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P19883

- FST_HUMAN

UniProt

P19883 - FST_HUMAN

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Protein
Follistatin
Gene
FST
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. activin binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. signal transducer activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. BMP signaling pathway Source: Ensembl
  2. female gonad development Source: Ensembl
  3. gamete generation Source: Ensembl
  4. hair follicle morphogenesis Source: Ensembl
  5. hematopoietic progenitor cell differentiation Source: UniProtKB
  6. keratinocyte proliferation Source: Ensembl
  7. negative regulation of activin receptor signaling pathway Source: UniProtKB
  8. negative regulation of cell differentiation Source: Ensembl
  9. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  10. odontogenesis of dentin-containing tooth Source: Ensembl
  11. pattern specification process Source: Ensembl
  12. positive regulation of hair follicle development Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_150276. Antagonism of Activin by Follistatin.

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
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:3971. FST.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. extracellular region Source: Reactome
  3. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

Orphaneti3185. Polycystic ovary syndrome.
PharmGKBiPA28388.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 29291 Publication
Add
BLAST
Chaini30 – 344315Follistatin
PRO_0000010103Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi32 ↔ 553 Publications
Disulfide bondi42 ↔ 883 Publications
Disulfide bondi56 ↔ 913 Publications
Disulfide bondi95 ↔ 1063 Publications
Disulfide bondi100 ↔ 1163 Publications
Disulfide bondi118 ↔ 1503 Publications
Disulfide bondi122 ↔ 1433 Publications
Glycosylationi124 – 1241N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi132 ↔ 1643 Publications
Disulfide bondi192 ↔ 2253 Publications
Disulfide bondi196 ↔ 2183 Publications
Disulfide bondi207 ↔ 2393 Publications
Disulfide bondi270 ↔ 3023 Publications
Disulfide bondi274 ↔ 2953 Publications
Disulfide bondi284 ↔ 3163 Publications
Glycosylationi288 – 2881N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP19883.
PaxDbiP19883.
PRIDEiP19883.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiP19883.
BgeeiP19883.
CleanExiHS_FST.
GenevestigatoriP19883.

Organism-specific databases

HPAiCAB026025.
HPA018155.

Interactioni

Subunit structurei

Monomer Reviewed prediction.

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 366
Beta strandi42 – 498
Helixi52 – 554
Beta strandi64 – 663
Helixi72 – 8110
Beta strandi82 – 876
Beta strandi89 – 913
Beta strandi93 – 953
Beta strandi104 – 1085
Turni110 – 1123
Beta strandi114 – 1185
Helixi123 – 1253
Beta strandi131 – 1333
Beta strandi138 – 1414
Helixi142 – 15110
Beta strandi158 – 1636
Beta strandi166 – 1683
Beta strandi178 – 1814
Beta strandi185 – 1906
Beta strandi202 – 2043
Beta strandi206 – 2083
Beta strandi213 – 2164
Helixi217 – 22711
Beta strandi233 – 2375
Helixi245 – 2473
Turni251 – 2533
Beta strandi255 – 2595
Turni260 – 2634
Beta strandi264 – 2685
Beta strandi283 – 2853
Beta strandi290 – 2934
Helixi294 – 30411
Beta strandi310 – 3145

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2B0UX-ray2.80C/D30-317[»]
2P6AX-ray3.40C/D30-344[»]
3HH2X-ray2.15C/D30-317[»]
ProteinModelPortaliP19883.
SMRiP19883. Positions 30-317.

Miscellaneous databases

EvolutionaryTraceiP19883.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 10374TB
Add
BLAST
Domaini94 – 11724Follistatin-like 1
Add
BLAST
Domaini112 – 16655Kazal-like 1
Add
BLAST
Domaini167 – 19024Follistatin-like 2
Add
BLAST
Domaini186 – 24156Kazal-like 2
Add
BLAST
Domaini244 – 26825Follistatin-like 3
Add
BLAST
Domaini264 – 31855Kazal-like 3
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi321 – 33313Asp/Glu-rich (highly acidic)
Add
BLAST

Sequence similaritiesi

Contains 3 Kazal-like domains.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG267610.
HOGENOMiHOG000261649.
HOVERGENiHBG051666.
InParanoidiP19883.
KOiK04661.
OMAiEAVCASD.
OrthoDBiEOG7GBFXR.
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.
PF00050. Kazal_1. 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. Align

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

MVRARHQPGG LCLLLLLLCQ FMEDRSAQAG NCWLRQAKNG RCQVLYKTEL    50
SKEECCSTGR LSTSWTEEDV NDNTLFKWMI FNGGAPNCIP CKETCENVDC 100
GPGKKCRMNK KNKPRCVCAP DCSNITWKGP VCGLDGKTYR NECALLKARC 150
KEQPELEVQY QGRCKKTCRD VFCPGSSTCV VDQTNNAYCV TCNRICPEPA 200
SSEQYLCGND GVTYSSACHL RKATCLLGRS IGLAYEGKCI KAKSCEDIQC 250
TGGKKCLWDF KVGRGRCSLC DELCPDSKSD EPVCASDNAT YASECAMKEA 300
ACSSGVLLEV KHSGSCNSIS EDTEEEEEDE DQDYSFPISS ILEW 344
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti152 – 1521E → Q.
Corresponds to variant rs11745088 [ dbSNP | Ensembl ].
VAR_049091

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei318 – 34427Missing in isoform 2.
VSP_001565Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.3. human. [P19883-1]

Polymorphism databases

DMDMi23831079.

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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS3959.1. [P19883-1 ]
CCDS43315.1. [P19883-2 ]
PIRi A32141.
RefSeqi NP_006341.1. NM_006350.3. [P19883-2 ]
NP_037541.1. NM_013409.2. [P19883-1 ]
UniGenei Hs.9914.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2B0U X-ray 2.80 C/D 30-317 [» ]
2P6A X-ray 3.40 C/D 30-344 [» ]
3HH2 X-ray 2.15 C/D 30-317 [» ]
ProteinModelPortali P19883.
SMRi P19883. Positions 30-317.
ModBasei Search...

Protein-protein interaction databases

BioGridi 115731. 8 interactions.
IntActi P19883. 9 interactions.
MINTi MINT-3009113.
STRINGi 9606.ENSP00000256759.

Protein family/group databases

MEROPSi I01.966.

Polymorphism databases

DMDMi 23831079.

Proteomic databases

MaxQBi P19883.
PaxDbi P19883.
PRIDEi P19883.

Protocols and materials databases

DNASUi 10468.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000256759 ; ENSP00000256759 ; ENSG00000134363 . [P19883-1 ]
ENST00000396947 ; ENSP00000380151 ; ENSG00000134363 . [P19883-2 ]
GeneIDi 10468.
KEGGi hsa:10468.
UCSCi uc003jpc.3. human. [P19883-1 ]

Organism-specific databases

CTDi 10468.
GeneCardsi GC05P052776.
HGNCi HGNC:3971. FST.
HPAi CAB026025.
HPA018155.
MIMi 136470. gene.
neXtProti NX_P19883.
Orphaneti 3185. Polycystic ovary syndrome.
PharmGKBi PA28388.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG267610.
HOGENOMi HOG000261649.
HOVERGENi HBG051666.
InParanoidi P19883.
KOi K04661.
OMAi EAVCASD.
OrthoDBi EOG7GBFXR.
PhylomeDBi P19883.
TreeFami TF106409.

Enzyme and pathway databases

Reactomei REACT_150276. Antagonism of Activin by Follistatin.

Miscellaneous databases

EvolutionaryTracei P19883.
GeneWikii Follistatin.
GenomeRNAii 10468.
NextBioi 39699.
PROi P19883.
SOURCEi Search...

Gene expression databases

ArrayExpressi P19883.
Bgeei P19883.
CleanExi HS_FST.
Genevestigatori P19883.

Family and domain databases

InterProi IPR003645. Fol_N.
IPR015369. Follistatin/Osteonectin_EGF.
IPR002350. Kazal_dom.
IPR017878. TB_dom.
[Graphical view ]
Pfami PF09289. FOLN. 1 hit.
PF00050. Kazal_1. 3 hits.
[Graphical view ]
SMARTi SM00274. FOLN. 3 hits.
SM00280. KAZAL. 3 hits.
[Graphical view ]
SUPFAMi SSF57581. SSF57581. 1 hit.
PROSITEi PS51465. KAZAL_2. 3 hits.
PS51364. TB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

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: September 3, 2014
This is version 153 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

External Data

Dasty 3

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