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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P69905: Variant p.Lys62Asn

Hemoglobin subunit alpha
Gene: HBA2
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Variant information Variant position: help 62 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LB/B The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change: help From Lysine (K) to Asparagine (N) at position 62 (K62N, p.Lys62Asn). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from large size and basic (K) to medium size and polar (N) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Variant description: help In J-Buda. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 62 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 142 The length of the canonical sequence.
Location on the sequence: help TYFPHFDLSHGSAQVKGHGK K VADALTNAVAHVDDMPNALS 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human                         TYFPHF-DLSHGSAQVKGHGKKVADALTNAVAHVDDMPNALS

Gorilla                       TYFPHF-DLSHGSAQVKGHGKKVADALTNAVAHVDDMPNAL

                              TYFPHF-DLSPGSAQVKAHGKKVADALTTAVAHLDDLPGAL

Rhesus macaque                TYFPHF-DLSHGSAQVKGHGKKVADALTLAVGHVDDMPNAL

Chimpanzee                    TYFPHF-DLSHGSAQVKGHGKKVADALTNAVAHVDDMPNAL

Mouse                         TYFPHF-DVSHGSAQVKGHGKKVADALASAAGHLDDLPGAL

Rat                           TYFSHI-DVSPGSAQVKAHGKKVADALAKAADHVEDLPGAL

Pig                           TYFPHF-NLSHGSDQVKAHGQKVADALTKAVGHLDDLPGAL

Bovine                        TYFPHF-DLSHGSAQVKGHGAKVAAALTKAVEHLDDLPGAL

Rabbit                        TYFPHF-DFTHGSEQIKAHGKKVSEALTKAVGHLDDLPGAL

Sheep                         TYFPHF-DLSHGSAQVKGHGEKVAAALTKAVGHLDDLPGTL

Cat                           TYFPHF-DLSHGSAQVKAHGQKVADALTQAVAHMDDLPTAM

Horse                         TYFPHF-DLSHGSAQVKAHGKKVGDALTLAVGHLDDLPGAL

Chicken                       TYFPHF-DLSHGSAQIKGHGKKVVAALIEAANHIDDIAGTL

Xenopus tropicalis            TYFPDF-DFSEHSKHILAHGKKVSDALNEACNHLDNIAGCL

Zebrafish                     TYFSHWADLSPGSGPVKKHGKTIMGAVGEAISKIDDLVGGL

Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 2 – 142 Hemoglobin subunit alpha
Domain 2 – 142 Globin
Binding site 59 – 59
Site 57 – 57 Not glycated
Site 61 – 61 Not glycated
Modified residue 50 – 50 Phosphoserine
Glycosylation 62 – 62 N-linked (Glc) (glycation) lysine
Helix 54 – 72



Literature citations
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 ASN-62 AND ASN-75;
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.