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UniProtKB/Swiss-Prot P69905: Variant p.Ser139Pro

Hemoglobin subunit alpha
Gene: HBA2
Variant information Variant position: help 139 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 Serine (S) to Proline (P) at position 139 (S139P, p.Ser139Pro). 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 small size and polar (S) to medium size and hydrophobic (P) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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: help In Attleboro; O(2) affinity up. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.

Sequence information Variant position: help 139 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 TPAVHASLDKFLASVSTVLT S KYR 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                         TPAVHASLDKFLASVSTVLTSKYR

Gorilla                       TPAVHASLDKFLASVSTVLTSKYR

Rhesus macaque                TPAVHASLDKFLASVSTVLTSKYR

Chimpanzee                    TPAVHASLDKFLASVSTVLTSKYR

Mouse                         TPAVHASLDKFLASVSTVLTSKYR

Rat                           TPAMHASLDKFLASVSTVLTSKYR

Pig                           NPSVHASLDKFLANVSTVLTSKYR

Bovine                        TPAVHASLDKFLANVSTVLTSKYR

Rabbit                        TPAVHASLDKFLANVSTVLTSKYR

Sheep                         TPAVHASLDKFLANVSTVLTSKYR

Cat                           TPAVHASLDKFFSAVSTVLTSKYR

Horse                         TPAVHASLDKFLSSVSTVLTSKYR

Chicken                       TPEVHASLDKFLCAVGTVLTAKYR

Xenopus tropicalis            DPATHKALDKFLVSVSNVLTSKYR

Zebrafish                     TPEVHVSVDKFFNNLALALSEKYR

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.
Chain 2 – 142 Hemoglobin subunit alpha
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 139 – 141

Literature citations
Structural, functional, and subunit assembly properties of hemoglobin Attleboro [alpha 138 (H21) Ser----Pro], a variant possessing a site maturation at a critical C-terminal residue.
McDonald M.J.; Michalski L.A.; Turci S.M.; Guillette R.A.; Jue D.L.; Johnson M.H.; Moo-Penn W.F.;
Biochemistry 29:173-178(1990)
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.