UniProt ID | FSCN1_RAT | |
---|---|---|
UniProt AC | P85845 | |
Protein Name | Fascin | |
Gene Name | Fscn1 {ECO:0000250|UniProtKB:Q16658} | |
Organism | Rattus norvegicus (Rat). | |
Sequence Length | 493 | |
Subcellular Localization | Cytoplasm, cytosol . Cytoplasm, cytoskeleton . Cell projection, growth cone . Cell projection, filopodium . Cell projection, invadopodium . Cell projection, microvillus . Cell junction . Colocalized with RUFY3 and F-actin at filipodia of the axonal g | |
Protein Description | Organizes filamentous actin into bundles with a minimum of 4.1:1 actin/fascin ratio. Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility.. | |
Protein Sequence | MTANGTAEAVQIQFGLISCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDEAGSAAVCLRSHLGPYLAADKDGNVTCEREVPDGDCRFLVVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQSVSPAEKWSVHIAMHPQVNIYSVTRKRYAHLSARPADEIAVDRDVPWGVDSLITLAFQDQRYSVQTSDHRFLRHDGRLVARPEPATGFTLEFRSGKVAFRDCEGRYLAPSGPSGTLKAGKATKVGKDELFALEQSCAQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTRKCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIEWCERRITLRASNGKFVTAKKNGQLAATVETAGDSELFLMKLINRPIIVFRGEHGFIGCRKVTGTLDANRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSSVTSSSDTPVDFFLEFCDYNKVALKVGGRYLKGDHAGVLKACAETIDPATLWEY | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MTANGTAEA ------CCCCCCEEE | 28.91 | - | |
36 | Phosphorylation | FGFKVNASASSLKKK HCCEEECCCHHHCCC | 24.39 | 23984901 | |
38 | Phosphorylation | FKVNASASSLKKKQI CEEECCCHHHCCCEE | 33.44 | 27097102 | |
39 | Phosphorylation | KVNASASSLKKKQIW EEECCCHHHCCCEEE | 43.88 | 23984901 | |
74 | Acetylation | GPYLAADKDGNVTCE CCCCCCCCCCCEEEE | 63.91 | - | |
105 | Phosphorylation | DGRWSLQSEAHRRYF CCCEEECCHHHHHHC | 41.88 | 27097102 | |
111 | Phosphorylation | QSEAHRRYFGGTEDR CCHHHHHHCCCCCHH | 13.41 | 23984901 | |
115 | Phosphorylation | HRRYFGGTEDRLSCF HHHHCCCCCHHHHHH | 34.78 | 23984901 | |
120 | Phosphorylation | GGTEDRLSCFAQSVS CCCCHHHHHHEEECC | 14.21 | 23984901 | |
125 | Phosphorylation | RLSCFAQSVSPAEKW HHHHHEEECCHHHHC | 22.57 | 27097102 | |
127 | Phosphorylation | SCFAQSVSPAEKWSV HHHEEECCHHHHCEE | 24.52 | 27097102 | |
213 | Phosphorylation | PEPATGFTLEFRSGK CCCCCCEEEEECCCC | 27.07 | 23984901 | |
234 | Phosphorylation | EGRYLAPSGPSGTLK CCCEECCCCCCCCEE | 58.70 | 23984901 | |
237 | Phosphorylation | YLAPSGPSGTLKAGK EECCCCCCCCEECCC | 48.19 | 23984901 | |
239 | Phosphorylation | APSGPSGTLKAGKAT CCCCCCCCEECCCEE | 29.44 | 23984901 | |
241 | Acetylation | SGPSGTLKAGKATKV CCCCCCEECCCEEEC | 55.73 | 25786129 | |
353 | Acetylation | TLRASNGKFVTAKKN EEEECCCCEEEEEEC | 40.69 | 22902405 | |
399 | Ubiquitination | HGFIGCRKVTGTLDA CCEECEEEEEEEEEC | 48.50 | - | |
401 | Phosphorylation | FIGCRKVTGTLDANR EECEEEEEEEEECCC | 27.73 | 25403869 | |
403 | Phosphorylation | GCRKVTGTLDANRSS CEEEEEEEEECCCCC | 16.46 | 27097102 | |
471 | Acetylation | KVGGRYLKGDHAGVL EECCEECCCCCHHHH | 54.05 | 22902405 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
39 | S | Phosphorylation | Kinase | PKC | - | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
39 | S | Phosphorylation |
| - |
* 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 FSCN1_RAT !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of FSCN1_RAT !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...