rs33954264
Orientation | minus |
Stabilized | minus |
Geno | Mag | Summary |
---|---|---|
(A;A) | 0 | common in complete genomics |
Make rs33954264(A;C) |
Make rs33954264(C;C) |
Reference | GRCh38 38.1/141 |
Chromosome | 11 |
Position | 5225602 |
Gene | HBB |
is a | snp |
is | mentioned by |
dbSNP | rs33954264 |
dbSNP (classic) | rs33954264 |
ClinGen | rs33954264 |
ebi | rs33954264 |
HLI | rs33954264 |
Exac | rs33954264 |
Gnomad | rs33954264 |
Varsome | rs33954264 |
LitVar | rs33954264 |
Map | rs33954264 |
PheGenI | rs33954264 |
Biobank | rs33954264 |
1000 genomes | rs33954264 |
hgdp | rs33954264 |
ensembl | rs33954264 |
geneview | rs33954264 |
scholar | rs33954264 |
rs33954264 | |
pharmgkb | rs33954264 |
gwascentral | rs33954264 |
openSNP | rs33954264 |
23andMe | rs33954264 |
SNPshot | rs33954264 |
SNPdbe | rs33954264 |
MSV3d | rs33954264 |
GWAS Ctlg | rs33954264 |
Max Magnitude | 0 |
ClinVar | |
---|---|
Risk | rs33954264(C;C) rs33954264(G;G) rs33954264(T;T) |
Alt | rs33954264(C;C) rs33954264(G;G) rs33954264(T;T) |
Reference | Rs33954264(A;A) |
Significance | Other |
Disease | HEMOGLOBIN COWTOWN HEMOGLOBIN COCHIN-PORT ROYAL HEMOGLOBIN YORK |
Variation | info |
Gene | HBB |
CLNDBN | HEMOGLOBIN COWTOWN HEMOGLOBIN COCHIN-PORT ROYAL HEMOGLOBIN YORK |
Reversed | 1 |
HGVS | NC_000011.9:g.5246832T>A; NC_000011.9:g.5246832T>C; NC_000011.9:g.5246832T>G |
CLNSRC | HBVAR OMIM Allelic Variant UniProtKB (protein) |
CLNACC | RCV000016307.3, RCV000016302.3, RCV000016648.2, |
[PMID 1246355] Altered C-terminal salt bridges in haemoglobin York cause high oxygen affinity.
[PMID 3707904] Assessment of role of beta 146-histidyl and other histidyl residues in the Bohr effect of human normal adult hemoglobin.
[PMID 6874372] Characterization and properties of Hb York (beta 146 His leads to Pro).
[PMID 240418] Hemoglobin Cochin-Port-Royal: consequences of the replacement of the beta chain C-terminal by an arginine.
[PMID 42311] Hemoglobin Cowtown (beta 146 HC3 His-Leu): a mutant with high oxygen affinity and erythrocytosis.
[PMID 6589624] Structure of deoxyhemoglobin Cowtown [His HC3(146) beta----Leu]: origin of the alkaline Bohr effect and electrostatic interactions in hemoglobin.