LATS2 PRM
Protein Sequence
Sequence Variants
| ID | Name | Remain region | Mutation sites | Ref seq |
|---|---|---|---|---|
| psp04893 | LATS2 | 1-1088 | - | ✓ |
| psp03141 | LATS2 PRM | 161-401, 1088-1088 | - | |
| psp00628 | LATS2 Δ464-667 | 1-463, 668-1088 | - | |
| psp01084 | LAST2 ΔLCD1 | 161-1088 | - | |
| psp01594 | LAST2 ΔLCD2 | 1-402, 465-1088 | - | |
| psp02580 | LAST2 Δ668-1033 | 1-667, 1034-1088 | - | |
| psp02787 | LAST2 Δ161-402 | 1-160, 403-1088 | - | |
| psp03686 | LATS2 Δ1-667 | 668-1088 | - | |
| psp01391 | LATS2 P-to-Q | - | P164Q, P166Q, P171Q, P190Q, P194Q, P201Q, P208Q, P210Q, P217Q, P221Q, P224Q, P231Q, P232Q, P247Q, P256Q, P261Q, P264Q, P273Q, P280Q, P281Q, P290Q, P297Q, P298Q, P305Q, P306Q, P307Q, P314Q, P316Q, P323Q, P343Q, P344Q, P350Q, P371Q, P384Q, P389Q, P390Q, P398Q, P401Q | |
| psp04495 | LATS2 P-to-A | - | P164A, P166A, P171A, P190A, P194A, P201A, P208A, P210A, P217A, P221A, P224A, P231A, P232A, P247A, P256A, P261A, P264A, P273A, P280A, P281A, P290A, P297A, P298A, P305A, P306A, P307A, P314A, P316A, P323A, P343A, P344A, P350A, P371A, P384A, P389A, P390A, P398A, P401A |
Orthologs and Paralogs
| ID | Name | Organism | Length |
|---|---|---|---|
| psp02431 | LATS1 | Homo sapiens | 1130 |
| psp01828 | LATS1 (ΔPrLD) | Homo sapiens | 774 |
| psp04673 | LATS1 (PrLD) | Homo sapiens | 356 |
Biophysical Features
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IDR (Intrinsically Disordered Region) was predicted by Mobidb-lite 4.0, please refer to: MobiDB-lite 4.0: faster prediction of intrinsic protein disorder and structural compactness.
Pi-Pi interaction was predicted by PScore, please refer to: Pi-Pi contacts are an overlooked protein feature relevant to phase separation.
PLAAC and PrD. like were both predicted by PLAAC, please refer to: PLAAC: a web and command-line application to identify proteins with prion-like amino acid composition.
LCR (Low Complexity Region) was predicted by SEG, please refer to: Statistics of local complexity in amino acid sequences and sequence databases.
NCPR (Net Charge Per Residue), FCR (Fraction of Charged Residues) and hydrophobicity were both computated by CIDER, please refer to: CIDER: Resources to Analyze Sequence-Ensemble Relationships of Intrinsically Disordered Proteins.
Polarity was computated by ProtScale, please refer to: ProtScale.
SASA (Solvent-Accessible Surface Area) was computated by BioPython based on the predicted structure, please refer to: Bio.PDB.SASA module.
Protein Structure
Protein structure was predicted by Chai-1, which also produces predicted local distance difference test (pLDDT) score between 0 and 100.
For pLDDT, please refer to: pLDDT: Understanding local confidence