[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2959959 [NCBI, ExPASy, EBI, Israel, Japan] Yoshida T., Miyagawa K., Odagiri H., Sakamoto H., Little P.F.R., Terada M., Sugimura T.; "Genomic sequence of hst, a transforming gene encoding a protein homologous to fibroblast growth factors and the int-2-encoded protein."; Proc. Natl. Acad. Sci. U.S.A. 84:7305-7309(1987).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2953031 [NCBI, ExPASy, EBI, Israel, Japan] Taira M., Yoshida T., Miyagawa K., Sakamoto H., Terada M., Sugimura T.; "cDNA sequence of human transforming gene hst and identification of the coding sequence required for transforming activity."; Proc. Natl. Acad. Sci. U.S.A. 84:2980-2984(1987).
[3]	NUCLEOTIDE SEQUENCE. DOI=10.1016/0092-8674(87)90331-X; PubMed=2957062 [NCBI, ExPASy, EBI, Israel, Japan] Delli-Bovi P., Curatola A.M., Kern F.G., Greco A., Ittmann M., Basilico C.; "An oncogene isolated by transfection of Kaposi's sarcoma DNA encodes a growth factor that is a member of the FGF family."; Cell 50:729-737(1987).
[4]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 79-206. DOI=10.1128/MCB.21.17.5946-5957.2001; PubMed=11486033 [NCBI, ExPASy, EBI, Israel, Japan] Bellosta P., Iwahori A., Plotnikov A.N., Eliseenkova A.V., Basilico C., Mohammadi M.; "Identification of receptor and heparin binding sites in fibroblast growth factor 4 by structure-based mutagenesis."; Mol. Cell. Biol. 21:5946-5957(2001).

Comments

FUNCTION: Can transform NIH 3T3 cells from a human stomach tumor (hst) and from karposi's sarcoma (KS3). It has a mitogenic activity.
SIMILARITY: Belongs to the heparin-binding growth factors family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

J02986; AAB59555.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M17446; AAA59473.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A28417; TVHUHS.

NP_001998.1; -.

3D structure databases

PDB

1IJT; X-ray; 1.80 A; A=79-206.

[ExPASy / RCSB / EBI]

PDBsum

1IJT; -.

ModBase

P08620.

Protein-protein interaction databases

DIP

DIP:4017N; -.

Enzyme and pathway databases

Reactome

REACT_9470; Signaling by FGFR.

Organism-specific databases

HIX0036033; -.

HGNC:3682; FGF4.

FGF4; Homo sapiens.

HPA011209; -.

164980; gene. [NCBI / EBI]

PharmGKB

PA28121; -.

GeneCards

P08620.

Gene expression databases

ArrayExpress

P08620; -.

CleanEx

HS_FGF4; -.

GermOnline

ENSG00000075388; Homo sapiens.

Ontologies

GO:0005576;	Cellular component: extracellular region (traceable author statement from ProtInc).
GO:0008083;	Molecular function: growth factor activity (traceable author statement from ProtInc).
GO:0007267;	Biological process: cell-cell signaling (traceable author statement from ProtInc).
GO:0008543;	Biological process: fibroblast growth factor receptor signaling pathway (inferred from experiment from Reactome).
GO:0008284;	Biological process: positive regulation of cell proliferation (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR002209; GF_heparin_bd.
IPR002348; IL1_HBGF.
Graphical view of domain structure.

PANTHER

PTHR11486; IL1_HBGF; 1.

Pfam

PF00167; FGF; 1.
Pfam graphical view of domain structure.

PRINTS

PR00263; HBGFFGF.
PR00262; IL1HBGF.

ProDom

PD000831; IL1_HBGF; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00442; FGF; 1.
SMART graphical view of domain structure.

PROSITE

PS00247; HBGF_FGF; 1.

BLOCKS

P08620.

Genome annotation databases

Ensembl

ENSG00000075388; Homo sapiens. [Contig view]

GeneID

2249; -.

KEGG

hsa:2249; -.

Phylogenomic databases

HOGENOM

P08620; -.

HOVERGEN

P08620; -.

Other

DrugBank

DB00686; Pentosan Polysulfate.

FGF4; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Growth factor; Heparin-binding; Mitogen; Proto-oncogene; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 30`	`30`	`Potential.`
`CHAIN`	`31 206`	`176`	`Fibroblast growth factor 4.`	`PRO_0000008953`
`STRAND`	`82 88`	`7`
`STRAND`	`94 98`	`5`
`STRAND`	`104 109`	`6`
`HELIX`	`112 114`	`3`
`STRAND`	`116 122`	`7`
`STRAND`	`125 130`	`6`
`TURN`	`131 134`	`4`
`STRAND`	`135 139`	`5`
`STRAND`	`145 150`	`6`
`STRAND`	`155 161`	`7`
`HELIX`	`163 165`	`3`
`STRAND`	`167 174`	`8`
`STRAND`	`185 187`	`3`
`HELIX`	`190 192`	`3`
`HELIX`	`198 200`	`3`
`STRAND`	`202 205`	`4`

Sequence information

Length: 206 AA [This is the length of the unprocessed precursor]

Molecular weight: 22048 Da [This is the MW of the unprocessed precursor]

CRC64: C7FD54A0272A1569 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSGPGTAAVA LLPAVLLALL APWAGRGGAA APTAPNGTLE AELERRWESL VALSLARLPV 

        70         80         90        100        110        120 
AAQPKEAAVQ SGAGDYLLGI KRLRRLYCNV GIGFHLQALP DGRIGGAHAD TRDSLLELSP 

       130        140        150        160        170        180 
VERGVVSIFG VASRFFVAMS SKGKLYGSPF FTDECTFKEI LLPNNYNAYE SYKYPGMFIA 

       190        200 
LSKNGKTKKG NRVSPTMKVT HFLPRL

P08620 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools