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Protein

Fibroblast growth factor 10

Gene

FGF10

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 branching morphogenesis. May play a role in wound healing.1 Publication

GO - Molecular functioni

  • chemoattractant activity Source: UniProtKB
  • fibroblast growth factor receptor binding Source: UniProtKB
  • growth factor activity Source: UniProtKB
  • heparin binding Source: UniProtKB
  • type 2 fibroblast growth factor receptor binding Source: UniProtKB

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_13778. Regulation of gene expression in early pancreatic precursor cells.
REACT_147727. Constitutive Signaling by Aberrant PI3K in Cancer.
REACT_355069. FRS-mediated FGFR2 signaling.
REACT_355146. Phospholipase C-mediated cascade, FGFR2.
REACT_355194. SHC-mediated cascade:FGFR1.
REACT_355202. Signaling by FGFR4 mutants.
REACT_355218. Negative regulation of FGFR1 signaling.
REACT_355225. SHC-mediated cascade:FGFR2.
REACT_355227. Negative regulation of FGFR2 signaling.
REACT_355450. PI-3K cascade:FGFR2.
REACT_355511. Signaling by FGFR2 mutants.
REACT_355552. PI-3K cascade:FGFR1.
REACT_355584. FRS-mediated FGFR1 signaling.
REACT_75829. PIP3 activates AKT signaling.
REACT_9400. FGFR1b ligand binding and activation.
REACT_9416. FGFR2b ligand binding and activation.
REACT_976. PI3K Cascade.
SignaLinkiO15520.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibroblast growth factor 10
Short name:
FGF-10
Alternative name(s):
Keratinocyte growth factor 2
Gene namesi
Name:FGF10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:3666. FGF10.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Aplasia of lacrimal and salivary glands (ALSG)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA rare condition characterized by dry conjunctival mucosae, irritable eyes, epiphora (constant tearing), and xerostomia (dryness of the mouth), which increases risk of dental erosion, dental caries, periodontal disease, and oral infections. ALSG has variable expressivity, and affected individuals may have aplasia or hypoplasia of the lacrimal, parotid, submandibular, and sublingual glands and absence of the lacrimal puncta.

See also OMIM:180920
Lacrimo-auriculo-dento-digital syndrome (LADDS)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal dominant ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. Lacrimo-auriculo-dento-digital syndrome is characterized by aplastic/hypoplastic lacrimal and salivary glands and ducts, cup-shaped ears, hearing loss, hypodontia and enamel hypoplasia, and distal limb segments anomalies. In addition to these cardinal features, facial dysmorphism, malformations of the kidney and respiratory system and abnormal genitalia have been reported. Craniosynostosis and severe syndactyly are not observed.

See also OMIM:149730
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti106 – 1061C → F in LADDS. 1 Publication
VAR_029888
Natural varianti156 – 1561I → R in LADDS. 1 Publication
VAR_029889

Keywords - Diseasei

Disease mutation, Ectodermal dysplasia, Lacrimo-auriculo-dento-digital syndrome

Organism-specific databases

MIMi149730. phenotype.
180920. phenotype.
Orphaneti86815. Aplasia of lacrimal and salivary glands.
2363. Lacrimoauriculodentodigital syndrome.
PharmGKBiPA28106.

Polymorphism and mutation databases

BioMutaiFGF10.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3737Sequence AnalysisAdd
BLAST
Chaini38 – 208171Fibroblast growth factor 10PRO_0000008981Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi51 – 511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi196 – 1961N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiO15520.
PRIDEiO15520.

PTM databases

PhosphoSiteiO15520.

Expressioni

Gene expression databases

BgeeiO15520.
CleanExiHS_FGF10.
ExpressionAtlasiO15520. baseline and differential.
GenevisibleiO15520. HS.

Organism-specific databases

HPAiCAB010315.

Interactioni

Subunit structurei

Interacts with FGFR1 and FGFR2. Interacts with FGFBP1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FGFR2P218022EBI-1035684,EBI-1028658

Protein-protein interaction databases

BioGridi108546. 4 interactions.
DIPiDIP-6037N.
IntActiO15520. 1 interaction.
MINTiMINT-257957.
STRINGi9606.ENSP00000264664.

Structurei

Secondary structure

1
208
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi70 – 734Combined sources
Beta strandi76 – 849Combined sources
Beta strandi89 – 924Combined sources
Beta strandi98 – 1014Combined sources
Beta strandi111 – 1177Combined sources
Beta strandi120 – 1256Combined sources
Turni126 – 1294Combined sources
Beta strandi130 – 1345Combined sources
Beta strandi138 – 1458Combined sources
Beta strandi150 – 1567Combined sources
Beta strandi162 – 17110Combined sources
Beta strandi174 – 1774Combined sources
Helixi189 – 1913Combined sources
Helixi197 – 1993Combined sources
Beta strandi201 – 2055Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NUNX-ray2.90A64-208[»]
ProteinModelPortaliO15520.
SMRiO15520. Positions 69-207.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15520.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi52 – 6211Poly-SerAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG327524.
GeneTreeiENSGT00760000118859.
HOGENOMiHOG000236341.
HOVERGENiHBG007580.
InParanoidiO15520.
KOiK04358.
OMAiSSIPVTC.
OrthoDBiEOG7992S1.
PhylomeDBiO15520.
TreeFamiTF317805.

Family and domain databases

InterProiIPR008996. Cytokine_IL1-like.
IPR028252. FGF10.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERiPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF21. PTHR11486:SF21. 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.

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

O15520-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWKWILTHCA SAFPHLPGCC CCCFLLLFLV SSVPVTCQAL GQDMVSPEAT
60 70 80 90 100
NSSSSSFSSP SSAGRHVRSY NHLQGDVRWR KLFSFTKYFL KIEKNGKVSG
110 120 130 140 150
TKKENCPYSI LEITSVEIGV VAVKAINSNY YLAMNKKGKL YGSKEFNNDC
160 170 180 190 200
KLKERIEENG YNTYASFNWQ HNGRQMYVAL NGKGAPRRGQ KTRRKNTSAH

FLPMVVHS
Length:208
Mass (Da):23,436
Last modified:January 1, 1998 - v1
Checksum:iC0A0705C108680B3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431D → V in CAG46489 (Ref. 5) Curated
Sequence conflicti120 – 1201V → A in AAL05875 (Ref. 3) Curated
Sequence conflicti134 – 1341M → R in AAL05875 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti106 – 1061C → F in LADDS. 1 Publication
VAR_029888
Natural varianti156 – 1561I → R in LADDS. 1 Publication
VAR_029889

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB002097 mRNA. Translation: BAA22331.1.
U67918 mRNA. Translation: AAB61991.1.
AF411527 mRNA. Translation: AAL05875.1.
GQ351295 mRNA. Translation: ACU00617.1.
CR541665 mRNA. Translation: CAG46466.1.
CR541688 mRNA. Translation: CAG46489.1.
AY604046 Genomic DNA. Translation: AAS99733.1.
CH471119 Genomic DNA. Translation: EAW56075.1.
BC069561 mRNA. Translation: AAH69561.1.
BC105021 mRNA. Translation: AAI05022.1.
BC105023 mRNA. Translation: AAI05024.1.
CCDSiCCDS3950.1.
RefSeqiNP_004456.1. NM_004465.1.
XP_005248321.1. XM_005248264.2.
UniGeneiHs.664499.

Genome annotation databases

EnsembliENST00000264664; ENSP00000264664; ENSG00000070193.
GeneIDi2255.
KEGGihsa:2255.
UCSCiuc003jog.1. human.

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB002097 mRNA. Translation: BAA22331.1.
U67918 mRNA. Translation: AAB61991.1.
AF411527 mRNA. Translation: AAL05875.1.
GQ351295 mRNA. Translation: ACU00617.1.
CR541665 mRNA. Translation: CAG46466.1.
CR541688 mRNA. Translation: CAG46489.1.
AY604046 Genomic DNA. Translation: AAS99733.1.
CH471119 Genomic DNA. Translation: EAW56075.1.
BC069561 mRNA. Translation: AAH69561.1.
BC105021 mRNA. Translation: AAI05022.1.
BC105023 mRNA. Translation: AAI05024.1.
CCDSiCCDS3950.1.
RefSeqiNP_004456.1. NM_004465.1.
XP_005248321.1. XM_005248264.2.
UniGeneiHs.664499.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NUNX-ray2.90A64-208[»]
ProteinModelPortaliO15520.
SMRiO15520. Positions 69-207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108546. 4 interactions.
DIPiDIP-6037N.
IntActiO15520. 1 interaction.
MINTiMINT-257957.
STRINGi9606.ENSP00000264664.

PTM databases

PhosphoSiteiO15520.

Polymorphism and mutation databases

BioMutaiFGF10.

Proteomic databases

PaxDbiO15520.
PRIDEiO15520.

Protocols and materials databases

DNASUi2255.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264664; ENSP00000264664; ENSG00000070193.
GeneIDi2255.
KEGGihsa:2255.
UCSCiuc003jog.1. human.

Organism-specific databases

CTDi2255.
GeneCardsiGC05M044340.
HGNCiHGNC:3666. FGF10.
HPAiCAB010315.
MIMi149730. phenotype.
180920. phenotype.
602115. gene.
neXtProtiNX_O15520.
Orphaneti86815. Aplasia of lacrimal and salivary glands.
2363. Lacrimoauriculodentodigital syndrome.
PharmGKBiPA28106.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG327524.
GeneTreeiENSGT00760000118859.
HOGENOMiHOG000236341.
HOVERGENiHBG007580.
InParanoidiO15520.
KOiK04358.
OMAiSSIPVTC.
OrthoDBiEOG7992S1.
PhylomeDBiO15520.
TreeFamiTF317805.

Enzyme and pathway databases

ReactomeiREACT_110235. Phospholipase C-mediated cascade: FGFR1.
REACT_120863. Activated point mutants of FGFR2.
REACT_13778. Regulation of gene expression in early pancreatic precursor cells.
REACT_147727. Constitutive Signaling by Aberrant PI3K in Cancer.
REACT_355069. FRS-mediated FGFR2 signaling.
REACT_355146. Phospholipase C-mediated cascade, FGFR2.
REACT_355194. SHC-mediated cascade:FGFR1.
REACT_355202. Signaling by FGFR4 mutants.
REACT_355218. Negative regulation of FGFR1 signaling.
REACT_355225. SHC-mediated cascade:FGFR2.
REACT_355227. Negative regulation of FGFR2 signaling.
REACT_355450. PI-3K cascade:FGFR2.
REACT_355511. Signaling by FGFR2 mutants.
REACT_355552. PI-3K cascade:FGFR1.
REACT_355584. FRS-mediated FGFR1 signaling.
REACT_75829. PIP3 activates AKT signaling.
REACT_9400. FGFR1b ligand binding and activation.
REACT_9416. FGFR2b ligand binding and activation.
REACT_976. PI3K Cascade.
SignaLinkiO15520.

Miscellaneous databases

EvolutionaryTraceiO15520.
GeneWikiiFGF10.
GenomeRNAii2255.
NextBioi9135.
PROiO15520.
SOURCEiSearch...

Gene expression databases

BgeeiO15520.
CleanExiHS_FGF10.
ExpressionAtlasiO15520. baseline and differential.
GenevisibleiO15520. HS.

Family and domain databases

InterProiIPR008996. Cytokine_IL1-like.
IPR028252. FGF10.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERiPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF21. PTHR11486:SF21. 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  2. "Cutaneous wound healing by keratinocyte growth factor 2."
    Jimenez P.A., Gruber J.R., Liu B., Feng P., Florence C., Blunt A., Huddleston K.A., Teliska M., Alfonso P., Coleman T.A., Ornitz D.M., Dillon P.A., Duan R.D.
    Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  3. Zhang Y., Zhang B., Zhou Y., Peng X., Yuan J., Qiang B.
    Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Expression of FGF10 in human prostate stromal cells."
    Nakhla A.M., Hryb D.J., Kahn S.M., Romas N.A., Rosner W.
    Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. NIEHS SNPs program
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. 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].
    Tissue: Brain.
  9. "The fibroblast growth factor binding protein is a novel interaction partner of FGF-7, FGF-10 and FGF-22 and regulates FGF activity: implications for epithelial repair."
    Beer H.-D., Bittner M., Niklaus G., Munding C., Max N., Goppelt A., Werner S.
    Oncogene 24:5269-5277(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FGFBP1.
  10. "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 FGFR1 AND FGFR2, FUNCTION IN STIMULATION OF CELL PROLIFERATION.
  11. "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.
  12. "Structural basis by which alternative splicing confers specificity in fibroblast growth factor receptors."
    Yeh B.K., Igarashi M., Eliseenkova A.V., Plotnikov A.N., Sher I., Ron D., Aaronson S.A., Mohammadi M.
    Proc. Natl. Acad. Sci. U.S.A. 100:2266-2271(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 69-208 IN COMPLEX WITH FGFR2.
  13. "Mutations in the gene encoding fibroblast growth factor 10 are associated with aplasia of lacrimal and salivary glands."
    Entesarian M., Matsson H., Klar J., Bergendal B., Olson L., Arakaki R., Hayashi Y., Ohuchi H., Falahat B., Bolstad A.I., Jonsson R., Wahren-Herlenius M., Dahl N.
    Nat. Genet. 37:125-127(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN ALSG.
  14. Cited for: VARIANT LADDS ARG-156.
  15. Cited for: VARIANT LADDS PHE-106.

Entry informationi

Entry nameiFGF10_HUMAN
AccessioniPrimary (citable) accession number: O15520
Secondary accession number(s): C7FDY0
, Q6FHR3, Q6FHT6, Q96P59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: June 24, 2015
This is version 142 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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.