rs33954264

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
google	rs33954264
pharmgkb	rs33954264
gwascentral	rs33954264
openSNP	rs33954264
23andMe	rs33954264
SNPshot	rs33954264
SNPdbe	rs33954264
MSV3d	rs33954264
GWAS Ctlg	rs33954264

Max Magnitude

0

OMIM	141900
Desc
Variant	0051
Related	also

OMIM	141900
Desc
Variant	0056
Related	also

OMIM	141900
Desc
Variant	0305
Related	also

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.