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 - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Growth factor

Enzyme and pathway databases

ReactomeiREACT_110235. Phospholipase C-mediated cascade: FGFR1.
REACT_120863. Activated point mutants of FGFR2.
REACT_121153. Signaling by activated point mutants of FGFR1.
REACT_121249. FGFR3 mutant receptor activation.
REACT_121337. Signaling by activated point mutants of FGFR3.
REACT_147727. Constitutive Signaling by Aberrant PI3K in Cancer.
REACT_355069. FRS-mediated FGFR2 signaling.
REACT_355144. Negative regulation of FGFR3 signaling.
REACT_355146. Phospholipase C-mediated cascade, FGFR2.
REACT_355159. SHC-mediated cascade:FGFR4.
REACT_355160. PI-3K cascade:FGFR3.
REACT_355194. SHC-mediated cascade:FGFR1.
REACT_355197. SHC-mediated cascade:FGFR3.
REACT_355202. Signaling by FGFR4 mutants.
REACT_355212. FRS-mediated FGFR3 signaling.
REACT_355216. Phospholipase C-mediated cascade, FGFR4.
REACT_355218. Negative regulation of FGFR1 signaling.
REACT_355221. Signaling by FGFR1 mutants.
REACT_355225. SHC-mediated cascade:FGFR2.
REACT_355227. Negative regulation of FGFR2 signaling.
REACT_355304. PI-3K cascade:FGFR4.
REACT_355313. Signaling by FGFR3 mutants.
REACT_355450. PI-3K cascade:FGFR2.
REACT_355511. Signaling by FGFR2 mutants.
REACT_355514. Phospholipase C-mediated cascade, FGFR3.
REACT_355552. PI-3K cascade:FGFR1.
REACT_355580. FRS2-mediated FGFR4 signaling.
REACT_355584. FRS-mediated FGFR1 signaling.
REACT_355588. Negative regulation of FGFR4 signaling.
REACT_75829. PIP3 activates AKT signaling.
REACT_9413. FGFR2c ligand binding and activation.
REACT_9452. FGFR4 ligand binding and activation.
REACT_9508. FGFR3b ligand binding and activation.
REACT_9510. FGFR3c ligand binding and activation.
REACT_9515. FGFR1c ligand binding and activation.
REACT_976. PI3K Cascade.

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
ProteomesiUP000005640 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

MIMi615721. phenotype.
Orphaneti1848. Bilateral renal agenesis.
PharmGKBiPA28116.

Polymorphism and mutation databases

BioMutaiFGF20.
DMDMi13626702.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 211211Fibroblast growth factor 20PRO_0000147616Add
BLAST

Proteomic databases

PaxDbiQ9NP95.
PRIDEiQ9NP95.

PTM databases

PhosphoSiteiQ9NP95.

Expressioni

Tissue specificityi

Predominantly expressed in the cerebellum.1 Publication

Gene expression databases

BgeeiQ9NP95.
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

Protein-protein interaction databases

STRINGi9606.ENSP00000180166.

Structurei

Secondary structure

1
211
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi56 – 649Combined sources
Beta strandi66 – 716Combined sources
Turni72 – 743Combined sources
Beta strandi75 – 795Combined sources
Beta strandi85 – 895Combined sources
Beta strandi94 – 10411Combined sources
Beta strandi107 – 1126Combined sources
Turni113 – 1153Combined sources
Beta strandi118 – 1214Combined sources
Beta strandi127 – 1326Combined sources
Helixi135 – 1373Combined sources
Beta strandi139 – 1457Combined sources
Beta strandi148 – 15710Combined sources
Turni159 – 1613Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi173 – 1753Combined sources
Helixi178 – 1803Combined sources
Helixi186 – 1883Combined sources
Beta strandi190 – 1934Combined sources
Helixi197 – 1993Combined sources
Helixi201 – 2033Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3F1RX-ray2.50A/B1-211[»]
ProteinModelPortaliQ9NP95.
SMRiQ9NP95. Positions 52-208.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NP95.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG269410.
GeneTreeiENSGT00760000118859.
HOGENOMiHOG000236341.
HOVERGENiHBG007580.
InParanoidiQ9NP95.
KOiK04358.
OMAiYKDILMY.
OrthoDBiEOG7992S1.
PhylomeDBiQ9NP95.
TreeFamiTF317805.

Family and domain databases

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.
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti116 – 1161G → R.1 Publication
Corresponds to variant rs3793405 [ dbSNP | Ensembl ].
VAR_020946
Natural varianti175 – 1751P → A.1 Publication
Corresponds to variant rs10089600 [ dbSNP | Ensembl ].
VAR_020947
Natural varianti206 – 2061D → N.1 Publication
Corresponds to variant rs17550360 [ dbSNP | Ensembl ].
VAR_020948

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.1. 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
EntryMethodResolution (Å)ChainPositionsPDBsum
3F1RX-ray2.50A/B1-211[»]
ProteinModelPortaliQ9NP95.
SMRiQ9NP95. Positions 52-208.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000180166.

PTM databases

PhosphoSiteiQ9NP95.

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.1. human.

Organism-specific databases

CTDi26281.
GeneCardsiGC08M016894.
HGNCiHGNC:3677. FGF20.
MIMi605558. gene.
615721. phenotype.
neXtProtiNX_Q9NP95.
Orphaneti1848. Bilateral renal agenesis.
PharmGKBiPA28116.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG269410.
GeneTreeiENSGT00760000118859.
HOGENOMiHOG000236341.
HOVERGENiHBG007580.
InParanoidiQ9NP95.
KOiK04358.
OMAiYKDILMY.
OrthoDBiEOG7992S1.
PhylomeDBiQ9NP95.
TreeFamiTF317805.

Enzyme and pathway databases

ReactomeiREACT_110235. Phospholipase C-mediated cascade: FGFR1.
REACT_120863. Activated point mutants of FGFR2.
REACT_121153. Signaling by activated point mutants of FGFR1.
REACT_121249. FGFR3 mutant receptor activation.
REACT_121337. Signaling by activated point mutants of FGFR3.
REACT_147727. Constitutive Signaling by Aberrant PI3K in Cancer.
REACT_355069. FRS-mediated FGFR2 signaling.
REACT_355144. Negative regulation of FGFR3 signaling.
REACT_355146. Phospholipase C-mediated cascade, FGFR2.
REACT_355159. SHC-mediated cascade:FGFR4.
REACT_355160. PI-3K cascade:FGFR3.
REACT_355194. SHC-mediated cascade:FGFR1.
REACT_355197. SHC-mediated cascade:FGFR3.
REACT_355202. Signaling by FGFR4 mutants.
REACT_355212. FRS-mediated FGFR3 signaling.
REACT_355216. Phospholipase C-mediated cascade, FGFR4.
REACT_355218. Negative regulation of FGFR1 signaling.
REACT_355221. Signaling by FGFR1 mutants.
REACT_355225. SHC-mediated cascade:FGFR2.
REACT_355227. Negative regulation of FGFR2 signaling.
REACT_355304. PI-3K cascade:FGFR4.
REACT_355313. Signaling by FGFR3 mutants.
REACT_355450. PI-3K cascade:FGFR2.
REACT_355511. Signaling by FGFR2 mutants.
REACT_355514. Phospholipase C-mediated cascade, FGFR3.
REACT_355552. PI-3K cascade:FGFR1.
REACT_355580. FRS2-mediated FGFR4 signaling.
REACT_355584. FRS-mediated FGFR1 signaling.
REACT_355588. Negative regulation of FGFR4 signaling.
REACT_75829. PIP3 activates AKT signaling.
REACT_9413. FGFR2c ligand binding and activation.
REACT_9452. FGFR4 ligand binding and activation.
REACT_9508. FGFR3b ligand binding and activation.
REACT_9510. FGFR3c ligand binding and activation.
REACT_9515. FGFR1c ligand binding and activation.
REACT_976. PI3K Cascade.

Miscellaneous databases

EvolutionaryTraceiQ9NP95.
GenomeRNAii26281.
NextBioi48605.
PROiQ9NP95.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NP95.
CleanExiHS_FGF20.
ExpressionAtlasiQ9NP95. baseline and differential.
GenevisibleiQ9NP95. HS.

Family and domain databases

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.
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. "Molecular cloning and characterization of human FGF-20 on chromosome 8p21.3-p22."
    Kirikoshi H., Sagara N., Saitoh T., Tanaka K., Sekihara H., Shiokawa K., Katoh M.
    Biochem. Biophys. Res. Commun. 274:337-343(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "FGF-20, a novel neurotrophic factor, preferentially expressed in the substantia nigra pars compacta of rat brain."
    Ohmachi S., Watanabe Y., Mikami T., Kusu N., Ibi T., Akaike A., Itoh N.
    Biochem. Biophys. Res. Commun. 277:355-360(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "Identification of a novel human fibroblast growth factor and characterization of its role in oncogenesis."
    Jeffers M., Shimkets R., Prayaga S., Boldog F., Yang M., Burgess C., Fernandes E., Rittman B., Shimkets J., LaRochelle W.J., Lichenstein H.S.
    Cancer Res. 61:3131-3138(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  4. NIEHS SNPs program
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-116; ALA-175 AND ASN-206.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Brain.
  7. "Receptor specificity of the fibroblast growth factor family. The complete mammalian FGF family."
    Zhang X., Ibrahimi O.A., Olsen S.K., Umemori H., Mohammadi M., Ornitz D.M.
    J. Biol. Chem. 281:15694-15700(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FGFR2 AND FGFR4, FUNCTION IN STIMULATION OF CELL PROLIFERATION.
  8. "Variation in the miRNA-433 binding site of FGF20 confers risk for Parkinson disease by overexpression of alpha-synuclein."
    Wang G., van der Walt J.M., Mayhew G., Li Y.J., Zuchner S., Scott W.K., Martin E.R., Vance J.M.
    Am. J. Hum. Genet. 82:283-289(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE ASSOCIATION WITH PARKINSON DISEASE.
  9. Cited for: NO EVIDENCE OF ASSOCIATION WITH PARKINSON DISEASE.
  10. "Fibroblast growth factor signalling: from development to cancer."
    Turner N., Grose R.
    Nat. Rev. Cancer 10:116-129(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  11. Cited for: INVOLVEMENT IN RHDA2.
  12. "Homodimerization controls the fibroblast growth factor 9 subfamily's receptor binding and heparan sulfate-dependent diffusion in the extracellular matrix."
    Kalinina J., Byron S.A., Makarenkova H.P., Olsen S.K., Eliseenkova A.V., Larochelle W.J., Dhanabal M., Blais S., Ornitz D.M., Day L.A., Neubert T.A., Pollock P.M., Mohammadi M.
    Mol. Cell. Biol. 29:4663-4678(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT, HEPARIN-BINDING.

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: June 24, 2015
This is version 117 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

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.