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P54130

- FGF9_MOUSE

UniProt

P54130 - FGF9_MOUSE

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Protein
Fibroblast growth factor 9
Gene
Fgf9, Fgf-9
Organism
Mus musculus (Mouse)
Status
Reviewed - 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. fibroblast growth factor receptor signaling pathway Source: MGI
  10. inner ear morphogenesis Source: MGI
  11. lung development Source: MGI
  12. lung-associated mesenchyme development Source: MGI
  13. male gonad development Source: MGI
  14. male sex determination Source: MGI
  15. negative regulation of Wnt signaling pathway Source: MGI
  16. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  17. osteoblast differentiation Source: MGI
  18. positive regulation of MAPK cascade Source: Ensembl
  19. positive regulation of canonical Wnt signaling pathway Source: MGI
  20. positive regulation of cardiac muscle cell proliferation Source: DFLAT
  21. positive regulation of cell division Source: UniProtKB-KW
  22. positive regulation of cell proliferation Source: MGI
  23. positive regulation of epithelial cell proliferation Source: MGI
  24. positive regulation of gene expression Source: MGI
  25. positive regulation of mesenchymal cell proliferation Source: MGI
  26. positive regulation of smoothened signaling pathway Source: MGI
  27. positive regulation of transcription, DNA-templated Source: DFLAT
  28. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: MGI
  29. protein import into nucleus Source: MGI
  30. regulation of timing of cell differentiation Source: MGI
  31. 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_196455. Signaling by FGFR mutants.
REACT_196505. Signaling by FGFR3 mutants.
REACT_196507. Signaling by activated point mutants of FGFR3.
REACT_196536. Activated point mutants of FGFR2.
REACT_196538. Signaling by activated point mutants of FGFR1.
REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_198525. Negative regulation of FGFR signaling.
REACT_206694. FGFR4 ligand binding and activation.
REACT_206745. FGFR2c ligand binding and activation.
REACT_213224. FGFR3b ligand binding and activation.
REACT_220750. FGFR3c ligand binding and activation.
REACT_223993. PI-3K cascade.
REACT_225874. FGFR1c ligand binding and activation.
REACT_226341. PIP3 activates AKT signaling.
REACT_94437. SHC-mediated cascade.

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: 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: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 33 By similarity
PRO_0000008975
Chaini4 – 208205Fibroblast growth factor 9
PRO_0000008976Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiP54130.

PTM databases

PhosphoSiteiP54130.

Expressioni

Gene expression databases

ArrayExpressiP54130.
CleanExiMM_FGF9.
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.

Protein-protein interaction databases

DIPiDIP-6032N.

Structurei

3D structure databases

ProteinModelPortaliP54130.
SMRiP54130. Positions 52-208.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG269410.
GeneTreeiENSGT00730000110261.
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.
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]

Sequencei

Sequence statusi: Complete.

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

P54130-1 [UniParc]FASTAAdd to Basket

« Hide

MAPLGEVGSY 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):23,414
Last modified:October 3, 2012 - v2
Checksum:i4A3CE894DFF643EB
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341S → N in AAC52529. 1 Publication
Sequence conflicti34 – 341S → N in AAD49222. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS27164.1.
RefSeqi NP_038546.2. NM_013518.4.
UniGenei Mm.8846.

3D structure databases

ProteinModelPortali P54130.
SMRi P54130. Positions 52-208.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6032N.

PTM databases

PhosphoSitei P54130.

Proteomic databases

PRIDEi P54130.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022545 ; ENSMUSP00000022545 ; ENSMUSG00000021974 .
GeneIDi 14180.
KEGGi mmu:14180.
UCSCi uc007udx.2. mouse.

Organism-specific databases

CTDi 2254.
MGIi MGI:104723. Fgf9.

Phylogenomic databases

eggNOGi NOG269410.
GeneTreei ENSGT00730000110261.
HOGENOMi HOG000236341.
HOVERGENi HBG007580.
InParanoidi P54130.
KOi K04358.
OMAi GELYGSD.
OrthoDBi EOG7992S1.
TreeFami TF317805.

Enzyme and pathway databases

Reactomei REACT_196455. Signaling by FGFR mutants.
REACT_196505. Signaling by FGFR3 mutants.
REACT_196507. Signaling by activated point mutants of FGFR3.
REACT_196536. Activated point mutants of FGFR2.
REACT_196538. Signaling by activated point mutants of FGFR1.
REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_198525. Negative regulation of FGFR signaling.
REACT_206694. FGFR4 ligand binding and activation.
REACT_206745. FGFR2c ligand binding and activation.
REACT_213224. FGFR3b ligand binding and activation.
REACT_220750. FGFR3c ligand binding and activation.
REACT_223993. PI-3K cascade.
REACT_225874. FGFR1c ligand binding and activation.
REACT_226341. PIP3 activates AKT signaling.
REACT_94437. SHC-mediated cascade.

Miscellaneous databases

NextBioi 285370.
PROi P54130.
SOURCEi Search...

Gene expression databases

ArrayExpressi P54130.
CleanExi MM_FGF9.
Genevestigatori P54130.

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

« 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: September 3, 2014
This is version 109 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