IthaID: 1485
Names and Sequences
| Functionality: | Globin gene causative mutation | Pathogenicity: | N/A |
|---|---|---|---|
| Common Name: | CD 121 GAA>AAA [Glu>Lys] | HGVS Name: | HBG1:c.364G>A |
| Hb Name: | Hb F-Hull | Protein Info: | Aγ 121(GH4) Glu>Lys |
Context nucleotide sequence:
CGTTTTGGCAATCCATTTCGGCAAA [G>A] AATTCACCCCTGAGGTGCAGGCTTC (Strand: -)
Protein sequence:
MGHFTEEDKATITSLWGKVNVEDAGGETLGRLLVVYPWTQRFFDSFGNLSSASAIMGNPKVKAHGKKVLTSLGDATKHLDDLKGTFAQLSELHCDKLHVDPENFKLLGNVLVTVLAIHFGKKFTPEVQASWQKMVTAVASALSSRYH
Also known as: Hb F-Siena
Comments: Initially found as an electrophoretically slow component of the cord-blood haemoglobin (Hb) of three normal babies, making up 7-14% of the total Hb, and was characterized by protein analysis as a glutamic acid > lysine sustitution at position 121 in the γ-chain [PMID: 6038320]. Further characterization reported that this variant occurs in a Αγ chain [PMID: 4710228]. Molecular analysis with selected restriction endonucleases characterized Hb F-Hull as a GAA > AAA change at position Αγ121 [PMID: 2412617].
We follow the HGVS sequence variant nomenclature and IUPAC standards.
Phenotype
| Hemoglobinopathy Group: | Structural Haemoglobinopathy |
|---|---|
| Hemoglobinopathy Subgroup: | γ-chain variant |
| Allele Phenotype: | N/A |
| Stability: | N/A |
| Oxygen Affinity: | N/A |
| Associated Phenotypes: | N/A |
Location
| Chromosome: | 11 |
|---|---|
| Locus: | NG_000007.3 |
| Locus Location: | 49177 |
| Size: | 1 bp |
| Located at: | Aγ |
| Specific Location: | Exon 3 |
Other details
| Type of Mutation: | Point-Mutation(Substitution) |
|---|---|
| Effect on Gene/Protein Function: | N/A |
| Ethnic Origin: | English, Italian |
| Molecular mechanism: | N/A |
| Inheritance: | Recessive |
| DNA Sequence Determined: | Yes |
In silico pathogenicity prediction
Publications / Origin
- Sacker LS, Beale D, Black AJ, Huntsman RG, Lehmann H, Lorkin PA, Haemoglobin F Hull (gamma-121 glutamic acid--lysine), homologous with haemoglobins O Arab and O Indonesia., British medical journal, 3(5564), 531-3, 1967
- Ahern EJ, Ahern V, Wiltshire BG, Lehmann H, Further characterization of haemoglobin F Hull 121 glutamic acid leads to lysine; 136 alanine., Biochim Biophys Acta, 303(2), 242-5, 1973
- Carè A, Marinucci M, Massa A, Maffi D, Sposi NM, Improta T, Tentori L, Hb F-Siena (alpha 2 a gamma t2 121 (GH4) Glu leads to Lys). A new fetal hemoglobin variant., Hemoglobin, 7(1), 79-83, 1983
- Nakatsuji T, Burnley MS, Huisman TH, Fetal hemoglobin variants identified in adults through restriction endonuclease gene mapping methodology., Blood, 66(4), 803-7, 1985