P09038 (FGF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heparin-binding growth factor 2
Short name=HBGF-2

Alternative name(s):
Basic fibroblast growth factor
Short name=bFGF

Gene names

Name:	FGF2
Synonyms:	FGFB

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.20 Ref.21 Ref.22 Ref.23 Ref.24
Subcellular location	Secreted. Note: Exported from cells by an endoplasmic reticulum (ER)/Golgi-independent mechanism. Unconventional secretion of FGF2 occurs by direct translocation across the plasma membrane. Ref.24
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	Secreted
Coding sequence diversity	Alternative initiation
Ligand	Heparin-binding
Molecular function	Developmental protein Growth factor Mitogen
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	Ras protein signal transduction Traceable author statement. Source: ProtInc activation of MAPK activity Traceable author statement. Source: ProtInc branching involved in ureteric bud morphogenesis Inferred from direct assay. Source: UniProtKB cell migration involved in sprouting angiogenesis Inferred from direct assay. Source: BHF-UCL chondroblast differentiation Inferred from direct assay. Source: UniProtKB embryonic morphogenesis Traceable author statement. Source: DFLAT fibroblast growth factor receptor signaling pathway Inferred from direct assay. Source: UniProtKB inositol phosphate biosynthetic process Inferred from direct assay. Source: DFLAT insulin receptor signaling pathway Traceable author statement. Source: Reactome negative regulation of blood vessel endothelial cell migration Inferred from direct assay. Source: BHF-UCL negative regulation of cell death Inferred from direct assay. Source: UniProtKB organ morphogenesis Traceable author statement. Source: ProtInc phosphatidylinositol biosynthetic process Inferred from direct assay. Source: DFLAT positive regulation of ERK1 and ERK2 cascade Inferred from direct assay. Source: UniProtKB positive regulation of angiogenesis Inferred from direct assay. Source: DFLAT positive regulation of blood vessel endothelial cell migration Inferred from direct assay. Source: BHF-UCL positive regulation of cardiac muscle cell proliferation Inferred from direct assay. 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. Source: MGI positive regulation of endothelial cell proliferation Inferred from mutant phenotype. Source: BHF-UCL positive regulation of phosphatidylinositol 3-kinase activity Inferred from direct assay. Source: DFLAT positive regulation of phospholipase C activity Inferred from direct assay. Source: DFLAT positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay. Source: BHF-UCL release of sequestered calcium ion into cytosol Inferred from direct assay. Source: DFLAT wound healing Traceable author statement. Source: DFLAT
Cellular component	extracellular space Traceable author statement. Source: ProtInc
Molecular function	chemoattractant activity Inferred from direct assay. Source: BHF-UCL cytokine activity Inferred from direct assay. Source: BHF-UCL fibroblast growth factor receptor binding Inferred from physical interaction. Source: MGI growth factor activity Inferred from direct assay. Source: BHF-UCL heparin binding Inferred from electronic annotation. Source: UniProtKB-KW ligand-dependent nuclear receptor transcription coactivator activity Inferred from direct assay. Source: UniProtKB protein tyrosine kinase activity Traceable author statement. Source: Reactome
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

Heparin-binding 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

215

1

Phosphotyrosine; by TEC Ref.24

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

163 – 167

5

Turn

168 – 171

4

Beta strand

172 – 176

5

Beta strand

182 – 185

4

Helix

191 – 193

3

Beta strand

195 – 201

7

Beta strand

204 – 209

6

Turn

210 – 213

4

Beta strand

214 – 218

5

Beta strand

224 – 229

6

Helix

232 – 234

3

Beta strand

236 – 240

5

Beta strand

246 – 253

8

Beta strand

264 – 266

3

Helix

269 – 271

3

Helix

277 – 279

3

Beta strand

281 – 284

4

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: 3472745] [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: 3780670] [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: 2538817] [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: 19054851] [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: 15815621] [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: 1785797] [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: 2435575] [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: 1721615] [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: 8564983] [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: 3579930] [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: 2435284] [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: 3964259] [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: 3732516] [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: 1417798] [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: 1885605] [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: 8663044] [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: 10358027] [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: 11509569] [Abstract] Cited for: INTERACTION WITH FGFBP1.
[23]	"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: 16257968] [Abstract] Cited for: INTERACTION WITH FGFBP1.
[24]	"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: 20230531] [Abstract] Cited for: PHOSPHORYLATION AT TYR-215, INTERACTION WITH TEC, SUBCELLULAR LOCATION.
[25]	"Cellular signaling by fibroblast growth factor receptors." Eswarakumar V.P., Lax I., Schlessinger J. Cytokine Growth Factor Rev. 16:139-149(2005) [PubMed: 15863030] [Abstract] Cited for: REVIEW.
[26]	"Fibroblast growth factor signalling: from development to cancer." Turner N., Grose R. Nat. Rev. Cancer 10:116-129(2010) [PubMed: 20094046] [Abstract] Cited for: REVIEW.
[27]	"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: 1769963] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 143-288.
[28]	"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: 1707542] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 143-288.
[29]	"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: 1849658] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 143-288.
[30]	"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: 1702556] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 135-288.
[31]	"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: 7691311] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 143-288.
[32]	"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: 11390973] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 134-288 IN COMPLEX WITH FGFR2.
[33]	"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: 8885834] [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.

SMR

P09038. Positions 134-288.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4012N.

IntAct

P09038. 5 interactions.

MINT

MINT-222469.

STRING

P09038.

PTM databases

PhosphoSite

P09038.

Polymorphism databases

DMDM

261260095.

Proteomic databases

PRIDE

P09038.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264498; ENSP00000264498; ENSG00000138685.

GeneID

2247.

KEGG

hsa:2247.

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

prNOG13573.

GeneTree

ENSGT00600000084030.

HOVERGEN

HBG107917.

InParanoid

P09038.

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.

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]

KO

K04358.

PANTHER

PTHR11486. IL1_HBGF. 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

DrugBank

DB00686. Pentosan Polysulfate.

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:	January 25, 2012
This is version 153 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.