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
A new hemoglobin, beta chain variant 'Hb S-Wake' confirmed to be on the same chromosome with hemoglobin S mutation, detected in an African-American family.
Kutlar F.; Lallinger R.R.; Holley L.; Glendenning M.; Kutlar A.;
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANT SKCA VAL-7; VARIANT SER-140;
Gene mutations in human haemoglobin: the chemical difference between normal and sickle cell haemoglobin.
Ingram V.M.;
Nature 180:326-328(1957)
Cited for: PROTEIN SEQUENCE OF 3-9; INVOLVEMENT IN SKCA; VARIANT SKCA VAL-7;
How malaria has affected the human genome and what human genetics can teach us about malaria.
Kwiatkowski D.P.;
Am. J. Hum. Genet. 77:171-192(2005)
Cited for: POLYMORPHISM; ASSOCIATION OF VARIANT SKCA VAL-7 WITH RESISTANCE TO MALARIA;
Crystal structure of sickle-cell deoxyhemoglobin at 5 A resolution.
Wishner B.C.; Ward K.B.; Lattman E.E.; Love W.E.;
J. Mol. Biol. 98:179-194(1975)
Cited for: X-RAY CRYSTALLOGRAPHY (5 ANGSTROMS) OF VARIANT SKCA VAL-7;
Structure of fully liganded Hb zeta2beta2s trapped in a tense conformation.
Safo M.K.; Ko T.P.; Abdulmalik O.; He Z.; Wang A.H.; Schreiter E.R.; Russell J.E.;
Acta Crystallogr. D 69:2061-2071(2013)
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF VARIANT SKCA VAL-7 IN COMPLEX WITH HEME AND HBZ; SUBUNIT;
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.