| UniProt ID | FGF1_HUMAN | |
|---|---|---|
| UniProt AC | P05230 | |
| Protein Name | Fibroblast growth factor 1 | |
| Gene Name | FGF1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 155 | |
| Subcellular Localization | Secreted. Cytoplasm. Cytoplasm, cell cortex. Cytoplasm, cytosol. Nucleus. 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 S100A | |
| Protein Description | 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] | |
| Protein Sequence | MAEGEITTFTALTEKFNLPPGNYKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESVGEVYIKSTETGQYLAMDTDGLLYGSQTPNEECLFLERLEENHYNTYISKKHAEKNWFVGLKKNGSCKRGPRTHYGQKAILFLPLPVSSD | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MAEGEITTF ------CCCCEEEEE | 33.24 | - | |
| 7 | Phosphorylation | -MAEGEITTFTALTE -CCCCEEEEEEHHHH | 16.14 | 24043423 | |
| 8 | Phosphorylation | MAEGEITTFTALTEK CCCCEEEEEEHHHHH | 25.34 | 24043423 | |
| 10 | Phosphorylation | EGEITTFTALTEKFN CCEEEEEEHHHHHHC | 20.75 | 24043423 | |
| 13 | Phosphorylation | ITTFTALTEKFNLPP EEEEEHHHHHHCCCC | 34.36 | 24043423 | |
| 30 | Nitration | YKKPKLLYCSNGGHF CCCCEEEEECCCCCE | 12.31 | - | |
| 45 | Phosphorylation | LRILPDGTVDGTRDR EEECCCCCCCCCCCC | 23.86 | - | |
| 70 | Nitration | AESVGEVYIKSTETG CEECCEEEEEECCCC | 9.79 | - | |
| 109 | Nitration | ERLEENHYNTYISKK HHHHHHCCCCEECHH | 22.30 | - | |
| 112 | Nitration | EENHYNTYISKKHAE HHHCCCCEECHHHHH | 10.27 | - | |
| 131 | Phosphorylation | VGLKKNGSCKRGPRT EEEECCCCCCCCCCC | 26.34 | - | |
| 140 | Nitration | KRGPRTHYGQKAILF CCCCCCCCCCCEEEE | 22.19 | - | |
| 153 | Phosphorylation | LFLPLPVSSD----- EEEECCCCCC----- | 27.18 | 29514088 | |
| 154 | Phosphorylation | FLPLPVSSD------ EEECCCCCC------ | 47.80 | 29514088 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 131 | S | Phosphorylation | Kinase | PKCD | Q05655 | PSP |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FGF1_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of FGF1_HUMAN !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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