EH1 EH1-2 KR>E

ID psp04600
Organism Arabidopsis thaliana
Length 1019

PS Record in Articles

Reference (Pubmed ID) In vitro results In vivo results
38347182 - Positive

Protein Sequence

Sequence Variants

ID Name Remain region Mutation sites Ref seq
psp04549 EH1 1-1019 -
psp04600 EH1 EH1-2 KR>E - K42E, K78E, R79E, R391E, R394E, R431E
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 -
psp02929 EH1 ΔCCΔIDR3 1-534 -
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
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) - -

Orthologs and Paralogs

ID Name Organism Length
psp03468 EH2 Arabidopsis thaliana 1247

Biophysical Features

The chart can zoom in and zoom out by mouse wheel.

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