Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P19883

- FST_HUMAN

UniProt

P19883 - FST_HUMAN

Protein

Follistatin

Gene

FST

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 2 (10 Oct 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    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

    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 PublicationAdd
    BLAST
    Chaini30 – 344315FollistatinPRO_0000010103Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi32 ↔ 55
    Disulfide bondi42 ↔ 88
    Disulfide bondi56 ↔ 91
    Disulfide bondi95 ↔ 106
    Disulfide bondi100 ↔ 116
    Disulfide bondi118 ↔ 150
    Disulfide bondi122 ↔ 143
    Glycosylationi124 – 1241N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi132 ↔ 164
    Disulfide bondi192 ↔ 225
    Disulfide bondi196 ↔ 218
    Disulfide bondi207 ↔ 239
    Disulfide bondi270 ↔ 302
    Disulfide bondi274 ↔ 295
    Disulfide bondi284 ↔ 316
    Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence Analysis

    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.Curated

    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

    1
    344
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19883.

    Family & Domainsi

    Domains and Repeats

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

    Compositional bias

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

    Sequence similaritiesi

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

    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. 1 PublicationVSP_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...
    MobiDBi 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

    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: October 1, 2014
    This is version 154 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