Sequence information
Variant position: 7 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 147 The length of the canonical sequence.
Location on the sequence:
MVHLTP
E EKSAVTALWGKVNVDEVGGE
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human MVHLTPE EKSAVTALWGKVNVDEVGGE
Gorilla MVHLTPE EKSAVTALWGKVNVDEVGGE
Rhesus macaque -VHLTPE EKNAVTTLWGKVNVDEVGGE
Chimpanzee MVHLTPE EKSAVTALWGKVNVDEVGGE
Pig MVHLSAE EKEAVLGLWGKVNVDEVGGE
Bovine --MLTAE EKAAVTAFWGKVKVDEVGGE
Rabbit MVHLSSE EKSAVTALWGKVNVEEVGGE
Sheep --MLTAE EKAAVTGFWGKVKVDEVGAE
Cat -GFLTAE EKGLVNGLWGKVNVDEVGGE
Horse -VQLSGE EKAAVLALWDKVNEEEVGGE
Chicken MVHWTAE EKQLITGLWGKVNVAECGAE
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
Initiator methionine
1 – 1
Removed
Chain
2 – 147
Hemoglobin subunit beta
Binding site
2 – 2
Binding site
3 – 3
Modified residue
2 – 2
N-acetylvaline
Modified residue
2 – 2
N-pyruvate 2-iminyl-valine; in Hb A1b
Modified residue
10 – 10
Phosphoserine
Modified residue
13 – 13
Phosphothreonine
Glycosylation
2 – 2
N-linked (Glc) (glycation) valine; in Hb A1c
Glycosylation
9 – 9
N-linked (Glc) (glycation) lysine
Glycosylation
18 – 18
N-linked (Glc) (glycation) lysine
Helix
6 – 17
Literature citations
The beta-globin recombinational hotspot reduces the effects of strong selection around HbC, a recently arisen mutation providing resistance to malaria.
Wood E.T.; Stover D.A.; Slatkin M.; Nachman M.W.; Hammer M.F.;
Am. J. Hum. Genet. 77:637-642(2005)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANT LYS-7;
Hemoglobin C associated with protection from severe malaria in the Dogon of Mali, a West African population with a low prevalence of hemoglobin S.
Agarwal A.; Guindo A.; Cissoko Y.; Taylor J.G.; Coulibaly D.; Kone A.; Kayentao K.; Djimde A.; Plowe C.V.; Doumbo O.; Wellems T.E.; Diallo D.;
Blood 96:2358-2363(2000)
Cited for: POLYMORPHISM; ASSOCIATION OF VARIANT LYS-7 WITH RESISTANCE TO MALARIA;
Structure of mutant human carbonmonoxyhemoglobin C (betaE6K) at 2.0 A resolution.
Dewan J.C.; Feeling-Taylor A.; Puius Y.A.; Patskovska L.; Patskovsky Y.; Nagel R.L.; Almo S.C.; Hirsch R.E.;
Acta Crystallogr. D 58:2038-2042(2002)
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF VARIANT LYS-7;
Disclaimer:
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.