UniProtKB/Swiss-Prot P69905: Variant p.His113Asp

Hemoglobin subunit alpha
Gene: HBA2
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Variant information Variant position:

113 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

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:

From Histidine (H) to Aspartate (D) at position 113 (H113D, p.His113Asp). 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:

Change from medium size and polar (H) to medium size and acidic (D) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-1 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:

In Hopkins-II; unstable. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs281864885 [ dbSNP | Ensembl ]

Sequence information Variant position:

113 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:

RVDPVNFKLLSHCLLVTLAA H LPAEFTPAVHASLDKFLASV 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                         RVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASV

Gorilla                       RVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASV

                              RVDPVNFKLLSHCLLVTLACHHPTEFTPAVHASLDKFFAAV

Rhesus macaque                RVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASV

Chimpanzee                    RVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASV

Mouse                         RVDPVNFKLLSHCLLVTLASHHPADFTPAVHASLDKFLASV

Rat                           RVDPVNFKFLSHCLLVTLACHHPGDFTPAMHASLDKFLASV

Pig                           RVDPVNFKLLSHCLLVTLAAHHPDDFNPSVHASLDKFLANV

Bovine                        RVDPVNFKLLSHSLLVTLASHLPSDFTPAVHASLDKFLANV

Rabbit                        RVDPVNFKLLSHCLLVTLANHHPSEFTPAVHASLDKFLANV

Sheep                         RVDPVNFKLLSHSLLVTLACHLPNDFTPAVHASLDKFLANV

Cat                           RVDPVNFKFLSHCLLVTLACHHPAEFTPAVHASLDKFFSAV

Horse                         RVDPVNFKLLSHCLLSTLAVHLPNDFTPAVHASLDKFLSSV

Chicken                       RVDPVNFKLLGQCFLVVVAIHHPAALTPEVHASLDKFLCAV

Xenopus tropicalis            RVDPGNFPLLAHQILVVVAIHFPKQFDPATHKALDKFLVSV

Zebrafish                     RVDPANFKILSHNVIVVIAMLFPADFTPEVHVSVDKFFNNL

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
Chain	2 – 142	Hemoglobin subunit alpha
Domain	2 – 142	Globin
Site	100 – 100	Not glycated
Modified residue	103 – 103	Phosphoserine
Modified residue	109 – 109	Phosphothreonine
Modified residue	125 – 125	Phosphoserine
Modified residue	132 – 132	Phosphoserine
Helix	97 – 113

Literature citations
Clinical studies and physiological properties of Hopkins-2 haemoglobin.
Charache S.; Ostertag W.; von Ehrenstein G.;
Nature New Biol. 234:248-251(1971)
Cited for: VARIANT HOPKINS-II ASP-113;

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.