091G0NAY
PhylomeDBⁱ	P05230
TreeFamⁱ	TF317805

Enzyme and pathway databases

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

ChiTaRSⁱ	FGF1 human
EvolutionaryTraceⁱ	P05230
GeneWikiⁱ	FGF1
GenomeRNAiⁱ	2246
Protein Ontology More...PROⁱ	PR:P05230
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000113578 Expressed in 171 organ(s), highest expression level in metanephric glomerulus
CleanExⁱ	HS_FGF1
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...

Entry informationⁱ

Entry nameⁱ	FGF1_HUMAN
Accessionⁱ	P05230Primary (citable) accession number: P05230 Secondary accession number(s): B2R5T0 , D3DQF2, P07502, Q16588
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
	Last sequence update:	August 13, 1987
	Last modified:	October 10, 2018
	This is version 219 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
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
Human chromosome 5
Human chromosome 5: entries, gene names and cross-references to MIM

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UniProtKB - P05230 (FGF1_HUMAN)

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Fibroblast growth factor 1

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<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

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<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

Organism-specific databases

<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

Cytosol

Nucleus

Extracellular region or secreted

Other locations

Cytosol

Extracellular region or secreted

Nucleus

Other locations

Keywords - Cellular componenti

<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

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<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

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<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

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<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

3D structure databases

Miscellaneous databases

<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

Motif

<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

Phylogenomic databases

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Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<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_references_section">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

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ