SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P31371

- FGF9_HUMAN

UniProt

P31371 - FGF9_HUMAN

Protein

Fibroblast growth factor 9

Gene

FGF9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 3 (01 Oct 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. May have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors.2 Publications

    GO - Molecular functioni

    1. growth factor activity Source: ProtInc
    2. heparin binding Source: UniProtKB-KW

    GO - Biological processi

    1. angiogenesis Source: Ensembl
    2. cell-cell signaling Source: ProtInc
    3. chondrocyte differentiation Source: Ensembl
    4. embryonic digestive tract development Source: Ensembl
    5. embryonic limb morphogenesis Source: Ensembl
    6. embryonic skeletal system development Source: Ensembl
    7. epidermal growth factor receptor signaling pathway Source: Reactome
    8. Fc-epsilon receptor signaling pathway Source: Reactome
    9. fibroblast growth factor receptor signaling pathway Source: MGI
    10. innate immune response Source: Reactome
    11. inner ear morphogenesis Source: Ensembl
    12. insulin receptor signaling pathway Source: Reactome
    13. lung-associated mesenchyme development Source: Ensembl
    14. male gonad development Source: UniProtKB
    15. male sex determination Source: Ensembl
    16. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    17. negative regulation of Wnt signaling pathway Source: Ensembl
    18. neurotrophin TRK receptor signaling pathway Source: Reactome
    19. osteoblast differentiation Source: Ensembl
    20. phosphatidylinositol-mediated signaling Source: Reactome
    21. positive regulation of canonical Wnt signaling pathway Source: Ensembl
    22. positive regulation of cardiac muscle cell proliferation Source: Ensembl
    23. positive regulation of cell division Source: UniProtKB-KW
    24. positive regulation of cell proliferation Source: MGI
    25. positive regulation of epithelial cell proliferation Source: Ensembl
    26. positive regulation of gene expression Source: Ensembl
    27. positive regulation of MAPK cascade Source: Ensembl
    28. positive regulation of mesenchymal cell proliferation Source: Ensembl
    29. positive regulation of smoothened signaling pathway Source: Ensembl
    30. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: Ensembl
    31. protein import into nucleus Source: Ensembl
    32. regulation of timing of cell differentiation Source: Ensembl
    33. signal transduction Source: ProtInc
    34. substantia nigra development Source: UniProt

    Keywords - Molecular functioni

    Developmental protein, Growth factor, Mitogen

    Keywords - Biological processi

    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_9413. FGFR2c 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.
    SignaLinkiP31371.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fibroblast growth factor 9
    Short name:
    FGF-9
    Alternative name(s):
    Glia-activating factor
    Short name:
    GAF
    Heparin-binding growth factor 9
    Short name:
    HBGF-9
    Gene namesi
    Name:FGF9
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

    Organism-specific databases

    HGNCiHGNC:3687. FGF9.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: Ensembl
    2. cytoplasm Source: Ensembl
    3. extracellular region Source: Reactome
    4. extracellular space Source: MGI
    5. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Multiple synostoses syndrome 3 (SYNS3) [MIM:612961]: A bone disease characterized by multiple progressive joint fusions that commonly involve proximal interphalangeal, tarsal-carpal, humeroradial and cervical spine joints. Additional features can include progressive conductive deafness and facial dysmorphism.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti99 – 991S → N in SYNS3; expressed and secreted as efficiently as wild-type; however it induces compromised chondrocyte proliferation and differentiation accompanied by enhanced osteogenic differentiation and matrix mineralization of bone marrow-derived mesenchymal stem cells. 1 Publication
    VAR_063254

    Keywords - Diseasei

    Deafness, Disease mutation

    Organism-specific databases

    MIMi612961. phenotype.
    Orphaneti3237. Multiple synostoses syndrome.
    PharmGKBiPA28126.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 331 PublicationPRO_0000008973
    Chaini4 – 208205Fibroblast growth factor 9PRO_0000008974Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi79 – 791N-linked (GlcNAc...)

    Post-translational modificationi

    Three molecular species were found (30 kDa, 29 kDa and 25 kDa), cleaved at Leu-4, Val-13 and Ser-34 respectively. The smaller ones might be products of proteolytic digestion. Furthermore, there may be a functional signal sequence in the 30 kDa species which is uncleavable in the secretion step.
    N-glycosylated.

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiP31371.
    PRIDEiP31371.

    PTM databases

    PhosphoSiteiP31371.

    Expressioni

    Tissue specificityi

    Glial cells.

    Gene expression databases

    BgeeiP31371.
    CleanExiHS_FGF9.
    GenevestigatoriP31371.

    Organism-specific databases

    HPAiCAB004392.

    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.4 Publications

    Protein-protein interaction databases

    BioGridi108545. 2 interactions.
    DIPiDIP-6036N.
    STRINGi9606.ENSP00000371790.

    Structurei

    Secondary structure

    1
    208
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi53 – 608
    Beta strandi63 – 686
    Beta strandi73 – 764
    Beta strandi82 – 876
    Helixi91 – 933
    Beta strandi95 – 1017
    Beta strandi104 – 1096
    Turni110 – 1123
    Beta strandi115 – 1184
    Beta strandi124 – 1296
    Helixi132 – 1343
    Beta strandi136 – 1427
    Beta strandi145 – 15410
    Turni156 – 1583
    Beta strandi161 – 1633
    Helixi175 – 1773
    Helixi183 – 1853
    Beta strandi187 – 1904
    Helixi194 – 1963
    Helixi200 – 2034

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G82X-ray2.60A/B/C/D49-208[»]
    1IHKX-ray2.20A35-208[»]
    ProteinModelPortaliP31371.
    SMRiP31371. Positions 52-208.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP31371.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG269410.
    HOGENOMiHOG000236341.
    HOVERGENiHBG007580.
    InParanoidiP31371.
    KOiK04358.
    OMAiGELYGSD.
    OrthoDBiEOG7992S1.
    PhylomeDBiP31371.
    TreeFamiTF317805.

    Family and domain databases

    InterProiIPR008996. Cytokine_IL1-like.
    IPR028251. FGF9.
    IPR002209. Fibroblast_GF_fam.
    IPR028142. IL-1_fam/FGF_fam.
    [Graphical view]
    PANTHERiPTHR11486. PTHR11486. 1 hit.
    PTHR11486:SF28. PTHR11486:SF28. 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]
    ProtoNetiSearch...

    Sequencei

    Sequence statusi: Complete.

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

    P31371-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPLGEVGNY FGVQDAVPFG NVPVLPVDSP VLLSDHLGQS EAGGLPRGPA    50
    VTDLDHLKGI LRRRQLYCRT GFHLEIFPNG TIQGTRKDHS RFGILEFISI 100
    AVGLVSIRGV DSGLYLGMNE KGELYGSEKL TQECVFREQF EENWYNTYSS 150
    NLYKHVDTGR RYYVALNKDG TPREGTRTKR HQKFTHFLPR PVDPDKVPEL 200
    YKDILSQS 208
    Length:208
    Mass (Da):23,441
    Last modified:October 1, 1994 - v3
    Checksum:iF32A0E7106EF59C9
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti94 – 941I → V.1 Publication
    Corresponds to variant rs12427696 [ dbSNP | Ensembl ].
    VAR_020944
    Natural varianti99 – 991S → N in SYNS3; expressed and secreted as efficiently as wild-type; however it induces compromised chondrocyte proliferation and differentiation accompanied by enhanced osteogenic differentiation and matrix mineralization of bone marrow-derived mesenchymal stem cells. 1 Publication
    VAR_063254

    Sequence conflict

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 263VLP → SLL AA sequence (PubMed:8428960)Curated
    Sequence conflicti34 – 341S → A AA sequence (PubMed:8428960)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14838 mRNA. Translation: BAA03572.1.
    AY682094 Genomic DNA. Translation: AAT74624.1.
    AK290792 mRNA. Translation: BAF83481.1.
    AL139378 Genomic DNA. Translation: CAC17692.1.
    CH471075 Genomic DNA. Translation: EAX08316.1.
    BC069692 mRNA. Translation: AAH69692.1.
    BC103978 mRNA. Translation: AAI03979.1.
    BC103979 mRNA. Translation: AAI03980.1.
    CCDSiCCDS9298.1.
    PIRiA48137.
    RefSeqiNP_002001.1. NM_002010.2.
    UniGeneiHs.111.

    Genome annotation databases

    EnsembliENST00000382353; ENSP00000371790; ENSG00000102678.
    GeneIDi2254.
    KEGGihsa:2254.
    UCSCiuc001uog.2. human.

    Polymorphism databases

    DMDMi544290.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    R&D Systems' cytokine source book: FGF-9
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14838 mRNA. Translation: BAA03572.1 .
    AY682094 Genomic DNA. Translation: AAT74624.1 .
    AK290792 mRNA. Translation: BAF83481.1 .
    AL139378 Genomic DNA. Translation: CAC17692.1 .
    CH471075 Genomic DNA. Translation: EAX08316.1 .
    BC069692 mRNA. Translation: AAH69692.1 .
    BC103978 mRNA. Translation: AAI03979.1 .
    BC103979 mRNA. Translation: AAI03980.1 .
    CCDSi CCDS9298.1.
    PIRi A48137.
    RefSeqi NP_002001.1. NM_002010.2.
    UniGenei Hs.111.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G82 X-ray 2.60 A/B/C/D 49-208 [» ]
    1IHK X-ray 2.20 A 35-208 [» ]
    ProteinModelPortali P31371.
    SMRi P31371. Positions 52-208.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108545. 2 interactions.
    DIPi DIP-6036N.
    STRINGi 9606.ENSP00000371790.

    PTM databases

    PhosphoSitei P31371.

    Polymorphism databases

    DMDMi 544290.

    Proteomic databases

    PaxDbi P31371.
    PRIDEi P31371.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000382353 ; ENSP00000371790 ; ENSG00000102678 .
    GeneIDi 2254.
    KEGGi hsa:2254.
    UCSCi uc001uog.2. human.

    Organism-specific databases

    CTDi 2254.
    GeneCardsi GC13P022245.
    HGNCi HGNC:3687. FGF9.
    HPAi CAB004392.
    MIMi 600921. gene.
    612961. phenotype.
    neXtProti NX_P31371.
    Orphaneti 3237. Multiple synostoses syndrome.
    PharmGKBi PA28126.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG269410.
    HOGENOMi HOG000236341.
    HOVERGENi HBG007580.
    InParanoidi P31371.
    KOi K04358.
    OMAi GELYGSD.
    OrthoDBi EOG7992S1.
    PhylomeDBi P31371.
    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_9413. FGFR2c 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 P31371.

    Miscellaneous databases

    EvolutionaryTracei P31371.
    GeneWikii FGF9.
    GenomeRNAii 2254.
    NextBioi 9131.
    PROi P31371.
    SOURCEi Search...

    Gene expression databases

    Bgeei P31371.
    CleanExi HS_FGF9.
    Genevestigatori P31371.

    Family and domain databases

    InterProi IPR008996. Cytokine_IL1-like.
    IPR028251. FGF9.
    IPR002209. Fibroblast_GF_fam.
    IPR028142. IL-1_fam/FGF_fam.
    [Graphical view ]
    PANTHERi PTHR11486. PTHR11486. 1 hit.
    PTHR11486:SF28. PTHR11486:SF28. 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. "Molecular cloning of a novel cytokine cDNA encoding the ninth member of the fibroblast growth factor family, which has a unique secretion property."
      Miyamoto M., Naruo K., Seko C., Matsumoto S., Kondo T., Kurokawa T.
      Mol. Cell. Biol. 13:4251-4259(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Foreskin.
    2. NIEHS SNPs program
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-94.
    3. "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].
      Tissue: Kidney.
    4. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
    7. "Novel secretory heparin-binding factors from human glioma cells (glia-activating factors) involved in glial cell growth. Purification and biological properties."
      Naruo K., Seko C., Kuroshima K., Matsutani E., Sasada R., Kondo T., Kurokawa T.
      J. Biol. Chem. 268:2857-2864(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 4-26 AND 34-54.
      Tissue: Glial tumor.
    8. Cited for: INTERACTION WITH FGFR2 AND FGFR3, FUNCTION IN CELL PROLIFERATION.
    9. "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.
    10. "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.
    11. "Structure of fibroblast growth factor 9 shows a symmetric dimer with unique receptor- and heparin-binding interfaces."
      Hecht H.J., Adar R., Hofmann B., Bogin O., Weich H., Yayon A.
      Acta Crystallogr. D 57:378-384(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), SUBUNIT, HEPARIN-BINDING.
    12. "Crystal structure of fibroblast growth factor 9 reveals regions implicated in dimerization and autoinhibition."
      Plotnikov A.N., Eliseenkova A.V., Ibrahimi O.A., Shriver Z., Sasisekharan R., Lemmon M.A., Mohammadi M.
      J. Biol. Chem. 276:4322-4329(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 35-208, SUBUNIT.
    13. Cited for: VARIANT SYNS3 ASN-99, CHARACTERIZATION OF VARIANT SYNS3 ASN-99.

    Entry informationi

    Entry nameiFGF9_HUMAN
    AccessioniPrimary (citable) accession number: P31371
    Secondary accession number(s): A8K427, Q3SY32
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 155 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

    Biochemical analysis of the Asn-99 mutation reveals a significantly impaired FGF signaling, as evidenced by diminished activity of the MAPK1/MAPK2 pathway and decreases CTNNB1 and MYC expression when compared with wild-type protein. Binding of mutant protein to the receptor FGFR3 is severely impaired, although homodimerization of mutant to itself or wild-type is not detectably affected, providing a basis for the observed defective FGF9 signaling.

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 13
      Human chromosome 13: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi