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Reviewed, UniProtKB/Swiss-Prot O15520 (FGF10_HUMAN)

Last modified February 9, 2010. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Fibroblast growth factor 10
      Short name=FGF-10
Alternative name(s):
    Keratinocyte growth factor 2
Gene names
Name: FGF10
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length208 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Could be a growth factor active in the process of wound healing. Acts as a mitogen in the lung. May act in a manner similar to FGF-7.

Subunit structure

Interacts with FGFBP1. Ref.7

Subcellular location

Secreted Potential.

Involvement in disease

Defects in FGF10 are the cause of autosomal dominant aplasia of lacrimal and salivary glands (ALSG) [MIM:180920]. 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. The disorder is characterized by irritable eyes, recurrent eye infections, epiphora (constant tearing) and xerostomia (dryness of the mouth), which increases the risk of dental erosion, dental caries, periodontal disease and oral infections. Ref.9

Defects in FGF10 are a cause of lacrimo-auriculo-dento-digital syndrome (LADDS) [MIM:149730]; also known as Levy-Hollister syndrome. LADDS is a form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. LADDS is an autosomal dominant syndrome 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. Ref.10 Ref.11

Sequence similarities

Belongs to the heparin-binding growth factors family.

Ontologies

Keywords
   Cellular componentSecreted
   DiseaseDisease mutation
Ectodermal dysplasia
Lacrimo-auriculo-dento-digital syndrome
   DomainSignal
   Molecular functionGrowth factor
   PTMGlycoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processERK1 and ERK2 cascade

Inferred from direct assay. Source: UniProtKB

actin cytoskeleton reorganization

Inferred from direct assay. Source: UniProtKB

activation of MAPK activity

Inferred from direct assay. Source: UniProtKB

branching morphogenesis of a tube

Inferred from direct assay. Source: UniProtKB

fibroblast growth factor receptor signaling pathway

Inferred from Experiment. Source: Reactome

lacrimal gland development

Inferred from mutant phenotype. Source: UniProtKB

lung saccule development

Inferred from mutant phenotype. Source: UniProtKB

mesonephros development

Inferred from expression pattern. Source: UniProtKB

metanephros development

Inferred from expression pattern. Source: UniProtKB

negative regulation of cell cycle arrest

Inferred from direct assay. Source: UniProtKB

positive chemotaxis

Inferred from direct assay. Source: UniProtKB

positive regulation of ATPase activity

Inferred from direct assay. Source: UniProtKB

positive regulation of DNA repair

Inferred from direct assay. Source: UniProtKB

positive regulation of DNA replication

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of ERK1 and ERK2 cascade

Inferred from direct assay. Source: UniProtKB

positive regulation of Ras protein signal transduction

Inferred from direct assay. Source: UniProtKB

positive regulation of cyclin-dependent protein kinase activity during G1/S

Inferred from direct assay. Source: UniProtKB

positive regulation of epithelial cell proliferation involved in wound healing

Non-traceable author statement. Source: UniProtKB

positive regulation of hair follicle cell proliferation

Inferred from direct assay. Source: UniProtKB

positive regulation of keratinocyte migration

Inferred from direct assay. Source: UniProtKB

positive regulation of keratinocyte proliferation

Inferred from direct assay. Source: UniProtKB

positive regulation of lymphocyte proliferation

Inferred from direct assay. Source: UniProtKB

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay. Source: UniProtKB

positive regulation of urothelial cell proliferation

Inferred from direct assay. Source: UniProtKB

protein localization at cell surface

Inferred from direct assay. Source: UniProtKB

radial glial cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of saliva secretion

Inferred from mutant phenotype. Source: UniProtKB

salivary gland development

Inferred from mutant phenotype. Source: UniProtKB

tear secretion

Inferred from mutant phenotype. Source: UniProtKB

thymus development

Inferred from direct assay. Source: UniProtKB

urothelial cell proliferation

Inferred from direct assay. Source: UniProtKB

   Cellular componentcell surface

Inferred from direct assay. Source: UniProtKB

extracellular space

Inferred from direct assay. Source: UniProtKB

nucleus

Inferred from direct assay. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: UniProtKB

   Molecular functionchemoattractant activity

Inferred from direct assay. Source: UniProtKB

growth factor activity

Inferred from direct assay. Source: UniProtKB

heparin binding

Inferred from direct assay. Source: UniProtKB

type 2 fibroblast growth factor receptor binding

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FGFR2P218021EBI-1035684,EBI-1028658

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3737 Potential
Chain38 – 208171Fibroblast growth factor 10
PRO_0000008981

Regions

Compositional bias52 – 6211Poly-Ser

Amino acid modifications

Glycosylation511N-linked (GlcNAc...) Potential
Glycosylation1961N-linked (GlcNAc...) Potential

Natural variations

Natural variant1061C → F in LADDS. Ref.11
VAR_029888
Natural variant1561I → R in LADDS. Ref.10
VAR_029889

Experimental info

Sequence conflict1201V → A in AAL05875. Ref.3
Sequence conflict1341M → R in AAL05875. Ref.3

Secondary structure

............................. 208
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O15520-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: C0A0705C108680B3

FASTA20823,436
        10         20         30         40         50         60 
MWKWILTHCA SAFPHLPGCC CCCFLLLFLV SSVPVTCQAL GQDMVSPEAT NSSSSSFSSP 

        70         80         90        100        110        120 
SSAGRHVRSY NHLQGDVRWR KLFSFTKYFL KIEKNGKVSG TKKENCPYSI LEITSVEIGV 

       130        140        150        160        170        180 
VAVKAINSNY YLAMNKKGKL YGSKEFNNDC KLKERIEENG YNTYASFNWQ HNGRQMYVAL 

       190        200 
NGKGAPRRGQ KTRRKNTSAH FLPMVVHS 

« Hide

References

« Hide 'large scale' references
[1]"Structure and expression of human fibroblast growth factor-10."
Emoto H., Tagashira S., Mattei M.-G., Yamasaki M., Hashimoto G., Katsumata T., Negoro T., Nakatsuka M., Birnbaum D., Coulier F., Itoh N.
J. Biol. Chem. 272:23191-23194(1997) [PubMed: 9287324] [Abstract]
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]"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].
[5]NIEHS SNPs program
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[7]"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: 15806171] [Abstract]
Cited for: INTERACTION WITH FGFBP1.
[8]"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: 12591959] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 69-208 IN COMPLEX WITH FGFR2.
[9]"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: 15654336] [Abstract]
Cited for: INVOLVEMENT IN ALSG.
[10]"LADD syndrome is caused by FGF10 mutations."
Milunsky J.M., Zhao G., Maher T.A., Colby R., Everman D.B.
Clin. Genet. 69:349-354(2006) [PubMed: 16630169] [Abstract]
Cited for: VARIANT LADDS ARG-156.
[11]"Mutations in different components of FGF signaling in LADD syndrome."
Rohmann E., Brunner H.G., Kayserili H., Uyguner O., Nuernberg G., Lew E.D., Dobbie A., Eswarakumar V.P., Uzumcu A., Ulubil-Emeroglu M., Leroy J.G., Li Y., Becker C., Lehnerdt K., Cremers C.W.R.J., Yueksel-Apak M., Nuernberg P., Kubisch C. expand/collapse author list , Schlessinger J., van Bokhoven H., Wollnik B.
Nat. Genet. 38:414-417(2006) [PubMed: 16501574] [Abstract]
Cited for: VARIANT LADDS PHE-106.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB002097 mRNA. Translation: BAA22331.1.
U67918 mRNA. Translation: AAB61991.1.
AF411527 mRNA. Translation: AAL05875.1.
CR541665 mRNA. Translation: CAG46466.1.
AY604046 Genomic DNA. Translation: AAS99733.1.
BC069561 mRNA. Translation: AAH69561.1.
BC105021 mRNA. Translation: AAI05022.1.
BC105023 mRNA. Translation: AAI05024.1.
IPIIPI00007307.
RefSeqNP_004456.1.
UniGeneHs.664499

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NUNX-ray2.90A64-208[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-6037N.
IntActO15520. 1 interaction.
STRINGO15520.

PTM databases

PhosphoSiteO15520.

Proteomic databases

PRIDEO15520.

Genome annotation databases

EnsemblENST00000264664; ENSP00000264664; ENSG00000070193; Homo sapiens. [Genome view]
GeneID2255.
KEGGhsa:2255.
UCSCuc003jog.1. human.

Organism-specific databases

CTD2255.
GeneCardsGC05M044340.
H-InvDBHIX0031935.
HGNCHGNC:3666. FGF10.
HPACAB010315.
MIM149730. phenotype.
180920. phenotype.
602115. gene.
Orphanet86815. Aplasia of lacrimal and salivary glands.
PharmGKBPA28106.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG07737.
HOGENOMHBG715603.
HOVERGENO15520.
InParanoidO15520.
OMAXKEFNND.
OrthoDBEOG9QRKPR.
PhylomeDBO15520.

Enzyme and pathway databases

ReactomeREACT_9470. Signaling by FGFR.

Gene expression databases

ArrayExpressO15520.
BgeeO15520.
CleanExHS_FGF10.
GenevestigatorO15520.
GermOnlineENSG00000070193. Homo sapiens.

Family and domain databases

InterProIPR008996. Cytokine_IL1-like.
IPR002209. GF_heparin_bd.
IPR002348. IL1_HBGF.
[Graphical view]
PANTHERPTHR11486. IL1_HBGF. 1 hit.
PfamPF00167. FGF. 1 hit.
[Graphical view]
PRINTSPR00263. HBGFFGF.
PR00262. IL1HBGF.
SMARTSM00442. FGF. 1 hit.
[Graphical view]
PROSITEPS00247. HBGF_FGF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio9135.
SOURCESearch...

Entry information

Entry nameFGF10_HUMAN
AccessionPrimary (citable) accession number: O15520
Secondary accession number(s): Q6FHT6, Q96P59
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: February 9, 2010
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents