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Reviewed, UniProtKB/Swiss-Prot P19883 (FST_HUMAN)

Last modified July 7, 2009. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Follistatin
      Short name=FS
Alternative name(s):
    Activin-binding protein
Gene names
Name: FST
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

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

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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 in serum but is undetectable in follicular fluid. Ref.4

Sequence similarities

Contains 3 follistatin-like domains.

Contains 3 Kazal-like domains.

Contains 1 TB (TGF-beta binding) domain.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

ANGP039502EBI-1571188,EBI-525291
ANGP039502EBI-1571208,EBI-525291

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Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P19883-1)

Also known as: FS315;

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;

The sequence of this isoform differs from the canonical sequence as follows:
     318-344: Missing.
Isoform 3 (identifier: P19883-3)

Also known as: FS303;

The sequence of this isoform differs from the canonical sequence as follows:
     318-323: Missing.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Ref.3
Chain30 – 344315Follistatin
PRO_0000010103

Regions

Domain30 – 10374TB
Domain94 – 11724Follistatin-like 1
Domain118 – 16447Kazal-like 1
Domain167 – 19024Follistatin-like 2
Domain192 – 23948Kazal-like 2
Domain244 – 26825Follistatin-like 3
Domain270 – 31647Kazal-like 3
Compositional bias321 – 33313Asp/Glu-rich (highly acidic)

Amino acid modifications

Glycosylation1241N-linked (GlcNAc...) Potential
Glycosylation2881N-linked (GlcNAc...) Potential
Disulfide bond32 ↔ 55 Ref.5 Ref.6
Disulfide bond42 ↔ 88 Ref.5 Ref.6
Disulfide bond56 ↔ 91 Ref.5 Ref.6
Disulfide bond95 ↔ 106 Ref.5 Ref.6
Disulfide bond100 ↔ 116 Ref.5 Ref.6
Disulfide bond118 ↔ 150 Ref.5 Ref.6
Disulfide bond122 ↔ 143 Ref.5 Ref.6
Disulfide bond132 ↔ 164 Ref.5 Ref.6
Disulfide bond192 ↔ 225 Ref.5 Ref.6
Disulfide bond196 ↔ 218 Ref.5 Ref.6
Disulfide bond207 ↔ 239 Ref.5 Ref.6
Disulfide bond270 ↔ 302 Ref.5 Ref.6
Disulfide bond274 ↔ 295 Ref.5 Ref.6
Disulfide bond284 ↔ 316 Ref.5 Ref.6

Natural variations

Alternative sequence318 – 34427Missing in isoform 2.
VSP_001565
Alternative sequence318 – 3236Missing in isoform 3.
VSP_001566
Natural variant1521E → Q: dbSNP rs11745088.
VAR_049091

Secondary structure

1 .......................................................... 344
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (FS315) [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).

Checksum: B516643224C7F8FF
Show »

FASTA31734,803
Isoform 3 (FS303).

Checksum: 9EAA51B47F02E3B0
Show »

FASTA33837,375

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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: 3380788] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2 AND 3).
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Pancreas.
[3]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed: 15340161] [Abstract]
Cited for: PROTEIN SEQUENCE OF 30-44.
[4]"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: 15472207] [Abstract]
Cited for: TISSUE SPECIFICITY.
[5]"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: 16198295] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 30-317 IN COMPLEX WITH ACTIVIN A, DISULFIDE BONDS.
[6]"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: 17409095] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 30-344 IN COMPLEX WITH ACTIVIN A, DISULFIDE BONDS.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M19481, M19480 Genomic DNA. Translation: AAA35851.1.
BC004107 mRNA. Translation: AAH04107.1.
IPIIPI00021081.
IPI00217070.
IPI00217071.
PIRA32141.
RefSeqNP_037541.1.
UniGeneHs.9914

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2B0UX-ray2.80C/D30-317[»]
2P6AX-ray3.40C/D30-344[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP19883. 2 interactions.

Protein family/group databases

MEROPSI01.966.

Proteomic databases

PRIDEP19883.

Genome annotation databases

EnsemblENSG00000134363. Homo sapiens. [Contig view]
GeneID10468.
UCSCuc003jpc.1. human.
uc003jpd.1. human.

Organism-specific databases

GeneCardsGC05P052812.
H-InvDBHIX0004856.
HGNCHGNC:3971. FST.
HPAHPA018155.
MIM136470. gene.
Orphanet3185. Stein-Leventhal syndrome.
PharmGKBPA28388.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP19883.
HOVERGENP19883.
OMAP19883. CEDIQCS.

Enzyme and pathway databases

Pathway_Interaction_DBbmppathway. BMP receptor signaling.

Gene expression databases

ArrayExpressP19883.
BgeeP19883.
CleanExHS_FST.
GermOnlineENSG00000134363. Homo sapiens.

Family and domain databases

InterProIPR003645. Fol_N.
IPR015369. Follistatin/Osteonectin_EGF.
IPR012913. PRKCSH.
IPR002350. Prot_inh_Kazal.
IPR017878. TFG_b-bd.
[Graphical view]
PfamPF09289. FOLN. 1 hit.
PF00050. Kazal_1. 3 hits.
PF07915. PRKCSH. 1 hit.
[Graphical view]
SMARTSM00274. FOLN. 3 hits.
SM00280. KAZAL. 3 hits.
[Graphical view]
PROSITEPS00282. KAZAL. False negative.
PS51364. TB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio39699.
SOURCESearch...

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Entry information

Entry nameFST_HUMAN
AccessionPrimary (citable) accession number: P19883
Secondary accession number(s): Q9BTH0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 10, 2002
Last modified: July 7, 2009
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 5

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents