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Protein

Fibroblast growth factor 1

Gene

FGF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331Heparin2 Publications

GO - Molecular functioni

  • fibroblast growth factor receptor binding Source: MGI
  • growth factor activity Source: UniProtKB
  • heparin binding Source: UniProtKB
  • S100 protein binding Source: UniProtKB

GO - Biological processi

  • anatomical structure morphogenesis Source: ProtInc
  • angiogenesis Source: UniProtKB-KW
  • branch elongation involved in ureteric bud branching Source: UniProtKB
  • cellular response to heat Source: UniProtKB
  • epidermal growth factor receptor signaling pathway Source: Reactome
  • Fc-epsilon receptor signaling pathway Source: Reactome
  • fibroblast growth factor receptor signaling pathway Source: UniProtKB
  • innate immune response Source: Reactome
  • insulin receptor signaling pathway Source: Reactome
  • lung development Source: Ensembl
  • mesonephric epithelium development Source: UniProtKB
  • multicellular organismal development Source: ProtInc
  • neurotrophin TRK receptor signaling pathway Source: Reactome
  • organ induction Source: Ensembl
  • phosphatidylinositol-mediated signaling Source: Reactome
  • positive regulation of angiogenesis Source: UniProtKB
  • positive regulation of cell division Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of cell proliferation Source: MGI
  • positive regulation of cholesterol biosynthetic process Source: BHF-UCL
  • positive regulation of epithelial cell proliferation Source: Ensembl
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of intracellular signal transduction Source: BHF-UCL
  • positive regulation of MAP kinase activity Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • regulation of endothelial cell chemotaxis to fibroblast growth factor Source: UniProtKB
  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Growth factor, Mitogen

Keywords - Biological processi

Angiogenesis, Differentiation

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_110235. Phospholipase C-mediated cascade: FGFR1.
REACT_120863. Activated point mutants of FGFR2.
REACT_121153. Signaling by activated point mutants of FGFR1.
REACT_121249. FGFR3 mutant receptor activation.
REACT_121337. Signaling by activated point mutants of FGFR3.
REACT_147727. Constitutive Signaling by Aberrant PI3K in Cancer.
REACT_355069. FRS-mediated FGFR2 signaling.
REACT_355144. Negative regulation of FGFR3 signaling.
REACT_355146. Phospholipase C-mediated cascade, FGFR2.
REACT_355159. SHC-mediated cascade:FGFR4.
REACT_355160. PI-3K cascade:FGFR3.
REACT_355194. SHC-mediated cascade:FGFR1.
REACT_355197. SHC-mediated cascade:FGFR3.
REACT_355202. Signaling by FGFR4 mutants.
REACT_355212. FRS-mediated FGFR3 signaling.
REACT_355216. Phospholipase C-mediated cascade, FGFR4.
REACT_355218. Negative regulation of FGFR1 signaling.
REACT_355221. Signaling by FGFR1 mutants.
REACT_355225. SHC-mediated cascade:FGFR2.
REACT_355227. Negative regulation of FGFR2 signaling.
REACT_355304. PI-3K cascade:FGFR4.
REACT_355313. Signaling by FGFR3 mutants.
REACT_355450. PI-3K cascade:FGFR2.
REACT_355511. Signaling by FGFR2 mutants.
REACT_355514. Phospholipase C-mediated cascade, FGFR3.
REACT_355552. PI-3K cascade:FGFR1.
REACT_355580. FRS2-mediated FGFR4 signaling.
REACT_355584. FRS-mediated FGFR1 signaling.
REACT_355588. Negative regulation of FGFR4 signaling.
REACT_75829. PIP3 activates AKT signaling.
REACT_9400. FGFR1b ligand binding and activation.
REACT_9413. FGFR2c ligand binding and activation.
REACT_9416. FGFR2b ligand binding and activation.
REACT_9452. FGFR4 ligand binding and activation.
REACT_9508. FGFR3b ligand binding and activation.
REACT_9510. FGFR3c ligand binding and activation.
REACT_9515. FGFR1c ligand binding and activation.
REACT_976. PI3K Cascade.
SignaLinkiP05230.

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
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:3665. FGF1.

Subcellular locationi

  • Secreted
  • Cytoplasm
  • Cytoplasmcell cortex
  • Cytoplasmcytosol
  • Nucleus

  • Note: Lacks a cleavable signal sequence. Within the cytoplasm, it is transported to the cell membrane and then secreted by a non-classical pathway that requires Cu2+ ions and S100A13. Secreted in a complex with SYT1 (By similarity). Binding of exogenous FGF1 to FGFR facilitates endocytosis followed by translocation of FGF1 across endosomal membrane into the cytosol. Nuclear import from the cytosol requires the classical nuclear import machinery, involving proteins KPNA1 and KPNB1, as well as LRRC59.By similarity

GO - Cellular componenti

  • cell cortex Source: UniProtKB-SubCell
  • cytosol Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
  • nucleoplasm Source: HPA
  • proteinaceous extracellular matrix Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi24 – 274KKPK → AAPA: Loss of nuclear import leading to loss of phosphorylation by PKC/PRKCD. 1 Publication
Mutagenesisi114 – 1141S → A: Decrease in LRRC59-binding. 1 Publication
Mutagenesisi131 – 1311S → A: Decrease in LRRC59-binding. 1 Publication
Mutagenesisi131 – 1311S → E: Decrease in LRRC59-binding. 1 Publication
Mutagenesisi133 – 1331K → A: Loss of LRRC59-binding. 1 Publication
Mutagenesisi133 – 1331K → E: Loss of CSNK2A-, CSNK2B- and LRRC59-binding. 1 Publication
Mutagenesisi133 – 1331K → R: No effect on LRRC59-binding. 1 Publication

Organism-specific databases

PharmGKBiPA28105.

Chemistry

DrugBankiDB01025. Amlexanox.
DB06589. Pazopanib.
DB00686. Pentosan Polysulfate.

Polymorphism and mutation databases

BioMutaiFGF1.
DMDMi122737.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Propeptidei2 – 1514PRO_0000008907Add
BLAST
Chaini16 – 155140Fibroblast growth factor 1PRO_0000008908Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP05230.
PaxDbiP05230.
PRIDEiP05230.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP05230.
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 (By similarity). 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.By similarity12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FGFR1P113623EBI-698068,EBI-1028277
FGFR2P218023EBI-698068,EBI-1028658
FGFR3P226073EBI-698068,EBI-348399

Protein-protein interaction databases

BioGridi108537. 26 interactions.
DIPiDIP-3787N.
IntActiP05230. 7 interactions.
MINTiMINT-118570.
STRINGi9606.ENSP00000338548.

Structurei

Secondary structure

1
155
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni11 – 133Combined sources
Beta strandi23 – 253Combined sources
Beta strandi27 – 315Combined sources
Turni32 – 354Combined sources
Beta strandi36 – 405Combined sources
Turni42 – 443Combined sources
Beta strandi46 – 494Combined sources
Helixi55 – 573Combined sources
Beta strandi59 – 657Combined sources
Beta strandi68 – 736Combined sources
Turni74 – 763Combined sources
Beta strandi79 – 824Combined sources
Beta strandi84 – 863Combined sources
Beta strandi88 – 936Combined sources
Helixi96 – 983Combined sources
Beta strandi100 – 1056Combined sources
Turni106 – 1083Combined sources
Beta strandi109 – 1157Combined sources
Helixi118 – 1203Combined sources
Beta strandi123 – 1264Combined sources
Beta strandi130 – 1323Combined sources
Helixi135 – 1373Combined sources
Turni138 – 1414Combined sources
Helixi143 – 1453Combined sources
Beta strandi147 – 1515Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
2LDNNMR-A23-152[»]
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[»]
ProteinModelPortaliP05230.
SMRiP05230. Positions 16-152.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05230.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni127 – 14317Heparin-bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi24 – 274Nuclear localization signal

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG246422.
GeneTreeiENSGT00730000110923.
HOGENOMiHOG000236341.
HOVERGENiHBG007580.
InParanoidiP05230.
KOiK18496.
OMAiLGPRTHY.
OrthoDBiEOG7992S1.
PhylomeDBiP05230.
TreeFamiTF317805.

Family and domain databases

InterProiIPR008996. Cytokine_IL1-like.
IPR028210. FGF1.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERiPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF65. PTHR11486:SF65. 1 hit.
PRINTSiPR00263. HBGFFGF.
PR00262. IL1HBGF.
SMARTiSM00442. FGF. 1 hit.
[Graphical view]
SUPFAMiSSF50353. SSF50353. 1 hit.
PROSITEiPS00247. HBGF_FGF. 1 hit.
[Graphical view]

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

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211G → E.1 Publication
Corresponds to variant rs17223632 [ dbSNP | Ensembl ].
VAR_021357

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei57 – 604IQLQ → TDTK in isoform 2. 1 PublicationVSP_036536
Alternative sequencei61 – 15595Missing in isoform 2. 1 PublicationVSP_036537Add
BLAST

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]
NP_149128.1. NM_033137.2.
UniGeneiHs.483635.

Genome annotation databases

EnsembliENST00000337706; ENSP00000338548; ENSG00000113578.
ENST00000359370; ENSP00000352329; ENSG00000113578.
ENST00000360966; ENSP00000354231; ENSG00000113578. [P05230-2]
ENST00000378046; ENSP00000367285; ENSG00000113578.
ENST00000419524; ENSP00000396195; ENSG00000113578.
ENST00000441680; ENSP00000404742; ENSG00000113578.
ENST00000610990; ENSP00000481868; ENSG00000113578.
ENST00000612258; ENSP00000479024; ENSG00000113578.
ENST00000619447; ENSP00000480980; ENSG00000113578.
ENST00000621536; ENSP00000480791; ENSG00000113578.
GeneIDi2246.
KEGGihsa:2246.
UCSCiuc003lmm.4. human. [P05230-1]
uc003lmp.5. human. [P05230-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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]
NP_149128.1. NM_033137.2.
UniGeneiHs.483635.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
2LDNNMR-A23-152[»]
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[»]
ProteinModelPortaliP05230.
SMRiP05230. Positions 16-152.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108537. 26 interactions.
DIPiDIP-3787N.
IntActiP05230. 7 interactions.
MINTiMINT-118570.
STRINGi9606.ENSP00000338548.

Chemistry

BindingDBiP05230.
ChEMBLiCHEMBL2120.
DrugBankiDB01025. Amlexanox.
DB06589. Pazopanib.
DB00686. Pentosan Polysulfate.

Polymorphism and mutation databases

BioMutaiFGF1.
DMDMi122737.

Proteomic databases

MaxQBiP05230.
PaxDbiP05230.
PRIDEiP05230.

Protocols and materials databases

DNASUi2246.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000337706; ENSP00000338548; ENSG00000113578.
ENST00000359370; ENSP00000352329; ENSG00000113578.
ENST00000360966; ENSP00000354231; ENSG00000113578. [P05230-2]
ENST00000378046; ENSP00000367285; ENSG00000113578.
ENST00000419524; ENSP00000396195; ENSG00000113578.
ENST00000441680; ENSP00000404742; ENSG00000113578.
ENST00000610990; ENSP00000481868; ENSG00000113578.
ENST00000612258; ENSP00000479024; ENSG00000113578.
ENST00000619447; ENSP00000480980; ENSG00000113578.
ENST00000621536; ENSP00000480791; ENSG00000113578.
GeneIDi2246.
KEGGihsa:2246.
UCSCiuc003lmm.4. human. [P05230-1]
uc003lmp.5. human. [P05230-2]

Organism-specific databases

CTDi2246.
GeneCardsiGC05M141953.
HGNCiHGNC:3665. FGF1.
HPAiCAB017519.
HPA003265.
MIMi131220. gene.
neXtProtiNX_P05230.
PharmGKBiPA28105.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG246422.
GeneTreeiENSGT00730000110923.
HOGENOMiHOG000236341.
HOVERGENiHBG007580.
InParanoidiP05230.
KOiK18496.
OMAiLGPRTHY.
OrthoDBiEOG7992S1.
PhylomeDBiP05230.
TreeFamiTF317805.

Enzyme and pathway databases

ReactomeiREACT_110235. Phospholipase C-mediated cascade: FGFR1.
REACT_120863. Activated point mutants of FGFR2.
REACT_121153. Signaling by activated point mutants of FGFR1.
REACT_121249. FGFR3 mutant receptor activation.
REACT_121337. Signaling by activated point mutants of FGFR3.
REACT_147727. Constitutive Signaling by Aberrant PI3K in Cancer.
REACT_355069. FRS-mediated FGFR2 signaling.
REACT_355144. Negative regulation of FGFR3 signaling.
REACT_355146. Phospholipase C-mediated cascade, FGFR2.
REACT_355159. SHC-mediated cascade:FGFR4.
REACT_355160. PI-3K cascade:FGFR3.
REACT_355194. SHC-mediated cascade:FGFR1.
REACT_355197. SHC-mediated cascade:FGFR3.
REACT_355202. Signaling by FGFR4 mutants.
REACT_355212. FRS-mediated FGFR3 signaling.
REACT_355216. Phospholipase C-mediated cascade, FGFR4.
REACT_355218. Negative regulation of FGFR1 signaling.
REACT_355221. Signaling by FGFR1 mutants.
REACT_355225. SHC-mediated cascade:FGFR2.
REACT_355227. Negative regulation of FGFR2 signaling.
REACT_355304. PI-3K cascade:FGFR4.
REACT_355313. Signaling by FGFR3 mutants.
REACT_355450. PI-3K cascade:FGFR2.
REACT_355511. Signaling by FGFR2 mutants.
REACT_355514. Phospholipase C-mediated cascade, FGFR3.
REACT_355552. PI-3K cascade:FGFR1.
REACT_355580. FRS2-mediated FGFR4 signaling.
REACT_355584. FRS-mediated FGFR1 signaling.
REACT_355588. Negative regulation of FGFR4 signaling.
REACT_75829. PIP3 activates AKT signaling.
REACT_9400. FGFR1b ligand binding and activation.
REACT_9413. FGFR2c ligand binding and activation.
REACT_9416. FGFR2b ligand binding and activation.
REACT_9452. FGFR4 ligand binding and activation.
REACT_9508. FGFR3b ligand binding and activation.
REACT_9510. FGFR3c ligand binding and activation.
REACT_9515. FGFR1c ligand binding and activation.
REACT_976. PI3K Cascade.
SignaLinkiP05230.

Miscellaneous databases

ChiTaRSiFGF1. human.
EvolutionaryTraceiP05230.
GeneWikiiFGF1.
GenomeRNAii2246.
NextBioi9087.
PROiP05230.
SOURCEiSearch...

Gene expression databases

BgeeiP05230.
CleanExiHS_FGF1.
ExpressionAtlasiP05230. baseline and differential.
GenevisibleiP05230. HS.

Family and domain databases

InterProiIPR008996. Cytokine_IL1-like.
IPR028210. FGF1.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERiPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF65. PTHR11486:SF65. 1 hit.
PRINTSiPR00263. HBGFFGF.
PR00262. IL1HBGF.
SMARTiSM00442. FGF. 1 hit.
[Graphical view]
SUPFAMiSSF50353. SSF50353. 1 hit.
PROSITEiPS00247. HBGF_FGF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human endothelial cell growth factor: cloning, nucleotide sequence, and chromosome localization."
    Jaye M., Howk R., Burgess W., Ricca G.A., Chiu I.-M., Ravera M.W., O'Brien S.J., Modi W.S., Maciag T., Drohan W.N.
    Science 233:541-545(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain stem.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Cloning of the gene coding for human class 1 heparin-binding growth factor and its expression in fetal tissues."
    Wang W.P., Lehtoma K., Varban M.L., Krishnan I., Chiu I.M.
    Mol. Cell. Biol. 9:2387-2395(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Brain stem.
  4. "Alternative splicing generates two forms of mRNA coding for human heparin-binding growth factor 1."
    Chiu I.M., Wang W.P., Lehtoma K.
    Oncogene 5:755-762(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain stem.
  5. "Cloning and sequence analysis of the human acidic fibroblast growth factor gene and its preservation in leukemia patients."
    Wang W.P., Quick D., Balcerzak S.P., Needleman S.W., Chiu I.M.
    Oncogene 6:1521-1529(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "An acidic fibroblast growth factor protein generated by alternate splicing acts like an antagonist."
    Li Y.L., Kha H., Golden J.A., Migchielsen A.A.J., Goetzl E.J., Turck E.J.
    J. Exp. Med. 175:1073-1080(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  7. "The expression of acidic fibroblast growth factor (heparin-binding growth factor-1) and cytokine genes in human cardiac allografts and T cells."
    Zhao X.M., Yeoh T.K., Hiebert M., Frist W.H., Miller G.G.
    Transplantation 56:1177-1182(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 1-154 (ISOFORM 1), TISSUE SPECIFICITY.
  8. NIEHS SNPs program
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-21.
  9. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Cerebellum.
  10. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Liver.
  13. "The gene for human acidic fibroblast growth factor encodes two upstream exons alternatively spliced to the first coding exon."
    Crumley G., Dionne C.A., Jaye M.
    Biochem. Biophys. Res. Commun. 171:7-13(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-40 (ISOFORMS 1/2).
  14. "Human class 1 heparin-binding growth factor: structure and homology to bovine acidic brain fibroblast growth factor."
    Harper J.W., Strydom D.J., Lobb R.R.
    Biochemistry 25:4097-4103(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 16-155 (ISOFORM 1).
  15. "The complete amino acid sequence of human brain-derived acidic fibroblast growth factor."
    Gimenez-Gallego G., Conn G., Hatcher V.B., Thomas K.A.
    Biochem. Biophys. Res. Commun. 138:611-617(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 16-155 (ISOFORM 1).
  16. "Amino acid sequence of human acidic fibroblast growth factor."
    Gautschi-Sova P., Mueller T., Boehlen P.
    Biochem. Biophys. Res. Commun. 140:874-880(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 16-155 (ISOFORM 1).
  17. "Human brain-derived acidic and basic fibroblast growth factors: amino terminal sequences and specific mitogenic activities."
    Gimenez-Gallego G., Conn G., Hatcher V.B., Thomas K.A.
    Biochem. Biophys. Res. Commun. 135:541-548(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 16-47 (ISOFORMS 1/2).
  18. "Partial molecular characterization of endothelial cell mitogens from human brain: acidic and basic fibroblast growth factors."
    Gautschi P., Frater-Schroeder M., Boehlen P.
    FEBS Lett. 204:203-207(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 16-49 (ISOFORMS 1/2).
  19. "Characterization and molecular cloning of a putative binding protein for heparin-binding growth factors."
    Wu D.Q., Kan M.K., Sato G.H., Okamoto T., Sato J.D.
    J. Biol. Chem. 266:16778-16785(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH FGFBP1 AND FGF2, INTERACTION WITH FGFBP1.
  20. Cited for: INTERACTION WITH FGFR1; FGFR2; FGFR3 AND FGFR4, FUNCTION IN CELL PROLIFERATION.
  21. "Copper induces the assembly of a multiprotein aggregate implicated in the release of fibroblast growth factor 1 in response to stress."
    Landriscina M., Bagala C., Mandinova A., Soldi R., Micucci I., Bellum S., Prudovsky I., Maciag T.
    J. Biol. Chem. 276:25549-25557(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, COPPER-BINDING, INTERACTION WITH S100A13 AND SYT1.
  22. "Identification of ribosome-binding protein p34 as an intracellular protein that binds acidic fibroblast growth factor."
    Skjerpen C.S., Wesche J., Olsnes S.
    J. Biol. Chem. 277:23864-23871(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSNK2A; CSNK2B; FGF2; FIBP AND LRRC59, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF SER-114; SER-131 AND LYS-133.
  23. "Receptor specificity of the fibroblast growth factor family. The complete mammalian FGF family."
    Zhang X., Ibrahimi O.A., Olsen S.K., Umemori H., Mohammadi M., Ornitz D.M.
    J. Biol. Chem. 281:15694-15700(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FGFR1; FGFR2; FGFR3 AND FGFR4, FUNCTION IN STIMULATION OF CELL PROLIFERATION.
  24. "The release of fibroblast growth factor-1 from melanoma cells requires copper ions and is mediated by phosphatidylinositol 3-kinase/Akt intracellular signaling pathway."
    Di Serio C., Doria L., Pellerito S., Prudovsky I., Micucci I., Massi D., Landriscina M., Marchionni N., Masotti G., Tarantini F.
    Cancer Lett. 267:67-74(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  25. "Effect of human S100A13 gene silencing on FGF-1 transportation in human endothelial cells."
    Cao R., Yan B., Yang H., Zu X., Wen G., Zhong J.
    J. Formos. Med. Assoc. 109:632-640(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  26. "Cellular signaling by fibroblast growth factor receptors."
    Eswarakumar V.P., Lax I., Schlessinger J.
    Cytokine Growth Factor Rev. 16:139-149(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  27. "Fibroblast growth factor signalling: from development to cancer."
    Turner N., Grose R.
    Nat. Rev. Cancer 10:116-129(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  28. "Nuclear import of exogenous FGF1 requires the ER-protein LRRC59 and the importins Kpnalpha1 and Kpnbeta1."
    Zhen Y., Sorensen V., Skjerpen C.S., Haugsten E.M., Jin Y., Walchli S., Olsnes S., Wiedlocha A.
    Traffic 13:650-664(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF 24-LYS--LYS-27.
  29. "Three-dimensional structures of acidic and basic fibroblast growth factors."
    Zhu X., Komiya H., Chirino A., Faham S., Fox G.M., Arakawa T., Hsu B.T., Rees D.C.
    Science 251:90-93(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 16-155.
  30. "X-ray crystal structure of human acidic fibroblast growth factor."
    Blaber M., Disalvo J., Thomas K.A.
    Biochemistry 35:2086-2094(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-155.
  31. "Structure of a heparin-linked biologically active dimer of fibroblast growth factor."
    DiGabriele A.D., Lax I., Chen D.I., Svahn C.M., Jaye M., Schlessinger J., Hendrickson W.A.
    Nature 393:812-817(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 21-155 IN COMPLEX WITH HEPARIN.
  32. "Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity."
    Plotnikov A.N., Hubbard S.R., Schlessinger J., Mohammadi M.
    Cell 101:413-424(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-155 IN COMPLEX WITH FGFR1.
  33. "Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin."
    Pellegrini L., Burke D.F., von Delft F., Mulloy B., Blundell T.L.
    Nature 407:1029-1034(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 16-155 IN COMPLEX WITH FGFR2 AND HEPARIN.
  34. "Structural interactions of fibroblast growth factor receptor with its ligands."
    Stauber D.J., DiGabriele A.D., Hendrickson W.A.
    Proc. Natl. Acad. Sci. U.S.A. 97:49-54(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 21-155 IN COMPLEX WITH FGFR2.
  35. "Alternative type I and I' turn conformations in the beta8/beta9 beta-hairpin of human acidic fibroblast growth factor."
    Kim J., Blaber S.I., Blaber M.
    Protein Sci. 11:459-466(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 16-155.
  36. "Insights into the molecular basis for fibroblast growth factor receptor autoinhibition and ligand-binding promiscuity."
    Olsen S.K., Ibrahimi O.A., Raucci A., Zhang F., Eliseenkova A.V., Yayon A., Basilico C., Linhardt R.J., Schlessinger J., Mohammadi M.
    Proc. Natl. Acad. Sci. U.S.A. 101:935-940(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH FGFR3.
  37. "1H-NMR assignment and solution structure of human acidic fibroblast growth factor activated by inositol hexasulfate."
    Pineda-Lucena A., Jimenez M.A., Nieto J.L., Santoro J., Rico M., Gimenez-Gallego G.
    J. Mol. Biol. 242:81-98(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 24-155 IN COMPLEX WITH INOSITOL HEXASULFATE, PROTEIN SEQUENCE OF 24-27.
  38. "Three-dimensional structure of acidic fibroblast growth factor in solution: effects of binding to a heparin functional analog."
    Pineda-Lucena A., Jimenez M.A., Lozano R.M., Nieto J.L., Santoro J., Rico M., Gimenez-Gallego G.
    J. Mol. Biol. 264:162-178(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 24-155.
  39. "Solution structure of acidic fibroblast growth factor bound to 1,3, 6-naphthalenetrisulfonate: a minimal model for the anti-tumoral action of suramins and suradistas."
    Lozano R.M., Jimenez M., Santoro J., Rico M., Gimenez-Gallego G.
    J. Mol. Biol. 281:899-915(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 24-155.
  40. "Gentisic acid, a compound associated with plant defense and a metabolite of aspirin, heads a new class of in vivo fibroblast growth factor inhibitors."
    Fernandez I.S., Cuevas P., Angulo J., Lopez-Navajas P., Canales-Mayordomo A., Gonzalez-Corrochano R., Lozano R.M., Valverde S., Jimenez-Barbero J., Romero A., Gimenez-Gallego G.
    J. Biol. Chem. 285:11714-11729(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 24-153 IN COMPLEX WITH GENTISIC ACID AND 2,5-DIHYDROXYPHENYLSULFONATE, FUNCTION, HEPARIN-BINDING, INTERACTION WITH WITH FGFR1.
  41. "The heterohexameric complex structure, a component in the non-classical pathway for fibroblast growth factor 1 (FGF1) secretion."
    Mohan S.K., Rani S.G., Yu C.
    J. Biol. Chem. 285:15464-15475(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 23-155.

Entry informationi

Entry nameiFGF1_HUMAN
AccessioniPrimary (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: July 22, 2015
This is version 192 of the entry and version 1 of the sequence. [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. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.