Prothymosin alpha (human) studies and research data
PepBank has no study results for Prothymosin alpha (human) yet. Data as of 2026-10-30.
Searches 0 results and 0 papers. Newer studies from Europe PMC
Prothymosin alpha (human) identity
Identifiers, parent molecule, targets and development stage, from curated data.
Prothymosin alpha is encoded by PTMA (UniProt P06454). UniProt lists two chains: the full 111-residue form (N-acetylmethionine) and an N-terminally processed form starting at Ser2 (N-acetylserine). Thymosin alpha-1 corresponds to residues 2-29. UniProt places the protein in the nucleus and states it may mediate immune function by conferring resistance to certain opportunistic infections.
- Kind
- Natural peptide · 111 residues
- Identifiers
- UniProtP06454 (opens in a new tab)
- Development
- No known clinical developmentNo development of the full protein found. The derived peptide thymosin alpha-1 is approved outside the US and EU as Zadaxin. Source (opens in a new tab)
Targets
No molecular target is recorded for this peptide.
Sequence and structure
Residues, differences from the parent, calculated properties and 3D structure. Source values and calculated values are shown separately.
Sequence
111 amino acids · 1 modification
Properties
From identity sources
No formula or molecular weight is listed for Prothymosin alpha (human).
Calculated from the sequence
- Average mass
- 12,245.00 Da
- Sum of ExPASy residue masses + water + N-acetyl · ExPASy Compute pI/Mw; FindMod
- Monoisotopic mass
- 12,237.9793 Da
- Sum of ExPASy residue masses + water + N-acetyl · ExPASy FindMod
- Isoelectric point (pI)
- 3.36
- pH of zero net charge, EMBOSS pKa set · EMBOSS iep, Epk.dat
- Net charge at pH 7.4
- −44.98
- Henderson-Hasselbalch, EMBOSS pKa set · EMBOSS iep, Epk.dat
- GRAVY (hydropathy)
- −1.971
- Mean Kyte-Doolittle hydropathy · Kyte and Doolittle 1982
- Negative: hydrophilic on average.
- Extinction coefficient, 280 nm (Cys reduced)
- 0 M⁻¹ cm⁻¹
- 5500 x Trp + 1490 x Tyr · Pace et al. 1995 (ExPASy ProtParam)
- No Trp or Tyr: absorbance at 280 nm cannot measure this peptide.
- Instability index
- 72.90
- Dipeptide instability weights (DIWV) · Guruprasad et al. 1990
- Above 40: classed as possibly unstable (ExPASy).
- Aliphatic index
- 30.0
- Mole % A + 2.9 V + 3.9 (I + L) · Ikai 1980
- Boman index
- 4.48 kcal/mol
- Mean solubility value (negated) · Boman 2003
- Above 2.48: high protein-binding potential (Boman).
- Hydrophobic moment (μH)
- 0.448
- Eisenberg scale, 100° per residue, best 11-residue window · Eisenberg et al. 1982, 1984
- pI with each pKa set
- EMBOSS 3.36Bjellqvist (ExPASy) 3.63IPC peptide 3.44IPC protein 3.48
- Defined and validated for proteins; use with care for short peptides.
- Assumes an ideal alpha helix. Many short peptides are not helical.
@pepdb/chem 0.2.0 · EMBOSS pKa set · ExPASy residue masses
Net charge by pH
pI 3.36 · Net charge at pH 7.4: −44.98
Point or use arrow keys
Henderson-Hasselbalch, EMBOSS pKa set, N-acetyl. Calculated, not measured.
Show as table
| pH | Net charge |
|---|---|
| 0 | 9.99 |
| 1 | 9.95 |
| 2 | 9.46 |
| 3 | 5.10 |
| 4 | −16.80 |
| 5 | −39.65 |
| 6 | −44.41 |
| 7 | −44.94 |
| 8 | −45.01 |
| 9 | −45.12 |
| 10 | −46.10 |
| 11 | −49.97 |
| 12 | −53.01 |
| 13 | −54.47 |
| 14 | −54.93 |
Composition
- Hydrophobic17% (19)A I L M V
- Positive9% (10)K R
- Negative49% (54)D E
- Polar16% (18)N Q S T
- Special9% (10)G P
111 residues. Each residue counts in one class; F and W count as aromatic.
3D structure
Loads the 3D viewer (3Dmol.js, about 150 KB) and the model file from AlphaFold DB (EMBL-EBI).
Helical wheel
An ideal alpha-helix projection. It shows where the hydrophobic residues fall if the peptide folds as a helix. It does not show that it does.
- μH, residues shown
- 0.189
- μH, best 11-residue window
- 0.448
- Arrow direction
- 78°
- Residues
- 1–54 of 111 · 3 rings of 18
Eisenberg consensus (normalized) scale · + K, R · − D, E
Assumes an ideal α-helix: 100° per residue, 3.6 residues per turn. The arrow is the mean hydrophobic moment (Eisenberg et al. 1984) and points at the hydrophobic face.
Show as table
| Position | Residue | Angle | Eisenberg consensus (normalized) |
|---|---|---|---|
| 1 | M | 0° | 0.64 |
| 2 | S | 100° | -0.18 |
| 3 | D | 200° | -0.90 |
| 4 | A | 300° | 0.62 |
| 5 | A | 40° | 0.62 |
| 6 | V | 140° | 1.08 |
| 7 | D | 240° | -0.90 |
| 8 | T | 340° | -0.05 |
| 9 | S | 80° | -0.18 |
| 10 | S | 180° | -0.18 |
| 11 | E | 280° | -0.74 |
| 12 | I | 20° | 1.38 |
| 13 | T | 120° | -0.05 |
| 14 | T | 220° | -0.05 |
| 15 | K | 320° | -1.50 |
| 16 | D | 60° | -0.90 |
| 17 | L | 160° | 1.06 |
| 18 | K | 260° | -1.50 |
| 19 | E | 0° | -0.74 |
| 20 | K | 100° | -1.50 |
| 21 | K | 200° | -1.50 |
| 22 | E | 300° | -0.74 |
| 23 | V | 40° | 1.08 |
| 24 | V | 140° | 1.08 |
| 25 | E | 240° | -0.74 |
| 26 | E | 340° | -0.74 |
| 27 | A | 80° | 0.62 |
| 28 | E | 180° | -0.74 |
| 29 | N | 280° | -0.78 |
| 30 | G | 20° | 0.48 |
| 31 | R | 120° | -2.53 |
| 32 | D | 220° | -0.90 |
| 33 | A | 320° | 0.62 |
| 34 | P | 60° | 0.12 |
| 35 | A | 160° | 0.62 |
| 36 | N | 260° | -0.78 |
| 37 | G | 0° | 0.48 |
| 38 | N | 100° | -0.78 |
| 39 | A | 200° | 0.62 |
| 40 | E | 300° | -0.74 |
| 41 | N | 40° | -0.78 |
| 42 | E | 140° | -0.74 |
| 43 | E | 240° | -0.74 |
| 44 | N | 340° | -0.78 |
| 45 | G | 80° | 0.48 |
| 46 | E | 180° | -0.74 |
| 47 | Q | 280° | -0.85 |
| 48 | E | 20° | -0.74 |
| 49 | A | 120° | 0.62 |
| 50 | D | 220° | -0.90 |
| 51 | N | 320° | -0.78 |
| 52 | E | 60° | -0.74 |
| 53 | V | 160° | 1.08 |
| 54 | D | 260° | -0.90 |
What the studies measured
People first in each area, then animals, then lab cells. Counts are exact and come from studies that gave the peptide.
Newer studies
PepBank reads each paper before it shows the results. This search looks in Europe PMC for newer papers that PepBank has not read yet.
Prothymosin alpha (human) studies: 0 papers with results
No paper with results is linked to this peptide.