Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fibroblast growth factor 4

Gene

Fgf4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. Is essential for survival of the postimplantation mouse embryo. Required for normal limb and cardiac valve development during embryogenesis.

GO - Molecular functioni

  1. fibroblast growth factor receptor binding Source: MGI

GO - Biological processi

  1. apoptotic process involved in morphogenesis Source: MGI
  2. cartilage condensation Source: MGI
  3. chondroblast differentiation Source: MGI
  4. cranial suture morphogenesis Source: MGI
  5. embryonic hindlimb morphogenesis Source: MGI
  6. embryonic limb morphogenesis Source: MGI
  7. fibroblast growth factor receptor signaling pathway Source: MGI
  8. mesenchymal cell proliferation Source: MGI
  9. negative regulation of apoptotic process Source: MGI
  10. odontogenesis of dentin-containing tooth Source: MGI
  11. positive regulation of cell division Source: UniProtKB-KW
  12. positive regulation of cell proliferation Source: MGI
  13. positive regulation of ERK1 and ERK2 cascade Source: MGI
  14. positive regulation of gene expression Source: MGI
  15. positive regulation of protein phosphorylation Source: MGI
  16. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  17. regulation of gene expression Source: MGI
  18. stem cell maintenance Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Growth factor, Mitogen

Keywords - Biological processi

Differentiation

Enzyme and pathway databases

ReactomeiREACT_196455. Signaling by FGFR mutants.
REACT_196505. Signaling by FGFR3 mutants.
REACT_196507. Signaling by activated point mutants of FGFR3.
REACT_196536. Activated point mutants of FGFR2.
REACT_196538. Signaling by activated point mutants of FGFR1.
REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_198525. Negative regulation of FGFR signaling.
REACT_206694. FGFR4 ligand binding and activation.
REACT_206745. FGFR2c ligand binding and activation.
REACT_220750. FGFR3c ligand binding and activation.
REACT_223993. PI-3K cascade.
REACT_225874. FGFR1c ligand binding and activation.
REACT_226341. PIP3 activates AKT signaling.
REACT_230708. Phospholipase C-mediated cascade.
REACT_234357. FRS2-mediated cascade.
REACT_240139. PI3K Cascade.
REACT_94437. SHC-mediated cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibroblast growth factor 4
Short name:
FGF-4
Alternative name(s):
Heparin-binding growth factor 4
Short name:
HBGF-4
K-fibroblast growth factor
Gene namesi
Name:Fgf4
Synonyms:Fgf-4, Kfgf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:95518. Fgf4.

Subcellular locationi

Secreted Curated

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence AnalysisAdd
BLAST
Chaini30 – 202173Fibroblast growth factor 4PRO_0000008954Add
BLAST

Proteomic databases

PRIDEiP11403.

PTM databases

PhosphoSiteiP11403.

Expressioni

Tissue specificityi

Expressed in the blastocyst inner cell mass and later in distinct embryonic tissues.

Gene expression databases

CleanExiMM_FGF4.
GenevestigatoriP11403.

Interactioni

Subunit structurei

Interacts with FGFR1, FGFR2, FGFR3 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000056752.

Structurei

3D structure databases

ProteinModelPortaliP11403.
SMRiP11403. Positions 75-202.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG290420.
GeneTreeiENSGT00760000118859.
HOGENOMiHOG000236341.
HOVERGENiHBG007580.
InParanoidiP11403.
KOiK04358.
OMAiYNAYESH.
OrthoDBiEOG7992S1.
TreeFamiTF317805.

Family and domain databases

InterProiIPR008996. Cytokine_IL1-like.
IPR028239. FGF4.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERiPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF31. PTHR11486:SF31. 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.

P11403-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKRGPTTGT LLPRVLLALV VALADRGTAA PNGTRHAELG HGWDGLVARS
60 70 80 90 100
LARLPVAAQP PQAAVRSGAG DYLLGLKRLR RLYCNVGIGF HLQVLPDGRI
110 120 130 140 150
GGVHADTRDS LLELSPVQRG VVSIFGVASR FFVAMSSRGK LFGVPFFTDE
160 170 180 190 200
CKFKEILLPN NYNAYESYAY PGMFMALSKN GRTKKGNRVS PTMKVTHFLP

RL
Length:202
Mass (Da):21,919
Last modified:October 3, 2012 - v2
Checksum:i62D4563AF7D9AA31
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti167 – 1671S → A in CAA32967. (PubMed:2740210)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14849 Genomic DNA. Translation: CAA32967.1.
M30642 mRNA. Translation: AAA37619.1.
AK082814 mRNA. Translation: BAC38631.1.
AC149593 Genomic DNA. No translation available.
AC161763 Genomic DNA. No translation available.
CH466531 Genomic DNA. Translation: EDL18271.1.
BC104312 mRNA. Translation: AAI04313.1.
BC104313 mRNA. Translation: AAI04314.1.
CCDSiCCDS22052.1.
PIRiS04741. TVMSHS.
RefSeqiNP_034332.2. NM_010202.5.
UniGeneiMm.4956.

Genome annotation databases

EnsembliENSMUST00000060336; ENSMUSP00000056752; ENSMUSG00000050917.
GeneIDi14175.
KEGGimmu:14175.
UCSCiuc009kqq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14849 Genomic DNA. Translation: CAA32967.1.
M30642 mRNA. Translation: AAA37619.1.
AK082814 mRNA. Translation: BAC38631.1.
AC149593 Genomic DNA. No translation available.
AC161763 Genomic DNA. No translation available.
CH466531 Genomic DNA. Translation: EDL18271.1.
BC104312 mRNA. Translation: AAI04313.1.
BC104313 mRNA. Translation: AAI04314.1.
CCDSiCCDS22052.1.
PIRiS04741. TVMSHS.
RefSeqiNP_034332.2. NM_010202.5.
UniGeneiMm.4956.

3D structure databases

ProteinModelPortaliP11403.
SMRiP11403. Positions 75-202.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000056752.

PTM databases

PhosphoSiteiP11403.

Proteomic databases

PRIDEiP11403.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000060336; ENSMUSP00000056752; ENSMUSG00000050917.
GeneIDi14175.
KEGGimmu:14175.
UCSCiuc009kqq.1. mouse.

Organism-specific databases

CTDi2249.
MGIiMGI:95518. Fgf4.

Phylogenomic databases

eggNOGiNOG290420.
GeneTreeiENSGT00760000118859.
HOGENOMiHOG000236341.
HOVERGENiHBG007580.
InParanoidiP11403.
KOiK04358.
OMAiYNAYESH.
OrthoDBiEOG7992S1.
TreeFamiTF317805.

Enzyme and pathway databases

ReactomeiREACT_196455. Signaling by FGFR mutants.
REACT_196505. Signaling by FGFR3 mutants.
REACT_196507. Signaling by activated point mutants of FGFR3.
REACT_196536. Activated point mutants of FGFR2.
REACT_196538. Signaling by activated point mutants of FGFR1.
REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_198525. Negative regulation of FGFR signaling.
REACT_206694. FGFR4 ligand binding and activation.
REACT_206745. FGFR2c ligand binding and activation.
REACT_220750. FGFR3c ligand binding and activation.
REACT_223993. PI-3K cascade.
REACT_225874. FGFR1c ligand binding and activation.
REACT_226341. PIP3 activates AKT signaling.
REACT_230708. Phospholipase C-mediated cascade.
REACT_234357. FRS2-mediated cascade.
REACT_240139. PI3K Cascade.
REACT_94437. SHC-mediated cascade.

Miscellaneous databases

NextBioi285350.
PROiP11403.
SOURCEiSearch...

Gene expression databases

CleanExiMM_FGF4.
GenevestigatoriP11403.

Family and domain databases

InterProiIPR008996. Cytokine_IL1-like.
IPR028239. FGF4.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERiPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF31. PTHR11486:SF31. 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. "The mouse homologue of hst/k-FGF: sequence, genome organization and location relative to int-2."
    Dickson C.
    Nucleic Acids Res. 17:4037-4045(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Isolation of cDNAs encoding four mouse FGF family members and characterization of their expression patterns during embryogenesis."
    Hebert J.M., Basilico C., Goldfarb M., Haub O., Martin G.R.
    Dev. Biol. 138:454-463(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiFGF4_MOUSE
AccessioniPrimary (citable) accession number: P11403
Secondary accession number(s): P15657, Q542N0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 3, 2012
Last modified: February 4, 2015
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.