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P09038

- FGF2_HUMAN

UniProt

P09038 - FGF2_HUMAN

Protein

Fibroblast growth factor 2

Gene

FGF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 181 (01 Oct 2014)
      Sequence version 3 (13 Oct 2009)
      Previous versions | rss
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    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.2 Publications

    pH dependencei

    Retains almost half of its activity after treatment at pH 2.0 for 3 hours at 20 degrees Celsius.1 Publication

    Temperature dependencei

    Inactivated after 3 minutes at 60 degrees Celsius or 1 minute at 80 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei169 – 1691HeparinBy similarity

    GO - Molecular functioni

    1. chemoattractant activity Source: BHF-UCL
    2. cytokine activity Source: BHF-UCL
    3. fibroblast growth factor receptor binding Source: MGI
    4. growth factor activity Source: BHF-UCL
    5. heparin binding Source: UniProtKB-KW
    6. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
    7. protein binding Source: UniProtKB

    GO - Biological processi

    1. activation of MAPK activity Source: ProtInc
    2. activation of MAPKK activity Source: Ensembl
    3. branching involved in ureteric bud morphogenesis Source: UniProtKB
    4. C21-steroid hormone biosynthetic process Source: Ensembl
    5. cell migration involved in sprouting angiogenesis Source: BHF-UCL
    6. chemotaxis Source: ProtInc
    7. chondroblast differentiation Source: UniProtKB
    8. corticotropin hormone secreting cell differentiation Source: Ensembl
    9. embryonic morphogenesis Source: DFLAT
    10. epidermal growth factor receptor signaling pathway Source: Reactome
    11. extracellular matrix organization Source: Reactome
    12. Fc-epsilon receptor signaling pathway Source: Reactome
    13. fibroblast growth factor receptor signaling pathway Source: UniProtKB
    14. glial cell differentiation Source: Ensembl
    15. hyaluronan catabolic process Source: UniProtKB
    16. innate immune response Source: Reactome
    17. inositol phosphate biosynthetic process Source: DFLAT
    18. insulin receptor signaling pathway Source: Reactome
    19. lung development Source: Ensembl
    20. mammary gland epithelial cell differentiation Source: Ensembl
    21. MAPK import into nucleus Source: Ensembl
    22. negative regulation of blood vessel endothelial cell migration Source: BHF-UCL
    23. negative regulation of cell death Source: UniProtKB
    24. negative regulation of cell growth Source: Ensembl
    25. negative regulation of cell proliferation Source: Ensembl
    26. negative regulation of fibroblast migration Source: UniProtKB
    27. negative regulation of transcription, DNA-templated Source: Ensembl
    28. negative regulation of wound healing Source: UniProtKB
    29. nervous system development Source: ProtInc
    30. neurotrophin TRK receptor signaling pathway Source: Reactome
    31. organ induction Source: Ensembl
    32. organ morphogenesis Source: ProtInc
    33. phosphatidylinositol biosynthetic process Source: DFLAT
    34. phosphatidylinositol-mediated signaling Source: Reactome
    35. positive chemotaxis Source: GOC
    36. positive regulation of angiogenesis Source: DFLAT
    37. positive regulation of blood vessel endothelial cell migration Source: BHF-UCL
    38. positive regulation of cardiac muscle cell proliferation Source: BHF-UCL
    39. positive regulation of cell division Source: UniProtKB-KW
    40. positive regulation of cell fate specification Source: MGI
    41. positive regulation of cell proliferation Source: MGI
    42. positive regulation of cerebellar granule cell precursor proliferation Source: Ensembl
    43. positive regulation of endothelial cell proliferation Source: BHF-UCL
    44. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    45. positive regulation of osteoblast differentiation Source: Ensembl
    46. positive regulation of phosphatidylinositol 3-kinase activity Source: DFLAT
    47. positive regulation of phospholipase C activity Source: DFLAT
    48. positive regulation of transcription, DNA-templated Source: UniProtKB
    49. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    50. Ras protein signal transduction Source: ProtInc
    51. regulation of angiogenesis Source: DFLAT
    52. regulation of cell cycle Source: Ensembl
    53. regulation of retinal cell programmed cell death Source: Ensembl
    54. release of sequestered calcium ion into cytosol Source: DFLAT
    55. response to axon injury Source: Ensembl
    56. signal transduction Source: ProtInc
    57. stem cell development Source: Ensembl
    58. substantia nigra development Source: Ensembl
    59. thyroid-stimulating hormone-secreting cell differentiation Source: Ensembl
    60. wound healing Source: DFLAT

    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_163874. Non-integrin membrane-ECM interactions.
    REACT_163942. Syndecan interactions.
    REACT_200759. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
    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_9452. FGFR4 ligand binding and activation.
    REACT_9510. FGFR3c ligand binding and activation.
    REACT_9515. FGFR1c ligand binding and activation.
    REACT_976. PI3K Cascade.
    SignaLinkiP09038.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fibroblast growth factor 2
    Short name:
    FGF-2
    Alternative name(s):
    Basic fibroblast growth factor
    Short name:
    bFGF
    Heparin-binding growth factor 2
    Short name:
    HBGF-2
    Gene namesi
    Name:FGF2
    Synonyms:FGFB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:3676. FGF2.

    Subcellular locationi

    Secreted. Nucleus
    Note: Exported from cells by an endoplasmic reticulum (ER)/Golgi-independent mechanism. Unconventional secretion of FGF2 occurs by direct translocation across the plasma membrane. Binding of exogenous FGF2 to FGFR facilitates endocytosis followed by translocation of FGF2 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 CEP57.

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. extracellular region Source: Reactome
    3. extracellular space Source: ProtInc
    4. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28115.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 142142Or 93, or 124, or 125, or 131, or 161PRO_0000008932Add
    BLAST
    Chaini143 – 288146Fibroblast growth factor 2PRO_0000008933Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei108 – 1081Omega-N-methylarginine; alternateBy similarity
    Modified residuei108 – 1081Symmetric dimethylarginine; alternateBy similarity
    Modified residuei110 – 1101Omega-N-methylarginine; alternateBy similarity
    Modified residuei110 – 1101Symmetric dimethylarginine; alternateBy similarity
    Modified residuei112 – 1121Omega-N-methylarginine; alternateBy similarity
    Modified residuei112 – 1121Symmetric dimethylarginine; alternateBy similarity
    Modified residuei215 – 2151Phosphotyrosine; by TEC1 Publication

    Post-translational modificationi

    Phosphorylation at Tyr-215 regulates FGF2 unconventional secretion.1 Publication
    Several N-termini starting at positions 94, 125, 126, 132, 143 and 162 have been identified by direct sequencing.

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP09038.
    PaxDbiP09038.
    PRIDEiP09038.

    PTM databases

    PhosphoSiteiP09038.

    Expressioni

    Tissue specificityi

    Expressed in granulosa and cumulus cells. Expressed in hepatocellular carcinoma cells, but not in non-cancerous liver tissue.2 Publications

    Gene expression databases

    ArrayExpressiP09038.
    BgeeiP09038.
    CleanExiHS_FGF2.
    GenevestigatoriP09038.

    Organism-specific databases

    HPAiCAB000125.

    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. Interacts with CSPG4, FGFBP1 and TEC. Found in a complex with FGFBP1, FGF1 and FGF2.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CASP1P294662EBI-977447,EBI-516667
    FGFBP1Q145123EBI-977447,EBI-953742
    FGFR1P113624EBI-977447,EBI-1028277
    FGFR1P11362-142EBI-977447,EBI-6622185
    FGFR2P218023EBI-977447,EBI-1028658

    Protein-protein interaction databases

    BioGridi108538. 19 interactions.
    DIPiDIP-4012N.
    IntActiP09038. 6 interactions.
    MINTiMINT-222469.

    Structurei

    Secondary structure

    1
    288
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi136 – 1394
    Beta strandi151 – 1533
    Beta strandi156 – 1616
    Beta strandi163 – 1675
    Turni168 – 1714
    Beta strandi172 – 1765
    Beta strandi182 – 1854
    Helixi191 – 1933
    Beta strandi195 – 1995
    Beta strandi201 – 2033
    Beta strandi204 – 2096
    Turni210 – 2134
    Beta strandi214 – 2185
    Beta strandi220 – 2223
    Beta strandi224 – 2296
    Helixi232 – 2343
    Beta strandi236 – 2405
    Helixi242 – 2443
    Beta strandi246 – 2538
    Beta strandi264 – 2663
    Helixi269 – 2713
    Helixi277 – 2793
    Beta strandi281 – 2855

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BASX-ray1.90A135-288[»]
    1BFBX-ray1.90A142-288[»]
    1BFCX-ray2.20A142-288[»]
    1BFFX-ray2.00A160-288[»]
    1BFGX-ray1.60A143-288[»]
    1BLANMR-A134-288[»]
    1BLDNMR-A134-288[»]
    1CVSX-ray2.80A/B157-288[»]
    1EV2X-ray2.20A/B/C/D157-288[»]
    1FGAX-ray2.20A143-288[»]
    1FQ9X-ray3.00A/B157-288[»]
    1II4X-ray2.70A/B/C/D134-288[»]
    1IILX-ray2.30A/B/C/D134-288[»]
    2BFHX-ray2.50A161-288[»]
    2FGFX-ray1.77A143-288[»]
    2M49NMR-A/C161-286[»]
    4FGFX-ray1.60A143-288[»]
    ProteinModelPortaliP09038.
    SMRiP09038. Positions 134-288.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09038.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni261 – 27717Heparin-bindingBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi179 – 1813Cell attachment site; atypicalSequence Analysis
    Motifi221 – 2233Cell attachment site; atypicalSequence Analysis

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG325757.
    HOVERGENiHBG107917.
    InParanoidiP09038.
    KOiK04358.
    OrthoDBiEOG7992S1.
    PhylomeDBiP09038.
    TreeFamiTF317805.

    Family and domain databases

    InterProiIPR008996. Cytokine_IL1-like.
    IPR028223. FGF2.
    IPR002209. Fibroblast_GF_fam.
    IPR028142. IL-1_fam/FGF_fam.
    [Graphical view]
    PANTHERiPTHR11486. PTHR11486. 1 hit.
    PTHR11486:SF68. PTHR11486:SF68. 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 (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative initiation. Align

    Isoform 1 (identifier: P09038-4) [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

    MVGVGGGDVE DVTPRPGGCQ ISGRGARGCN GIPGAAAWEA ALPRRRPRRH    50
    PSVNPRSRAA GSPRTRGRRT EERPSGSRLG DRGRGRALPG GRLGGRGRGR 100
    APERVGGRGR GRGTAAPRAA PAARGSRPGP AGTMAAGSIT TLPALPEDGG 150
    SGAFPPGHFK DPKRLYCKNG GFFLRIHPDG RVDGVREKSD PHIKLQLQAE 200
    ERGVVSIKGV CANRYLAMKE DGRLLASKCV TDECFFFERL ESNNYNTYRS 250
    RKYTSWYVAL KRTGQYKLGS KTGPGQKAIL FLPMSAKS 288

    Note: Starts at an alternative CUG codon.

    Length:288
    Mass (Da):30,770
    Last modified:October 13, 2009 - v3
    Checksum:iEAE98552A39D5E19
    GO
    Isoform 2 (identifier: P09038-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-78: Missing.
         79-79: L → M

    Note: Starts at an alternative CUG codon.

    Show »
    Length:210
    Mass (Da):22,623
    Checksum:iA21C7A6E82E4F5BD
    GO
    Isoform 3 (identifier: P09038-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-133: Missing.

    Show »
    Length:155
    Mass (Da):17,254
    Checksum:iBE6CE13373007129
    GO
    Isoform 4 (identifier: P09038-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-92: Missing.
         93-93: L → M

    Note: Starts at an alternative CUG codon.

    Show »
    Length:196
    Mass (Da):21,203
    Checksum:iD6B5447137E60343
    GO

    Sequence cautioni

    The sequence AAB21432.2 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.
    The sequence ABO43041.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.
    The sequence CAA28027.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.
    The sequence CAA73868.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.
    The sequence EAX05222.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.
    The sequence AAA52448.1 differs from that shown. Reason: Frameshift at positions 25, 82, 98 and 133.
    The sequence AAB21432.2 differs from that shown. Reason: Frameshift at position 25.
    The sequence CAA28027.1 differs from that shown. Reason: Frameshift at positions 25 and 102.
    The sequence CAA73868.1 differs from that shown. Reason: Frameshift at position 25.
    The sequence ABO43041.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence EAX05222.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251G → R in AAA52448. (PubMed:2435575)Curated
    Sequence conflicti50 – 501H → Q in AAA52448. (PubMed:2435575)Curated
    Sequence conflicti59 – 591A → R in AAA52448. (PubMed:2435575)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 133133Missing in isoform 3. 2 PublicationsVSP_037383Add
    BLAST
    Alternative sequencei1 – 9292Missing in isoform 4. 1 PublicationVSP_037384Add
    BLAST
    Alternative sequencei1 – 7878Missing in isoform 2. 1 PublicationVSP_038236Add
    BLAST
    Alternative sequencei79 – 791L → M in isoform 2. 1 PublicationVSP_038237
    Alternative sequencei93 – 931L → M in isoform 4. 1 PublicationVSP_037385

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04431 Genomic DNA. Translation: CAA28027.1. Sequence problems.
    X04432 Genomic DNA. Translation: CAA28028.1.
    X04433 Genomic DNA. Translation: CAA28029.1.
    J04513 mRNA. Translation: AAA52531.1.
    J04513 mRNA. Translation: AAA52532.1.
    J04513 mRNA. Translation: AAA52533.1.
    AB451321 mRNA. Translation: BAG70135.1.
    AB451450 mRNA. Translation: BAG70264.1.
    EF506888 Genomic DNA. Translation: ABO43041.1. Sequence problems.
    AC021205 Genomic DNA. No translation available.
    CH471056 Genomic DNA. Translation: EAX05222.1. Sequence problems.
    S81809 Genomic DNA. Translation: AAB21432.2. Sequence problems.
    Y13468 Genomic DNA. Translation: CAA73868.1. Sequence problems.
    M27968 mRNA. Translation: AAA52448.1. Frameshift.
    M17599 mRNA. Translation: AAA52534.1.
    AY820133 mRNA. Translation: AAV70487.1.
    S47380 mRNA. Translation: AAD13853.1.
    CCDSiCCDS34059.1. [P09038-4]
    PIRiA32398.
    RefSeqiNP_001997.5. NM_002006.4. [P09038-4]
    UniGeneiHs.284244.

    Genome annotation databases

    EnsembliENST00000608478; ENSP00000477134; ENSG00000138685. [P09038-2]
    GeneIDi2247.
    KEGGihsa:2247.
    UCSCiuc003iev.1. human. [P09038-4]

    Polymorphism databases

    DMDMi261260095.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04431 Genomic DNA. Translation: CAA28027.1 . Sequence problems.
    X04432 Genomic DNA. Translation: CAA28028.1 .
    X04433 Genomic DNA. Translation: CAA28029.1 .
    J04513 mRNA. Translation: AAA52531.1 .
    J04513 mRNA. Translation: AAA52532.1 .
    J04513 mRNA. Translation: AAA52533.1 .
    AB451321 mRNA. Translation: BAG70135.1 .
    AB451450 mRNA. Translation: BAG70264.1 .
    EF506888 Genomic DNA. Translation: ABO43041.1 . Sequence problems.
    AC021205 Genomic DNA. No translation available.
    CH471056 Genomic DNA. Translation: EAX05222.1 . Sequence problems.
    S81809 Genomic DNA. Translation: AAB21432.2 . Sequence problems.
    Y13468 Genomic DNA. Translation: CAA73868.1 . Sequence problems.
    M27968 mRNA. Translation: AAA52448.1 . Frameshift.
    M17599 mRNA. Translation: AAA52534.1 .
    AY820133 mRNA. Translation: AAV70487.1 .
    S47380 mRNA. Translation: AAD13853.1 .
    CCDSi CCDS34059.1. [P09038-4 ]
    PIRi A32398.
    RefSeqi NP_001997.5. NM_002006.4. [P09038-4 ]
    UniGenei Hs.284244.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BAS X-ray 1.90 A 135-288 [» ]
    1BFB X-ray 1.90 A 142-288 [» ]
    1BFC X-ray 2.20 A 142-288 [» ]
    1BFF X-ray 2.00 A 160-288 [» ]
    1BFG X-ray 1.60 A 143-288 [» ]
    1BLA NMR - A 134-288 [» ]
    1BLD NMR - A 134-288 [» ]
    1CVS X-ray 2.80 A/B 157-288 [» ]
    1EV2 X-ray 2.20 A/B/C/D 157-288 [» ]
    1FGA X-ray 2.20 A 143-288 [» ]
    1FQ9 X-ray 3.00 A/B 157-288 [» ]
    1II4 X-ray 2.70 A/B/C/D 134-288 [» ]
    1IIL X-ray 2.30 A/B/C/D 134-288 [» ]
    2BFH X-ray 2.50 A 161-288 [» ]
    2FGF X-ray 1.77 A 143-288 [» ]
    2M49 NMR - A/C 161-286 [» ]
    4FGF X-ray 1.60 A 143-288 [» ]
    ProteinModelPortali P09038.
    SMRi P09038. Positions 134-288.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108538. 19 interactions.
    DIPi DIP-4012N.
    IntActi P09038. 6 interactions.
    MINTi MINT-222469.

    Chemistry

    BindingDBi P09038.
    ChEMBLi CHEMBL3107.
    DrugBanki DB00686. Pentosan Polysulfate.

    PTM databases

    PhosphoSitei P09038.

    Polymorphism databases

    DMDMi 261260095.

    Proteomic databases

    MaxQBi P09038.
    PaxDbi P09038.
    PRIDEi P09038.

    Protocols and materials databases

    DNASUi 2247.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000608478 ; ENSP00000477134 ; ENSG00000138685 . [P09038-2 ]
    GeneIDi 2247.
    KEGGi hsa:2247.
    UCSCi uc003iev.1. human. [P09038-4 ]

    Organism-specific databases

    CTDi 2247.
    GeneCardsi GC04P123747.
    HGNCi HGNC:3676. FGF2.
    HPAi CAB000125.
    MIMi 134920. gene.
    neXtProti NX_P09038.
    PharmGKBi PA28115.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG325757.
    HOVERGENi HBG107917.
    InParanoidi P09038.
    KOi K04358.
    OrthoDBi EOG7992S1.
    PhylomeDBi P09038.
    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_163874. Non-integrin membrane-ECM interactions.
    REACT_163942. Syndecan interactions.
    REACT_200759. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
    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_9452. FGFR4 ligand binding and activation.
    REACT_9510. FGFR3c ligand binding and activation.
    REACT_9515. FGFR1c ligand binding and activation.
    REACT_976. PI3K Cascade.
    SignaLinki P09038.

    Miscellaneous databases

    EvolutionaryTracei P09038.
    GeneWikii Basic_fibroblast_growth_factor.
    GenomeRNAii 2247.
    NextBioi 9095.
    PROi P09038.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09038.
    Bgeei P09038.
    CleanExi HS_FGF2.
    Genevestigatori P09038.

    Family and domain databases

    InterProi IPR008996. Cytokine_IL1-like.
    IPR028223. FGF2.
    IPR002209. Fibroblast_GF_fam.
    IPR028142. IL-1_fam/FGF_fam.
    [Graphical view ]
    PANTHERi PTHR11486. PTHR11486. 1 hit.
    PTHR11486:SF68. PTHR11486:SF68. 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 basic fibroblast growth factor: nucleotide sequence, genomic organization, and expression in mammalian cells."
      Abraham J.A., Whang J.L., Tumolo A., Mergia A., Fiddes J.C.
      Cold Spring Harb. Symp. Quant. Biol. 51:657-668(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Human basic fibroblast growth factor: nucleotide sequence and genomic organization."
      Abraham J.A., Whang J.L., Tumolo A., Mergia A., Friedman J., Gospodarowicz D., Fiddes J.C.
      EMBO J. 5:2523-2528(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    3. "High molecular mass forms of basic fibroblast growth factor are initiated by alternative CUG codons."
      Prats H., Kaghad M., Prats A.C., Klagsbrun M., Lelias J.M., Liauzun P., Chalon P., Tauber J.P., Amalric F., Smith J.A., Caput D.
      Proc. Natl. Acad. Sci. U.S.A. 86:1836-1840(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), PROTEIN SEQUENCE OF 126-145 (ISOFORMS 1/2/4), ALTERNATIVE INITIATION.
      Tissue: Hepatoma.
    4. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    5. NIEHS SNPs program
      Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-192.
    9. "Mutations in the 5' untranslated region of the FGF-2 gene."
      Handschug K., Archoukieh E., Glaeser C.
      Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-192.
      Tissue: Blood.
    10. "Cloning and expression of cDNA encoding human basic fibroblast growth factor."
      Kurokawa T., Sasada R., Iwane M., Igarashi K.
      FEBS Lett. 213:189-194(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-288 (ISOFORM 1).
    11. "Characterization of high-molecular-mass forms of basic fibroblast growth factor produced by hepatocellular carcinoma cells: possible involvement of basic fibroblast growth factor in hepatocarcinogenesis."
      Shimoyama Y., Gotoh M., Ino Y., Sakamoto M., Kato K., Hirohashi S.
      Jpn. J. Cancer Res. 82:1263-1270(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 94-107 AND 162-173, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
      Tissue: Hepatoma.
    12. "Human amniotic tumor that induces new bone formation in vivo produces growth-regulatory activity in vitro for osteoblasts identified as an extended form of basic fibroblast growth factor."
      Izbicka E., Dunstan C., Esparza J., Jacobs C., Sabatini M., Mundy G.R.
      Cancer Res. 56:633-636(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 125-140 (ISOFORMS 1/2/4).
    13. "A form of human basic fibroblast growth factor with an extended amino terminus."
      Sommer A., Brewer M.T., Thompson R.C., Moscatelli D., Presta M., Rifkin D.B.
      Biochem. Biophys. Res. Commun. 144:543-550(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 132-288 (ISOFORMS 1/2/4), PROTEIN SEQUENCE OF 132-148; 153-160; 165-247; 252-261 AND 267-288 (ISOFORMS 2/4).
      Tissue: Hepatoma and Placenta.
    14. "Amino-terminal sequence of a large form of basic fibroblast growth factor isolated from human benign prostatic hyperplastic tissue."
      Story M.T., Esch F., Shimasaki S., Sasse J., Jacobs S.C., Lawson R.K.
      Biochem. Biophys. Res. Commun. 142:702-709(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 135-155 (ISOFORMS 1/2/3/4).
    15. Zhang H.J., Zhang S.M., Zhuang H.
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 143-288 (ISOFORMS 1/2/3/4).
    16. "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 143-172 (ISOFORMS 1/2/3/4).
    17. "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 143-168 (ISOFORMS 1/2/3/4).
    18. "Reverse transcription with nested polymerase chain reaction shows expression of basic fibroblast growth factor transcripts in human granulosa and cumulus cells from in vitro fertilisation patients."
      Watson R., Anthony F., Pickett M., Lambden P., Masson G.M., Thomas E.J.
      Biochem. Biophys. Res. Commun. 187:1227-1231(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 173-260 (ISOFORMS 1/2/3/4), TISSUE SPECIFICITY.
    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 FGF1.
    20. Cited for: INTERACTION WITH FGFR1; FGFR2; FGFR3 AND FGFR4, FUNCTION IN CELL PROLIFERATION.
    21. "High-affinity binding of basic fibroblast growth factor and platelet-derived growth factor-AA to the core protein of the NG2 proteoglycan."
      Goretzki L., Burg M.A., Grako K.A., Stallcup W.B.
      J. Biol. Chem. 274:16831-16837(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CSPG4.
    22. "Enhancement of fibroblast growth factor (FGF) activity by an FGF-binding protein."
      Tassi E., Al-Attar A., Aigner A., Swift M.R., McDonnell K., Karavanov A., Wellstein A.
      J. Biol. Chem. 276:40247-40253(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FGFBP1.
    23. "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 FGF1.
    24. "Identification of the fibroblast growth factor (FGF)-interacting domain in a secreted FGF-binding protein by phage display."
      Xie B., Tassi E., Swift M.R., McDonnell K., Bowden E.T., Wang S., Ueda Y., Tomita Y., Riegel A.T., Wellstein A.
      J. Biol. Chem. 281:1137-1144(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FGFBP1.
    25. "Tec-kinase-mediated phosphorylation of fibroblast growth factor 2 is essential for unconventional secretion."
      Ebert A.D., Laussmann M., Wegehingel S., Kaderali L., Erfle H., Reichert J., Lechner J., Beer H.D., Pepperkok R., Nickel W.
      Traffic 11:813-826(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-215, INTERACTION WITH TEC, 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.
    29. "Crystal structure of basic fibroblast growth factor at 1.6-A resolution."
      Ago H., Kitagawa Y., Fujishima A., Matsuura Y., Katsube Y.
      J. Biochem. 110:360-363(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 143-288.
    30. "Three-dimensional structure of human basic fibroblast growth factor."
      Eriksson A.E., Cousens L.S., Weaver L.H., Matthews B.W.
      Proc. Natl. Acad. Sci. U.S.A. 88:3441-3445(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 143-288.
    31. "Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin 1 beta."
      Zhang J., Cousens L.S., Barr P.J., Sprang S.R.
      Proc. Natl. Acad. Sci. U.S.A. 88:3446-3450(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 143-288.
    32. "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 (2.8 ANGSTROMS) OF 135-288.
    33. "Refinement of the structure of human basic fibroblast growth factor at 1.6-A resolution and analysis of presumed heparin binding sites by selenate substitution."
      Eriksson A.E., Cousens L.S., Matthews B.W.
      Protein Sci. 2:1274-1284(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 143-288.
    34. "Structural basis for fibroblast growth factor receptor 2 activation in Apert syndrome."
      Ibrahimi O.A., Eliseenkova A.V., Plotnikov A.N., Yu K., Ornitz D.M., Mohammadi M.
      Proc. Natl. Acad. Sci. U.S.A. 98:7182-7187(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 134-288 IN COMPLEX WITH FGFR2.
    35. "High-resolution solution structure of basic fibroblast growth factor determined by multidimensional heteronuclear magnetic resonance spectroscopy."
      Moy F.J., Seddon A.P., Boehlen P., Powers R.
      Biochemistry 35:13552-13561(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 134-288.

    Entry informationi

    Entry nameiFGF2_HUMAN
    AccessioniPrimary (citable) accession number: P09038
    Secondary accession number(s): A4LBB8
    , O00527, P78443, Q16443, Q5PY50, Q7KZ11, Q7KZ72, Q9UC54, Q9UCS5, Q9UCS6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: October 13, 2009
    Last modified: October 1, 2014
    This is version 181 of the entry and version 3 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

    Miscellaneous

    This protein binds heparin more strongly than does aFGF.

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3