p53 (95-356)

ID psp03514
Organism Homo sapiens
Length 262

PS Record in Articles

Reference (Pubmed ID) In vitro results In vivo results
35618207 Positive -

Protein Sequence

Sequence Variants

ID Name Remain region Mutation sites Ref seq
psp03918 p53 1-393 -
psp03514 p53 (95-356) 95-356 -
psp00019 p53 ΔUBR 1-292 -
psp00111 p53 (326-393) 326-393 -
psp00186 p53 d_TD 1-306, 356-393 -
psp00285 p53 d_DBD 1-99, 301-393 -
psp00315 p53 (357-393) 357-393 -
psp01126 p53 (1-356) 1-356 -
psp01461 p53 TetCT (293-393) 293-393 -
psp01724 p53 CoreTetCT (94-393) 94-393 -
psp01833 p53 d_CTD 1-355 -
psp02895 p53 (95-393) 95-393 -
psp03509 p53 NCT 1-363 1-363 -
psp03711 p53 d_TAD 93-393 -
psp03895 p53 (1-94) 1-94 -
psp04231 p53 (1-325) 1-325 -
psp04318 p53C 94-312 -
psp00562 p53 (K139T) - K139T
psp01758 p53 S392D - S392D
psp01795 p53 (K139N) - K139N
psp02248 p53 L344P - L344P
psp02277 p53 L344A - L344A
psp02388 p53 S392E - S392E
psp02590 p53 S392A - S392A
psp03823 p53 (K120N) - K120N
psp03899 p53 (K139E) - K139E
psp04430 p53 (K139Q) - K139Q
psp04685 p53 (K120Q) - K120Q
psp04726 p53 (K120E) - K120E
psp00356 p53 UBR-R337H 293-393 R337H
psp01187 p53 UBR-R337C 293-393 R337C
psp02344 p53 UBR-R337P 293-393 R337P
psp02735 p53 UBR-L344P 293-393 L344P
psp03490 p53C R175H 94-312 R175H
psp04854 p53C R248Q 94-312 R248Q

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