UniProtKB/Swiss-Prot P69905: Variant p.Asp127Tyr

Hemoglobin subunit alpha
Gene: HBA2
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Variant information Variant position:

127 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 Aspartate (D) to Tyrosine (Y) at position 127 (D127Y, p.Asp127Tyr). 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 acidic (D) to large size and aromatic (Y) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-3 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 Montefiore; O(2) affinity up. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs33933481 [ dbSNP | Ensembl ]

Sequence information Variant position:

127 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:

LVTLAAHLPAEFTPAVHASL D KFLASVSTVLTSKYR 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                         LVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR

Gorilla                       LVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR

                              LVTLACHHPTEFTPAVHASLDKFFAAVSTVLTSKYR

Rhesus macaque                LVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR

Chimpanzee                    LVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR

Mouse                         LVTLASHHPADFTPAVHASLDKFLASVSTVLTSKYR

Rat                           LVTLACHHPGDFTPAMHASLDKFLASVSTVLTSKYR

Pig                           LVTLAAHHPDDFNPSVHASLDKFLANVSTVLTSKYR

Bovine                        LVTLASHLPSDFTPAVHASLDKFLANVSTVLTSKYR

Rabbit                        LVTLANHHPSEFTPAVHASLDKFLANVSTVLTSKYR

Sheep                         LVTLACHLPNDFTPAVHASLDKFLANVSTVLTSKYR

Cat                           LVTLACHHPAEFTPAVHASLDKFFSAVSTVLTSKYR

Horse                         LSTLAVHLPNDFTPAVHASLDKFLSSVSTVLTSKYR

Chicken                       LVVVAIHHPAALTPEVHASLDKFLCAVGTVLTAKYR

Xenopus tropicalis            LVVVAIHFPKQFDPATHKALDKFLVSVSNVLTSKYR

Zebrafish                     IVVIAMLFPADFTPEVHVSVDKFFNNLALALSEKYR

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
Modified residue	109 – 109	Phosphothreonine
Modified residue	125 – 125	Phosphoserine
Modified residue	132 – 132	Phosphoserine
Modified residue	135 – 135	Phosphothreonine
Modified residue	138 – 138	Phosphothreonine
Modified residue	139 – 139	Phosphoserine
Helix	120 – 138

Literature citations
Hb Montefiore (126(H9)Asp-->Tyr). High oxygen affinity and loss of cooperativity secondary to C-terminal disruption.
Wajcman H.; Kister J.; Galacteros F.; Spielvogel A.; Lin M.J.; Vidugiris G.J.; Hirsch R.E.; Friedman J.M.; Nagel R.L.;
J. Biol. Chem. 271:22990-22998(1996)
Cited for: VARIANT MONTEFIORE TYR-127;

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.