FGF1
entrez
2246
canonical
uniprot
P05230
canonical
ensembl
ENSG00000113578
resolver
ensp
ENSP00000338548
resolver
ensp
ENSP00000352329
resolver
ensp
ENSP00000354231
resolver
ensp
ENSP00000367285
resolver
ensp
ENSP00000396195
resolver
ensp
ENSP00000404742
resolver
ensp
ENSP00000479024
resolver
ensp
ENSP00000480791
resolver
ensp
ENSP00000480980
resolver
ensp
ENSP00000481868
resolver
ensp
ENSP00000536057
resolver
ensp
ENSP00000536059
resolver
ensp
ENSP00000536060
resolver
ensp
ENSP00000536061
resolver
ensp
ENSP00000536062
resolver
ensp
ENSP00000536063
resolver
ensp
ENSP00000536064
resolver
ensp
ENSP00000536068
resolver
ensp
ENSP00000624649
resolver
ensp
ENSP00000624651
resolver
ensp
ENSP00000655217
resolver
ensp
ENSP00000655218
resolver
ensp
ENSP00000711343
resolver
ensp
ENSP00000711344
resolver
ensp
ENSP00000711345
resolver
genesymbol
FGF1
resolver
genesymbol_syn
FGFA
resolver
hgnc
HGNC:3665
resolver
uniprot
A8K147
resolver
uniprot
B2R5T0
resolver
uniprot
D3DQF2
resolver
uniprot
P07502
resolver
uniprot
Q16089
resolver
uniprot
Q16588
resolver
uniprot_entry
A8K147_HUMAN
resolver
uniprot_entry
FGF1_HUMAN
resolver
uniprot_entry
Q16089_HUMAN
resolver
uniprot_sec
B2R5T0
resolver
uniprot_sec
D3DQF2
resolver
uniprot_sec
P07502
resolver
uniprot_sec
Q16588
resolver
amino_acid_sequence
MAEGEITTFTALTEKFNLPPGNYKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESVGEVYIKSTETGQYLAMDTDGLLYGSQTPNEECLFLERLEENHYNTYISKKHAEKNWFVGLKKNGSCKRGPRTHYGQKAILFLPLPVSSD
uniprot
proteins
function
FUNCTION: Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as a potent mitogen in vitro. Acts as a ligand for FGFR1 and integrins. Binds to FGFR1 in the presence of heparin leading to FGFR1 dimerization and activation via sequential autophosphorylation on tyrosine residues which act as docking sites for interacting proteins, leading to the activation of several signaling cascades. Binds to integrin ITGAV:ITGB3. Its binding to integrin, subsequent ternary complex formation with integrin and FGFR1, and the recruitment of PTPN11 to the complex are essential for FGF1 signaling. Induces the phosphorylation and activation of FGFR1, FRS2, MAPK3/ERK1, MAPK1/ERK2 and AKT1 (PubMed:18441324, PubMed:20422052). Can induce angiogenesis (PubMed:23469107). {ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:18441324, ECO:0000269|PubMed:20145243, ECO:0000269|PubMed:20422052, ECO:0000269|PubMed:23469107, ECO:0000269|PubMed:8663044}.
uniprot
proteins
mass_dalton
17460
uniprot
proteins
mutagenesis
MUTAGEN 24..27; /note="KKPK->AAPA: Loss of nuclear import leading to loss of phosphorylation by PKC/PRKCD."; /evidence="ECO:0000269|PubMed:22321063"; MUTAGEN 33; /note="N->A: No effect on integrin-binding."; /evidence="ECO:0000269|PubMed:18441324"; MUTAGEN 50; /note="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."; /evidence="ECO:0000269|PubMed:18441324, ECO:0000269|PubMed:20422052, ECO:0000269|PubMed:23469107"; MUTAGEN 102; /note="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."; /evidence="ECO:0000269|PubMed:18441324"; MUTAGEN 109; /note="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."; /evidence="ECO:0000269|PubMed:18441324"; MUTAGEN 110; /note="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."; /evidence="ECO:0000269|PubMed:18441324"; MUTAGEN 114; /note="S->A: Decrease in LRRC59-binding."; /evidence="ECO:0000269|PubMed:11964394"; MUTAGEN 127; /note="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."; /evidence="ECO:0000269|PubMed:18441324"; MUTAGEN 128; /note="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."; /evidence="ECO:0000269|PubMed:18441324"; MUTAGEN 131; /note="S->A: Decrease in LRRC59-binding."; /evidence="ECO:0000269|PubMed:11964394"; MUTAGEN 131; /note="S->E: Decrease in LRRC59-binding."; /evidence="ECO:0000269|PubMed:11964394"; MUTAGEN 133; /note="K->A: Loss of LRRC59-binding."; /evidence="ECO:0000269|PubMed:11964394"; MUTAGEN 133; /note="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."; /evidence="ECO:0000269|PubMed:11964394, ECO:0000269|PubMed:18441324"; MUTAGEN 133; /note="K->R: No effect on LRRC59-binding."; /evidence="ECO:0000269|PubMed:11964394"; MUTAGEN 134; /note="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."; /evidence="ECO:0000269|PubMed:18441324
uniprot
proteins
post_translational_modification
PTM: In the nucleus, phosphorylated by PKC/PRKCD. {ECO:0000269|PubMed:22321063}.
uniprot
proteins
protein_family
Heparin-binding growth factors family
uniprot
proteins
pubmed
10618369
uniprot
proteins
pubmed
10830168
uniprot
proteins
pubmed
11069186
uniprot
proteins
pubmed
11432880
uniprot
proteins
pubmed
11847269
uniprot
proteins
pubmed
11964394
uniprot
proteins
pubmed
1372643
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14732692
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15863030
uniprot
proteins
pubmed
16597617
uniprot
proteins
pubmed
1693186
uniprot
proteins
pubmed
1702556
uniprot
proteins
pubmed
1717925
uniprot
proteins
pubmed
18400376
uniprot
proteins
pubmed
18441324
uniprot
proteins
pubmed
1885605
uniprot
proteins
pubmed
20094046
uniprot
proteins
pubmed
20145243
uniprot
proteins
pubmed
20220137
uniprot
proteins
pubmed
20422052
uniprot
proteins
pubmed
20863990
uniprot
proteins
pubmed
22321063
uniprot
proteins
pubmed
23469107
uniprot
proteins
pubmed
2393407
uniprot
proteins
pubmed
2427112
uniprot
proteins
pubmed
2474753
uniprot
proteins
pubmed
2590193
uniprot
proteins
pubmed
3523756
uniprot
proteins
pubmed
3527167
uniprot
proteins
pubmed
3732516
uniprot
proteins
pubmed
3778488
uniprot
proteins
pubmed
3964259
uniprot
proteins
pubmed
7504343
uniprot
proteins
pubmed
7521397
uniprot
proteins
pubmed
8652550
uniprot
proteins
pubmed
8663044
uniprot
proteins
pubmed
8950275
uniprot
proteins
pubmed
9655399
uniprot
proteins
pubmed
9719643
uniprot
proteins
sequence_length
155
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. Cytoplasm, cytosol. 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 Cu(2+) 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. {ECO:0000250}.
uniprot
proteins