UniProt ID | FSTL1_HUMAN | |
---|---|---|
UniProt AC | Q12841 | |
Protein Name | Follistatin-related protein 1 | |
Gene Name | FSTL1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 308 | |
Subcellular Localization | Secreted . | |
Protein Description | May modulate the action of some growth factors on cell proliferation and differentiation. Binds heparin (By similarity).. | |
Protein Sequence | MWKRWLALALALVAVAWVRAEEELRSKSKICANVFCGAGRECAVTEKGEPTCLCIEQCKPHKRPVCGSNGKTYLNHCELHRDACLTGSKIQVDYDGHCKEKKSVSPSASPVVCYQSNRDELRRRIIQWLEAEIIPDGWFSKGSNYSEILDKYFKNFDNGDSRLDSSEFLKFVEQNETAINITTYPDQENNKLLRGLCVDALIELSDENADWKLSFQEFLKCLNPSFNPPEKKCALEDETYADGAETEVDCNRCVCACGNWVCTAMTCDGKNQKGAQTQTEEEMTRYVQELQKHQETAEKTKRVSTKEI | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
88 | Phosphorylation | RDACLTGSKIQVDYD CCCCCCCCEEEECCC | 22.73 | 30631047 | |
103 | Phosphorylation | GHCKEKKSVSPSASP CCCCCCCCCCCCCCC | 38.61 | 25003641 | |
105 | Phosphorylation | CKEKKSVSPSASPVV CCCCCCCCCCCCCEE | 21.89 | 24505115 | |
107 | O-linked_Glycosylation | EKKSVSPSASPVVCY CCCCCCCCCCCEEEE | 33.59 | OGP | |
107 | Phosphorylation | EKKSVSPSASPVVCY CCCCCCCCCCCEEEE | 33.59 | 27251275 | |
109 | Phosphorylation | KSVSPSASPVVCYQS CCCCCCCCCEEEECC | 23.67 | 27251275 | |
114 | Phosphorylation | SASPVVCYQSNRDEL CCCCEEEECCCHHHH | 11.90 | 27251275 | |
116 | Phosphorylation | SPVVCYQSNRDELRR CCEEEECCCHHHHHH | 13.83 | 27251275 | |
141 | Ubiquitination | IPDGWFSKGSNYSEI CCCCCCCCCCCHHHH | 57.81 | - | |
144 | N-linked_Glycosylation | GWFSKGSNYSEILDK CCCCCCCCHHHHHHH | 53.68 | UniProtKB CARBOHYD | |
161 | Phosphorylation | KNFDNGDSRLDSSEF HCCCCCCCCCCHHHH | 35.82 | 22617229 | |
165 | Phosphorylation | NGDSRLDSSEFLKFV CCCCCCCHHHHHHHH | 36.04 | 19664994 | |
166 | Phosphorylation | GDSRLDSSEFLKFVE CCCCCCHHHHHHHHH | 31.84 | 29255136 | |
175 | N-linked_Glycosylation | FLKFVEQNETAINIT HHHHHHCCCCCEECC | 34.77 | 16335952 | |
180 | N-linked_Glycosylation | EQNETAINITTYPDQ HCCCCCEECCCCCCH | 24.08 | 16335952 | |
231 | Ubiquitination | PSFNPPEKKCALEDE CCCCCCCCCCCCCCC | 59.95 | - | |
277 | Phosphorylation | KNQKGAQTQTEEEMT CCCCCCCCCCHHHHH | 36.60 | 21406692 | |
279 | Phosphorylation | QKGAQTQTEEEMTRY CCCCCCCCHHHHHHH | 49.07 | 21406692 | |
284 | Phosphorylation | TQTEEEMTRYVQELQ CCCHHHHHHHHHHHH | 23.33 | 21406692 | |
286 | Phosphorylation | TEEEMTRYVQELQKH CHHHHHHHHHHHHHH | 9.41 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
165 | S | Phosphorylation | Kinase | FAM20C | Q8IXL6 | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FSTL1_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of FSTL1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
APBP2_HUMAN | APPBP2 | physical | 19060904 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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N-linked Glycosylation | |
Reference | PubMed |
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-175 AND ASN-180, AND MASSSPECTROMETRY. |