ELKS-1 (301-335Δ;747-775Δ;807-836Δ)

ID psp02389
Organism Caenorhabditis elegans
Length 742

PS Record in Articles

Reference (Pubmed ID) In vitro results In vivo results
33208945 Positive -

Protein Sequence

Sequence Variants

ID Name Remain region Mutation sites Ref seq
psp00435 ELKS-1 1-836 - ✓
psp02389 ELKS-1 (301-335Δ;747-775Δ;807-836Δ) 1-300, 336-746, 776-806 -
psp00014 ELKS-1 337-412 337-412 -
psp00047 ELKS-1 807-836 807-836 -
psp00101 ELKS-1 716-836(747-775Δ) 716-746, 776-836 -
psp00500 ELKS-1 262-375(301-335Δ) 262-300, 336-375 -
psp00886 ELKS-1 300-375 300-375 -
psp01064 ELKS-1 1-149 1-149 -
psp01657 ELKS-1 450-599 450-599 -
psp01832 ELKS-1 336-449 336-449 -
psp01847 ELKS-1 746-806 746-806 -
psp03064 ELKS-1 600-749 600-749 -
psp03113 ELKS-1 150-299 150-299 -
psp03179 ELKS-1 (301-335Δ;716-775Δ;807-836Δ) 1-300, 336-715, 776-806 -
psp03344 ELKS-1 262-372 262-372 -
psp03374 ELKS-1 (301-335Δ;747-775Δ) 1-300, 336-746, 776-836 -
psp03916 ELKS-1 413-488 413-488 -
psp03998 ELKS-1 300-499 300-499 -
psp04135 ELKS-1 716-806(747-775Δ) 716-746, 776-806 -
psp04196 ELKS-1 776-836 776-836 -
psp04340 ELKS-1 262-336 262-336 -
psp04521 ELKS-1 716-836 716-836 -
psp04735 ELKS-1 716-775 716-775 -
psp05006 ELKS-1 376-450 376-450 -
psp05149 ELKS-1 226-300 226-300 -

Orthologs and Paralogs

No orthologs or paralogs found for this protein in the database.

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

Colered by pLDDT:
Very high (pLDDT > 90)
Confident (90 > pLDDT > 70)
Low (70 > pLDDT > 50)
Very low (pLDDT < 50)

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