GATA3 R275A
Protein Sequence
Sequence Variants
| ID | Name | Remain region | Mutation sites | Ref seq |
|---|---|---|---|---|
| psp00483 | GATA3 | 1-443 | - | ✓ |
| psp01370 | GATA3 R275A | - | R275A | |
| psp00743 | GATA3 N-IDR (1-260) | 1-260 | - | |
| psp01239 | GATA3 DBD (261-360) | 260-360 | - | |
| psp01497 | GATA3 ΔDBD | 1-259, 362-443 | - | |
| psp01926 | GATA3 ΔN | 260-443 | - | |
| psp02380 | GATA3 Δ322-327 | 1-321, 328-443 | - | |
| psp02627 | GATA3 ΔC | 1-360 | - | |
| psp03469 | GATA3 C-IDR (361-443) | 361-443 | - | |
| psp05106 | GATA3 Δ88-93 | 1-87, 94-443 | - | |
| psp00027 | GATA3 R329A | - | R329A | |
| psp00057 | GATA3 R311A | - | R311A | |
| psp00331 | GATA3 R276A | - | R276A | |
| psp01386 | GATA3 K346A | - | K346A | |
| psp01519 | GATA3 ZnF2 2R-K | - | R305K, R306K | |
| psp01949 | GATA3 R261A | - | R261A | |
| psp01951 | GATA3 ZnF2 2R-A | - | R305A, R306A | |
| psp02321 | GATA3 K292A | - | K292A | |
| psp02484 | GATA3 R312A | - | R312A | |
| psp02602 | GATA3 R306A | - | R306A | |
| psp02718 | GATA3 R305A | - | R305A | |
| psp03615 | GATA3 R330A | - | R330A | |
| psp04054 | GATA3 K302A | - | K302A | |
| psp04237 | GATA3 ZnF1 2R-A | - | R275A, R276A | |
| psp04289 | GATA3 K304A | - | K304A | |
| psp05108 | GATA3 ZnF1 2R-K | - | R275K, R276K |
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