FGF9_HUMAN
ID FGF9_HUMAN Reviewed; 208 AA.
AC P31371; A8K427; Q3SY32;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 3.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Fibroblast growth factor 9;
DE Short=FGF-9;
DE AltName: Full=Glia-activating factor;
DE Short=GAF;
DE AltName: Full=Heparin-binding growth factor 9;
DE Short=HBGF-9;
DE Flags: Precursor;
GN Name=FGF9;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Foreskin;
RX PubMed=8321227; DOI=10.1128/mcb.13.7.4251-4259.1993;
RA Miyamoto M., Naruo K., Seko C., Matsumoto S., Kondo T., Kurokawa T.;
RT "Molecular cloning of a novel cytokine cDNA encoding the ninth member of
RT the fibroblast growth factor family, which has a unique secretion
RT property.";
RL Mol. Cell. Biol. 13:4251-4259(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-94.
RG NIEHS SNPs program;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 4-26 AND 34-54.
RC TISSUE=Glial tumor;
RX PubMed=8428960; DOI=10.1016/s0021-9258(18)53852-7;
RA Naruo K., Seko C., Kuroshima K., Matsutani E., Sasada R., Kondo T.,
RA Kurokawa T.;
RT "Novel secretory heparin-binding factors from human glioma cells (glia-
RT activating factors) involved in glial cell growth. Purification and
RT biological properties.";
RL J. Biol. Chem. 268:2857-2864(1993).
RN [8]
RP INTERACTION WITH FGFR2 AND FGFR3, AND FUNCTION IN CELL PROLIFERATION.
RX PubMed=8663044; DOI=10.1074/jbc.271.25.15292;
RA Ornitz D.M., Xu J., Colvin J.S., McEwen D.G., MacArthur C.A., Coulier F.,
RA Gao G., Goldfarb M.;
RT "Receptor specificity of the fibroblast growth factor family.";
RL J. Biol. Chem. 271:15292-15297(1996).
RN [9]
RP INTERACTION WITH FGFR1; FGFR2; FGFR3 AND FGFR4, AND FUNCTION IN STIMULATION
RP OF CELL PROLIFERATION.
RX PubMed=16597617; DOI=10.1074/jbc.m601252200;
RA Zhang X., Ibrahimi O.A., Olsen S.K., Umemori H., Mohammadi M., Ornitz D.M.;
RT "Receptor specificity of the fibroblast growth factor family. The complete
RT mammalian FGF family.";
RL J. Biol. Chem. 281:15694-15700(2006).
RN [10]
RP REVIEW.
RX PubMed=20094046; DOI=10.1038/nrc2780;
RA Turner N., Grose R.;
RT "Fibroblast growth factor signalling: from development to cancer.";
RL Nat. Rev. Cancer 10:116-129(2010).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), SUBUNIT, AND HEPARIN-BINDING.
RX PubMed=11223514; DOI=10.1107/s0907444900020813;
RA Hecht H.J., Adar R., Hofmann B., Bogin O., Weich H., Yayon A.;
RT "Structure of fibroblast growth factor 9 shows a symmetric dimer with
RT unique receptor- and heparin-binding interfaces.";
RL Acta Crystallogr. D 57:378-384(2001).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 35-208, AND SUBUNIT.
RX PubMed=11060292; DOI=10.1074/jbc.m006502200;
RA Plotnikov A.N., Eliseenkova A.V., Ibrahimi O.A., Shriver Z.,
RA Sasisekharan R., Lemmon M.A., Mohammadi M.;
RT "Crystal structure of fibroblast growth factor 9 reveals regions implicated
RT in dimerization and autoinhibition.";
RL J. Biol. Chem. 276:4322-4329(2001).
RN [13]
RP VARIANT SYNS3 ASN-99, AND CHARACTERIZATION OF VARIANT SYNS3 ASN-99.
RX PubMed=19589401; DOI=10.1016/j.ajhg.2009.06.007;
RA Wu X.L., Gu M.M., Huang L., Liu X.S., Zhang H.X., Ding X.Y., Xu J.Q.,
RA Cui B., Wang L., Lu S.Y., Chen X.Y., Zhang H.G., Huang W., Yuan W.T.,
RA Yang J.M., Gu Q., Fei J., Chen Z., Yuan Z.M., Wang Z.G.;
RT "Multiple synostoses syndrome is due to a missense mutation in exon 2 of
RT FGF9 gene.";
RL Am. J. Hum. Genet. 85:53-63(2009).
CC -!- FUNCTION: Plays an important role in the regulation of embryonic
CC development, cell proliferation, cell differentiation and cell
CC migration. May have a role in glial cell growth and differentiation
CC during development, gliosis during repair and regeneration of brain
CC tissue after damage, differentiation and survival of neuronal cells,
CC and growth stimulation of glial tumors. {ECO:0000269|PubMed:16597617,
CC ECO:0000269|PubMed:8663044}.
CC -!- SUBUNIT: Monomer. Homodimer. Interacts with FGFR1, FGFR2, FGFR3 and
CC FGFR4. Affinity between fibroblast growth factors (FGFs) and their
CC receptors is increased by heparan sulfate glycosaminoglycans that
CC function as coreceptors. {ECO:0000269|PubMed:11060292,
CC ECO:0000269|PubMed:11223514, ECO:0000269|PubMed:16597617,
CC ECO:0000269|PubMed:8663044}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Glial cells.
CC -!- PTM: Three molecular species were found (30 kDa, 29 kDa and 25 kDa),
CC cleaved at Leu-4, Val-13 and Ser-34 respectively. The smaller ones
CC might be products of proteolytic digestion. Furthermore, there may be a
CC functional signal sequence in the 30 kDa species which is uncleavable
CC in the secretion step.
CC -!- PTM: N-glycosylated.
CC -!- DISEASE: Multiple synostoses syndrome 3 (SYNS3) [MIM:612961]: A bone
CC disease characterized by multiple progressive joint fusions that
CC commonly involve proximal interphalangeal, tarsal-carpal, humeroradial
CC and cervical spine joints. Additional features can include progressive
CC conductive deafness and facial dysmorphism.
CC {ECO:0000269|PubMed:19589401}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Biochemical analysis of the Asn-99 mutation reveals a
CC significantly impaired FGF signaling, as evidenced by diminished
CC activity of the MAPK1/MAPK2 pathway and decreases CTNNB1 and MYC
CC expression when compared with wild-type protein. Binding of mutant
CC protein to the receptor FGFR3 is severely impaired, although
CC homodimerization of mutant to itself or wild-type is not detectably
CC affected, providing a basis for the observed defective FGF9 signaling.
CC -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/fgf9/";
CC ---------------------------------------------------------------------------
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DR EMBL; D14838; BAA03572.1; -; mRNA.
DR EMBL; AY682094; AAT74624.1; -; Genomic_DNA.
DR EMBL; AK290792; BAF83481.1; -; mRNA.
DR EMBL; AL139378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08316.1; -; Genomic_DNA.
DR EMBL; BC069692; AAH69692.1; -; mRNA.
DR EMBL; BC103978; AAI03979.1; -; mRNA.
DR EMBL; BC103979; AAI03980.1; -; mRNA.
DR CCDS; CCDS9298.1; -.
DR PIR; A48137; A48137.
DR RefSeq; NP_002001.1; NM_002010.2.
DR PDB; 1G82; X-ray; 2.60 A; A/B/C/D=49-208.
DR PDB; 1IHK; X-ray; 2.20 A; A=35-208.
DR PDB; 5W59; X-ray; 2.50 A; A=35-208.
DR PDBsum; 1G82; -.
DR PDBsum; 1IHK; -.
DR PDBsum; 5W59; -.
DR AlphaFoldDB; P31371; -.
DR SMR; P31371; -.
DR BioGRID; 108545; 14.
DR DIP; DIP-6036N; -.
DR IntAct; P31371; 11.
DR STRING; 9606.ENSP00000371790; -.
DR GlyGen; P31371; 1 site.
DR iPTMnet; P31371; -.
DR PhosphoSitePlus; P31371; -.
DR BioMuta; FGF9; -.
DR DMDM; 544290; -.
DR MassIVE; P31371; -.
DR PaxDb; P31371; -.
DR PeptideAtlas; P31371; -.
DR PRIDE; P31371; -.
DR ProteomicsDB; 54786; -.
DR Antibodypedia; 3827; 412 antibodies from 34 providers.
DR DNASU; 2254; -.
DR Ensembl; ENST00000382353.6; ENSP00000371790.5; ENSG00000102678.7.
DR GeneID; 2254; -.
DR KEGG; hsa:2254; -.
DR MANE-Select; ENST00000382353.6; ENSP00000371790.5; NM_002010.3; NP_002001.1.
DR UCSC; uc001uog.3; human.
DR CTD; 2254; -.
DR DisGeNET; 2254; -.
DR GeneCards; FGF9; -.
DR HGNC; HGNC:3687; FGF9.
DR HPA; ENSG00000102678; Tissue enhanced (brain, kidney, retina).
DR MalaCards; FGF9; -.
DR MIM; 600921; gene.
DR MIM; 612961; phenotype.
DR neXtProt; NX_P31371; -.
DR OpenTargets; ENSG00000102678; -.
DR Orphanet; 3237; Multiple synostoses syndrome.
DR PharmGKB; PA28126; -.
DR VEuPathDB; HostDB:ENSG00000102678; -.
DR eggNOG; KOG3885; Eukaryota.
DR GeneTree; ENSGT00940000160956; -.
DR HOGENOM; CLU_081609_0_0_1; -.
DR InParanoid; P31371; -.
DR OMA; FFWIYLS; -.
DR OrthoDB; 1097566at2759; -.
DR PhylomeDB; P31371; -.
DR TreeFam; TF317805; -.
DR PathwayCommons; P31371; -.
DR Reactome; R-HSA-109704; PI3K Cascade.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-1839122; Signaling by activated point mutants of FGFR1.
DR Reactome; R-HSA-1839130; Signaling by activated point mutants of FGFR3.
DR Reactome; R-HSA-190322; FGFR4 ligand binding and activation.
DR Reactome; R-HSA-190371; FGFR3b ligand binding and activation.
DR Reactome; R-HSA-190372; FGFR3c ligand binding and activation.
DR Reactome; R-HSA-190373; FGFR1c ligand binding and activation.
DR Reactome; R-HSA-190375; FGFR2c ligand binding and activation.
DR Reactome; R-HSA-2033519; Activated point mutants of FGFR2.
DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR Reactome; R-HSA-5654219; Phospholipase C-mediated cascade: FGFR1.
DR Reactome; R-HSA-5654221; Phospholipase C-mediated cascade, FGFR2.
DR Reactome; R-HSA-5654227; Phospholipase C-mediated cascade, FGFR3.
DR Reactome; R-HSA-5654228; Phospholipase C-mediated cascade, FGFR4.
DR Reactome; R-HSA-5654687; Downstream signaling of activated FGFR1.
DR Reactome; R-HSA-5654688; SHC-mediated cascade:FGFR1.
DR Reactome; R-HSA-5654689; PI-3K cascade:FGFR1.
DR Reactome; R-HSA-5654693; FRS-mediated FGFR1 signaling.
DR Reactome; R-HSA-5654695; PI-3K cascade:FGFR2.
DR Reactome; R-HSA-5654699; SHC-mediated cascade:FGFR2.
DR Reactome; R-HSA-5654700; FRS-mediated FGFR2 signaling.
DR Reactome; R-HSA-5654704; SHC-mediated cascade:FGFR3.
DR Reactome; R-HSA-5654706; FRS-mediated FGFR3 signaling.
DR Reactome; R-HSA-5654710; PI-3K cascade:FGFR3.
DR Reactome; R-HSA-5654712; FRS-mediated FGFR4 signaling.
DR Reactome; R-HSA-5654719; SHC-mediated cascade:FGFR4.
DR Reactome; R-HSA-5654720; PI-3K cascade:FGFR4.
DR Reactome; R-HSA-5654726; Negative regulation of FGFR1 signaling.
DR Reactome; R-HSA-5654727; Negative regulation of FGFR2 signaling.
DR Reactome; R-HSA-5654732; Negative regulation of FGFR3 signaling.
DR Reactome; R-HSA-5654733; Negative regulation of FGFR4 signaling.
DR Reactome; R-HSA-5655253; Signaling by FGFR2 in disease.
DR Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
DR Reactome; R-HSA-5655332; Signaling by FGFR3 in disease.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-HSA-9690406; Transcriptional regulation of testis differentiation.
DR SignaLink; P31371; -.
DR SIGNOR; P31371; -.
DR BioGRID-ORCS; 2254; 6 hits in 1071 CRISPR screens.
DR EvolutionaryTrace; P31371; -.
DR GeneWiki; FGF9; -.
DR GenomeRNAi; 2254; -.
DR Pharos; P31371; Tbio.
DR PRO; PR:P31371; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; P31371; protein.
DR Bgee; ENSG00000102678; Expressed in secondary oocyte and 164 other tissues.
DR Genevisible; P31371; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005104; F:fibroblast growth factor receptor binding; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0032924; P:activin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0048566; P:embryonic digestive tract development; IEA:Ensembl.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IEA:Ensembl.
DR GO; GO:0048706; P:embryonic skeletal system development; IEA:Ensembl.
DR GO; GO:0001654; P:eye development; IEA:Ensembl.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IGI:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IBA:GO_Central.
DR GO; GO:0060484; P:lung-associated mesenchyme development; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEP:UniProtKB.
DR GO; GO:0030238; P:male sex determination; IEA:Ensembl.
DR GO; GO:0010463; P:mesenchymal cell proliferation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:1905931; P:negative regulation of vascular associated smooth muscle cell differentiation involved in phenotypic switching; ISS:BHF-UCL.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IBA:GO_Central.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:2000243; P:positive regulation of reproductive process; IEA:Ensembl.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IEA:Ensembl.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; ISS:BHF-UCL.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IGI:BHF-UCL.
DR GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR GO; GO:0048505; P:regulation of timing of cell differentiation; IEA:Ensembl.
DR GO; GO:0060011; P:Sertoli cell proliferation; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IEA:Ensembl.
DR CDD; cd00058; FGF; 1.
DR InterPro; IPR028251; FGF9.
DR InterPro; IPR002209; Fibroblast_GF_fam.
DR InterPro; IPR008996; IL1/FGF.
DR PANTHER; PTHR11486; PTHR11486; 1.
DR PANTHER; PTHR11486:SF28; PTHR11486:SF28; 1.
DR Pfam; PF00167; FGF; 1.
DR PRINTS; PR00263; HBGFFGF.
DR SMART; SM00442; FGF; 1.
DR SUPFAM; SSF50353; SSF50353; 1.
DR PROSITE; PS00247; HBGF_FGF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Deafness; Developmental protein; Differentiation;
KW Direct protein sequencing; Disease variant; Glycoprotein; Growth factor;
KW Heparin-binding; Mitogen; Reference proteome; Secreted.
FT PROPEP 1..3
FT /evidence="ECO:0000269|PubMed:8428960"
FT /id="PRO_0000008973"
FT CHAIN 4..208
FT /note="Fibroblast growth factor 9"
FT /id="PRO_0000008974"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT VARIANT 94
FT /note="I -> V (in dbSNP:rs12427696)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_020944"
FT VARIANT 99
FT /note="S -> N (in SYNS3; expressed and secreted as
FT efficiently as wild-type; however it induces compromised
FT chondrocyte proliferation and differentiation accompanied
FT by enhanced osteogenic differentiation and matrix
FT mineralization of bone marrow-derived mesenchymal stem
FT cells; dbSNP:rs121918322)"
FT /evidence="ECO:0000269|PubMed:19589401"
FT /id="VAR_063254"
FT CONFLICT 24..26
FT /note="VLP -> SLL (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="S -> A (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:1IHK"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:1IHK"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:5W59"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:1IHK"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:1IHK"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1IHK"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:1IHK"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:1IHK"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:1IHK"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:1IHK"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:1IHK"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1IHK"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:1IHK"
FT STRAND 145..154
FT /evidence="ECO:0007829|PDB:1IHK"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:1IHK"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1IHK"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1IHK"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:1IHK"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:1IHK"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:1IHK"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:1IHK"
SQ SEQUENCE 208 AA; 23441 MW; F32A0E7106EF59C9 CRC64;
MAPLGEVGNY FGVQDAVPFG NVPVLPVDSP VLLSDHLGQS EAGGLPRGPA VTDLDHLKGI
LRRRQLYCRT GFHLEIFPNG TIQGTRKDHS RFGILEFISI AVGLVSIRGV DSGLYLGMNE
KGELYGSEKL TQECVFREQF EENWYNTYSS NLYKHVDTGR RYYVALNKDG TPREGTRTKR
HQKFTHFLPR PVDPDKVPEL YKDILSQS
