EH1 ΔCCΔIDR3
Protein Sequence
Sequence Variants
| ID | Name | Remain region | Mutation sites | Ref seq |
|---|---|---|---|---|
| psp04549 | EH1 | 1-1019 | - | ✓ |
| psp02929 | EH1 ΔCCΔIDR3 | 1-534 | - | |
| psp00102 | EH1 ΔIDR1 | 1-105, 349-1019 | - | |
| psp00554 | EH1 ΔCC | 1-534, 673-1019 | - | |
| psp00591 | EH1 ΔEH1 | 1-6, 107-1019 | - | |
| psp01967 | EH1 ΔIDR2 | 1-442, 535-1019 | - | |
| psp03110 | EH1 ΔIDR3 | 1-671 | - | |
| psp03865 | EH1 ΔEH2 | 1-358, 443-1019 | - | |
| psp00787 | EH1 12YF>W | - | F126W, Y140W, F141W, Y169W, F178W, F205W, Y211W, Y220W, F224W, F257W, F260W, F300W | |
| psp00800 | EH1 EH2 R>E | - | R391E, R394E, R431E | |
| psp00918 | EH1 26P>G | - | P129G, P132G, P142G, P143G, P151G, P163G, P167G, P171G, P180G, P182G, P189G, P190G, P192G, P194G, P200G | |
| psp02694 | EH1 12YF>S | - | F126S, Y140S, F141S, Y169S, F178S, F205S, Y211S, Y220S, F224S, F257S, F260S, F300S | |
| psp03028 | EH1 EH1 KR>E | - | K42E, K78E, R79E | |
| psp03333 | EH1 8KR>G | - | R150G, R162G, R170G, K237G, K245G, K263G, K289G, R313G | |
| psp03723 | EH1 6DE>A | - | E168A, E239A, D243A, D255A, E265A, D294A | |
| psp04600 | EH1 EH1-2 KR>E | - | K42E, K78E, R79E, R391E, R394E, R431E | |
| psp01212 | EH1 ΔIDR3 EH1-2 KR>E | 1-671 | K42E, K78E, R79E, R391E, R394E, R431E | |
| psp01688 | EH1 ΔIDR3 EH2 R>E | 1-671 | R391E, R394E, R431E | |
| psp01917 | EH1 ΔIDR3 EH1 KR>E | 1-671 | K42E, K78E, R79E | |
| psp02139 | EH1 (IDR1 replaced with HsITSN1) | - | - | |
| psp02582 | EH1 (IDR1 replaced with ScEde1) | - | - | |
| psp04052 | EH1 (IDR1 replaced with ScPan1) | - | - |
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