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Protein

Fibroblast growth factor 1

Gene

FGF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro. Acts as a ligand for FGFR1 and integrins. Binds to FGFR1 in the presence of heparin leading to FGFR1 dimerization and activation via sequential autophosphorylation on tyrosine residues which act as docking sites for interacting proteins, leading to the activation of several signaling cascades. Binds to integrin ITGAV:ITGB3. Its binding to integrin, subsequent ternary complex formation with integrin and FGFR1, and the recruitment of PTPN11 to the complex are essential for FGF1 signaling. Induces the phosphorylation and activation of FGFR1, FRS2, MAPK3/ERK1, MAPK1/ERK2 and AKT1 (PubMed:18441324, PubMed:20422052). Can induce angiogenesis (PubMed:23469107).6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei33Heparin2 Publications1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

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

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

EuPathDBiHostDB:ENSG00000113578.17
HGNCiHGNC:3665 FGF1
MIMi131220 gene
neXtProtiNX_P05230

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi24 – 27KKPK → AAPA: Loss of nuclear import leading to loss of phosphorylation by PKC/PRKCD. 1 Publication4
Mutagenesisi33N → A: No effect on integrin-binding. 1 Publication1
Mutagenesisi50R → E: Dominant-negative mutant. Defective in integrin-binding and in ternary complex formation with integrin and FGFR1. No effect on heparin- and FGFR1-binding. Defective in inducing FGF1 signaling, cell proliferation and cell migration. Defective in inducing angiogenesis, and suppression of angiogenesis in different in vitro and in vivo angiogenesis models. 3 Publications1
Mutagenesisi102E → A: No effect on integrin-binding. No effect on integrin- and heparin-binding, loss of FGFR1-binding, defective in inducing FGF1 signaling, cell proliferation and cell migration; when associated with A-109 and A-110. 1 Publication1
Mutagenesisi109Y → A: No effect on integrin- and heparin-binding, loss of FGFR1-binding, defective in inducing FGF1 signaling, cell proliferation and cell migration; when associated with A-102 and A-110. 1 Publication1
Mutagenesisi110N → A: No effect on integrin-binding. No effect on integrin- and heparin-binding, loss of FGFR1-binding, defective in inducing FGF1 signaling, cell proliferation and cell migration; when associated with A-102 and A-109. 1 Publication1
Mutagenesisi114S → A: Decrease in LRRC59-binding. 1 Publication1
Mutagenesisi127K → E: Reduced integrin-binding; when associated with E-128. Defective in integrin-, heparin- and FGFR1-binding, and defective in inducing FGF1 signaling, cell proliferation and cell migration; when associated with E-128; E-133 and E-134. 1 Publication1
Mutagenesisi128K → E: Reduced integrin-binding; when associated with E-127. Defective in integrin-, heparin- and FGFR1-binding, and defective in inducing FGF1 signaling, cell proliferation and cell migration; when associated with E-127; E-133 and E-134. 1 Publication1
Mutagenesisi131S → A: Decrease in LRRC59-binding. 1 Publication1
Mutagenesisi131S → E: Decrease in LRRC59-binding. 1 Publication1
Mutagenesisi133K → A: Loss of LRRC59-binding. 1 Publication1
Mutagenesisi133K → E: Loss of CSNK2A-, CSNK2B- and LRRC59-binding. Reduced integrin-binding; when associated with E-134. Defective in integrin-, heparin- and FGFR1-binding, and defective in inducing FGF1 signaling, cell proliferation and cell migration; when associated with E-128; E-133 and E-134. 2 Publications1
Mutagenesisi133K → R: No effect on LRRC59-binding. 1 Publication1
Mutagenesisi134R → E: Reduced integrin-binding; when associated with E-133. Defective in integrin-, heparin- and FGFR1-binding, and defective in inducing FGF1 signaling, cell proliferation and cell migration; when associated with E-127; E-128 and E-133. 1 Publication1

Organism-specific databases

DisGeNETi2246
OpenTargetsiENSG00000113578
PharmGKBiPA28105

Chemistry databases

ChEMBLiCHEMBL2120
DrugBankiDB08238 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

BioMutaiFGF1
DMDMi122737

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
PropeptideiPRO_00000089072 – 15Add BLAST14
ChainiPRO_000000890816 – 155Fibroblast growth factor 1Add BLAST140

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

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

PTM databases

iPTMnetiP05230
PhosphoSitePlusiP05230

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000113578 Expressed in 171 organ(s), highest expression level in metanephric glomerulus
CleanExiHS_FGF1
ExpressionAtlasiP05230 baseline and differential
GenevisibleiP05230 HS

Organism-specific databases

HPAiCAB017519
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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi108537, 27 interactors
DIPiDIP-3787N
IntActiP05230, 8 interactors
MINTiP05230
STRINGi9606.ENSP00000338548

Chemistry databases

BindingDBiP05230

Structurei

Secondary structure

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

3D structure databases

ProteinModelPortaliP05230
SMRiP05230
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05230

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni127 – 143Heparin-bindingAdd BLAST17

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi24 – 27Nuclear localization signal4

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3885 Eukaryota
ENOG4111IPH LUCA
GeneTreeiENSGT00730000110923
HOGENOMiHOG000236341
HOVERGENiHBG007580
InParanoidiP05230
KOiK18496
OMAiLGPRTHY
OrthoDBiEOG091G0NAY
PhylomeDBiP05230
TreeFamiTF317805

Family and domain databases

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

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. AlignAdd to basket

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

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

This isoform has been chosen as the '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]FASTAAdd to basket

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

Show »
Length:60
Mass (Da):6,698
Checksum:iB53E08C406484714
GO

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B5MCF4B5MCF4_HUMAN
Fibroblast growth factor 1
FGF1
93Annotation score:
C9JDC5C9JDC5_HUMAN
Fibroblast growth factor 1
FGF1
58Annotation score:
C9JUP6C9JUP6_HUMAN
Fibroblast growth factor 1
FGF1
41Annotation score:

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02135721G → E1 PublicationCorresponds to variant dbSNP:rs17223632Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_03653657 – 60IQLQ → TDTK in isoform 2. 1 Publication4
Alternative sequenceiVSP_03653761 – 155Missing in isoform 2. 1 PublicationAdd BLAST95

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13361 mRNA Translation: AAA79245.1
M30492, M30490, M30491 Genomic DNA Translation: AAA52446.1
M23087, M23086 Genomic DNA Translation: AAA52638.1
X51943 mRNA Translation: CAA36206.1
X65778 mRNA Translation: CAA46661.1
S67291 mRNA Translation: AAB29057.2
S67292 mRNA Translation: AAB29058.1
AY601819 Genomic DNA Translation: AAS99352.1
AC005370 Genomic DNA No translation available.
AK312301 mRNA Translation: BAG35227.1
CH471062 Genomic DNA Translation: EAW61881.1
CH471062 Genomic DNA Translation: EAW61882.1
CH471062 Genomic DNA Translation: EAW61885.1
BC032697 mRNA Translation: AAH32697.1
M60515 mRNA Translation: AAA51672.1
M60516 mRNA Translation: AAA51673.1
CCDSiCCDS4275.1 [P05230-1]
CCDS4276.1 [P05230-2]
PIRiA33665
JH0708
RefSeqiNP_000791.1, NM_000800.4 [P05230-1]
NP_001138364.1, NM_001144892.2 [P05230-1]
NP_001138406.1, NM_001144934.1 [P05230-1]
NP_001138407.1, NM_001144935.1 [P05230-1]
NP_001244134.1, NM_001257205.1 [P05230-1]
NP_001244136.1, NM_001257207.1 [P05230-1]
NP_001244137.1, NM_001257208.1 [P05230-1]
NP_001244138.1, NM_001257209.1 [P05230-1]
NP_001244139.1, NM_001257210.1 [P05230-1]
NP_149127.1, NM_033136.3 [P05230-2]
UniGeneiHs.483635

Genome annotation databases

EnsembliENST00000337706; 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]
GeneIDi2246
KEGGihsa:2246
UCSCiuc003lmm.5 human [P05230-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

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
CCDSiCCDS4275.1 [P05230-1]
CCDS4276.1 [P05230-2]
PIRiA33665
JH0708
RefSeqiNP_000791.1, NM_000800.4 [P05230-1]
NP_001138364.1, NM_001144892.2 [P05230-1]
NP_001138406.1, NM_001144934.1 [P05230-1]
NP_001138407.1, NM_001144935.1 [P05230-1]
NP_001244134.1, NM_001257205.1 [P05230-1]
NP_001244136.1, NM_001257207.1 [P05230-1]
NP_001244137.1, NM_001257208.1 [P05230-1]
NP_001244138.1, NM_001257209.1 [P05230-1]
NP_001244139.1, NM_001257210.1 [P05230-1]
NP_149127.1, NM_033136.3 [P05230-2]
UniGeneiHs.483635

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AXMX-ray3.00A/B/C/D/E/F21-155[»]
1DJSX-ray2.40B21-155[»]
1DZCNMR-A25-155[»]
1DZDNMR-A29-155[»]
1E0OX-ray2.80A/C16-155[»]
1EVTX-ray2.80A/B22-155[»]
1HKNX-ray2.00A/B/C/D/E/F17-155[»]
1JQZX-ray1.65A/B16-155[»]
1JT3X-ray1.95A/B16-155[»]
1JT4X-ray1.78A/B16-155[»]
1JT5X-ray1.85A/B16-155[»]
1JT7X-ray1.70A/B/C/D16-155[»]
1JTCX-ray1.70A/B/C/D16-155[»]
1JY0X-ray1.70A/B16-155[»]
1K5UX-ray2.00A/B/C16-154[»]
1K5VX-ray2.10A/B16-154[»]
1M16X-ray1.70A/B16-155[»]
1NZKX-ray1.95A/B/C/D16-152[»]
1P63X-ray1.60A/B16-155[»]
1PZZX-ray2.00A/B16-155[»]
1Q03X-ray2.05A/B16-152[»]
1Q04X-ray1.80A/B16-155[»]
1QCTmodel-A/D24-153[»]
1RG8X-ray1.10A/B16-155[»]
1RMLNMR-A1-155[»]
1RY7X-ray3.20A1-155[»]
1YTOX-ray2.10A/B/C/D16-155[»]
1Z2VX-ray1.90A/B16-155[»]
1Z4SX-ray2.60A/B/C/D16-155[»]
2AFGX-ray2.00A/B/C/D16-155[»]
2AQZX-ray1.85A/B16-155[»]
2AXMX-ray3.00A/B21-155[»]
2ERMNMR-A17-155[»]
2HW9X-ray1.60A/B16-155[»]
2HWAX-ray1.65A/B16-155[»]
2HWMX-ray1.60A/B16-155[»]
2HZ9X-ray1.70A/B16-155[»]
2K43NMR-A23-155[»]
2K4ANMR-B23-155[»]
2K8RNMR-A23-155[»]
2KI4NMR-A/D23-155[»]
2KI6NMR-B/E23-155[»]
2NTDX-ray2.52A/B/C/D16-155[»]
2Q9XX-ray1.70A16-155[»]
2RQ9NMR-A22-155[»]
3B9UX-ray1.55A16-155[»]
3BA4X-ray1.80A/B16-155[»]
3BA5X-ray1.75A/B16-155[»]
3BA7X-ray1.60A/B16-155[»]
3BADX-ray2.00A/B16-155[»]
3BAGX-ray1.75A/B16-155[»]
3BAHX-ray1.65A/B16-155[»]
3BAOX-ray1.55A/B16-155[»]
3BAQX-ray1.80A/B16-155[»]
3BAUX-ray1.60A/B16-155[»]
3BAVX-ray1.62A/B16-155[»]
3BB2X-ray1.50A/B16-155[»]
3CQAX-ray1.80A/B16-155[»]
3CRGX-ray1.85A/B16-155[»]
3CRHX-ray2.15A/B16-155[»]
3CRIX-ray2.10A/B16-155[»]
3CU1X-ray2.60B/D22-152[»]
3FGMX-ray1.95A/B16-155[»]
3FJ8X-ray2.00A/B16-155[»]
3FJ9X-ray1.90A/B16-155[»]
3FJAX-ray1.95A/B16-155[»]
3FJBX-ray2.00A/B16-155[»]
3FJCX-ray2.00A/B16-155[»]
3FJDX-ray1.90A/B16-155[»]
3FJEX-ray2.10A/B16-155[»]
3FJFX-ray1.90A/B16-155[»]
3FJHX-ray1.90A/B16-155[»]
3FJIX-ray2.55A/B/C/D16-155[»]
3FJJX-ray1.90A/B16-155[»]
3FJKX-ray2.15A/B/C/D16-155[»]
3HOMX-ray2.30A/B16-155[»]
3JUTX-ray2.25A/B/C/D/E/F24-153[»]
3K1XX-ray1.98A/B/C/D/E/F24-153[»]
3O3QX-ray1.60A/B/C/D16-155[»]
3OJ2X-ray2.20A/B1-155[»]
3OJMX-ray2.10A1-155[»]
3OJVX-ray2.60A/B21-155[»]
3UD7X-ray2.80A/B/C16-155[»]
3UD8X-ray2.37A/B/C16-155[»]
3UD9X-ray2.34A/B/C16-155[»]
3UDAX-ray2.51A/B/C16-155[»]
4J23X-ray3.88B21-155[»]
4Q91X-ray1.80A/B16-155[»]
4Q9GX-ray1.55A/B16-155[»]
4Q9PX-ray1.80A/B16-155[»]
4QALX-ray1.50A/B16-155[»]
4QBCX-ray1.52A/B16-155[»]
4QBVX-ray1.50A/B16-155[»]
4QC4X-ray1.49A/B16-155[»]
4QO3X-ray2.05A/B16-155[»]
4XKIX-ray2.00A/B16-155[»]
4YOLX-ray1.97A/B16-155[»]
ProteinModelPortaliP05230
SMRiP05230
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108537, 27 interactors
DIPiDIP-3787N
IntActiP05230, 8 interactors
MINTiP05230
STRINGi9606.ENSP00000338548

Chemistry databases

BindingDBiP05230
ChEMBLiCHEMBL2120
DrugBankiDB08238 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

iPTMnetiP05230
PhosphoSitePlusiP05230

Polymorphism and mutation databases

BioMutaiFGF1
DMDMi122737

Proteomic databases

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

Protocols and materials databases

DNASUi2246
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000337706; 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]
GeneIDi2246
KEGGihsa:2246
UCSCiuc003lmm.5 human [P05230-1]

Organism-specific databases

CTDi2246
DisGeNETi2246
EuPathDBiHostDB:ENSG00000113578.17
GeneCardsiFGF1
HGNCiHGNC:3665 FGF1
HPAiCAB017519
HPA003265
MIMi131220 gene
neXtProtiNX_P05230
OpenTargetsiENSG00000113578
PharmGKBiPA28105
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3885 Eukaryota
ENOG4111IPH LUCA
GeneTreeiENSGT00730000110923
HOGENOMiHOG000236341
HOVERGENiHBG007580
InParanoidiP05230
KOiK18496
OMAiLGPRTHY
OrthoDBiEOG091G0NAY
PhylomeDBiP05230
TreeFamiTF317805

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiFGF1 human
EvolutionaryTraceiP05230
GeneWikiiFGF1
GenomeRNAii2246
PROiPR:P05230
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000113578 Expressed in 171 organ(s), highest expression level in metanephric glomerulus
CleanExiHS_FGF1
ExpressionAtlasiP05230 baseline and differential
GenevisibleiP05230 HS

Family and domain databases

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

Entry informationi

Entry nameiFGF1_HUMAN
AccessioniPrimary (citable) accession number: P05230
Secondary accession number(s): B2R5T0
, D3DQF2, P07502, Q16588
Entry historyiIntegrated 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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