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P11403 (FGF4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Fgf4
Synonyms:Fgf-4, Kfgf
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length202 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Secreted Potential.

Tissue specificity

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

Sequence similarities

Belongs to the heparin-binding growth factors family.

Ontologies

Keywords
   Biological processDifferentiation
   Cellular componentSecreted
   DiseaseProto-oncogene
   DomainSignal
   Molecular functionDevelopmental protein
Growth factor
Mitogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process involved in morphogenesis

Inferred from genetic interaction PubMed 15649466. Source: MGI

cartilage condensation

Inferred from genetic interaction PubMed 8565825. Source: MGI

chondroblast differentiation

Inferred from electronic annotation. Source: Ensembl

cranial suture morphogenesis

Inferred from direct assay PubMed 9477322. Source: MGI

embryonic hindlimb morphogenesis

Inferred from genetic interaction PubMed 16245339. Source: MGI

embryonic limb morphogenesis

Inferred from genetic interaction PubMed 15328019. Source: MGI

fibroblast growth factor receptor signaling pathway

Inferred from genetic interaction PubMed 2161540. Source: MGI

mesenchymal cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from genetic interaction PubMed 16245339. Source: MGI

odontogenesis of dentin-containing tooth

Inferred from direct assay PubMed 12502739. Source: MGI

positive regulation of ERK1 and ERK2 cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cell proliferation

Inferred from direct assay PubMed 17951031PubMed 7494107. Source: MGI

positive regulation of gene expression

Inferred from direct assay PubMed 9244299. Source: MGI

positive regulation of protein phosphorylation

Inferred from direct assay PubMed 19289495. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 9477322. Source: MGI

regulation of gene expression

Inferred from direct assay PubMed 19289495. Source: MGI

stem cell maintenance

Inferred from genetic interaction PubMed 15328412. Source: MGI

   Cellular_componentcytosol

Inferred from direct assay PubMed 10644718. Source: MGI

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 10644718. Source: MGI

   Molecular_functionfibroblast growth factor receptor binding

Inferred from physical interaction PubMed 2161540. Source: MGI

protein binding

Inferred from physical interaction PubMed 8393815. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 202173Fibroblast growth factor 4
PRO_0000008954

Experimental info

Sequence conflict1671S → A in CAA32967. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P11403 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: 62D4563AF7D9AA31

FASTA20221,919
        10         20         30         40         50         60 
MAKRGPTTGT LLPRVLLALV VALADRGTAA PNGTRHAELG HGWDGLVARS LARLPVAAQP 

        70         80         90        100        110        120 
PQAAVRSGAG DYLLGLKRLR RLYCNVGIGF HLQVLPDGRI GGVHADTRDS LLELSPVQRG 

       130        140        150        160        170        180 
VVSIFGVASR FFVAMSSRGK LFGVPFFTDE CKFKEILLPN NYNAYESYAY PGMFMALSKN 

       190        200 
GRTKKGNRVS PTMKVTHFLP RL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS22052.1.
PIRTVMSHS. S04741.
RefSeqNP_034332.2. NM_010202.5.
UniGeneMm.4956.

3D structure databases

ProteinModelPortalP11403.
SMRP11403. Positions 75-202.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000056752.

PTM databases

PhosphoSiteP11403.

Proteomic databases

PRIDEP11403.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000060336; ENSMUSP00000056752; ENSMUSG00000050917.
GeneID14175.
KEGGmmu:14175.
UCSCuc009kqq.1. mouse.

Organism-specific databases

CTD2249.
MGIMGI:95518. Fgf4.

Phylogenomic databases

eggNOGNOG290420.
GeneTreeENSGT00730000110487.
HOGENOMHOG000236341.
HOVERGENHBG007580.
InParanoidP11403.
KOK04358.
OMAYNAYESH.
OrthoDBEOG7992S1.
TreeFamTF317805.

Gene expression databases

CleanExMM_FGF4.
GenevestigatorP11403.

Family and domain databases

InterProIPR008996. Cytokine_IL1-like.
IPR028239. FGF4.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF31. PTHR11486:SF31. 1 hit.
PfamPF00167. FGF. 1 hit.
[Graphical view]
PRINTSPR00263. HBGFFGF.
PR00262. IL1HBGF.
SMARTSM00442. FGF. 1 hit.
[Graphical view]
SUPFAMSSF50353. SSF50353. 1 hit.
PROSITEPS00247. HBGF_FGF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio285350.
PROP11403.
SOURCESearch...

Entry information

Entry nameFGF4_MOUSE
AccessionPrimary (citable) accession number: P11403
Secondary accession number(s): P15657, Q542N0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 3, 2012
Last modified: July 9, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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