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P19883 (FST_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Follistatin

Short name=FS
Alternative name(s):
Activin-binding protein
Gene names
Name:FST
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH).

Subunit structure

Monomer Potential.

Subcellular location

Secreted.

Tissue specificity

Isoform 1 is the predominant isoform inserum but is undetectable in follicular fluid. Ref.6

Sequence similarities

Contains 3 follistatin-like domains.

Contains 3 Kazal-like domains.

Contains 1 TB (TGF-beta binding) domain.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Inferred from electronic annotation. Source: Ensembl

female gonad development

Inferred from electronic annotation. Source: Ensembl

gamete generation

Inferred from electronic annotation. Source: Ensembl

hair follicle morphogenesis

Inferred from electronic annotation. Source: Ensembl

hematopoietic progenitor cell differentiation

Inferred from direct assay PubMed 15451575. Source: UniProtKB

keratinocyte proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of activin receptor signaling pathway

Inferred from direct assay PubMed 11948405PubMed 12697670. Source: UniProtKB

negative regulation of cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12702211. Source: UniProtKB

odontogenesis of dentin-containing tooth

Inferred from electronic annotation. Source: Ensembl

pattern specification process

Inferred from electronic annotation. Source: Ensembl

positive regulation of hair follicle development

Inferred from direct assay PubMed 12514121. Source: MGI

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionactivin binding

Inferred from physical interaction PubMed 12697670. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.7. Source: UniProtKB

signal transducer activity

Non-traceable author statement PubMed 12702211. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P19883-1)

Also known as: FS315; FS-315;

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.
Isoform 2 (identifier: P19883-2)

Also known as: FS288; FS-288;

The sequence of this isoform differs from the canonical sequence as follows:
     318-344: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Ref.5
Chain30 – 344315Follistatin
PRO_0000010103

Regions

Domain30 – 10374TB
Domain94 – 11724Follistatin-like 1
Domain112 – 16655Kazal-like 1
Domain167 – 19024Follistatin-like 2
Domain186 – 24156Kazal-like 2
Domain244 – 26825Follistatin-like 3
Domain264 – 31855Kazal-like 3
Compositional bias321 – 33313Asp/Glu-rich (highly acidic)

Amino acid modifications

Glycosylation1241N-linked (GlcNAc...) Potential
Glycosylation2881N-linked (GlcNAc...) Potential
Disulfide bond32 ↔ 55 Ref.7 Ref.8 Ref.9
Disulfide bond42 ↔ 88 Ref.7 Ref.8 Ref.9
Disulfide bond56 ↔ 91 Ref.7 Ref.8 Ref.9
Disulfide bond95 ↔ 106 Ref.7 Ref.8 Ref.9
Disulfide bond100 ↔ 116 Ref.7 Ref.8 Ref.9
Disulfide bond118 ↔ 150 Ref.7 Ref.8 Ref.9
Disulfide bond122 ↔ 143 Ref.7 Ref.8 Ref.9
Disulfide bond132 ↔ 164 Ref.7 Ref.8 Ref.9
Disulfide bond192 ↔ 225 Ref.7 Ref.8 Ref.9
Disulfide bond196 ↔ 218 Ref.7 Ref.8 Ref.9
Disulfide bond207 ↔ 239 Ref.7 Ref.8 Ref.9
Disulfide bond270 ↔ 302 Ref.7 Ref.8 Ref.9
Disulfide bond274 ↔ 295 Ref.7 Ref.8 Ref.9
Disulfide bond284 ↔ 316 Ref.7 Ref.8 Ref.9

Natural variations

Alternative sequence318 – 34427Missing in isoform 2.
VSP_001565
Natural variant1521E → Q.
Corresponds to variant rs11745088 [ dbSNP | Ensembl ].
VAR_049091

Secondary structure

............................................................. 344
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (FS315) (FS-315) [UniParc].

Last modified October 10, 2002. Version 2.
Checksum: D9BB45055D84AC90

FASTA34438,007
        10         20         30         40         50         60 
MVRARHQPGG LCLLLLLLCQ FMEDRSAQAG NCWLRQAKNG RCQVLYKTEL SKEECCSTGR 

        70         80         90        100        110        120 
LSTSWTEEDV NDNTLFKWMI FNGGAPNCIP CKETCENVDC GPGKKCRMNK KNKPRCVCAP 

       130        140        150        160        170        180 
DCSNITWKGP VCGLDGKTYR NECALLKARC KEQPELEVQY QGRCKKTCRD VFCPGSSTCV 

       190        200        210        220        230        240 
VDQTNNAYCV TCNRICPEPA SSEQYLCGND GVTYSSACHL RKATCLLGRS IGLAYEGKCI 

       250        260        270        280        290        300 
KAKSCEDIQC TGGKKCLWDF KVGRGRCSLC DELCPDSKSD EPVCASDNAT YASECAMKEA 

       310        320        330        340 
ACSSGVLLEV KHSGSCNSIS EDTEEEEEDE DQDYSFPISS ILEW 

« Hide

Isoform 2 (FS288) (FS-288) [UniParc].

Checksum: B516643224C7F8FF
Show »

FASTA31734,803

References

« Hide 'large scale' references
[1]"Primary structure of the human follistatin precursor and its genomic organization."
Shimasaki S., Koga M., Esch F., Cooksey K., Mercado M., Koba A., Ueno N., Ying S.-Y., Ling N., Guillemin R.
Proc. Natl. Acad. Sci. U.S.A. 85:4218-4222(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
[2]"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. expand/collapse author list , 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 2).
[3]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. expand/collapse author list , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORM 1).
Tissue: Pancreas.
[5]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 30-44.
[6]"Differential distribution of follistatin isoforms: application of a new FS315-specific immunoassay."
Schneyer A.L., Wang Q., Sidis Y., Sluss P.M.
J. Clin. Endocrinol. Metab. 89:5067-5075(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"The structure of the follistatin:activin complex reveals antagonism of both type I and type II receptor binding."
Thompson T.B., Lerch T.F., Cook R.W., Woodruff T.K., Jardetzky T.S.
Dev. Cell 9:535-543(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 30-317 IN COMPLEX WITH ACTIVIN A, DISULFIDE BONDS.
[8]"Structural and biophysical coupling of heparin and activin binding to follistatin isoform functions."
Lerch T.F., Shimasaki S., Woodruff T.K., Jardetzky T.S.
J. Biol. Chem. 282:15930-15939(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 30-344 IN COMPLEX WITH ACTIVIN A, DISULFIDE BONDS.
[9]"The structure of myostatin:follistatin 288: insights into receptor utilization and heparin binding."
Cash J.N., Rejon C.A., McPherron A.C., Bernard D.J., Thompson T.B.
EMBO J. 28:2662-2676(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 30-317 IN COMPLEX WITH MOUSE GDF8, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M19481, M19480 Genomic DNA. Translation: AAA35851.1.
AB451330 mRNA. Translation: BAG70144.1.
AB451474 mRNA. Translation: BAG70288.1.
CH471123 Genomic DNA. Translation: EAW54880.1.
BC004107 mRNA. Translation: AAH04107.1.
CCDSCCDS3959.1. [P19883-1]
CCDS43315.1. [P19883-2]
PIRA32141.
RefSeqNP_006341.1. NM_006350.3. [P19883-2]
NP_037541.1. NM_013409.2. [P19883-1]
UniGeneHs.9914.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2B0UX-ray2.80C/D30-317[»]
2P6AX-ray3.40C/D30-344[»]
3HH2X-ray2.15C/D30-317[»]
ProteinModelPortalP19883.
SMRP19883. Positions 30-317.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115731. 8 interactions.
IntActP19883. 9 interactions.
MINTMINT-3009113.
STRING9606.ENSP00000256759.

Protein family/group databases

MEROPSI01.966.

Polymorphism databases

DMDM23831079.

Proteomic databases

MaxQBP19883.
PaxDbP19883.
PRIDEP19883.

Protocols and materials databases

DNASU10468.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000256759; ENSP00000256759; ENSG00000134363. [P19883-1]
ENST00000396947; ENSP00000380151; ENSG00000134363. [P19883-2]
GeneID10468.
KEGGhsa:10468.
UCSCuc003jpc.3. human. [P19883-1]

Organism-specific databases

CTD10468.
GeneCardsGC05P052776.
HGNCHGNC:3971. FST.
HPACAB026025.
HPA018155.
MIM136470. gene.
neXtProtNX_P19883.
Orphanet3185. Polycystic ovary syndrome.
PharmGKBPA28388.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG267610.
HOGENOMHOG000261649.
HOVERGENHBG051666.
InParanoidP19883.
KOK04661.
OMAEAVCASD.
OrthoDBEOG7GBFXR.
PhylomeDBP19883.
TreeFamTF106409.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressP19883.
BgeeP19883.
CleanExHS_FST.
GenevestigatorP19883.

Family and domain databases

InterProIPR003645. Fol_N.
IPR015369. Follistatin/Osteonectin_EGF.
IPR002350. Kazal_dom.
IPR017878. TB_dom.
[Graphical view]
PfamPF09289. FOLN. 1 hit.
PF00050. Kazal_1. 3 hits.
[Graphical view]
SMARTSM00274. FOLN. 3 hits.
SM00280. KAZAL. 3 hits.
[Graphical view]
SUPFAMSSF57581. SSF57581. 1 hit.
PROSITEPS51465. KAZAL_2. 3 hits.
PS51364. TB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP19883.
GeneWikiFollistatin.
GenomeRNAi10468.
NextBio39699.
PROP19883.
SOURCESearch...

Entry information

Entry nameFST_HUMAN
AccessionPrimary (citable) accession number: P19883
Secondary accession number(s): B5BU94, Q9BTH0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 10, 2002
Last modified: July 9, 2014
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM