HP1b
Synonyms: Heterochromatin protein 1 homolog beta, CBX, CBX1, HP1Hsbeta, HP1 beta, p25beta, M31, Heterochromatin protein p25, Chromobox protein homolog 1, Modifier 1 protein
PS Record in Articles
| Reference (Pubmed ID) | In vitro results | In vivo results |
|---|---|---|
| 31543422 | Negative | Positive |
Protein Sequence
Orthologs and Paralogs
| ID | Name | Organism | Length |
|---|---|---|---|
| psp03294 | HP1α | Homo sapiens | 191 |
| psp02710 | HP1α | Mus musculus | 191 |
| psp02442 | HP1α | Drosophila melanogaster | 206 |
| psp05125 | HP1g | Homo sapiens | 183 |
| psp01467 | mCherry-HP1α | Homo sapiens | 427 |
| psp04116 | HP1a-8aa-UnaG | Homo sapiens | 338 |
| psp00318 | HP1α A-A (Ser11-14-92,95,97→Ala) | Homo sapiens | 191 |
| psp00548 | HP1α E-E (Ser11-14,92,95,97→Glu) | Homo sapiens | 191 |
| psp01111 | HP1a I165E | Homo sapiens | 191 |
| psp03055 | nPhos-HP1α StoD | Homo sapiens | 191 |
| psp04324 | nPhos-HP1α StoE | Homo sapiens | 191 |
| psp04942 | HP1α E-A (Ser11-14→Glu; Ser92,95,97→Ala) | Homo sapiens | 191 |
| psp00150 | HP1α | Homo sapiens | 190 |
| psp01875 | HP1α hinge domain | Homo sapiens | 48 |
| psp02792 | HP1α ΔNTE | Homo sapiens | 173 |
| psp03843 | HP1α ΔCTE | Homo sapiens | 176 |
| psp03985 | HP1α ΔNTE ΔCTE | Homo sapiens | 159 |
| psp01273 | HP1γ | Homo sapiens | 182 |
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