P09038 (FGF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fibroblast growth factor 2
Short name=FGF-2

Alternative name(s):
Basic fibroblast growth factor
Short name=bFGF
Heparin-binding growth factor 2
Short name=HBGF-2

Gene names

Name:	FGF2
Synonyms:	FGFB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	288 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro. Ref.11 Ref.20
Subunit structure	Monomer. Homodimer. 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. Interacts with CSPG4, FGFBP1 and TEC. Found in a complex with FGFBP1, FGF1 and FGF2. Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25
Subcellular location	Secreted. Nucleus. Note: Exported from cells by an endoplasmic reticulum (ER)/Golgi-independent mechanism. Unconventional secretion of FGF2 occurs by direct translocation across the plasma membrane. Binding of exogenous FGF2 to FGFR facilitates endocytosis followed by translocation of FGF2 across endosomal membrane into the cytosol. Nuclear import from the cytosol requires the classical nuclear import machinery, involving proteins KPNA1 and KPNB1, as well as CEP57. Ref.25 Ref.28
Tissue specificity	Expressed in granulosa and cumulus cells. Expressed in hepatocellular carcinoma cells, but not in non-cancerous liver tissue. Ref.11 Ref.18
Post-translational modification	Phosphorylation at Tyr-215 regulates FGF2 unconventional secretion. Several N-termini starting at positions 94, 125, 126, 132, 143 and 162 have been identified by direct sequencing.
Miscellaneous	This protein binds heparin more strongly than does aFGF.
Sequence similarities	Belongs to the heparin-binding growth factors family.
Biophysicochemical properties	pH dependence: Retains almost half of its activity after treatment at pH 2.0 for 3 hours at 20 degrees Celsius. Ref.11 Temperature dependence: Inactivated after 3 minutes at 60 degrees Celsius or 1 minute at 80 degrees Celsius.
Sequence caution	The sequence AAA52448.1 differs from that shown. Reason: Frameshift at positions 25, 82, 98 and 133. The sequence AAB21432.2 differs from that shown. Reason: Frameshift at position 25. The sequence AAB21432.2 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon. The sequence ABO43041.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence ABO43041.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon. The sequence CAA28027.1 differs from that shown. Reason: Frameshift at positions 25 and 102. The sequence CAA28027.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon. The sequence CAA73868.1 differs from that shown. Reason: Frameshift at position 25. The sequence CAA73868.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon. The sequence EAX05222.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence EAX05222.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.

Ontologies

Keywords
Biological process	Angiogenesis Differentiation
Cellular component	Nucleus Secreted
Coding sequence diversity	Alternative initiation
Ligand	Heparin-binding
Molecular function	Developmental protein Growth factor Mitogen
PTM	Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	C21-steroid hormone biosynthetic process Inferred from electronic annotation. Source: Compara MAPK import into nucleus Inferred from electronic annotation. Source: Compara Ras protein signal transduction Traceable author statement PubMed 10848592. Source: ProtInc activation of MAPK activity Traceable author statement PubMed 9712850. Source: ProtInc activation of MAPKK activity Inferred from electronic annotation. Source: Compara apoptotic process Inferred from electronic annotation. Source: Compara branching involved in ureteric bud morphogenesis Inferred from direct assay PubMed 12631064. Source: UniProtKB cell migration involved in sprouting angiogenesis Inferred from direct assay PubMed 18059339. Source: BHF-UCL chondroblast differentiation Inferred from direct assay PubMed 17167778. Source: UniProtKB corticotropin hormone secreting cell differentiation Inferred from electronic annotation. Source: Compara embryonic morphogenesis Traceable author statement PubMed 20011604. Source: DFLAT fibroblast growth factor receptor signaling pathway Inferred from direct assay PubMed 17500071. Source: UniProtKB glial cell differentiation Inferred from electronic annotation. Source: Compara hyaluronan catabolic process Inferred from direct assay PubMed 19577615. Source: UniProtKB inositol phosphate biosynthetic process Inferred from direct assay PubMed 20011604. Source: DFLAT insulin receptor signaling pathway Traceable author statement. Source: Reactome lung development Inferred from electronic annotation. Source: Compara mammary gland epithelial cell differentiation Inferred from electronic annotation. Source: Compara negative regulation of blood vessel endothelial cell migration Inferred from direct assay PubMed 18555217. Source: BHF-UCL negative regulation of cell death Inferred from direct assay PubMed 12631064. Source: UniProtKB negative regulation of cell growth Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of fibroblast migration Inferred from direct assay PubMed 19577615. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara negative regulation of wound healing Inferred from direct assay PubMed 19577615. Source: UniProtKB nervous system development Traceable author statement PubMed 9576942. Source: ProtInc organ induction Inferred from electronic annotation. Source: Compara organ morphogenesis Traceable author statement PubMed 10903182. Source: ProtInc phosphatidylinositol biosynthetic process Inferred from direct assay PubMed 20011604. Source: DFLAT positive regulation of ERK1 and ERK2 cascade Inferred from direct assay PubMed 17167778. Source: UniProtKB positive regulation of angiogenesis Inferred from direct assay PubMed 20011604. Source: DFLAT positive regulation of blood vessel endothelial cell migration Inferred from direct assay PubMed 18555217. Source: BHF-UCL positive regulation of cardiac muscle cell proliferation Inferred from direct assay PubMed 9553078. Source: BHF-UCL positive regulation of cell division Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of cell fate specification Inferred from direct assay PubMed 18635606. Source: MGI positive regulation of cerebellar granule cell precursor proliferation Inferred from electronic annotation. Source: Compara positive regulation of endothelial cell proliferation Inferred from mutant phenotype PubMed 18059339. Source: BHF-UCL positive regulation of osteoblast differentiation Inferred from electronic annotation. Source: Compara positive regulation of phosphatidylinositol 3-kinase activity Inferred from direct assay PubMed 20011604. Source: DFLAT positive regulation of phospholipase C activity Inferred from direct assay PubMed 20011604. Source: DFLAT positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 18059339. Source: BHF-UCL regulation of cell cycle Inferred from electronic annotation. Source: Compara regulation of retinal cell programmed cell death Inferred from electronic annotation. Source: Compara release of sequestered calcium ion into cytosol Inferred from direct assay PubMed 20011604. Source: DFLAT response to axon injury Inferred from electronic annotation. Source: Compara stem cell development Inferred from electronic annotation. Source: Compara substantia nigra development Inferred from electronic annotation. Source: Compara thyroid-stimulating hormone-secreting cell differentiation Inferred from electronic annotation. Source: Compara wound healing Traceable author statement PubMed 20011604. Source: DFLAT
Cellular_component	cytosol Inferred from electronic annotation. Source: Compara extracellular space Traceable author statement Ref.10. Source: ProtInc nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	chemoattractant activity Inferred from direct assay PubMed 18059339. Source: BHF-UCL cytokine activity Inferred from direct assay PubMed 18059339. Source: BHF-UCL growth factor activity Inferred from direct assay PubMed 18059339. Source: BHF-UCL heparin binding Inferred from electronic annotation. Source: UniProtKB-KW ligand-dependent nuclear receptor transcription coactivator activity Inferred from direct assay PubMed 17500071. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CASP1	P29466	2	EBI-977447,EBI-516667
FGFBP1	Q14512	3	EBI-977447,EBI-953742
FGFR1	P11362	2	EBI-977447,EBI-1028277
FGFR2	P21802	3	EBI-977447,EBI-1028658

Alternative products

This entry describes 4 isoforms produced by alternative initiation. [Align] [Select]

Isoform 1 (identifier: P09038-4)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: Starts at an alternative CUG codon.

Isoform 2 (identifier: P09038-1)

The sequence of this isoform differs from the canonical sequence as follows:
     1-78: Missing.
     79-79: L → M

Note: Starts at an alternative CUG codon.

Isoform 3 (identifier: P09038-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.

Isoform 4 (identifier: P09038-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-92: Missing.
     93-93: L → M

Note: Starts at an alternative CUG codon.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 142

142

Or 93, or 124, or 125, or 131, or 161

PRO_0000008932

Chain

143 – 288

146

Fibroblast growth factor 2

PRO_0000008933

Regions

Region

261 – 277

17

Heparin-binding By similarity

Motif

179 – 181

3

Cell attachment site; atypical Potential

Motif

221 – 223

3

Cell attachment site; atypical Potential

Sites

Binding site

169

1

Heparin By similarity

Amino acid modifications

Modified residue

108

1

Omega-N-methylarginine; alternate By similarity

Modified residue

108

1

Symmetric dimethylarginine; alternate By similarity

Modified residue

110

1

Omega-N-methylarginine; alternate By similarity

Modified residue

110

1

Symmetric dimethylarginine; alternate By similarity

Modified residue

112

1

Omega-N-methylarginine; alternate By similarity

Modified residue

112

1

Symmetric dimethylarginine; alternate By similarity

Modified residue

215

1

Phosphotyrosine; by TEC Ref.25

Natural variations

Alternative sequence

1 – 133

133

Missing in isoform 3.

VSP_037383

Alternative sequence

1 – 92

92

Missing in isoform 4.

VSP_037384

Alternative sequence

1 – 78

78

Missing in isoform 2.

VSP_038236

Alternative sequence

79

1

L → M in isoform 2.

VSP_038237

Alternative sequence

93

1

L → M in isoform 4.

VSP_037385

Experimental info

Sequence conflict

25

1

G → R in AAA52448. Ref.10

Sequence conflict

50

1

H → Q in AAA52448. Ref.10

Sequence conflict

59

1

A → R in AAA52448. Ref.10

Secondary structure

1

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288

Helix Strand Turn

Details...

Beta strand

136 – 139

4

Beta strand

151 – 153

3

Beta strand

156 – 161

6

Beta strand

163 – 167

5

Turn

168 – 171

4

Beta strand

172 – 176

5

Beta strand

182 – 185

4

Helix

191 – 193

3

Beta strand

195 – 199

5

Beta strand

201 – 203

3

Beta strand

204 – 209

6

Turn

210 – 213

4

Beta strand

214 – 218

5

Beta strand

220 – 222

3

Beta strand

224 – 229

6

Helix

232 – 234

3

Beta strand

236 – 240

5

Helix

242 – 244

3

Beta strand

246 – 253

8

Beta strand

264 – 266

3

Helix

269 – 271

3

Helix

277 – 279

3

Beta strand

281 – 285

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 13, 2009. Version 3. Checksum: EAE98552A39D5E19	FASTA	288	30,770
	10 20 30 40 50 60 MVGVGGGDVE DVTPRPGGCQ ISGRGARGCN GIPGAAAWEA ALPRRRPRRH PSVNPRSRAA 70 80 90 100 110 120 GSPRTRGRRT EERPSGSRLG DRGRGRALPG GRLGGRGRGR APERVGGRGR GRGTAAPRAA 130 140 150 160 170 180 PAARGSRPGP AGTMAAGSIT TLPALPEDGG SGAFPPGHFK DPKRLYCKNG GFFLRIHPDG 190 200 210 220 230 240 RVDGVREKSD PHIKLQLQAE ERGVVSIKGV CANRYLAMKE DGRLLASKCV TDECFFFERL 250 260 270 280 ESNNYNTYRS RKYTSWYVAL KRTGQYKLGS KTGPGQKAIL FLPMSAKS
	Isoform 2 [UniParc]. Checksum: A21C7A6E82E4F5BD	FASTA	210	22,623
	10 20 30 40 50 60 MGDRGRGRAL PGGRLGGRGR GRAPERVGGR GRGRGTAAPR AAPAARGSRP GPAGTMAAGS 70 80 90 100 110 120 ITTLPALPED GGSGAFPPGH FKDPKRLYCK NGGFFLRIHP DGRVDGVREK SDPHIKLQLQ 130 140 150 160 170 180 AEERGVVSIK GVCANRYLAM KEDGRLLASK CVTDECFFFE RLESNNYNTY RSRKYTSWYV 190 200 210 ALKRTGQYKL GSKTGPGQKA ILFLPMSAKS
	Isoform 3 [UniParc]. Checksum: BE6CE13373007129	FASTA	155	17,254
	10 20 30 40 50 60 MAAGSITTLP ALPEDGGSGA FPPGHFKDPK RLYCKNGGFF LRIHPDGRVD GVREKSDPHI 70 80 90 100 110 120 KLQLQAEERG VVSIKGVCAN RYLAMKEDGR LLASKCVTDE CFFFERLESN NYNTYRSRKY 130 140 150 TSWYVALKRT GQYKLGSKTG PGQKAILFLP MSAKS
	Isoform 4 [UniParc]. Checksum: D6B5447137E60343	FASTA	196	21,203
	10 20 30 40 50 60 MGGRGRGRAP ERVGGRGRGR GTAAPRAAPA ARGSRPGPAG TMAAGSITTL PALPEDGGSG 70 80 90 100 110 120 AFPPGHFKDP KRLYCKNGGF FLRIHPDGRV DGVREKSDPH IKLQLQAEER GVVSIKGVCA 130 140 150 160 170 180 NRYLAMKEDG RLLASKCVTD ECFFFERLES NNYNTYRSRK YTSWYVALKR TGQYKLGSKT 190 GPGQKAILFL PMSAKS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human basic fibroblast growth factor: nucleotide sequence, genomic organization, and expression in mammalian cells." Abraham J.A., Whang J.L., Tumolo A., Mergia A., Fiddes J.C. Cold Spring Harb. Symp. Quant. Biol. 51:657-668(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Human basic fibroblast growth factor: nucleotide sequence and genomic organization." Abraham J.A., Whang J.L., Tumolo A., Mergia A., Friedman J., Gospodarowicz D., Fiddes J.C. EMBO J. 5:2523-2528(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
[3]	"High molecular mass forms of basic fibroblast growth factor are initiated by alternative CUG codons." Prats H., Kaghad M., Prats A.C., Klagsbrun M., Lelias J.M., Liauzun P., Chalon P., Tauber J.P., Amalric F., Smith J.A., Caput D. Proc. Natl. Acad. Sci. U.S.A. 86:1836-1840(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), PROTEIN SEQUENCE OF 126-145 (ISOFORMS 1/2/4), ALTERNATIVE INITIATION. Tissue: Hepatoma.
[4]	"Human protein factory for converting the transcriptome into an in vitro-expressed proteome." Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N. Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[5]	NIEHS SNPs program Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"Basic fibroblast growth factor gene expression." Florkiewicz R.Z., Shibata F., Barankiewicz T., Baird A., Gonzalez A.M., Florkiewicz E., Shah N. Ann. N. Y. Acad. Sci. 638:109-126(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-192.
[9]	"Mutations in the 5' untranslated region of the FGF-2 gene." Handschug K., Archoukieh E., Glaeser C. Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-192. Tissue: Blood.
[10]	"Cloning and expression of cDNA encoding human basic fibroblast growth factor." Kurokawa T., Sasada R., Iwane M., Igarashi K. FEBS Lett. 213:189-194(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-288 (ISOFORM 1).
[11]	"Characterization of high-molecular-mass forms of basic fibroblast growth factor produced by hepatocellular carcinoma cells: possible involvement of basic fibroblast growth factor in hepatocarcinogenesis." Shimoyama Y., Gotoh M., Ino Y., Sakamoto M., Kato K., Hirohashi S. Jpn. J. Cancer Res. 82:1263-1270(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 94-107 AND 162-173, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY. Tissue: Hepatoma.
[12]	"Human amniotic tumor that induces new bone formation in vivo produces growth-regulatory activity in vitro for osteoblasts identified as an extended form of basic fibroblast growth factor." Izbicka E., Dunstan C., Esparza J., Jacobs C., Sabatini M., Mundy G.R. Cancer Res. 56:633-636(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 125-140 (ISOFORMS 1/2/4).
[13]	"A form of human basic fibroblast growth factor with an extended amino terminus." Sommer A., Brewer M.T., Thompson R.C., Moscatelli D., Presta M., Rifkin D.B. Biochem. Biophys. Res. Commun. 144:543-550(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 132-288 (ISOFORMS 1/2/4), PROTEIN SEQUENCE OF 132-148; 153-160; 165-247; 252-261 AND 267-288 (ISOFORMS 2/4). Tissue: Hepatoma and Placenta.
[14]	"Amino-terminal sequence of a large form of basic fibroblast growth factor isolated from human benign prostatic hyperplastic tissue." Story M.T., Esch F., Shimasaki S., Sasse J., Jacobs S.C., Lawson R.K. Biochem. Biophys. Res. Commun. 142:702-709(1987) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 135-155 (ISOFORMS 1/2/3/4).
[15]	Zhang H.J., Zhang S.M., Zhuang H. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 143-288 (ISOFORMS 1/2/3/4).
[16]	"Human brain-derived acidic and basic fibroblast growth factors: amino terminal sequences and specific mitogenic activities." Gimenez-Gallego G., Conn G., Hatcher V.B., Thomas K.A. Biochem. Biophys. Res. Commun. 135:541-548(1986) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 143-172 (ISOFORMS 1/2/3/4).
[17]	"Partial molecular characterization of endothelial cell mitogens from human brain: acidic and basic fibroblast growth factors." Gautschi P., Frater-Schroeder M., Boehlen P. FEBS Lett. 204:203-207(1986) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 143-168 (ISOFORMS 1/2/3/4).
[18]	"Reverse transcription with nested polymerase chain reaction shows expression of basic fibroblast growth factor transcripts in human granulosa and cumulus cells from in vitro fertilisation patients." Watson R., Anthony F., Pickett M., Lambden P., Masson G.M., Thomas E.J. Biochem. Biophys. Res. Commun. 187:1227-1231(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 173-260 (ISOFORMS 1/2/3/4), TISSUE SPECIFICITY.
[19]	"Characterization and molecular cloning of a putative binding protein for heparin-binding growth factors." Wu D.Q., Kan M.K., Sato G.H., Okamoto T., Sato J.D. J. Biol. Chem. 266:16778-16785(1991) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH FGFBP1 AND FGF1.
[20]	"Receptor specificity of the fibroblast growth factor family." Ornitz D.M., Xu J., Colvin J.S., McEwen D.G., MacArthur C.A., Coulier F., Gao G., Goldfarb M. J. Biol. Chem. 271:15292-15297(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FGFR1; FGFR2; FGFR3 AND FGFR4, FUNCTION IN CELL PROLIFERATION.
[21]	"High-affinity binding of basic fibroblast growth factor and platelet-derived growth factor-AA to the core protein of the NG2 proteoglycan." Goretzki L., Burg M.A., Grako K.A., Stallcup W.B. J. Biol. Chem. 274:16831-16837(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CSPG4.
[22]	"Enhancement of fibroblast growth factor (FGF) activity by an FGF-binding protein." Tassi E., Al-Attar A., Aigner A., Swift M.R., McDonnell K., Karavanov A., Wellstein A. J. Biol. Chem. 276:40247-40253(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FGFBP1.
[23]	"Identification of ribosome-binding protein p34 as an intracellular protein that binds acidic fibroblast growth factor." Skjerpen C.S., Wesche J., Olsnes S. J. Biol. Chem. 277:23864-23871(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FGF1.
[24]	"Identification of the fibroblast growth factor (FGF)-interacting domain in a secreted FGF-binding protein by phage display." Xie B., Tassi E., Swift M.R., McDonnell K., Bowden E.T., Wang S., Ueda Y., Tomita Y., Riegel A.T., Wellstein A. J. Biol. Chem. 281:1137-1144(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FGFBP1.
[25]	"Tec-kinase-mediated phosphorylation of fibroblast growth factor 2 is essential for unconventional secretion." Ebert A.D., Laussmann M., Wegehingel S., Kaderali L., Erfle H., Reichert J., Lechner J., Beer H.D., Pepperkok R., Nickel W. Traffic 11:813-826(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-215, INTERACTION WITH TEC, SUBCELLULAR LOCATION.
[26]	"Cellular signaling by fibroblast growth factor receptors." Eswarakumar V.P., Lax I., Schlessinger J. Cytokine Growth Factor Rev. 16:139-149(2005) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[27]	"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.
[28]	"Nuclear import of exogenous FGF1 requires the ER-protein LRRC59 and the importins Kpnalpha1 and Kpnbeta1." Zhen Y., Sorensen V., Skjerpen C.S., Haugsten E.M., Jin Y., Walchli S., Olsnes S., Wiedlocha A. Traffic 13:650-664(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[29]	"Crystal structure of basic fibroblast growth factor at 1.6-A resolution." Ago H., Kitagawa Y., Fujishima A., Matsuura Y., Katsube Y. J. Biochem. 110:360-363(1991) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 143-288.
[30]	"Three-dimensional structure of human basic fibroblast growth factor." Eriksson A.E., Cousens L.S., Weaver L.H., Matthews B.W. Proc. Natl. Acad. Sci. U.S.A. 88:3441-3445(1991) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 143-288.
[31]	"Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin 1 beta." Zhang J., Cousens L.S., Barr P.J., Sprang S.R. Proc. Natl. Acad. Sci. U.S.A. 88:3446-3450(1991) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 143-288.
[32]	"Three-dimensional structures of acidic and basic fibroblast growth factors." Zhu X., Komiya H., Chirino A., Faham S., Fox G.M., Arakawa T., Hsu B.T., Rees D.C. Science 251:90-93(1991) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 135-288.
[33]	"Refinement of the structure of human basic fibroblast growth factor at 1.6-A resolution and analysis of presumed heparin binding sites by selenate substitution." Eriksson A.E., Cousens L.S., Matthews B.W. Protein Sci. 2:1274-1284(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 143-288.
[34]	"Structural basis for fibroblast growth factor receptor 2 activation in Apert syndrome." Ibrahimi O.A., Eliseenkova A.V., Plotnikov A.N., Yu K., Ornitz D.M., Mohammadi M. Proc. Natl. Acad. Sci. U.S.A. 98:7182-7187(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 134-288 IN COMPLEX WITH FGFR2.
[35]	"High-resolution solution structure of basic fibroblast growth factor determined by multidimensional heteronuclear magnetic resonance spectroscopy." Moy F.J., Seddon A.P., Boehlen P., Powers R. Biochemistry 35:13552-13561(1996) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 134-288.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X04431 Genomic DNA. Translation: CAA28027.1. Sequence problems.
X04432 Genomic DNA. Translation: CAA28028.1.
X04433 Genomic DNA. Translation: CAA28029.1.
J04513 mRNA. Translation: AAA52531.1.
J04513 mRNA. Translation: AAA52532.1.
J04513 mRNA. Translation: AAA52533.1.
AB451321 mRNA. Translation: BAG70135.1.
AB451450 mRNA. Translation: BAG70264.1.
EF506888 Genomic DNA. Translation: ABO43041.1. Sequence problems.
AC021205 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX05222.1. Sequence problems.
S81809 Genomic DNA. Translation: AAB21432.2. Sequence problems.
Y13468 Genomic DNA. Translation: CAA73868.1. Sequence problems.
M27968 mRNA. Translation: AAA52448.1. Frameshift.
M17599 mRNA. Translation: AAA52534.1.
AY820133 mRNA. Translation: AAV70487.1.
S47380 mRNA. Translation: AAD13853.1.

IPI

IPI00154603.
IPI00930195.
IPI00930557.
IPI00946154.

PIR

A32398.

RefSeq

NP_001997.5. NM_002006.4.

UniGene

Hs.284244.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BAS	X-ray	1.90	A	135-288	[»]
1BFB	X-ray	1.90	A	142-288	[»]
1BFC	X-ray	2.20	A	142-288	[»]
1BFF	X-ray	2.00	A	160-288	[»]
1BFG	X-ray	1.60	A	143-288	[»]
1BLA	NMR	-	A	134-288	[»]
1BLD	NMR	-	A	134-288	[»]
1CVS	X-ray	2.80	A/B	157-288	[»]
1EV2	X-ray	2.20	A/B/C/D	157-288	[»]
1FGA	X-ray	2.20	A	143-288	[»]
1FQ9	X-ray	3.00	A/B	157-288	[»]
1II4	X-ray	2.70	A/B/C/D	134-288	[»]
1IIL	X-ray	2.30	A/B/C/D	134-288	[»]
2BFH	X-ray	2.50	A	161-288	[»]
2FGF	X-ray	1.77	A	143-288	[»]
4FGF	X-ray	1.60	A	143-288	[»]

ProteinModelPortal

P09038.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4012N.

IntAct

P09038. 6 interactions.

MINT

MINT-222469.

PTM databases

PhosphoSite

P09038.

Polymorphism databases

DMDM

261260095.

Proteomic databases

PaxDb

P09038.

PRIDE

P09038.

Protocols and materials databases

DNASU

2247.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264498; ENSP00000264498; ENSG00000138685.

GeneID

2247.

KEGG

hsa:2247.

UCSC

uc003iev.1. human.

Organism-specific databases

CTD

2247.

GeneCards

GC04P123747.

HGNC

HGNC:3676. FGF2.

HPA

CAB000125.

MIM

134920. gene.

neXtProt

NX_P09038.

PharmGKB

PA28115.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG325757.

HOVERGEN

HBG107917.

InParanoid

P09038.

KO

K04358.

OrthoDB

EOG4K0QPR.

Enzyme and pathway databases

Pathway_Interaction_DB

angiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
fgf_pathway. FGF signaling pathway.
glypican_1pathway. Glypican 1 network.
avb3_integrin_pathway. Integrins in angiogenesis.
syndecan_4_pathway. Syndecan-4-mediated signaling events.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P09038.

Bgee

P09038.

CleanEx

HS_FGF2.

Genevestigator

P09038.

GermOnline

ENSG00000138685. Homo sapiens.

Family and domain databases

InterPro

IPR008996. Cytokine_IL1-like.
IPR002209. GF_heparin-bd.
IPR002348. IL1_HBGF.
[Graphical view]

PANTHER

PTHR11486. PTHR11486. 1 hit.

Pfam

PF00167. FGF. 1 hit.
[Graphical view]

PRINTS

PR00263. HBGFFGF.
PR00262. IL1HBGF.

SMART

SM00442. FGF. 1 hit.
[Graphical view]

SUPFAM

SSF50353. Cytok_IL1_like. 1 hit.

PROSITE

PS00247. HBGF_FGF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P09038.

ChEMBL

CHEMBL3107.

DrugBank

DB00686. Pentosan Polysulfate.

EvolutionaryTrace

P09038.

GenomeRNAi

2247.

NextBio

9095.

SOURCE

Search...

Entry information

Entry name

FGF2_HUMAN

Accession

Primary (citable) accession number: P09038
Secondary accession number(s): A4LBB8 , O00527, P78443, Q16443, Q5PY50, Q7KZ11, Q7KZ72, Q9UC54, Q9UCS5, Q9UCS6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	October 13, 2009
Last modified:	May 1, 2013
This is version 166 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.