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Protein

Follistatin

Gene

FST

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  • activin binding Source: UniProtKB
  • heparan sulfate proteoglycan binding Source: Ensembl
  • signal transducer activity Source: UniProtKB

GO - Biological processi

  • hematopoietic progenitor cell differentiation Source: UniProtKB
  • negative regulation of activin receptor signaling pathway Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of hair follicle development Source: MGI
Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000134363-MONOMER.
ReactomeiR-HSA-2473224. Antagonism of Activin by Follistatin.
SIGNORiP19883.

Protein family/group databases

MEROPSiI01.966.

Names & Taxonomyi

Protein namesi
Recommended name:
Follistatin
Short name:
FS
Alternative name(s):
Activin-binding protein
Gene namesi
Name:FST
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:3971. FST.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi10468.
OpenTargetsiENSG00000134363.
Orphaneti3185. Polycystic ovary syndrome.
PharmGKBiPA28388.

Polymorphism and mutation databases

BioMutaiFST.
DMDMi23831079.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 291 PublicationAdd BLAST29
ChainiPRO_000001010330 – 344FollistatinAdd BLAST315

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi32 ↔ 55PROSITE-ProRule annotation
Disulfide bondi42 ↔ 88PROSITE-ProRule annotation
Disulfide bondi56 ↔ 91PROSITE-ProRule annotation
Disulfide bondi95 ↔ 106
Disulfide bondi100 ↔ 116
Disulfide bondi118 ↔ 150
Disulfide bondi122 ↔ 143
Glycosylationi124N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi132 ↔ 164
Disulfide bondi192 ↔ 225
Disulfide bondi196 ↔ 218
Disulfide bondi207 ↔ 239
Disulfide bondi270 ↔ 302
Disulfide bondi274 ↔ 295
Disulfide bondi284 ↔ 316
Glycosylationi288N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP19883.
PaxDbiP19883.
PeptideAtlasiP19883.
PRIDEiP19883.

PTM databases

UniCarbKBiP19883.

Expressioni

Tissue specificityi

Isoform 1 is the predominant isoform in serum but is undetectable in follicular fluid.1 Publication

Gene expression databases

BgeeiENSG00000134363.
CleanExiHS_FST.
ExpressionAtlasiP19883. baseline and differential.
GenevisibleiP19883. HS.

Organism-specific databases

HPAiCAB026025.
HPA018155.

Interactioni

Subunit structurei

Monomer.Curated

Binary interactionsi

WithEntry#Exp.IntActNotes
ANGP039503EBI-1571188,EBI-525291
DIP2AQ146892EBI-1571188,EBI-2564275

GO - Molecular functioni

  • activin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115731. 8 interactors.
IntActiP19883. 9 interactors.
MINTiMINT-3009113.
STRINGi9606.ENSP00000256759.

Structurei

Secondary structure

1344
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi31 – 36Combined sources6
Beta strandi42 – 49Combined sources8
Helixi52 – 55Combined sources4
Beta strandi64 – 66Combined sources3
Helixi72 – 81Combined sources10
Beta strandi82 – 87Combined sources6
Beta strandi89 – 91Combined sources3
Beta strandi93 – 95Combined sources3
Beta strandi104 – 108Combined sources5
Turni110 – 112Combined sources3
Beta strandi114 – 118Combined sources5
Helixi123 – 125Combined sources3
Beta strandi131 – 133Combined sources3
Beta strandi138 – 141Combined sources4
Helixi142 – 151Combined sources10
Beta strandi158 – 163Combined sources6
Beta strandi166 – 168Combined sources3
Beta strandi178 – 181Combined sources4
Beta strandi185 – 190Combined sources6
Beta strandi202 – 204Combined sources3
Beta strandi206 – 208Combined sources3
Beta strandi213 – 216Combined sources4
Helixi217 – 227Combined sources11
Beta strandi233 – 237Combined sources5
Helixi245 – 247Combined sources3
Turni251 – 253Combined sources3
Beta strandi255 – 259Combined sources5
Turni260 – 263Combined sources4
Beta strandi264 – 268Combined sources5
Beta strandi283 – 285Combined sources3
Beta strandi290 – 293Combined sources4
Helixi294 – 304Combined sources11
Beta strandi310 – 314Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2B0UX-ray2.80C/D30-317[»]
2P6AX-ray3.40C/D30-344[»]
3HH2X-ray2.15C/D30-317[»]
ProteinModelPortaliP19883.
SMRiP19883.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19883.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 103TBPROSITE-ProRule annotationAdd BLAST74
Domaini94 – 117Follistatin-like 1Add BLAST24
Domaini112 – 166Kazal-like 1PROSITE-ProRule annotationAdd BLAST55
Domaini167 – 190Follistatin-like 2Add BLAST24
Domaini186 – 241Kazal-like 2PROSITE-ProRule annotationAdd BLAST56
Domaini244 – 268Follistatin-like 3Add BLAST25
Domaini264 – 318Kazal-like 3PROSITE-ProRule annotationAdd BLAST55

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi321 – 333Asp/Glu-rich (highly acidic)Add BLAST13

Sequence similaritiesi

Contains 3 follistatin-like domains.Curated
Contains 3 Kazal-like domains.PROSITE-ProRule annotation
Contains 1 TB (TGF-beta binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IP0F. Eukaryota.
ENOG410YM8Q. LUCA.
GeneTreeiENSGT00440000033501.
HOGENOMiHOG000261649.
HOVERGENiHBG051666.
InParanoidiP19883.
KOiK04661.
OMAiEAVCASD.
OrthoDBiEOG091G09I0.
PhylomeDBiP19883.
TreeFamiTF106409.

Family and domain databases

InterProiIPR003645. Fol_N.
IPR015369. Follistatin/Osteonectin_EGF.
IPR002350. Kazal_dom.
IPR017878. TB_dom.
[Graphical view]
PfamiPF09289. FOLN. 1 hit.
PF07648. Kazal_2. 3 hits.
[Graphical view]
SMARTiSM00274. FOLN. 3 hits.
SM00280. KAZAL. 3 hits.
[Graphical view]
SUPFAMiSSF57581. SSF57581. 1 hit.
PROSITEiPS51465. KAZAL_2. 3 hits.
PS51364. TB. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P19883-1) [UniParc]FASTAAdd to basket
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.

« Hide

        10         20         30         40         50
MVRARHQPGG LCLLLLLLCQ FMEDRSAQAG NCWLRQAKNG RCQVLYKTEL
60 70 80 90 100
SKEECCSTGR LSTSWTEEDV NDNTLFKWMI FNGGAPNCIP CKETCENVDC
110 120 130 140 150
GPGKKCRMNK KNKPRCVCAP DCSNITWKGP VCGLDGKTYR NECALLKARC
160 170 180 190 200
KEQPELEVQY QGRCKKTCRD VFCPGSSTCV VDQTNNAYCV TCNRICPEPA
210 220 230 240 250
SSEQYLCGND GVTYSSACHL RKATCLLGRS IGLAYEGKCI KAKSCEDIQC
260 270 280 290 300
TGGKKCLWDF KVGRGRCSLC DELCPDSKSD EPVCASDNAT YASECAMKEA
310 320 330 340
ACSSGVLLEV KHSGSCNSIS EDTEEEEEDE DQDYSFPISS ILEW
Length:344
Mass (Da):38,007
Last modified:October 10, 2002 - v2
Checksum:iD9BB45055D84AC90
GO
Isoform 2 (identifier: P19883-2) [UniParc]FASTAAdd to basket
Also known as: FS288, FS-288

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

Show »
Length:317
Mass (Da):34,803
Checksum:iB516643224C7F8FF
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_049091152E → Q.Corresponds to variant rs11745088dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_001565318 – 344Missing in isoform 2. 1 PublicationAdd BLAST27

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3959.1. [P19883-1]
CCDS43315.1. [P19883-2]
PIRiA32141.
RefSeqiNP_006341.1. NM_006350.3. [P19883-2]
NP_037541.1. NM_013409.2. [P19883-1]
UniGeneiHs.9914.

Genome annotation databases

EnsembliENST00000256759; ENSP00000256759; ENSG00000134363. [P19883-1]
ENST00000396947; ENSP00000380151; ENSG00000134363. [P19883-2]
GeneIDi10468.
KEGGihsa:10468.
UCSCiuc003jpc.4. human. [P19883-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3959.1. [P19883-1]
CCDS43315.1. [P19883-2]
PIRiA32141.
RefSeqiNP_006341.1. NM_006350.3. [P19883-2]
NP_037541.1. NM_013409.2. [P19883-1]
UniGeneiHs.9914.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2B0UX-ray2.80C/D30-317[»]
2P6AX-ray3.40C/D30-344[»]
3HH2X-ray2.15C/D30-317[»]
ProteinModelPortaliP19883.
SMRiP19883.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115731. 8 interactors.
IntActiP19883. 9 interactors.
MINTiMINT-3009113.
STRINGi9606.ENSP00000256759.

Protein family/group databases

MEROPSiI01.966.

PTM databases

UniCarbKBiP19883.

Polymorphism and mutation databases

BioMutaiFST.
DMDMi23831079.

Proteomic databases

MaxQBiP19883.
PaxDbiP19883.
PeptideAtlasiP19883.
PRIDEiP19883.

Protocols and materials databases

DNASUi10468.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000256759; ENSP00000256759; ENSG00000134363. [P19883-1]
ENST00000396947; ENSP00000380151; ENSG00000134363. [P19883-2]
GeneIDi10468.
KEGGihsa:10468.
UCSCiuc003jpc.4. human. [P19883-1]

Organism-specific databases

CTDi10468.
DisGeNETi10468.
GeneCardsiFST.
HGNCiHGNC:3971. FST.
HPAiCAB026025.
HPA018155.
MIMi136470. gene.
neXtProtiNX_P19883.
OpenTargetsiENSG00000134363.
Orphaneti3185. Polycystic ovary syndrome.
PharmGKBiPA28388.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IP0F. Eukaryota.
ENOG410YM8Q. LUCA.
GeneTreeiENSGT00440000033501.
HOGENOMiHOG000261649.
HOVERGENiHBG051666.
InParanoidiP19883.
KOiK04661.
OMAiEAVCASD.
OrthoDBiEOG091G09I0.
PhylomeDBiP19883.
TreeFamiTF106409.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000134363-MONOMER.
ReactomeiR-HSA-2473224. Antagonism of Activin by Follistatin.
SIGNORiP19883.

Miscellaneous databases

ChiTaRSiFST. human.
EvolutionaryTraceiP19883.
GeneWikiiFollistatin.
GenomeRNAii10468.
PROiP19883.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000134363.
CleanExiHS_FST.
ExpressionAtlasiP19883. baseline and differential.
GenevisibleiP19883. HS.

Family and domain databases

InterProiIPR003645. Fol_N.
IPR015369. Follistatin/Osteonectin_EGF.
IPR002350. Kazal_dom.
IPR017878. TB_dom.
[Graphical view]
PfamiPF09289. FOLN. 1 hit.
PF07648. Kazal_2. 3 hits.
[Graphical view]
SMARTiSM00274. FOLN. 3 hits.
SM00280. KAZAL. 3 hits.
[Graphical view]
SUPFAMiSSF57581. SSF57581. 1 hit.
PROSITEiPS51465. KAZAL_2. 3 hits.
PS51364. TB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFST_HUMAN
AccessioniPrimary (citable) accession number: P19883
Secondary accession number(s): B5BU94, Q9BTH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 10, 2002
Last modified: November 2, 2016
This is version 170 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.