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Protein

Fibroblast growth factor 9

Gene

Fgf9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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.

GO - Molecular functioni

  1. heparin binding Source: UniProtKB-KW

GO - Biological processi

  1. angiogenesis Source: MGI
  2. cardiac left ventricle morphogenesis Source: DFLAT
  3. cardiac ventricle development Source: DFLAT
  4. cell-cell signaling Source: MGI
  5. chondrocyte differentiation Source: MGI
  6. embryonic digestive tract development Source: MGI
  7. embryonic limb morphogenesis Source: MGI
  8. embryonic skeletal system development Source: MGI
  9. eye development Source: CACAO
  10. fibroblast growth factor receptor signaling pathway Source: MGI
  11. inner ear morphogenesis Source: MGI
  12. lung-associated mesenchyme development Source: MGI
  13. lung development Source: MGI
  14. male gonad development Source: MGI
  15. male sex determination Source: MGI
  16. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  17. negative regulation of Wnt signaling pathway Source: MGI
  18. osteoblast differentiation Source: MGI
  19. positive regulation of activin receptor signaling pathway Source: MGI
  20. positive regulation of canonical Wnt signaling pathway Source: MGI
  21. positive regulation of cardiac muscle cell proliferation Source: DFLAT
  22. positive regulation of cell division Source: UniProtKB-KW
  23. positive regulation of cell proliferation Source: MGI
  24. positive regulation of epithelial cell proliferation Source: MGI
  25. positive regulation of gene expression Source: MGI
  26. positive regulation of MAPK cascade Source: MGI
  27. positive regulation of mesenchymal cell proliferation Source: MGI
  28. positive regulation of smoothened signaling pathway Source: MGI
  29. positive regulation of transcription, DNA-templated Source: DFLAT
  30. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: MGI
  31. protein import into nucleus Source: MGI
  32. regulation of timing of cell differentiation Source: MGI
  33. substantia nigra development Source: Ensembl
  34. vasculogenesis involved in coronary vascular morphogenesis Source: DFLAT
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Growth factor, Mitogen

Keywords - Biological processi

Differentiation

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_275126. Signaling by activated point mutants of FGFR3.
REACT_276236. FGFR4 ligand binding and activation.
REACT_312401. FGFR2c ligand binding and activation.
REACT_317910. FGFR3b ligand binding and activation.
REACT_321421. SHC-mediated cascade.
REACT_323826. Phospholipase C-mediated cascade.
REACT_326306. Signaling by FGFR mutants.
REACT_328674. Constitutive PI3K/AKT Signaling in Cancer.
REACT_332023. Negative regulation of FGFR signaling.
REACT_332809. FRS2-mediated cascade.
REACT_332866. PI3K Cascade.
REACT_333335. FGFR3c ligand binding and activation.
REACT_333474. PIP3 activates AKT signaling.
REACT_334662. PI-3K cascade.
REACT_338705. Signaling by FGFR3 mutants.
REACT_345290. Signaling by activated point mutants of FGFR1.
REACT_349060. Activated point mutants of FGFR2.
REACT_354830. FGFR1c ligand binding and activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibroblast growth factor 9
Short name:
FGF-9
Alternative name(s):
Glia-activating factor
Short name:
GAF
HBGF-9
Gene namesi
Name:Fgf9
Synonyms:Fgf-9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:104723. Fgf9.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: Ensembl
  2. cytoplasm Source: Ensembl
  3. extracellular space Source: MGI
  4. extracellular vesicular exosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 33By similarityPRO_0000008975
Chaini4 – 208205Fibroblast growth factor 9PRO_0000008976Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiP54130.

PTM databases

PhosphoSiteiP54130.

Expressioni

Gene expression databases

CleanExiMM_FGF9.
ExpressionAtlasiP54130. baseline and differential.
GenevestigatoriP54130.

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 (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-6032N.

Structurei

3D structure databases

ProteinModelPortaliP54130.
SMRiP54130. Positions 52-208.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG269410.
GeneTreeiENSGT00760000118859.
HOGENOMiHOG000236341.
HOVERGENiHBG007580.
InParanoidiP54130.
KOiK04358.
OMAiGELYGSD.
OrthoDBiEOG7992S1.
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.

P54130-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPLGEVGSY 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):23,414
Last modified:October 3, 2012 - v2
Checksum:i4A3CE894DFF643EB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341S → N in AAC52529 (PubMed:8576175).Curated
Sequence conflicti34 – 341S → N in AAD49222 (PubMed:10474167).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33535 mRNA. Translation: AAC52529.1.
D38258 mRNA. Translation: BAA07410.1.
S82023 mRNA. Translation: AAB36429.1.
AF144626, AF144624, AF144625 Genomic DNA. Translation: AAD49222.1.
AK158782 mRNA. Translation: BAE34661.1.
AC125399 Genomic DNA. No translation available.
AC154202 Genomic DNA. No translation available.
CH466535 Genomic DNA. Translation: EDL36153.1.
BC099872 mRNA. Translation: AAH99872.1.
BC099873 mRNA. Translation: AAH99873.1.
BC099874 mRNA. Translation: AAH99874.1.
BC099875 mRNA. Translation: AAH99875.1.
BC125237 mRNA. Translation: AAI25238.1.
CCDSiCCDS27164.1.
RefSeqiNP_038546.2. NM_013518.4.
UniGeneiMm.8846.

Genome annotation databases

EnsembliENSMUST00000022545; ENSMUSP00000022545; ENSMUSG00000021974.
GeneIDi14180.
KEGGimmu:14180.
UCSCiuc007udx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33535 mRNA. Translation: AAC52529.1.
D38258 mRNA. Translation: BAA07410.1.
S82023 mRNA. Translation: AAB36429.1.
AF144626, AF144624, AF144625 Genomic DNA. Translation: AAD49222.1.
AK158782 mRNA. Translation: BAE34661.1.
AC125399 Genomic DNA. No translation available.
AC154202 Genomic DNA. No translation available.
CH466535 Genomic DNA. Translation: EDL36153.1.
BC099872 mRNA. Translation: AAH99872.1.
BC099873 mRNA. Translation: AAH99873.1.
BC099874 mRNA. Translation: AAH99874.1.
BC099875 mRNA. Translation: AAH99875.1.
BC125237 mRNA. Translation: AAI25238.1.
CCDSiCCDS27164.1.
RefSeqiNP_038546.2. NM_013518.4.
UniGeneiMm.8846.

3D structure databases

ProteinModelPortaliP54130.
SMRiP54130. Positions 52-208.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6032N.

PTM databases

PhosphoSiteiP54130.

Proteomic databases

PRIDEiP54130.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022545; ENSMUSP00000022545; ENSMUSG00000021974.
GeneIDi14180.
KEGGimmu:14180.
UCSCiuc007udx.2. mouse.

Organism-specific databases

CTDi2254.
MGIiMGI:104723. Fgf9.

Phylogenomic databases

eggNOGiNOG269410.
GeneTreeiENSGT00760000118859.
HOGENOMiHOG000236341.
HOVERGENiHBG007580.
InParanoidiP54130.
KOiK04358.
OMAiGELYGSD.
OrthoDBiEOG7992S1.
TreeFamiTF317805.

Enzyme and pathway databases

ReactomeiREACT_275126. Signaling by activated point mutants of FGFR3.
REACT_276236. FGFR4 ligand binding and activation.
REACT_312401. FGFR2c ligand binding and activation.
REACT_317910. FGFR3b ligand binding and activation.
REACT_321421. SHC-mediated cascade.
REACT_323826. Phospholipase C-mediated cascade.
REACT_326306. Signaling by FGFR mutants.
REACT_328674. Constitutive PI3K/AKT Signaling in Cancer.
REACT_332023. Negative regulation of FGFR signaling.
REACT_332809. FRS2-mediated cascade.
REACT_332866. PI3K Cascade.
REACT_333335. FGFR3c ligand binding and activation.
REACT_333474. PIP3 activates AKT signaling.
REACT_334662. PI-3K cascade.
REACT_338705. Signaling by FGFR3 mutants.
REACT_345290. Signaling by activated point mutants of FGFR1.
REACT_349060. Activated point mutants of FGFR2.
REACT_354830. FGFR1c ligand binding and activation.

Miscellaneous databases

NextBioi285370.
PROiP54130.
SOURCEiSearch...

Gene expression databases

CleanExiMM_FGF9.
ExpressionAtlasiP54130. baseline and differential.
GenevestigatoriP54130.

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. "Expression and biological activity of mouse fibroblast growth factor-9."
    Santos-Ocampo S., Colvin J.S., Chellaiah A.T., Ornitz D.M.
    J. Biol. Chem. 271:1726-1731(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: FVB.
  2. "Retinoic acid induces gene expression of fibroblast growth factor-9 during induction of neuronal differentiation of mouse embryonal carcinoma P19 cells."
    Seo M., Noguchi K.
    FEBS Lett. 370:231-235(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Identification of fibroblast growth factor 9 (FGF9) as a high affinity, heparin dependent ligand for FGF receptors 3 and 2 but not for FGF receptors 1 and 4."
    Hecht D., Zimmerman N., Bedford M., Avivi A., Yayon A.
    Growth Factors 12:223-233(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Genomic organization and embryonic expression of the mouse fibroblast growth factor 9 gene."
    Colvin J.S., Feldman B., Nadeau J.H., Goldfarb M., Ornitz D.M.
    Dev. Dyn. 216:72-88(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Visual cortex.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  7. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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].

Entry informationi

Entry nameiFGF9_MOUSE
AccessioniPrimary (citable) accession number: P54130
Secondary accession number(s): Q499I9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 3, 2012
Last modified: April 29, 2015
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.