[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=3472745 [NCBI, ExPASy, EBI, Israel, Japan] Abraham J.A., Whang J.L., Tumolo A., Mergia A., Fiddes J.C.; "Human basic fibroblast growth factor: nucleotide sequence, genomic organization, and expression in mammalian cells."; Cold Spring Harb. Symp. Quant. Biol. 51:657-668(1986).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2). PubMed=3780670 [NCBI, ExPASy, EBI, Israel, Japan] Abraham J.A., Whang J.L., Tumolo A., Mergia A., Friedman J., Gospodarowicz D., Fiddes J.C.; "Human basic fibroblast growth factor: nucleotide sequence and genomic organization."; EMBO J. 5:2523-2528(1986).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). DOI=10.1016/0014-5793(87)81489-8; PubMed=2435575 [NCBI, ExPASy, EBI, Israel, Japan] Kurokawa T., Sasada R., Iwane M., Igarashi K.; "Cloning and expression of cDNA encoding human basic fibroblast growth factor."; FEBS Lett. 213:189-194(1987).
[4]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), PROTEIN SEQUENCE OF 48-67, AND ALTERNATIVE INITIATION. TISSUE=Hepatoma; DOI=10.1073/pnas.86.6.1836; PubMed=2538817 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "High molecular mass forms of basic fibroblast growth factor are initiated by alternative CUG codons."; Proc. Natl. Acad. Sci. U.S.A. 86:1836-1840(1989).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). DOI=10.1038/nmeth.1273; PubMed=19054851 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."; Nat. Methods 5:1011-1017(2008).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. NIEHS SNPs program; Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
[7]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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.
[8]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-114. DOI=10.1111/j.1749-6632.1991.tb49022.x; PubMed=1785797 [NCBI, ExPASy, EBI, Israel, Japan] Florkiewicz R.Z., Shibata F., Barankiewicz T., Baird A., Gonzalez A.M., Florkiewicz E., Shah N.; "Basic fibroblast growth factor gene expression."; Ann. N. Y. Acad. Sci. 638:109-126(1991).
[9]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-114. TISSUE=Blood; Handschug K., Archoukieh E., Glaeser C.; "Mutations in the 5' untranslated region of the FGF-2 gene."; Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
[10]	PROTEIN SEQUENCE OF 47-62 (ISOFORMS 1/3). PubMed=8564983 [NCBI, ExPASy, EBI, Israel, Japan] Izbicka E., Dunstan C., Esparza J., Jacobs C., Sabatini M., Mundy G.R.; "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."; Cancer Res. 56:633-636(1996).
[11]	NUCLEOTIDE SEQUENCE [MRNA] OF 54-210 (ISOFORMS 1/3), AND PROTEIN SEQUENCE OF 54-70; 75-82; 87-169; 174-183 AND 189-210 (ISOFORMS 1/3). TISSUE=Hepatoma, and Placenta; DOI=10.1016/S0006-291X(87)80001-3; PubMed=3579930 [NCBI, ExPASy, EBI, Israel, Japan] Sommer A., Brewer M.T., Thompson R.C., Moscatelli D., Presta M., Rifkin D.B.; "A form of human basic fibroblast growth factor with an extended amino terminus."; Biochem. Biophys. Res. Commun. 144:543-550(1987).
[12]	PROTEIN SEQUENCE OF 57-77. DOI=10.1016/0006-291X(87)91471-9; PubMed=2435284 [NCBI, ExPASy, EBI, Israel, Japan] Story M.T., Esch F., Shimasaki S., Sasse J., Jacobs S.C., Lawson R.K.; "Amino-terminal sequence of a large form of basic fibroblast growth factor isolated from human benign prostatic hyperplastic tissue."; Biochem. Biophys. Res. Commun. 142:702-709(1987).
[13]	NUCLEOTIDE SEQUENCE [MRNA] OF 95-182 (ISOFORMS 1/2/3), AND TISSUE SPECIFICITY. DOI=10.1016/0006-291X(92)90434-M; PubMed=1417798 [NCBI, ExPASy, EBI, Israel, Japan] Watson R., Anthony F., Pickett M., Lambden P., Masson G.M., Thomas E.J.; "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."; Biochem. Biophys. Res. Commun. 187:1227-1231(1992).
[14]	NUCLEOTIDE SEQUENCE [MRNA] OF 65-210 (ISOFORMS 1/2/3). Zhang H.J., Zhang S.M., Zhuang H.; Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
[15]	PROTEIN SEQUENCE OF 65-94. DOI=10.1016/0006-291X(86)90028-8; PubMed=3964259 [NCBI, ExPASy, EBI, Israel, Japan] Gimenez-Gallego G., Conn G., Hatcher V.B., Thomas K.A.; "Human brain-derived acidic and basic fibroblast growth factors: amino terminal sequences and specific mitogenic activities."; Biochem. Biophys. Res. Commun. 135:541-548(1986).
[16]	PROTEIN SEQUENCE OF 65-90. DOI=10.1016/0014-5793(86)80812-2; PubMed=3732516 [NCBI, ExPASy, EBI, Israel, Japan] Gautschi P., Frater-Schroeder M., Boehlen P.; "Partial molecular characterization of endothelial cell mitogens from human brain: acidic and basic fibroblast growth factors."; FEBS Lett. 204:203-207(1986).
[17]	IDENTIFICATION IN A COMPLEX WITH FGFBP1 AND FGF1. PubMed=1885605 [NCBI, ExPASy, EBI, Israel, Japan] Wu D.Q., Kan M.K., Sato G.H., Okamoto T., Sato J.D.; "Characterization and molecular cloning of a putative binding protein for heparin-binding growth factors."; J. Biol. Chem. 266:16778-16785(1991).
[18]	INTERACTION WITH CSPG4. DOI=10.1074/jbc.274.24.16831; PubMed=10358027 [NCBI, ExPASy, EBI, Israel, Japan] Goretzki L., Burg M.A., Grako K.A., Stallcup W.B.; "High-affinity binding of basic fibroblast growth factor and platelet-derived growth factor-AA to the core protein of the NG2 proteoglycan."; J. Biol. Chem. 274:16831-16837(1999).
[19]	INTERACTION WITH FGFBP1. DOI=10.1074/jbc.M104933200; PubMed=11509569 [NCBI, ExPASy, EBI, Israel, Japan] Tassi E., Al-Attar A., Aigner A., Swift M.R., McDonnell K., Karavanov A., Wellstein A.; "Enhancement of fibroblast growth factor (FGF) activity by an FGF-binding protein."; J. Biol. Chem. 276:40247-40253(2001).
[20]	INTERACTION WITH FGFBP1. DOI=10.1074/jbc.M510754200; PubMed=16257968 [NCBI, ExPASy, EBI, Israel, Japan] Xie B., Tassi E., Swift M.R., McDonnell K., Bowden E.T., Wang S., Ueda Y., Tomita Y., Riegel A.T., Wellstein A.; "Identification of the fibroblast growth factor (FGF)-interacting domain in a secreted FGF-binding protein by phage display."; J. Biol. Chem. 281:1137-1144(2006).
[21]	X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). PubMed=1769963 [NCBI, ExPASy, EBI, Israel, Japan] Ago H., Kitagawa Y., Fujishima A., Matsuura Y., Katsube Y.; "Crystal structure of basic fibroblast growth factor at 1.6-A resolution."; J. Biochem. 110:360-363(1991).
[22]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). DOI=10.1073/pnas.88.8.3441; PubMed=1707542 [NCBI, ExPASy, EBI, Israel, Japan] Eriksson A.E., Cousens L.S., Weaver L.H., Matthews B.W.; "Three-dimensional structure of human basic fibroblast growth factor."; Proc. Natl. Acad. Sci. U.S.A. 88:3441-3445(1991).
[23]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). DOI=10.1073/pnas.88.8.3446; PubMed=1849658 [NCBI, ExPASy, EBI, Israel, Japan] Zhang J., Cousens L.S., Barr P.J., Sprang S.R.; "Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin 1 beta."; Proc. Natl. Acad. Sci. U.S.A. 88:3446-3450(1991).
[24]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). DOI=10.1126/science.1702556; PubMed=1702556 [NCBI, ExPASy, EBI, Israel, Japan] Zhu X., Komiya H., Chirino A., Faham S., Fox G.M., Arakawa T., Hsu B.T., Rees D.C.; "Three-dimensional structures of acidic and basic fibroblast growth factors."; Science 251:90-93(1991).
[25]	X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). PubMed=7691311 [NCBI, ExPASy, EBI, Israel, Japan] Eriksson A.E., Cousens L.S., Matthews B.W.; "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."; Protein Sci. 2:1274-1284(1993).
[26]	X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 79-210 IN COMPLEX WITH FGFR2. DOI=10.1073/pnas.121183798; PubMed=11390973 [NCBI, ExPASy, EBI, Israel, Japan] Ibrahimi O.A., Eliseenkova A.V., Plotnikov A.N., Yu K., Ornitz D.M., Mohammadi M.; "Structural basis for fibroblast growth factor receptor 2 activation in Apert syndrome."; Proc. Natl. Acad. Sci. U.S.A. 98:7182-7187(2001).
[27]	STRUCTURE BY NMR. DOI=10.1021/bi961260p; PubMed=8885834 [NCBI, ExPASy, EBI, Israel, Japan] Moy F.J., Seddon A.P., Boehlen P., Powers R.; "High-resolution solution structure of basic fibroblast growth factor determined by multidimensional heteronuclear magnetic resonance spectroscopy."; Biochemistry 35:13552-13561(1996).

Comments

FUNCTION: The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
SUBUNIT: Monomer. Interacts with CSPG4 and FGFBP1. Found in a complex with FGFBP1, FGF1 and FGF2.
INTERACTION:
P29466:CASP1; NbExp=1; IntAct=EBI-977447, EBI-516667;
Q14512:FGFBP1; NbExp=3; IntAct=EBI-977447, EBI-953742;
P21802-5:FGFR2; NbExp=1; IntAct=EBI-977447, EBI-1028732;

ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative initiation.

Name	1
Isoform ID	P09038-1
Note: Starts at an alternative CUG codon.
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	P09038-2
Features which should be applied to build the isoform sequence: VSP_037383.

Name	3
Isoform ID	P09038-3
Note: Starts at an alternative CUG codon.
Features which should be applied to build the isoform sequence: VSP_037384, VSP_037385.

TISSUE SPECIFICITY: Expressed in granulosa and cumulus cells.
PTM: Several N-termini starting at positions 48, 54, 47 and 65 have been identified by direct sequencing.
MISCELLANEOUS: This protein binds heparin more strongly than does aFGF.
SIMILARITY: Belongs to the heparin-binding growth factors family.
SEQUENCE CAUTION:
- Sequence=AAB21432.2; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/fgf2/";.

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

X04431; CAA28027.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X04432; CAA28028.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X04433; CAA28029.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M27968; AAA52448.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J04513; AAA52531.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J04513; AAA52532.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J04513; AAA52533.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB451321; BAG70135.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB451450; BAG70264.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
EF506888; ABO43041.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471056; EAX05222.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S81809; AAB21432.2; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Y13468; CAA73868.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M17599; AAA52534.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY820133; AAV70487.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S47380; AAD13853.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00154603; -.

A32398; A32398.

NP_001997.5; -.

3D structure databases

PDB

1BAS; X-ray; 1.90 A; A=57-210.	[ExPASy / RCSB / EBI]
1BFB; X-ray; 1.90 A; A=64-210.	[ExPASy / RCSB / EBI]
1BFC; X-ray; 2.20 A; A=64-210.	[ExPASy / RCSB / EBI]
1BFF; X-ray; 2.00 A; A=82-210.	[ExPASy / RCSB / EBI]
1BFG; X-ray; 1.60 A; A=65-210.	[ExPASy / RCSB / EBI]
1BLA; NMR; -; A=56-210.	[ExPASy / RCSB / EBI]
1BLD; NMR; -; A=56-210.	[ExPASy / RCSB / EBI]
1CVS; X-ray; 2.80 A; A/B=79-210.	[ExPASy / RCSB / EBI]
1EV2; X-ray; 2.20 A; A/B/C/D=79-210.	[ExPASy / RCSB / EBI]
1FGA; X-ray; 2.20 A; A=65-210.	[ExPASy / RCSB / EBI]
1FQ9; X-ray; 3.00 A; A/B=79-210.	[ExPASy / RCSB / EBI]
1II4; X-ray; 2.70 A; A/B/C/D=56-210.	[ExPASy / RCSB / EBI]
1IIL; X-ray; 2.30 A; A/B/C/D=56-210.	[ExPASy / RCSB / EBI]
2BFH; X-ray; 2.50 A; A=83-210.	[ExPASy / RCSB / EBI]
2FGF; X-ray; 1.77 A; A=65-210.	[ExPASy / RCSB / EBI]
4FGF; X-ray; 1.60 A; A=65-210.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1BAS; -.
1BFB; -.
1BFC; -.
1BFF; -.
1BFG; -.
1BLA; -.
1BLD; -.
1CVS; -.
1EV2; -.
1FGA; -.
1FQ9; -.
1II4; -.
1IIL; -.
2BFH; -.
2FGF; -.
4FGF; -.

ModBase

P09038.

Protein-protein interaction databases

DIP

DIP:4012N; -.

IntAct

P09038; 5.

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_9470; Signaling by FGFR.

Organism-specific databases

GC04P124027; -.

HIX0031422; -.

HGNC:3676; FGF2.

CAB000125; -.

134920; gene. [NCBI / EBI]

PharmGKB

PA28115; -.

Gene expression databases

P09038; -.

P09038; -.

HS_FGF2; -.

ENSG00000138685; Homo sapiens.

Ontologies

GO:0005615;	Cellular component: extracellular space (traceable author statement from ProtInc).
GO:0008083;	Molecular function: growth factor activity (inferred from electronic annotation from UniProtKB-KW).
GO:0008201;	Molecular function: heparin binding (inferred from electronic annotation from UniProtKB-KW).
GO:0000187;	Biological process: activation of MAPK activity (traceable author statement from ProtInc).
GO:0001525;	Biological process: angiogenesis (inferred from electronic annotation from UniProtKB-KW).
GO:0008283;	Biological process: cell proliferation (inferred from electronic annotation from UniProtKB-KW).
GO:0006935;	Biological process: chemotaxis (traceable author statement from ProtInc).
GO:0008543;	Biological process: fibroblast growth factor receptor signaling pathway (inferred from experiment from Reactome).
GO:0043537;	Biological process: negative regulation of blood vessel endothelial cell migration (inferred from direct assay from UniProtKB).
GO:0043536;	Biological process: positive regulation of blood vessel endothelial cell migration (inferred from direct assay from UniProtKB).
GO:0060045;	Biological process: positive regulation of cardiac muscle cell proliferation (inferred from direct assay from UniProtKB).
GO:0007265;	Biological process: Ras protein signal transduction (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

ProDom

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

PROSITE

PS00247; HBGF_FGF; 1.

Other

SWISS-3DIMAGE

P09038.

Proteomic databases

PRIDE

P09038; -.

Genome annotation databases

Ensembl

ENSG00000138685; Homo sapiens. [Contig view]

GeneID

2247; -.

KEGG

hsa:2247; -.

Phylogenomic databases

HOVERGEN

P09038; -.

Other

DrugBank

DB00686; Pentosan Polysulfate.

9095; -.

FGF2; Homo sapiens.

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

Keywords

3D-structure; Alternative initiation; Angiogenesis; Developmental protein; Differentiation; Direct protein sequencing; Growth factor; Heparin-binding; Mitogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`PROPEP`	`1 64`	`64`	`Or 47, or 53, or 46.`	`PRO_0000008932`
`CHAIN`	`65 210`	`146`	`Heparin-binding growth factor 2.`	`PRO_0000008933`
`REGION`	`183 199`	`17`	`Heparin-binding (By similarity).`
`MOTIF`	`101 103`	`3`	`Cell attachment site; atypical (Potential).`
`MOTIF`	`143 145`	`3`	`Cell attachment site; atypical (Potential).`
`BINDING`	`91 91`		`Heparin (By similarity).`
`VAR_SEQ`	`1 55`		`Missing (in isoform 2).`	`VSP_037383`
`VAR_SEQ`	`1 14`		`Missing (in isoform 3).`	`VSP_037384`
`VAR_SEQ`	`15 15`		`L -> M (in isoform 3).`	`VSP_037385`
`STRAND`	`85 89`	`5`
`TURN`	`90 93`	`4`
`STRAND`	`94 98`	`5`
`STRAND`	`104 107`	`4`
`HELIX`	`113 115`	`3`
`STRAND`	`117 123`	`7`
`STRAND`	`126 131`	`6`
`TURN`	`132 135`	`4`
`STRAND`	`136 140`	`5`
`STRAND`	`146 151`	`6`
`HELIX`	`154 156`	`3`
`STRAND`	`158 162`	`5`
`STRAND`	`168 175`	`8`
`STRAND`	`186 188`	`3`
`HELIX`	`191 193`	`3`
`HELIX`	`199 201`	`3`
`STRAND`	`203 206`	`4`

Sequence information

Length: 210 AA [This is the length of the unprocessed precursor]

Molecular weight: 22623 Da [This is the MW of the unprocessed precursor]

CRC64: A21C7A6E82E4F5BD [This is a checksum on the sequence]

        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

P09038 in FASTA 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