Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fibroblast growth factor 20

Gene

FGF20

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Neurotrophic factor that regulates central nervous development and function.1 Publication

GO - Molecular functioni

GO - Biological processi

  • cell-cell signaling Source: ProtInc
  • fibroblast growth factor receptor signaling pathway Source: ParkinsonsUK-UCL
  • inner ear receptor cell differentiation Source: Ensembl
  • MAPK cascade Source: Reactome
  • negative regulation of neuron apoptotic process Source: ParkinsonsUK-UCL
  • phosphatidylinositol-mediated signaling Source: Reactome
  • positive regulation of cell proliferation Source: ParkinsonsUK-UCL
  • positive regulation of dopaminergic neuron differentiation Source: ParkinsonsUK-UCL
  • positive regulation of ERK1 and ERK2 cascade Source: Ensembl
  • regulation of cardiac muscle cell proliferation Source: Ensembl
  • regulation of dopamine secretion Source: ParkinsonsUK-UCL
  • regulation of phosphatidylinositol 3-kinase signaling Source: Reactome
  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Growth factor

Enzyme and pathway databases

BioCyciZFISH:ENSG00000078579-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.
SIGNORiQ9NP95.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibroblast growth factor 20
Short name:
FGF-20
Gene namesi
Name:FGF20
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:3677. FGF20.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Renal hypodysplasia/aplasia 2 (RHDA2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA perinatally lethal renal disease encompassing a spectrum of kidney development defects, including renal agenesis, bilateral renal aplasia, hypoplasia, (cystic) dysplasia, and severe obstructive uropathy.
See also OMIM:615721

Organism-specific databases

DisGeNETi26281.
MalaCardsiFGF20.
MIMi615721. phenotype.
OpenTargetsiENSG00000078579.
Orphaneti1848. Bilateral renal agenesis.
PharmGKBiPA28116.

Polymorphism and mutation databases

BioMutaiFGF20.
DMDMi13626702.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001476161 – 211Fibroblast growth factor 20Add BLAST211

Proteomic databases

PaxDbiQ9NP95.
PRIDEiQ9NP95.

PTM databases

iPTMnetiQ9NP95.
PhosphoSitePlusiQ9NP95.

Expressioni

Tissue specificityi

Predominantly expressed in the cerebellum.1 Publication

Gene expression databases

BgeeiENSG00000078579.
CleanExiHS_FGF20.
ExpressionAtlasiQ9NP95. baseline and differential.
GenevisibleiQ9NP95. HS.

Interactioni

Subunit structurei

Homodimer. Interacts with FGFR2 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors.2 Publications

GO - Molecular functioni

  • growth factor activity Source: ParkinsonsUK-UCL
  • receptor binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi117664. 1 interactor.
STRINGi9606.ENSP00000180166.

Structurei

Secondary structure

1211
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi56 – 64Combined sources9
Beta strandi66 – 71Combined sources6
Turni72 – 74Combined sources3
Beta strandi75 – 79Combined sources5
Beta strandi85 – 89Combined sources5
Beta strandi94 – 104Combined sources11
Beta strandi107 – 112Combined sources6
Turni113 – 115Combined sources3
Beta strandi118 – 121Combined sources4
Beta strandi127 – 132Combined sources6
Helixi135 – 137Combined sources3
Beta strandi139 – 145Combined sources7
Beta strandi148 – 157Combined sources10
Turni159 – 161Combined sources3
Beta strandi164 – 166Combined sources3
Beta strandi173 – 175Combined sources3
Helixi178 – 180Combined sources3
Helixi186 – 188Combined sources3
Beta strandi190 – 193Combined sources4
Helixi197 – 199Combined sources3
Helixi201 – 203Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3F1RX-ray2.50A/B1-211[»]
ProteinModelPortaliQ9NP95.
SMRiQ9NP95.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NP95.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3885. Eukaryota.
ENOG4111IPH. LUCA.
GeneTreeiENSGT00760000118859.
HOGENOMiHOG000236341.
HOVERGENiHBG007580.
InParanoidiQ9NP95.
KOiK04358.
OMAiYKDILMY.
OrthoDBiEOG091G0NAY.
PhylomeDBiQ9NP95.
TreeFamiTF317805.

Family and domain databases

CDDicd00058. FGF. 1 hit.
InterProiIPR008996. Cytokine_IL1-like.
IPR028291. FGF20.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERiPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF72. PTHR11486:SF72. 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.

Q9NP95-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPLAEVGGF LGGLEGLGQQ VGSHFLLPPA GERPPLLGER RSAAERSARG
60 70 80 90 100
GPGAAQLAHL HGILRRRQLY CRTGFHLQIL PDGSVQGTRQ DHSLFGILEF
110 120 130 140 150
ISVAVGLVSI RGVDSGLYLG MNDKGELYGS EKLTSECIFR EQFEENWYNT
160 170 180 190 200
YSSNIYKHGD TGRRYFVALN KDGTPRDGAR SKRHQKFTHF LPRPVDPERV
210
PELYKDLLMY T
Length:211
Mass (Da):23,499
Last modified:October 1, 2000 - v1
Checksum:iAB04608C16060CC1
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_020946116G → R.1 PublicationCorresponds to variant rs3793405dbSNPEnsembl.1
Natural variantiVAR_020947175P → A.1 PublicationCorresponds to variant rs10089600dbSNPEnsembl.1
Natural variantiVAR_020948206D → N.1 PublicationCorresponds to variant rs17550360dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB044277 mRNA. Translation: BAB03633.1.
AB030648 mRNA. Translation: BAB03530.1.
AY696296 Genomic DNA. Translation: AAT85804.1.
CH471080 Genomic DNA. Translation: EAW63828.1.
BC137446 mRNA. Translation: AAI37447.1.
BC137447 mRNA. Translation: AAI37448.1.
CCDSiCCDS5998.1.
PIRiJC7353.
RefSeqiNP_062825.1. NM_019851.2.
UniGeneiHs.199905.

Genome annotation databases

EnsembliENST00000180166; ENSP00000180166; ENSG00000078579.
GeneIDi26281.
KEGGihsa:26281.
UCSCiuc003wxc.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB044277 mRNA. Translation: BAB03633.1.
AB030648 mRNA. Translation: BAB03530.1.
AY696296 Genomic DNA. Translation: AAT85804.1.
CH471080 Genomic DNA. Translation: EAW63828.1.
BC137446 mRNA. Translation: AAI37447.1.
BC137447 mRNA. Translation: AAI37448.1.
CCDSiCCDS5998.1.
PIRiJC7353.
RefSeqiNP_062825.1. NM_019851.2.
UniGeneiHs.199905.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3F1RX-ray2.50A/B1-211[»]
ProteinModelPortaliQ9NP95.
SMRiQ9NP95.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117664. 1 interactor.
STRINGi9606.ENSP00000180166.

PTM databases

iPTMnetiQ9NP95.
PhosphoSitePlusiQ9NP95.

Polymorphism and mutation databases

BioMutaiFGF20.
DMDMi13626702.

Proteomic databases

PaxDbiQ9NP95.
PRIDEiQ9NP95.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000180166; ENSP00000180166; ENSG00000078579.
GeneIDi26281.
KEGGihsa:26281.
UCSCiuc003wxc.2. human.

Organism-specific databases

CTDi26281.
DisGeNETi26281.
GeneCardsiFGF20.
HGNCiHGNC:3677. FGF20.
MalaCardsiFGF20.
MIMi605558. gene.
615721. phenotype.
neXtProtiNX_Q9NP95.
OpenTargetsiENSG00000078579.
Orphaneti1848. Bilateral renal agenesis.
PharmGKBiPA28116.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3885. Eukaryota.
ENOG4111IPH. LUCA.
GeneTreeiENSGT00760000118859.
HOGENOMiHOG000236341.
HOVERGENiHBG007580.
InParanoidiQ9NP95.
KOiK04358.
OMAiYKDILMY.
OrthoDBiEOG091G0NAY.
PhylomeDBiQ9NP95.
TreeFamiTF317805.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000078579-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.
SIGNORiQ9NP95.

Miscellaneous databases

EvolutionaryTraceiQ9NP95.
GenomeRNAii26281.
PROiQ9NP95.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000078579.
CleanExiHS_FGF20.
ExpressionAtlasiQ9NP95. baseline and differential.
GenevisibleiQ9NP95. HS.

Family and domain databases

CDDicd00058. FGF. 1 hit.
InterProiIPR008996. Cytokine_IL1-like.
IPR028291. FGF20.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERiPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF72. PTHR11486:SF72. 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 nameiFGF20_HUMAN
AccessioniPrimary (citable) accession number: Q9NP95
Secondary accession number(s): B2RPH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 1, 2000
Last modified: November 30, 2016
This is version 129 of the entry and version 1 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

Caution

It is uncertain whether variants in this gene are associated with Parkinson disease. Some authors mention association with the disease (PubMed:18252210). In contrast, some others do not observe any association (PubMed:19133659).2 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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.