UniProt ID | SNAI1_MOUSE | |
---|---|---|
UniProt AC | Q02085 | |
Protein Name | Zinc finger protein SNAI1 | |
Gene Name | Snai1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 264 | |
Subcellular Localization | Nucleus . Cytoplasm . Once phosphorylated (probably on Ser-107, Ser-111, Ser-115 and Ser-119) it is exported from the nucleus to the cytoplasm where subsequent phosphorylation of the destruction motif and ubiquitination involving BTRC occurs.. | |
Protein Description | Involved in induction of the epithelial to mesenchymal transition (EMT), formation and maintenance of embryonic mesoderm, growth arrest, survival and cell migration. Binds to 3 E-boxes of the E-cadherin gene promoter and to the promoters of CLDN7 and KRT8 and, in association with histone demethylase KDM1A which it recruits to the promoters, causes a decrease in dimethylated H3K4 levels and represses transcription. During EMT, involved with LOXL2 in negatively regulating pericentromeric heterochromatin transcription. [PubMed: 24239292 SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits] | |
Protein Sequence | MPRSFLVRKPSDPRRKPNYSELQDACVEFTFQQPYDQAHLLAAIPPPEVLNPAASLPTLIWDSLLVPQVRPVAWATLPLRESPKAVELTSLSDEDSGKSSQPPSPPSPAPSSFSSTSASSLEAEAFIAFPGLGQLPKQLARLSVAKDPQSRKIFNCKYCNKEYLSLGALKMHIRSHTLPCVCTTCGKAFSRPWLLQGHVRTHTGEKPFSCSHCNRAFADRSNLRAHLQTHSDVKRYQCQACARTFSRMSLLHKHQESGCSGGPR | |
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 |
---|---|---|---|---|---|
11 | Phosphorylation | SFLVRKPSDPRRKPN CCCCCCCCCCCCCCC | 64.38 | - | |
82 | Phosphorylation | ATLPLRESPKAVELT EECCCCCCCCEEEEE | 25.85 | - | |
89 | Phosphorylation | SPKAVELTSLSDEDS CCCEEEEEECCCCCC | 17.70 | 25619855 | |
90 | Phosphorylation | PKAVELTSLSDEDSG CCEEEEEECCCCCCC | 38.20 | 25619855 | |
92 | Phosphorylation | AVELTSLSDEDSGKS EEEEEECCCCCCCCC | 38.43 | 25619855 | |
96 | Phosphorylation | TSLSDEDSGKSSQPP EECCCCCCCCCCCCC | 46.18 | 12832491 | |
100 | Phosphorylation | DEDSGKSSQPPSPPS CCCCCCCCCCCCCCC | 50.63 | 12832491 | |
104 | Phosphorylation | GKSSQPPSPPSPAPS CCCCCCCCCCCCCCC | 57.01 | - | |
107 | Phosphorylation | SQPPSPPSPAPSSFS CCCCCCCCCCCCCCC | 36.76 | 12832491 | |
111 | Phosphorylation | SPPSPAPSSFSSTSA CCCCCCCCCCCCCCC | 46.23 | 12832491 | |
112 | O-linked_Glycosylation | PPSPAPSSFSSTSAS CCCCCCCCCCCCCCC | 28.26 | - | |
115 | Phosphorylation | PAPSSFSSTSASSLE CCCCCCCCCCCCHHC | 25.11 | 12832491 | |
119 | Phosphorylation | SFSSTSASSLEAEAF CCCCCCCCHHCEEEE | 34.91 | 12832491 | |
143 | Phosphorylation | PKQLARLSVAKDPQS HHHHHHHHCCCCCCC | 17.93 | 24719451 | |
203 | Phosphorylation | QGHVRTHTGEKPFSC CCCEEECCCCCCCCC | 46.56 | - | |
231 | Phosphorylation | RAHLQTHSDVKRYQC HHHHHHHHHHHHHHH | 47.70 | 27149854 | |
246 | Phosphorylation | QACARTFSRMSLLHK HHHHHHHHHHHHHHH | 26.85 | - |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
11 | S | Phosphorylation |
| - |
96 | S | Phosphorylation |
| - |
98 | K | ubiquitylation |
| - |
100 | S | Phosphorylation |
| - |
104 | S | Phosphorylation |
| - |
104 | S | Phosphorylation |
| - |
112 | S | Phosphorylation |
| - |
137 | K | ubiquitylation |
| - |
146 | K | ubiquitylation |
| - |
* 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 SNAI1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
FXL14_HUMAN | FBXL14 | physical | 19955572 | |
TNAP3_MOUSE | Tnfaip3 | physical | 28892081 | |
GSK3B_MOUSE | Gsk3b | physical | 28892081 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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