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Protein

Fibroblast growth factor 3

Gene

FGF3

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, and cell differentiation. Required for normal ear development.1 Publication

GO - Molecular functioni

GO - Biological processi

  • anatomical structure morphogenesis Source: ProtInc
  • cell-cell signaling Source: ProtInc
  • cell differentiation Source: UniProtKB-KW
  • fibroblast growth factor receptor signaling pathway Source: MGI
  • MAPK cascade Source: Reactome
  • multicellular organism development Source: UniProtKB-KW
  • negative regulation of cardiac muscle tissue development Source: BHF-UCL
  • phosphatidylinositol-mediated signaling Source: Reactome
  • positive regulation of cell division Source: UniProtKB-KW
  • positive regulation of cell proliferation Source: MGI
  • regulation of phosphatidylinositol 3-kinase signaling Source: Reactome
  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Growth factor, Mitogen

Keywords - Biological processi

Differentiation

Enzyme and pathway databases

BioCyciZFISH:G66-32533-MONOMER.
ReactomeiR-HSA-109704. PI3K Cascade.
R-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-190370. FGFR1b ligand binding and activation.
R-HSA-190377. FGFR2b ligand binding and 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-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-5654726. Negative regulation of FGFR1 signaling.
R-HSA-5654727. Negative regulation of FGFR2 signaling.
R-HSA-5655253. Signaling by FGFR2 in disease.
R-HSA-5658623. FGFRL1 modulation of FGFR1 signaling.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
SignaLinkiP11487.
SIGNORiP11487.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibroblast growth factor 3
Short name:
FGF-3
Alternative name(s):
Heparin-binding growth factor 3
Short name:
HBGF-3
Proto-oncogene Int-2
Gene namesi
Name:FGF3
Synonyms:INT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:3681. FGF3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Deafness with labyrinthine aplasia, microtia and microdontia (LAMM)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionUnique autosomal recessive syndrome characterized by type I microtia, microdontia, and profound congenital deafness associated with a complete absence of inner ear structures (Michel aplasia).
See also OMIM:610706
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0604926L → P in LAMM; probably impairs secretion. 1 PublicationCorresponds to variant rs121917706dbSNPEnsembl.1
Natural variantiVAR_031848156S → P in LAMM. 1 PublicationCorresponds to variant rs121917703dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

DisGeNETi2248.
MalaCardsiFGF3.
MIMi610706. phenotype.
OpenTargetsiENSG00000186895.
Orphaneti90024. Deafness with labyrinthine aplasia, microtia, and microdontia.
99806. Oculootodental syndrome.
2791. Otodental syndrome.
PharmGKBiPA28120.

Polymorphism and mutation databases

BioMutaiFGF3.
DMDMi122748.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
ChainiPRO_000000894618 – 239Fibroblast growth factor 3Add BLAST222

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi65N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP11487.
PRIDEiP11487.

PTM databases

iPTMnetiP11487.
PhosphoSitePlusiP11487.

Expressioni

Gene expression databases

BgeeiENSG00000186895.
CleanExiHS_FGF3.
GenevisibleiP11487. HS.

Organism-specific databases

HPAiHPA012692.

Interactioni

Subunit structurei

Interacts with FGFR1 and FGFR2. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors.1 Publication

GO - Molecular functioni

  • growth factor activity Source: ProtInc

Protein-protein interaction databases

BioGridi108539. 56 interactors.
DIPiDIP-4014N.
STRINGi9606.ENSP00000334122.

Structurei

3D structure databases

ProteinModelPortaliP11487.
SMRiP11487.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3885. Eukaryota.
ENOG4111IPH. LUCA.
GeneTreeiENSGT00760000118859.
HOGENOMiHOG000236341.
HOVERGENiHBG007580.
InParanoidiP11487.
KOiK04358.
OMAiGNKDHEM.
OrthoDBiEOG091G0NAY.
PhylomeDBiP11487.
TreeFamiTF317805.

Family and domain databases

CDDicd00058. FGF. 1 hit.
InterProiIPR008996. Cytokine_IL1-like.
IPR028232. FGF3.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERiPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF26. PTHR11486:SF26. 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.

P11487-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLIWLLLLS LLEPGWPAAG PGARLRRDAG GRGGVYEHLG GAPRRRKLYC
60 70 80 90 100
ATKYHLQLHP SGRVNGSLEN SAYSILEITA VEVGIVAIRG LFSGRYLAMN
110 120 130 140 150
KRGRLYASEH YSAECEFVER IHELGYNTYA SRLYRTVSST PGARRQPSAE
160 170 180 190 200
RLWYVSVNGK GRPRRGFKTR RTQKSSLFLP RVLDHRDHEM VRQLQSGLPR
210 220 230
PPGKGVQPRR RRQKQSPDNL EPSHVQASRL GSQLEASAH
Length:239
Mass (Da):26,887
Last modified:October 1, 1989 - v1
Checksum:i8DBEF17D2B2E3C63
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0604926L → P in LAMM; probably impairs secretion. 1 PublicationCorresponds to variant rs121917706dbSNPEnsembl.1
Natural variantiVAR_031848156S → P in LAMM. 1 PublicationCorresponds to variant rs121917703dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14445 Genomic DNA. Translation: CAA32615.1.
BC113739 mRNA. Translation: AAI13740.1.
CCDSiCCDS8195.1.
PIRiS04742.
RefSeqiNP_005238.1. NM_005247.2.
UniGeneiHs.37092.

Genome annotation databases

EnsembliENST00000334134; ENSP00000334122; ENSG00000186895.
GeneIDi2248.
KEGGihsa:2248.
UCSCiuc001oph.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14445 Genomic DNA. Translation: CAA32615.1.
BC113739 mRNA. Translation: AAI13740.1.
CCDSiCCDS8195.1.
PIRiS04742.
RefSeqiNP_005238.1. NM_005247.2.
UniGeneiHs.37092.

3D structure databases

ProteinModelPortaliP11487.
SMRiP11487.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108539. 56 interactors.
DIPiDIP-4014N.
STRINGi9606.ENSP00000334122.

PTM databases

iPTMnetiP11487.
PhosphoSitePlusiP11487.

Polymorphism and mutation databases

BioMutaiFGF3.
DMDMi122748.

Proteomic databases

PaxDbiP11487.
PRIDEiP11487.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000334134; ENSP00000334122; ENSG00000186895.
GeneIDi2248.
KEGGihsa:2248.
UCSCiuc001oph.4. human.

Organism-specific databases

CTDi2248.
DisGeNETi2248.
GeneCardsiFGF3.
GeneReviewsiFGF3.
HGNCiHGNC:3681. FGF3.
HPAiHPA012692.
MalaCardsiFGF3.
MIMi164950. gene.
610706. phenotype.
neXtProtiNX_P11487.
OpenTargetsiENSG00000186895.
Orphaneti90024. Deafness with labyrinthine aplasia, microtia, and microdontia.
99806. Oculootodental syndrome.
2791. Otodental syndrome.
PharmGKBiPA28120.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3885. Eukaryota.
ENOG4111IPH. LUCA.
GeneTreeiENSGT00760000118859.
HOGENOMiHOG000236341.
HOVERGENiHBG007580.
InParanoidiP11487.
KOiK04358.
OMAiGNKDHEM.
OrthoDBiEOG091G0NAY.
PhylomeDBiP11487.
TreeFamiTF317805.

Enzyme and pathway databases

BioCyciZFISH:G66-32533-MONOMER.
ReactomeiR-HSA-109704. PI3K Cascade.
R-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-190370. FGFR1b ligand binding and activation.
R-HSA-190377. FGFR2b ligand binding and 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-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-5654726. Negative regulation of FGFR1 signaling.
R-HSA-5654727. Negative regulation of FGFR2 signaling.
R-HSA-5655253. Signaling by FGFR2 in disease.
R-HSA-5658623. FGFRL1 modulation of FGFR1 signaling.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
SignaLinkiP11487.
SIGNORiP11487.

Miscellaneous databases

GeneWikiiFGF3.
GenomeRNAii2248.
PROiP11487.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000186895.
CleanExiHS_FGF3.
GenevisibleiP11487. HS.

Family and domain databases

CDDicd00058. FGF. 1 hit.
InterProiIPR008996. Cytokine_IL1-like.
IPR028232. FGF3.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERiPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF26. PTHR11486:SF26. 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 nameiFGF3_HUMAN
AccessioniPrimary (citable) accession number: P11487
Secondary accession number(s): Q0VG69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: November 30, 2016
This is version 147 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. 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.