Variant position: 7 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 142 The length of the canonical sequence.
Location on the sequence:
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 MVLSPA DKTNVKAAWGKVGAHAGEYGA
Gorilla -VLSPA DKTNVKAAWGKVGAHAGDYGA
Rhesus macaque MVLSPA DKSNVKAAWGKVGGHAGEYGA
Chimpanzee MVLSPA DKTNVKAAWGKVGAHAGEYGA
Mouse MVLSGE DKSNIKAAWGKIGGHGAEYGA
Rat MVLSAD DKTNIKNCWGKIGGHGGEYGE
Pig -VLSAA DKANVKAAWGKVGGQAGAHGA
Bovine MVLSAA DKGNVKAAWGKVGGHAAEYGA
Rabbit MVLSPA DKTNIKTAWEKIGSHGGEYGA
Sheep MVLSAA DKSNVKAAWGKVGGNAGAYGA
Cat -VLSAA DKSNVKACWGKIGSHAGEYGA
Horse MVLSAA DKTNVKAAWSKVGGHAGEYGA
Chicken MVLSAA DKNNVKGIFTKIAGHAEEYGA
Xenopus tropicalis MHLTAD DKKHIKAIWPSVAAHGDKYGG
Zebrafish MSLSDT DKAVVKAIWAKISPKADEIGA
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
1 – 1 Removed
2 – 142 Hemoglobin subunit alpha
12 – 12 Not glycated
4 – 4 Phosphoserine
8 – 8 N6-succinyllysine; alternate
9 – 9 Phosphothreonine
12 – 12 N6-succinyllysine
17 – 17 N6-acetyllysine; alternate
17 – 17 N6-succinyllysine; alternate
25 – 25 Phosphotyrosine
8 – 8 N-linked (Glc) (glycation) lysine; alternate
17 – 17 N-linked (Glc) (glycation) lysine; alternate
5 – 18
Hemoglobin Dunn: alpha 6 (A4) aspartic acid replaced by asparagine.
Jue D.L.; Johnson M.H.; Patchen L.C.; Moo-Penn W.F.;
Cited for: VARIANT DUNN ASN-7;
Oxygen affinity and stability of hemoglobin Dunn alpha 6(A4)Asp replaced by Asn): use of isoelectric focusing in recognition of a new abnormal hemoglobin.
Charache S.; Brimhall B.; Zaatari G.;
Am. J. Hematol. 9:151-160(1980)
Cited for: CHARACTERIZATION OF VARIANT DUNN ASN-7;
Structural characterizations of hemoglobins J-Buda (alpha 61 (E10) Lys-to-Asn) and G-Pest (alpha 74 (EF3) Asp-to-Asn).
Brimhall B.J.; Duerst M.; Hollan S.R.; Stenzel P.; Szelenyi J.; Jones R.T.;
Cited for: VARIANTS J-BUDA ASN-62 AND G-PEST ASN-75;
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.