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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

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

BioCyciZFISH:ENSG00000102678-MONOMER.
ReactomeiR-HSA-109704. PI3K Cascade.
R-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-1839122. Signaling by activated point mutants of FGFR1.
R-HSA-1839130. Signaling by activated point mutants of FGFR3.
R-HSA-190322. FGFR4 ligand binding and activation.
R-HSA-190371. FGFR3b ligand binding and activation.
R-HSA-190372. FGFR3c ligand binding and activation.
R-HSA-190373. FGFR1c ligand binding and activation.
R-HSA-190375. FGFR2c ligand binding and activation.
R-HSA-2033514. FGFR3 mutant receptor activation.
R-HSA-2033519. Activated point mutants of FGFR2.
R-HSA-2219530. Constitutive Signaling by Aberrant PI3K in Cancer.
R-HSA-5654219. Phospholipase C-mediated cascade: FGFR1.
R-HSA-5654221. Phospholipase C-mediated cascade, FGFR2.
R-HSA-5654227. Phospholipase C-mediated cascade, FGFR3.
R-HSA-5654228. Phospholipase C-mediated cascade, FGFR4.
R-HSA-5654687. Downstream signaling of activated FGFR1.
R-HSA-5654688. SHC-mediated cascade:FGFR1.
R-HSA-5654689. PI-3K cascade:FGFR1.
R-HSA-5654693. FRS-mediated FGFR1 signaling.
R-HSA-5654695. PI-3K cascade:FGFR2.
R-HSA-5654699. SHC-mediated cascade:FGFR2.
R-HSA-5654700. FRS-mediated FGFR2 signaling.
R-HSA-5654704. SHC-mediated cascade:FGFR3.
R-HSA-5654706. FRS-mediated FGFR3 signaling.
R-HSA-5654710. PI-3K cascade:FGFR3.
R-HSA-5654712. FRS-mediated FGFR4 signaling.
R-HSA-5654719. SHC-mediated cascade:FGFR4.
R-HSA-5654720. PI-3K cascade:FGFR4.
R-HSA-5654726. Negative regulation of FGFR1 signaling.
R-HSA-5654727. Negative regulation of FGFR2 signaling.
R-HSA-5654732. Negative regulation of FGFR3 signaling.
R-HSA-5654733. Negative regulation of FGFR4 signaling.
R-HSA-5655253. Signaling by FGFR2 in disease.
R-HSA-5655302. Signaling by FGFR1 in disease.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-8853338. Signaling by FGFR3 point mutants in cancer.
SignaLinkiP31371.
SIGNORiP31371.

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
Proteomesi
  • UP000005640 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)DescriptionActionsGraphical viewLength
Natural variantiVAR_06325499S → 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 PublicationCorresponds to variant rs121918322dbSNPEnsembl.1

Keywords - Diseasei

Deafness, Disease mutation

Organism-specific databases

DisGeNETi2254.
MalaCardsiFGF9.
MIMi612961. phenotype.
OpenTargetsiENSG00000102678.
Orphaneti3237. Multiple synostoses syndrome.
PharmGKBiPA28126.

Polymorphism and mutation databases

BioMutaiFGF9.
DMDMi544290.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000089731 – 31 Publication3
ChainiPRO_00000089744 – 208Fibroblast growth factor 9Add BLAST205

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi79N-linked (GlcNAc...)1

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

iPTMnetiP31371.
PhosphoSitePlusiP31371.

Expressioni

Tissue specificityi

Glial cells.

Gene expression databases

BgeeiENSG00000102678.
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

GO - Molecular functioni

  • growth factor activity Source: ProtInc

Protein-protein interaction databases

BioGridi108545. 11 interactors.
DIPiDIP-6036N.
STRINGi9606.ENSP00000371790.

Structurei

Secondary structure

1208
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi53 – 60Combined sources8
Beta strandi63 – 68Combined sources6
Beta strandi73 – 76Combined sources4
Beta strandi82 – 87Combined sources6
Helixi91 – 93Combined sources3
Beta strandi95 – 101Combined sources7
Beta strandi104 – 109Combined sources6
Turni110 – 112Combined sources3
Beta strandi115 – 118Combined sources4
Beta strandi124 – 129Combined sources6
Helixi132 – 134Combined sources3
Beta strandi136 – 142Combined sources7
Beta strandi145 – 154Combined sources10
Turni156 – 158Combined sources3
Beta strandi161 – 163Combined sources3
Helixi175 – 177Combined sources3
Helixi183 – 185Combined sources3
Beta strandi187 – 190Combined sources4
Helixi194 – 196Combined sources3
Helixi200 – 203Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP31371.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3885. Eukaryota.
ENOG4111IPH. LUCA.
GeneTreeiENSGT00760000118859.
HOGENOMiHOG000236341.
HOVERGENiHBG007580.
InParanoidiP31371.
KOiK04358.
OMAiGELYGSD.
OrthoDBiEOG091G0NAY.
PhylomeDBiP31371.
TreeFamiTF317805.

Family and domain databases

CDDicd00058. FGF. 1 hit.
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.

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)DescriptionActionsGraphical viewLength
Sequence conflicti24 – 26VLP → SLL AA sequence (PubMed:8428960).Curated3
Sequence conflicti34S → A AA sequence (PubMed:8428960).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02094494I → V.1 PublicationCorresponds to variant rs12427696dbSNPEnsembl.1
Natural variantiVAR_06325499S → 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 PublicationCorresponds to variant rs121918322dbSNPEnsembl.1

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.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G82X-ray2.60A/B/C/D49-208[»]
1IHKX-ray2.20A35-208[»]
ProteinModelPortaliP31371.
SMRiP31371.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108545. 11 interactors.
DIPiDIP-6036N.
STRINGi9606.ENSP00000371790.

PTM databases

iPTMnetiP31371.
PhosphoSitePlusiP31371.

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.3. human.

Organism-specific databases

CTDi2254.
DisGeNETi2254.
GeneCardsiFGF9.
HGNCiHGNC:3687. FGF9.
HPAiCAB004392.
MalaCardsiFGF9.
MIMi600921. gene.
612961. phenotype.
neXtProtiNX_P31371.
OpenTargetsiENSG00000102678.
Orphaneti3237. Multiple synostoses syndrome.
PharmGKBiPA28126.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3885. Eukaryota.
ENOG4111IPH. LUCA.
GeneTreeiENSGT00760000118859.
HOGENOMiHOG000236341.
HOVERGENiHBG007580.
InParanoidiP31371.
KOiK04358.
OMAiGELYGSD.
OrthoDBiEOG091G0NAY.
PhylomeDBiP31371.
TreeFamiTF317805.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000102678-MONOMER.
ReactomeiR-HSA-109704. PI3K Cascade.
R-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-1839122. Signaling by activated point mutants of FGFR1.
R-HSA-1839130. Signaling by activated point mutants of FGFR3.
R-HSA-190322. FGFR4 ligand binding and activation.
R-HSA-190371. FGFR3b ligand binding and activation.
R-HSA-190372. FGFR3c ligand binding and activation.
R-HSA-190373. FGFR1c ligand binding and activation.
R-HSA-190375. FGFR2c ligand binding and activation.
R-HSA-2033514. FGFR3 mutant receptor activation.
R-HSA-2033519. Activated point mutants of FGFR2.
R-HSA-2219530. Constitutive Signaling by Aberrant PI3K in Cancer.
R-HSA-5654219. Phospholipase C-mediated cascade: FGFR1.
R-HSA-5654221. Phospholipase C-mediated cascade, FGFR2.
R-HSA-5654227. Phospholipase C-mediated cascade, FGFR3.
R-HSA-5654228. Phospholipase C-mediated cascade, FGFR4.
R-HSA-5654687. Downstream signaling of activated FGFR1.
R-HSA-5654688. SHC-mediated cascade:FGFR1.
R-HSA-5654689. PI-3K cascade:FGFR1.
R-HSA-5654693. FRS-mediated FGFR1 signaling.
R-HSA-5654695. PI-3K cascade:FGFR2.
R-HSA-5654699. SHC-mediated cascade:FGFR2.
R-HSA-5654700. FRS-mediated FGFR2 signaling.
R-HSA-5654704. SHC-mediated cascade:FGFR3.
R-HSA-5654706. FRS-mediated FGFR3 signaling.
R-HSA-5654710. PI-3K cascade:FGFR3.
R-HSA-5654712. FRS-mediated FGFR4 signaling.
R-HSA-5654719. SHC-mediated cascade:FGFR4.
R-HSA-5654720. PI-3K cascade:FGFR4.
R-HSA-5654726. Negative regulation of FGFR1 signaling.
R-HSA-5654727. Negative regulation of FGFR2 signaling.
R-HSA-5654732. Negative regulation of FGFR3 signaling.
R-HSA-5654733. Negative regulation of FGFR4 signaling.
R-HSA-5655253. Signaling by FGFR2 in disease.
R-HSA-5655302. Signaling by FGFR1 in disease.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-8853338. Signaling by FGFR3 point mutants in cancer.
SignaLinkiP31371.
SIGNORiP31371.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000102678.
CleanExiHS_FGF9.
GenevisibleiP31371. HS.

Family and domain databases

CDDicd00058. FGF. 1 hit.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 176 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

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 one 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.