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P31371

- FGF9_HUMAN

UniProt

P31371 - FGF9_HUMAN

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Protein

Fibroblast growth factor 9

Gene

FGF9

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

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
Complete GO annotation...

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
ProteomesiUP000005640: Chromosome 13

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
Complete GO annotation...

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.
GeneTreeiENSGT00760000118859.
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.
PRINTSiPR00263. HBGFFGF.
PR00262. IL1HBGF.
SMARTiSM00442. FGF. 1 hit.
[Graphical view]
SUPFAMiSSF50353. SSF50353. 1 hit.
PROSITEiPS00247. HBGF_FGF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P31371-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPLGEVGNY FGVQDAVPFG NVPVLPVDSP VLLSDHLGQS EAGGLPRGPA
60 70 80 90 100
VTDLDHLKGI LRRRQLYCRT GFHLEIFPNG TIQGTRKDHS RFGILEFISI
110 120 130 140 150
AVGLVSIRGV DSGLYLGMNE KGELYGSEKL TQECVFREQF EENWYNTYSS
160 170 180 190 200
NLYKHVDTGR RYYVALNKDG TPREGTRTKR HQKFTHFLPR PVDPDKVPEL

YKDILSQS
Length:208
Mass (Da):23,441
Last modified:October 1, 1994 - v3
Checksum:iF32A0E7106EF59C9
GO

Experimental Info

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

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 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.
GeneTreei ENSGT00760000118859.
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.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 156 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