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Protein

Fibroblast growth factor 16

Gene

FGF16

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, and is required for normal cardiomyocyte proliferation and heart development.1 Publication

GO - Molecular functioni

  • growth factor activity Source: ProtInc

GO - Biological processi

  • cell-cell signaling Source: ProtInc
  • epidermal growth factor receptor signaling pathway Source: Reactome
  • Fc-epsilon receptor signaling pathway Source: Reactome
  • fibroblast growth factor receptor signaling pathway Source: Reactome
  • innate immune response Source: Reactome
  • insulin receptor signaling pathway Source: Reactome
  • metabolic process Source: ProtInc
  • neurotrophin TRK receptor signaling pathway Source: Reactome
  • organ morphogenesis Source: ProtInc
  • phosphatidylinositol-mediated signaling Source: Reactome
  • positive regulation of brown fat cell proliferation Source: Ensembl
  • positive regulation of endothelial cell chemotaxis to fibroblast growth factor Source: UniProtKB
  • response to temperature stimulus Source: ProtInc
  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Growth factor

Enzyme and pathway databases

ReactomeiREACT_120863. Activated point mutants of FGFR2.
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_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_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_355580. FRS2-mediated FGFR4 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_9510. FGFR3c ligand binding and activation.
REACT_976. PI3K Cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibroblast growth factor 16
Short name:
FGF-16
Gene namesi
Name:FGF16
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:3672. FGF16.

Subcellular locationi

  • Secreted By similarity

GO - Cellular componenti

  • extracellular region Source: Reactome
  • extracellular space Source: ProtInc
  • intracellular Source: GOC
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Metacarpal 4-5 fusion (MF4)2 Publications

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

Disease descriptionA rare congenital malformation of the hand characterized by the partial or complete fusion of the fourth and fifth metacarpals. The anomaly occurs as an isolated trait or part of a syndrome.

See also OMIM:309630
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti68 – 681R → L in MF4. 1 Publication
VAR_072396

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi309630. phenotype.
Orphaneti2498. Syndactyly type 8.
PharmGKBiPA28111.

Polymorphism and mutation databases

BioMutaiFGF16.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 207207Fibroblast growth factor 16PRO_0000147613Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi78 – 781N-linked (GlcNAc...)Sequence Analysis
Modified residuei111 – 1111Phosphoserine1 Publication
Modified residuei114 – 1141Phosphotyrosine1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiO43320.
PRIDEiO43320.

PTM databases

PhosphoSiteiO43320.

Expressioni

Gene expression databases

CleanExiHS_FGF16.
GenevisibleiO43320. HS.

Interactioni

Subunit structurei

Interacts with FGFR1 and FGFR2.1 Publication

Protein-protein interaction databases

BioGridi114350. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliO43320.
SMRiO43320. Positions 51-202.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG269618.
GeneTreeiENSGT00760000118859.
HOVERGENiHBG007580.
InParanoidiO43320.
KOiK04358.
OMAiNRTKKHQ.
PhylomeDBiO43320.

Family and domain databases

InterProiIPR008996. Cytokine_IL1-like.
IPR028285. FGF16.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERiPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF27. PTHR11486:SF27. 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.

O43320-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEVGGVFAS LDWDLHGFSS SLGNVPLADS PGFLNERLGQ IEGKLQRGSP
60 70 80 90 100
TDFAHLKGIL RRRQLYCRTG FHLEIFPNGT VHGTRHDHSR FGILEFISLA
110 120 130 140 150
VGLISIRGVD SGLYLGMNER GELYGSKKLT RECVFREQFE ENWYNTYAST
160 170 180 190 200
LYKHSDSERQ YYVALNKDGS PREGYRTKRH QKFTHFLPRP VDPSKLPSMS

RDLFHYR
Length:207
Mass (Da):23,759
Last modified:June 1, 1998 - v1
Checksum:iD8AD160BDABDB5F8
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti68 – 681R → L in MF4. 1 Publication
VAR_072396

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009391 mRNA. Translation: BAA24956.1.
BX682239 Genomic DNA. No translation available.
CCDSiCCDS75996.1.
PIRiJC5941.
RefSeqiNP_003859.1. NM_003868.2.
UniGeneiHs.666364.

Genome annotation databases

EnsembliENST00000439435; ENSP00000399324; ENSG00000196468.
GeneIDi8823.
KEGGihsa:8823.
UCSCiuc011mqp.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009391 mRNA. Translation: BAA24956.1.
BX682239 Genomic DNA. No translation available.
CCDSiCCDS75996.1.
PIRiJC5941.
RefSeqiNP_003859.1. NM_003868.2.
UniGeneiHs.666364.

3D structure databases

ProteinModelPortaliO43320.
SMRiO43320. Positions 51-202.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114350. 1 interaction.

PTM databases

PhosphoSiteiO43320.

Polymorphism and mutation databases

BioMutaiFGF16.

Proteomic databases

PaxDbiO43320.
PRIDEiO43320.

Protocols and materials databases

DNASUi8823.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000439435; ENSP00000399324; ENSG00000196468.
GeneIDi8823.
KEGGihsa:8823.
UCSCiuc011mqp.2. human.

Organism-specific databases

CTDi8823.
GeneCardsiGC0XP076709.
HGNCiHGNC:3672. FGF16.
MIMi300827. gene.
309630. phenotype.
neXtProtiNX_O43320.
Orphaneti2498. Syndactyly type 8.
PharmGKBiPA28111.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG269618.
GeneTreeiENSGT00760000118859.
HOVERGENiHBG007580.
InParanoidiO43320.
KOiK04358.
OMAiNRTKKHQ.
PhylomeDBiO43320.

Enzyme and pathway databases

ReactomeiREACT_120863. Activated point mutants of FGFR2.
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_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_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_355580. FRS2-mediated FGFR4 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_9510. FGFR3c ligand binding and activation.
REACT_976. PI3K Cascade.

Miscellaneous databases

GenomeRNAii8823.
NextBioi33100.
PROiO43320.
SOURCEiSearch...

Gene expression databases

CleanExiHS_FGF16.
GenevisibleiO43320. HS.

Family and domain databases

InterProiIPR008996. Cytokine_IL1-like.
IPR028285. FGF16.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERiPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF27. PTHR11486:SF27. 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. "Structure and expression of a novel member, FGF-16, on the fibroblast growth factor family."
    Miyake A., Konishi M., Martin F.H., Hernday N.A., Ozaki K., Yamamoto S., Mikami T., Arakawa T., Itoh N.
    Biochem. Biophys. Res. Commun. 243:148-152(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  2. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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 FGFR3, FUNCTION IN STIMULATION OF CELL PROLIFERATION.
  4. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111 AND TYR-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  5. "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.
  6. "Whole exome sequencing identifies FGF16 nonsense mutations as the cause of X-linked recessive metacarpal 4/5 fusion."
    Jamsheer A., Zemojtel T., Kolanczyk M., Stricker S., Hecht J., Krawitz P., Doelken S.C., Glazar R., Socha M., Mundlos S.
    J. Med. Genet. 50:579-584(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MF4.
  7. "Identification of three novel FGF16 mutations in X-linked recessive fusion of the fourth and fifth metacarpals and possible correlation with heart disease."
    Laurell T., Nilsson D., Hofmeister W., Lindstrand A., Ahituv N., Vandermeer J., Amilon A., Anneren G., Arner M., Pettersson M., Jaentti N., Rosberg H.E., Cattini P.A., Nordenskjoeld A., Maekitie O., Grigelioniene G., Nordgren A.
    Mol. Genet. Genomic Med. 2:402-411(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MF4, VARIANT MF4 LEU-68.

Entry informationi

Entry nameiFGF16_HUMAN
AccessioniPrimary (citable) accession number: O43320
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: July 22, 2015
This is version 113 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 X
    Human chromosome X: 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

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.