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P05230

- FGF1_HUMAN

UniProt

P05230 - FGF1_HUMAN

Protein

Fibroblast growth factor 1

Gene

FGF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    1. fibroblast growth factor receptor binding Source: MGI
    2. growth factor activity Source: UniProtKB
    3. heparin binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. S100 protein binding Source: UniProtKB

    GO - Biological processi

    1. anatomical structure morphogenesis Source: ProtInc
    2. angiogenesis Source: UniProtKB-KW
    3. branch elongation involved in ureteric bud branching Source: UniProtKB
    4. cellular response to heat Source: UniProtKB
    5. epidermal growth factor receptor signaling pathway Source: Reactome
    6. Fc-epsilon receptor signaling pathway Source: Reactome
    7. fibroblast growth factor receptor signaling pathway Source: UniProtKB
    8. innate immune response Source: Reactome
    9. insulin receptor signaling pathway Source: Reactome
    10. lung development Source: Ensembl
    11. mesonephric epithelium development Source: UniProtKB
    12. multicellular organismal development Source: ProtInc
    13. neurotrophin TRK receptor signaling pathway Source: Reactome
    14. organ induction Source: Ensembl
    15. phosphatidylinositol-mediated signaling Source: Reactome
    16. positive regulation of angiogenesis Source: UniProtKB
    17. positive regulation of cell division Source: UniProtKB
    18. positive regulation of cell migration Source: UniProtKB
    19. positive regulation of cell proliferation Source: MGI
    20. positive regulation of cholesterol biosynthetic process Source: BHF-UCL
    21. positive regulation of epithelial cell proliferation Source: Ensembl
    22. positive regulation of intracellular signal transduction Source: BHF-UCL
    23. positive regulation of protein phosphorylation Source: Ensembl
    24. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    25. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Developmental protein, Growth factor, Mitogen

    Keywords - Biological processi

    Angiogenesis, Differentiation

    Keywords - Ligandi

    Heparin-binding

    Enzyme and pathway databases

    ReactomeiREACT_111184. Negative regulation of FGFR signaling.
    REACT_120863. Activated point mutants of FGFR2.
    REACT_121153. Signaling by activated point mutants of FGFR1.
    REACT_121249. Signaling by FGFR3 mutants.
    REACT_121337. Signaling by activated point mutants of FGFR3.
    REACT_121398. Signaling by FGFR mutants.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_21247. FRS2-mediated cascade.
    REACT_21270. PI-3K cascade.
    REACT_21310. Phospholipase C-mediated cascade.
    REACT_21374. SHC-mediated cascade.
    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: 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

    1. cell cortex Source: UniProtKB-SubCell
    2. cytosol Source: UniProtKB
    3. extracellular region Source: UniProtKB
    4. extracellular space Source: UniProtKB
    5. nucleus Source: HPA
    6. proteinaceous extracellular matrix Source: Ensembl

    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. 2 Publications
    Mutagenesisi131 – 1311S → A: Decrease in LRRC59-binding. 2 Publications
    Mutagenesisi131 – 1311S → E: Decrease in LRRC59-binding. 2 Publications
    Mutagenesisi133 – 1331K → A: Loss of LRRC59-binding. 2 Publications
    Mutagenesisi133 – 1331K → E: Loss of CSNK2A-, CSNK2B- and LRRC59-binding. 2 Publications
    Mutagenesisi133 – 1331K → R: No effect on LRRC59-binding. 2 Publications

    Organism-specific databases

    PharmGKBiPA28105.

    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

    ArrayExpressiP05230.
    BgeeiP05230.
    CleanExiHS_FGF1.
    GenevestigatoriP05230.

    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. 14 interactions.
    DIPiDIP-3787N.
    IntActiP05230. 6 interactions.
    MINTiMINT-118570.
    STRINGi9606.ENSP00000338548.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    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.
    HOGENOMiHOG000236341.
    HOVERGENiHBG007580.
    InParanoidiP05230.
    KOiK04358.
    OMAiNGLLYGS.
    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.
    PfamiPF00167. FGF. 1 hit.
    [Graphical view]
    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. Align

    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

    MAEGEITTFT ALTEKFNLPP GNYKKPKLLY CSNGGHFLRI LPDGTVDGTR    50
    DRSDQHIQLQ LSAESVGEVY IKSTETGQYL AMDTDGLLYG SQTPNEECLF 100
    LERLEENHYN TYISKKHAEK NWFVGLKKNG SCKRGPRTHY GQKAILFLPL 150
    PVSSD 155
    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:
    EMBL
    GenBank
    DDBJ
    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. [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]
    GeneIDi2246.
    KEGGihsa:2246.
    UCSCiuc003lmm.4. human. [P05230-1]
    uc003lmp.5. human. [P05230-2]

    Polymorphism databases

    DMDMi122737.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 ]
    NP_149128.1. NM_033137.2.
    UniGenei Hs.483635.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    2LDN NMR - A 23-152 [» ]
    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 [» ]
    ProteinModelPortali P05230.
    SMRi P05230. Positions 16-152.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108537. 14 interactions.
    DIPi DIP-3787N.
    IntActi P05230. 6 interactions.
    MINTi MINT-118570.
    STRINGi 9606.ENSP00000338548.

    Chemistry

    BindingDBi P05230.
    ChEMBLi CHEMBL2120.
    DrugBanki DB00686. Pentosan Polysulfate.

    Polymorphism databases

    DMDMi 122737.

    Proteomic databases

    MaxQBi P05230.
    PaxDbi P05230.
    PRIDEi P05230.

    Protocols and materials databases

    DNASUi 2246.
    Structural Biology Knowledgebase Search...

    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 ]
    GeneIDi 2246.
    KEGGi hsa:2246.
    UCSCi uc003lmm.4. human. [P05230-1 ]
    uc003lmp.5. human. [P05230-2 ]

    Organism-specific databases

    CTDi 2246.
    GeneCardsi GC05M141953.
    HGNCi HGNC:3665. FGF1.
    HPAi CAB017519.
    HPA003265.
    MIMi 131220. gene.
    neXtProti NX_P05230.
    PharmGKBi PA28105.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG246422.
    HOGENOMi HOG000236341.
    HOVERGENi HBG007580.
    InParanoidi P05230.
    KOi K04358.
    OMAi NGLLYGS.
    OrthoDBi EOG7992S1.
    PhylomeDBi P05230.
    TreeFami TF317805.

    Enzyme and pathway databases

    Reactomei REACT_111184. Negative regulation of FGFR signaling.
    REACT_120863. Activated point mutants of FGFR2.
    REACT_121153. Signaling by activated point mutants of FGFR1.
    REACT_121249. Signaling by FGFR3 mutants.
    REACT_121337. Signaling by activated point mutants of FGFR3.
    REACT_121398. Signaling by FGFR mutants.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_21247. FRS2-mediated cascade.
    REACT_21270. PI-3K cascade.
    REACT_21310. Phospholipase C-mediated cascade.
    REACT_21374. SHC-mediated cascade.
    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.
    SignaLinki P05230.

    Miscellaneous databases

    ChiTaRSi FGF1. human.
    EvolutionaryTracei P05230.
    GeneWikii FGF1.
    GenomeRNAii 2246.
    NextBioi 9087.
    PROi P05230.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P05230.
    Bgeei P05230.
    CleanExi HS_FGF1.
    Genevestigatori P05230.

    Family and domain databases

    InterProi IPR008996. Cytokine_IL1-like.
    IPR028210. FGF1.
    IPR002209. Fibroblast_GF_fam.
    IPR028142. IL-1_fam/FGF_fam.
    [Graphical view ]
    PANTHERi PTHR11486. PTHR11486. 1 hit.
    PTHR11486:SF65. PTHR11486:SF65. 1 hit.
    Pfami PF00167. FGF. 1 hit.
    [Graphical view ]
    PRINTSi PR00263. HBGFFGF.
    PR00262. IL1HBGF.
    SMARTi SM00442. FGF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50353. SSF50353. 1 hit.
    PROSITEi PS00247. HBGF_FGF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 183 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