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Protein

Fibroblast growth factor 9

Gene

FGF9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • growth factor activity Source: ProtInc
  • heparin binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Growth factor, Mitogen

Keywords - Biological processi

Differentiation

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_110235. Phospholipase C-mediated cascade: FGFR1.
REACT_120863. Activated point mutants of FGFR2.
REACT_121153. Signaling by activated point mutants of FGFR1.
REACT_121249. FGFR3 mutant receptor activation.
REACT_121337. Signaling by activated point mutants of FGFR3.
REACT_147727. Constitutive Signaling by Aberrant PI3K in Cancer.
REACT_355069. FRS-mediated FGFR2 signaling.
REACT_355144. Negative regulation of FGFR3 signaling.
REACT_355146. Phospholipase C-mediated cascade, FGFR2.
REACT_355159. SHC-mediated cascade:FGFR4.
REACT_355160. PI-3K cascade:FGFR3.
REACT_355194. SHC-mediated cascade:FGFR1.
REACT_355197. SHC-mediated cascade:FGFR3.
REACT_355202. Signaling by FGFR4 mutants.
REACT_355212. FRS-mediated FGFR3 signaling.
REACT_355216. Phospholipase C-mediated cascade, FGFR4.
REACT_355218. Negative regulation of FGFR1 signaling.
REACT_355221. Signaling by FGFR1 mutants.
REACT_355225. SHC-mediated cascade:FGFR2.
REACT_355227. Negative regulation of FGFR2 signaling.
REACT_355304. PI-3K cascade:FGFR4.
REACT_355313. Signaling by FGFR3 mutants.
REACT_355450. PI-3K cascade:FGFR2.
REACT_355511. Signaling by FGFR2 mutants.
REACT_355514. Phospholipase C-mediated cascade, FGFR3.
REACT_355552. PI-3K cascade:FGFR1.
REACT_355580. FRS2-mediated FGFR4 signaling.
REACT_355584. FRS-mediated FGFR1 signaling.
REACT_355588. Negative regulation of FGFR4 signaling.
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 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:3687. FGF9.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: Ensembl
  • cytoplasm Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Multiple synostoses syndrome 3 (SYNS3)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:612961
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.

Polymorphism and mutation databases

BioMutaiFGF9.
DMDMi544290.

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.
GenevisibleiP31371. HS.

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 – 608Combined sources
Beta strandi63 – 686Combined sources
Beta strandi73 – 764Combined sources
Beta strandi82 – 876Combined sources
Helixi91 – 933Combined sources
Beta strandi95 – 1017Combined sources
Beta strandi104 – 1096Combined sources
Turni110 – 1123Combined sources
Beta strandi115 – 1184Combined sources
Beta strandi124 – 1296Combined sources
Helixi132 – 1343Combined sources
Beta strandi136 – 1427Combined sources
Beta strandi145 – 15410Combined sources
Turni156 – 1583Combined sources
Beta strandi161 – 1633Combined sources
Helixi175 – 1773Combined sources
Helixi183 – 1853Combined sources
Beta strandi187 – 1904Combined sources
Helixi194 – 1963Combined sources
Helixi200 – 2034Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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:
EMBLi
GenBanki
DDBJi
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.

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiP31371.

Polymorphism and mutation databases

BioMutaiFGF9.
DMDMi544290.

Proteomic databases

PaxDbiP31371.
PRIDEiP31371.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2254.
GeneCardsiGC13P022245.
HGNCiHGNC:3687. FGF9.
HPAiCAB004392.
MIMi600921. gene.
612961. phenotype.
neXtProtiNX_P31371.
Orphaneti3237. Multiple synostoses syndrome.
PharmGKBiPA28126.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG269410.
GeneTreeiENSGT00760000118859.
HOGENOMiHOG000236341.
HOVERGENiHBG007580.
InParanoidiP31371.
KOiK04358.
OMAiGELYGSD.
OrthoDBiEOG7992S1.
PhylomeDBiP31371.
TreeFamiTF317805.

Enzyme and pathway databases

ReactomeiREACT_110235. Phospholipase C-mediated cascade: FGFR1.
REACT_120863. Activated point mutants of FGFR2.
REACT_121153. Signaling by activated point mutants of FGFR1.
REACT_121249. FGFR3 mutant receptor activation.
REACT_121337. Signaling by activated point mutants of FGFR3.
REACT_147727. Constitutive Signaling by Aberrant PI3K in Cancer.
REACT_355069. FRS-mediated FGFR2 signaling.
REACT_355144. Negative regulation of FGFR3 signaling.
REACT_355146. Phospholipase C-mediated cascade, FGFR2.
REACT_355159. SHC-mediated cascade:FGFR4.
REACT_355160. PI-3K cascade:FGFR3.
REACT_355194. SHC-mediated cascade:FGFR1.
REACT_355197. SHC-mediated cascade:FGFR3.
REACT_355202. Signaling by FGFR4 mutants.
REACT_355212. FRS-mediated FGFR3 signaling.
REACT_355216. Phospholipase C-mediated cascade, FGFR4.
REACT_355218. Negative regulation of FGFR1 signaling.
REACT_355221. Signaling by FGFR1 mutants.
REACT_355225. SHC-mediated cascade:FGFR2.
REACT_355227. Negative regulation of FGFR2 signaling.
REACT_355304. PI-3K cascade:FGFR4.
REACT_355313. Signaling by FGFR3 mutants.
REACT_355450. PI-3K cascade:FGFR2.
REACT_355511. Signaling by FGFR2 mutants.
REACT_355514. Phospholipase C-mediated cascade, FGFR3.
REACT_355552. PI-3K cascade:FGFR1.
REACT_355580. FRS2-mediated FGFR4 signaling.
REACT_355584. FRS-mediated FGFR1 signaling.
REACT_355588. Negative regulation of FGFR4 signaling.
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.

Miscellaneous databases

EvolutionaryTraceiP31371.
GeneWikiiFGF9.
GenomeRNAii2254.
NextBioi9131.
PROiP31371.
SOURCEiSearch...

Gene expression databases

BgeeiP31371.
CleanExiHS_FGF9.
GenevisibleiP31371. HS.

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]
ProtoNetiSearch...

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: June 24, 2015
This is version 163 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.