AHSP (Alpha Hemoglobin Stabilizing Protein)
A key chaperone for alpha-globin in erythropoiesis
Gene Information Card
| Symbol | AHSP |
|---|---|
| Full Name | Alpha Hemoglobin Stabilizing Protein |
| Gene Type | Protein coding |
| Chromosomal Location | 16p11.2 |
| NCBI Gene ID | 51327 ncbi.nlm.nih.gov/gene/51327 |
| Ensembl ID | ENSG00000164111 |
| UniProt ID | Q9NZD4 |
| OMIM ID | 608621 |
| HGNC ID | 18075 |
| Aliases | EDRF, ERAF, EDRF1 |
Description
AHSP encodes alpha hemoglobin stabilizing protein, a small chaperone that binds specifically to free alpha-globin chains, preventing their precipitation and facilitating proper hemoglobin assembly. It is essential for normal erythropoiesis and red blood cell survival.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Alpha-thalassemia | Loss of AHSP function exacerbates alpha-globin chain precipitation and oxidative damage in red blood cells | OMIM 608621, NCBI Gene |
| Hemolytic anemia | AHSP deficiency leads to increased red blood cell destruction due to unstable hemoglobin | ClinVar, NCBI Gene |
| Beta-thalassemia intermedia | AHSP variants may modify disease severity by affecting alpha-globin stabilization | NCBI Gene, OMIM |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Bone marrow | 25.6 | Medium |
| Spleen | 12.3 | Low |
| Blood | 8.9 | Low |
| Liver | 4.2 | Low |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| K562 | 15.4 | Erythroleukemia cell line |
| HEL | 12.1 | Erythroleukemia cell line |
| TF-1 | 10.3 | Erythroid progenitor cell line |
| HepG2 | 2.1 | Hepatocellular carcinoma cell line |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.2T>C (p.Met1?) | Missense | Rare | Loss of start codon, reduced protein expression |
| c.82G>A (p.Gly28Ser) | Missense | Rare | Impaired alpha-globin binding |
| c.199C>T (p.Arg67Cys) | Missense | Rare | Reduced chaperone activity |
| c.301A>G (p.Lys101Glu) | Missense | Rare | Altered protein stability |
Mutation functional classification
Loss of Function (LOF)
Mutations that reduce AHSP expression or alpha-globin binding lead to loss of chaperone function, contributing to alpha-thalassemia and hemolytic anemia.
Gain of Function (GOF)
No gain-of-function mutations have been reported for AHSP.
Dominant Negative (DN)
No dominant-negative mutations have been described for AHSP.
View complete mutation data：
Gene Ontology (GO)
| • GO:0005515 - protein binding | • GO:0019825 - oxygen binding |
| • GO:0030492 - hemoglobin binding | • GO:0051082 - unfolded protein binding |
| • GO:0005634 - nucleus | • GO:0005737 - cytoplasm |
Pathways
• Erythropoiesis (Reactome R-HSA-917937)
• Hemoglobin synthesis (Reactome R-HSA-983147)
Protein Summary
AHSP is a 102-amino acid protein that acts as a molecular chaperone for alpha-globin. It binds free alpha-globin chains, preventing their aggregation and oxidative damage, and facilitates their incorporation into hemoglobin. AHSP is highly expressed in erythroid cells and is critical for red blood cell development and survival.
Related Services
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| AHSP Knockout HEK293 Cell Line | EDJ-KQ11052 | Human | 51327 | Details Get a Quote |
| AHSP Knockout HeLa Cell Line | EDJ-KQ56286 | Human | 51327 | Details Get a Quote |
| AHSP Knockout A-549 Cell Line | EDJ-KQ64774 | Human | 51327 | Details Get a Quote |
| AHSP Knockout HCT 116 Cell Line | EDJ-KQ73223 | Human | 51327 | Details Get a Quote |
Displaying Records 1 To 4 Of 4 Records
