MED19a (113-221)

ID psp01644
Organism Arabidopsis thaliana
Length 109

PS Record in Articles

Reference (Pubmed ID) In vitro results In vivo results
36093737 Positive -

Protein Sequence

Sequence Variants

ID Name Remain region Mutation sites Ref seq
psp04974 MED19a 1-221 -
psp01644 MED19a (113-221) 113-221 -
psp01678 AtMed19a (1-112)+HsMED19 (176-261) - -
psp04879 AtMed19a (1-112)+ScMED19 (127-220) - -

Orthologs and Paralogs

ID Name Organism Length
psp00862 MED1 Homo sapiens 1581
psp02174 Med19 Mus musculus 244
psp00852 MED15 Saccharomyces cerevisiae 1081
psp05059 MED8 Arabidopsis thaliana 524
psp00928 MED8 (60Q to A) Arabidopsis thaliana 524
psp03150 MED8 (79Q to A) Arabidopsis thaliana 524
psp04880 MED8 (40Q to A) Arabidopsis thaliana 524
psp00578 MED1 IDR Homo sapiens 634
psp01413 MED1 IDRXL Homo sapiens 974
psp01583 MED1 IDR Homo sapiens 626
psp02320 MED1 IDR (963-1320) Homo sapiens 358
psp03832 MED1 IDR (948-1574) Homo sapiens 627
psp03133 MED13 exon 20 Homo sapiens 153

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