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Fibroblast growth factor 16 (FGF-16)

 FGF16_HUMAN             Reviewed;         207 AA.
O43320;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
25-OCT-2017, entry version 133.
RecName: Full=Fibroblast growth factor 16;
Short=FGF-16;
Name=FGF16;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart;
PubMed=9473496; DOI=10.1006/bbrc.1998.8073;
Miyake A., Konishi M., Martin F.H., Hernday N.A., Ozaki K.,
Yamamoto S., Mikami T., Arakawa T., Itoh N.;
"Structure and expression of a novel member, FGF-16, on the fibroblast
growth factor family.";
Biochem. Biophys. Res. Commun. 243:148-152(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
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.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[3]
INTERACTION WITH FGFR2 AND FGFR3, AND FUNCTION IN STIMULATION OF CELL
PROLIFERATION.
PubMed=16597617; DOI=10.1074/jbc.M601252200;
Zhang X., Ibrahimi O.A., Olsen S.K., Umemori H., Mohammadi M.,
Ornitz D.M.;
"Receptor specificity of the fibroblast growth factor family. The
complete mammalian FGF family.";
J. Biol. Chem. 281:15694-15700(2006).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[5]
REVIEW.
PubMed=20094046; DOI=10.1038/nrc2780;
Turner N., Grose R.;
"Fibroblast growth factor signalling: from development to cancer.";
Nat. Rev. Cancer 10:116-129(2010).
[6]
INVOLVEMENT IN MF4.
PubMed=23709756; DOI=10.1136/jmedgenet-2013-101659;
Jamsheer A., Zemojtel T., Kolanczyk M., Stricker S., Hecht J.,
Krawitz P., Doelken S.C., Glazar R., Socha M., Mundlos S.;
"Whole exome sequencing identifies FGF16 nonsense mutations as the
cause of X-linked recessive metacarpal 4/5 fusion.";
J. Med. Genet. 50:579-584(2013).
[7]
INVOLVEMENT IN MF4, AND VARIANT MF4 LEU-68.
PubMed=25333065; DOI=10.1002/mgg3.81;
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.;
"Identification of three novel FGF16 mutations in X-linked recessive
fusion of the fourth and fifth metacarpals and possible correlation
with heart disease.";
Mol. Genet. Genomic Med. 2:402-411(2014).
-!- FUNCTION: 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. {ECO:0000269|PubMed:16597617}.
-!- SUBUNIT: Interacts with FGFR1 and FGFR2.
{ECO:0000269|PubMed:16597617}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O54769}.
-!- DISEASE: Metacarpal 4-5 fusion (MF4) [MIM:309630]: A 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.
{ECO:0000269|PubMed:23709756, ECO:0000269|PubMed:25333065}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the heparin-binding growth factors family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AB009391; BAA24956.1; -; mRNA.
EMBL; BX682239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS75996.1; -.
PIR; JC5941; JC5941.
RefSeq; NP_003859.1; NM_003868.2.
UniGene; Hs.666364; -.
ProteinModelPortal; O43320; -.
SMR; O43320; -.
BioGrid; 114350; 1.
IntAct; O43320; 5.
STRING; 9606.ENSP00000399324; -.
iPTMnet; O43320; -.
PhosphoSitePlus; O43320; -.
BioMuta; FGF16; -.
PRIDE; O43320; -.
DNASU; 8823; -.
Ensembl; ENST00000439435; ENSP00000399324; ENSG00000196468.
GeneID; 8823; -.
KEGG; hsa:8823; -.
UCSC; uc033ejs.2; human.
CTD; 8823; -.
DisGeNET; 8823; -.
EuPathDB; HostDB:ENSG00000196468.7; -.
GeneCards; FGF16; -.
HGNC; HGNC:3672; FGF16.
MalaCards; FGF16; -.
MIM; 300827; gene.
MIM; 309630; phenotype.
neXtProt; NX_O43320; -.
OpenTargets; ENSG00000196468; -.
Orphanet; 2498; Syndactyly type 8.
PharmGKB; PA28111; -.
GeneTree; ENSGT00760000118859; -.
HOVERGEN; HBG007580; -.
InParanoid; O43320; -.
KO; K04358; -.
OMA; RYYYVAL; -.
OrthoDB; EOG091G0NAY; -.
PhylomeDB; O43320; -.
Reactome; R-HSA-109704; PI3K Cascade.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1839130; Signaling by activated point mutants of FGFR3.
Reactome; R-HSA-190322; FGFR4 ligand binding and activation.
Reactome; R-HSA-190372; FGFR3c ligand binding and activation.
Reactome; R-HSA-190375; FGFR2c ligand binding and activation.
Reactome; R-HSA-2033514; FGFR3 mutant receptor activation.
Reactome; R-HSA-2033519; Activated point mutants of FGFR2.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-5654221; Phospholipase C-mediated cascade, FGFR2.
Reactome; R-HSA-5654227; Phospholipase C-mediated cascade, FGFR3.
Reactome; R-HSA-5654228; Phospholipase C-mediated cascade, FGFR4.
Reactome; R-HSA-5654695; PI-3K cascade:FGFR2.
Reactome; R-HSA-5654699; SHC-mediated cascade:FGFR2.
Reactome; R-HSA-5654700; FRS-mediated FGFR2 signaling.
Reactome; R-HSA-5654704; SHC-mediated cascade:FGFR3.
Reactome; R-HSA-5654706; FRS-mediated FGFR3 signaling.
Reactome; R-HSA-5654710; PI-3K cascade:FGFR3.
Reactome; R-HSA-5654712; FRS-mediated FGFR4 signaling.
Reactome; R-HSA-5654719; SHC-mediated cascade:FGFR4.
Reactome; R-HSA-5654720; PI-3K cascade:FGFR4.
Reactome; R-HSA-5654727; Negative regulation of FGFR2 signaling.
Reactome; R-HSA-5654732; Negative regulation of FGFR3 signaling.
Reactome; R-HSA-5654733; Negative regulation of FGFR4 signaling.
Reactome; R-HSA-5655253; Signaling by FGFR2 in disease.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-8853338; Signaling by FGFR3 point mutants in cancer.
GenomeRNAi; 8823; -.
PRO; PR:O43320; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000196468; -.
CleanEx; HS_FGF16; -.
Genevisible; O43320; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; TAS:ProtInc.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; TAS:Reactome.
GO; GO:0005104; F:fibroblast growth factor receptor binding; IEA:Ensembl.
GO; GO:0008083; F:growth factor activity; TAS:ProtInc.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:Reactome.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0008152; P:metabolic process; TAS:ProtInc.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0070349; P:positive regulation of brown fat cell proliferation; IEA:Ensembl.
GO; GO:2000546; P:positive regulation of endothelial cell chemotaxis to fibroblast growth factor; IDA:UniProtKB.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0009266; P:response to temperature stimulus; TAS:ProtInc.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd00058; FGF; 1.
InterPro; IPR028285; FGF16.
InterPro; IPR002209; Fibroblast_GF_fam.
InterPro; IPR008996; IL1/FGF.
PANTHER; PTHR11486; PTHR11486; 1.
PANTHER; PTHR11486:SF27; PTHR11486:SF27; 1.
Pfam; PF00167; FGF; 1.
PRINTS; PR00263; HBGFFGF.
SMART; SM00442; FGF; 1.
SUPFAM; SSF50353; SSF50353; 1.
PROSITE; PS00247; HBGF_FGF; 1.
1: Evidence at protein level;
Complete proteome; Disease mutation; Glycoprotein; Growth factor;
Phosphoprotein; Reference proteome; Secreted.
CHAIN 1 207 Fibroblast growth factor 16.
/FTId=PRO_0000147613.
MOD_RES 111 111 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
CARBOHYD 78 78 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 68 68 R -> L (in MF4).
{ECO:0000269|PubMed:25333065}.
/FTId=VAR_072396.
SEQUENCE 207 AA; 23759 MW; D8AD160BDABDB5F8 CRC64;
MAEVGGVFAS LDWDLHGFSS SLGNVPLADS PGFLNERLGQ IEGKLQRGSP TDFAHLKGIL
RRRQLYCRTG FHLEIFPNGT VHGTRHDHSR FGILEFISLA VGLISIRGVD SGLYLGMNER
GELYGSKKLT RECVFREQFE ENWYNTYAST LYKHSDSERQ YYVALNKDGS PREGYRTKRH
QKFTHFLPRP VDPSKLPSMS RDLFHYR


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