Erythropoietin (human) studies and research data
PepBank has no study results for Erythropoietin (human) yet. Data as of 2026-10-30.
Searches 0 results and 0 papers. Newer studies from Europe PMC
Erythropoietin (human) identity
Identifiers, parent molecule, targets and development stage, from curated data.
Erythropoietin is a glycosylated hormone of 165 to 166 residues produced mainly by the kidney. It binds the erythropoietin receptor, which dimerises and activates JAK2 and the STAT pathway, and so controls the proliferation and differentiation of red cell precursors. A separate receptor heterocomplex of the erythropoietin receptor with CD131 mediates tissue protection, which is the basis for non-erythropoietic analogues such as cibinetide, and recombinant epoetins are approved in the United States and the European Union for anaemia. This record is a reference parent for cibinetide (ARA-290).
- Kind
- Natural peptide · 166 residues
- Identifiers
- UniProtP01588 (opens in a new tab)UNIICM7EU2L6MS (opens in a new tab)64FS3BFH5W (opens in a new tab)DrugBankDB00016 (opens in a new tab)CAS11096-26-7PDB1BUY (opens in a new tab)1CN4 (opens in a new tab)1EER (opens in a new tab)KEGGC18200 (opens in a new tab)IUPHAR4921 (opens in a new tab)
- Development
- Approved in the US and EU (Epogen / Procrit, 1989)Amgen (first recombinant product, Epogen); several later epoetin and biosimilar sponsorsThe 961 ClinicalTrials.gov records that name erythropoietin or epoetin as an intervention (query.intr=EXPANSION[Term]erythropoietin OR EXPANSION[Term]epoetin) cover many products and indications, so the number is not a development-stage measure for a single substance. Source (opens in a new tab)
Targets
| Target | Action | Evidence |
|---|---|---|
| Erythropoietin receptorEPORP19235 (opens in a new tab) | Agonist | primary literatureSource (opens in a new tab) |
| Innate repair receptor (erythropoietin receptor and CD131 heterocomplex)CSF2RBP32927 (opens in a new tab) | Agonist | primary literatureSource (opens in a new tab) |
Sequence and structure
Residues, differences from the parent, calculated properties and 3D structure. Source values and calculated values are shown separately.
Sequence
166 amino acids · 6 modifications · 2 disulfide bonds
Properties
From identity sources
- Formula
- C815H1313N233O241S5
- Molecular weight
- 18,392.2 g/mol
- Monoisotopic mass
- 18,380.6253 Da
- UniProt P01588(opens in a new tab)retrieved 2026-10-09
- GSRS UNII CM7EU2L6MS(opens in a new tab)retrieved 2026-10-09
- GSRS UNII 64FS3BFH5W(opens in a new tab)retrieved 2026-10-09
Calculated from the sequence
Some values cannot be calculated. A modification changes this value and is not modeled here (for example a lipid, metal or linker).
- Average mass
- Not calculated
- Monoisotopic mass
- Not calculated
- Isoelectric point (pI)
- Not calculated
- Net charge at pH 7.4
- Not calculated
- GRAVY (hydropathy)
- −0.188
- Mean Kyte-Doolittle hydropathy · Kyte and Doolittle 1982
- Negative: hydrophilic on average.
- Extinction coefficient, 280 nm (Cys reduced)
- 22,460 M⁻¹ cm⁻¹
- 5500 x Trp + 1490 x Tyr · Pace et al. 1995 (ExPASy ProtParam)
- Extinction coefficient, 280 nm (all Cys as cystines)
- 22,710 M⁻¹ cm⁻¹
- 5500 x Trp + 1490 x Tyr + 125 x cystine · Pace et al. 1995 (ExPASy ProtParam)
- Instability index
- 36.76
- Dipeptide instability weights (DIWV) · Guruprasad et al. 1990
- 40 or below: classed as stable (ExPASy).
- Aliphatic index
- 96.4
- Mole % A + 2.9 V + 3.9 (I + L) · Ikai 1980
- Boman index
- 1.64 kcal/mol
- Mean solubility value (negated) · Boman 2003
- 2.48 or below: lower protein-binding potential (Boman).
- Hydrophobic moment (μH)
- 0.859
- Eisenberg scale, 100° per residue, best 11-residue window · Eisenberg et al. 1982, 1984
- Not included: other modification. Mass, charge and pI are not calculated; use the identity-source values.
- 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
No charge curve
A modification changes this value and is not modeled here (for example a lipid, metal or linker).
Composition
- Hydrophobic36% (59)A I L M V
- Aromatic7% (11)F W Y
- Positive14% (23)H K R
- Negative11% (18)D E
- Polar20% (34)N Q S T
- Special13% (21)C G P
166 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 RCSB PDB.
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
- 0.104
- μH, best 11-residue window
- 0.859
- Arrow direction
- 348°
- Residues
- 1–54 of 166 · 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 | A | 0° | 0.62 |
| 2 | P | 100° | 0.12 |
| 3 | P | 200° | 0.12 |
| 4 | R | 300° | -2.53 |
| 5 | L | 40° | 1.06 |
| 6 | I | 140° | 1.38 |
| 7 | C | 240° | 0.29 |
| 8 | D | 340° | -0.90 |
| 9 | S | 80° | -0.18 |
| 10 | R | 180° | -2.53 |
| 11 | V | 280° | 1.08 |
| 12 | L | 20° | 1.06 |
| 13 | E | 120° | -0.74 |
| 14 | R | 220° | -2.53 |
| 15 | Y | 320° | 0.26 |
| 16 | L | 60° | 1.06 |
| 17 | L | 160° | 1.06 |
| 18 | E | 260° | -0.74 |
| 19 | A | 0° | 0.62 |
| 20 | K | 100° | -1.50 |
| 21 | E | 200° | -0.74 |
| 22 | A | 300° | 0.62 |
| 23 | E | 40° | -0.74 |
| 24 | N | 140° | -0.78 |
| 25 | I | 240° | 1.38 |
| 26 | T | 340° | -0.05 |
| 27 | T | 80° | -0.05 |
| 28 | G | 180° | 0.48 |
| 29 | C | 280° | 0.29 |
| 30 | A | 20° | 0.62 |
| 31 | E | 120° | -0.74 |
| 32 | H | 220° | -0.40 |
| 33 | C | 320° | 0.29 |
| 34 | S | 60° | -0.18 |
| 35 | L | 160° | 1.06 |
| 36 | N | 260° | -0.78 |
| 37 | E | 0° | -0.74 |
| 38 | N | 100° | -0.78 |
| 39 | I | 200° | 1.38 |
| 40 | T | 300° | -0.05 |
| 41 | V | 40° | 1.08 |
| 42 | P | 140° | 0.12 |
| 43 | D | 240° | -0.90 |
| 44 | T | 340° | -0.05 |
| 45 | K | 80° | -1.50 |
| 46 | V | 180° | 1.08 |
| 47 | N | 280° | -0.78 |
| 48 | F | 20° | 1.19 |
| 49 | Y | 120° | 0.26 |
| 50 | A | 220° | 0.62 |
| 51 | W | 320° | 0.81 |
| 52 | K | 60° | -1.50 |
| 53 | R | 160° | -2.53 |
| 54 | M | 260° | 0.64 |
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.
Erythropoietin (human) studies: 0 papers with results
No paper with results is linked to this peptide.