P19883 · FST_HUMAN
- ProteinFollistatin
- GeneFST
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids344 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameFollistatin
- Short namesFS
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP19883
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_085164 | 56 | found in patients with orofacial clefting; uncertain significance; dbSNP:rs1747328996 | |||
Sequence: C → Y | ||||||
Natural variant | VAR_049091 | 152 | in dbSNP:rs11745088 | |||
Sequence: E → Q |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 284 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-29 | |||||
Sequence: MVRARHQPGGLCLLLLLLCQFMEDRSAQA | ||||||
Chain | PRO_0000010103 | 30-344 | Follistatin | |||
Sequence: GNCWLRQAKNGRCQVLYKTELSKEECCSTGRLSTSWTEEDVNDNTLFKWMIFNGGAPNCIPCKETCENVDCGPGKKCRMNKKNKPRCVCAPDCSNITWKGPVCGLDGKTYRNECALLKARCKEQPELEVQYQGRCKKTCRDVFCPGSSTCVVDQTNNAYCVTCNRICPEPASSEQYLCGNDGVTYSSACHLRKATCLLGRSIGLAYEGKCIKAKSCEDIQCTGGKKCLWDFKVGRGRCSLCDELCPDSKSDEPVCASDNATYASECAMKEAACSSGVLLEVKHSGSCNSISEDTEEEEEDEDQDYSFPISSILEW | ||||||
Disulfide bond | 32↔55 | |||||
Sequence: CWLRQAKNGRCQVLYKTELSKEEC | ||||||
Disulfide bond | 42↔88 | |||||
Sequence: CQVLYKTELSKEECCSTGRLSTSWTEEDVNDNTLFKWMIFNGGAPNC | ||||||
Disulfide bond | 56↔91 | |||||
Sequence: CSTGRLSTSWTEEDVNDNTLFKWMIFNGGAPNCIPC | ||||||
Disulfide bond | 95↔106 | |||||
Sequence: CENVDCGPGKKC | ||||||
Disulfide bond | 100↔116 | |||||
Sequence: CGPGKKCRMNKKNKPRC | ||||||
Disulfide bond | 118↔150 | |||||
Sequence: CAPDCSNITWKGPVCGLDGKTYRNECALLKARC | ||||||
Disulfide bond | 122↔143 | |||||
Sequence: CSNITWKGPVCGLDGKTYRNEC | ||||||
Glycosylation | 124 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 132↔164 | |||||
Sequence: CGLDGKTYRNECALLKARCKEQPELEVQYQGRC | ||||||
Disulfide bond | 168↔179 | |||||
Sequence: CRDVFCPGSSTC | ||||||
Disulfide bond | 173↔189 | |||||
Sequence: CPGSSTCVVDQTNNAYC | ||||||
Disulfide bond | 192↔225 | |||||
Sequence: CNRICPEPASSEQYLCGNDGVTYSSACHLRKATC | ||||||
Disulfide bond | 196↔218 | |||||
Sequence: CPEPASSEQYLCGNDGVTYSSAC | ||||||
Disulfide bond | 207↔239 | |||||
Sequence: CGNDGVTYSSACHLRKATCLLGRSIGLAYEGKC | ||||||
Disulfide bond | 245↔256 | |||||
Sequence: CEDIQCTGGKKC | ||||||
Disulfide bond | 250↔267 | |||||
Sequence: CTGGKKCLWDFKVGRGRC | ||||||
Disulfide bond | 270↔302 | |||||
Sequence: CDELCPDSKSDEPVCASDNATYASECAMKEAAC | ||||||
Disulfide bond | 274↔295 | |||||
Sequence: CPDSKSDEPVCASDNATYASEC | ||||||
Disulfide bond | 284↔316 | |||||
Sequence: CASDNATYASECAMKEAACSSGVLLEVKHSGSC | ||||||
Glycosylation | 288 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Isoform 1 is the predominant isoform in serum but is undetectable in follicular fluid. In the embryo, strong expression is seen in the palatal epithelia, including the medial edge epithelial and midline epithelial seam of the palatal shelves. Less pronounced expression is also seen throughout the palatal shelf and tongue mesenchyme (PubMed:31215115).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P19883 | ANG P03950 | 3 | EBI-1571188, EBI-525291 | |
BINARY | P19883 | BEX2 Q9BXY8 | 3 | EBI-1571188, EBI-745073 | |
BINARY | P19883 | CATSPER1 Q8NEC5 | 3 | EBI-1571188, EBI-744545 | |
BINARY | P19883 | CREB5 Q02930-3 | 5 | EBI-1571188, EBI-10192698 | |
BINARY | P19883 | DIP2A Q14689 | 2 | EBI-1571188, EBI-2564275 | |
BINARY | P19883 | HOXA1 P49639 | 3 | EBI-1571188, EBI-740785 | |
BINARY | P19883 | TXN P10599 | 3 | EBI-1571188, EBI-594644 | |
BINARY | P19883 | ZNF417 Q8TAU3 | 3 | EBI-1571188, EBI-740727 | |
BINARY | P19883 | ZNF587 Q96SQ5 | 3 | EBI-1571188, EBI-6427977 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 30-103 | TB | ||||
Sequence: GNCWLRQAKNGRCQVLYKTELSKEECCSTGRLSTSWTEEDVNDNTLFKWMIFNGGAPNCIPCKETCENVDCGPG | ||||||
Domain | 94-117 | Follistatin-like 1 | ||||
Sequence: TCENVDCGPGKKCRMNKKNKPRCV | ||||||
Domain | 112-166 | Kazal-like 1 | ||||
Sequence: NKPRCVCAPDCSNITWKGPVCGLDGKTYRNECALLKARCKEQPELEVQYQGRCKK | ||||||
Domain | 167-190 | Follistatin-like 2 | ||||
Sequence: TCRDVFCPGSSTCVVDQTNNAYCV | ||||||
Domain | 186-241 | Kazal-like 2 | ||||
Sequence: NAYCVTCNRICPEPASSEQYLCGNDGVTYSSACHLRKATCLLGRSIGLAYEGKCIK | ||||||
Domain | 244-268 | Follistatin-like 3 | ||||
Sequence: SCEDIQCTGGKKCLWDFKVGRGRCS | ||||||
Domain | 264-318 | Kazal-like 3 | ||||
Sequence: RGRCSLCDELCPDSKSDEPVCASDNATYASECAMKEAACSSGVLLEVKHSGSCNS | ||||||
Region | 314-344 | Disordered | ||||
Sequence: GSCNSISEDTEEEEEDEDQDYSFPISSILEW | ||||||
Compositional bias | 320-334 | Acidic residues | ||||
Sequence: SEDTEEEEEDEDQDY |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P19883-1
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.
- Name1
- SynonymsFS315, FS-315
- Length344
- Mass (Da)38,007
- Last updated2002-10-10 v2
- ChecksumD9BB45055D84AC90
P19883-2
- Name2
- SynonymsFS288, FS-288
- Differences from canonical
- 318-344: Missing
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_001565 | 318-344 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 320-334 | Acidic residues | ||||
Sequence: SEDTEEEEEDEDQDY |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M19481 EMBL· GenBank· DDBJ | AAA35851.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M19480 EMBL· GenBank· DDBJ | AAA35851.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB451330 EMBL· GenBank· DDBJ | BAG70144.1 EMBL· GenBank· DDBJ | mRNA | ||
AB451474 EMBL· GenBank· DDBJ | BAG70288.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471123 EMBL· GenBank· DDBJ | EAW54880.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC004107 EMBL· GenBank· DDBJ | AAH04107.1 EMBL· GenBank· DDBJ | mRNA |