Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P68871: Variant p.Arg105Ser

Hemoglobin subunit beta
Gene: HBB
Variant information Variant position: help 105 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 Arginine (R) to Serine (S) at position 105 (R105S, p.Arg105Ser). 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 (R) to small size and polar (S) 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

Polymorphism: help Genetic variations in HBB are involved in resistance to malaria [MIM:611162]. Hemoglobin S (Hb S), which at homozygosity is responsible for sickle cell anemia, is not associated with any clinical abnormality when heterozygous. At heterozygosity, Hb S confers an increase in protection from life-threatening malaria. Additional variants conferring resistance against severe malaria are hemoglobin C (Hb C) and hemoglobin E (Hb E). Additional information on the polymorphism described.
Variant description: help In Camperdown and Duino; associated in cis with P-92 in Duino; unstable. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.

Sequence information Variant position: help 105 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 147 The length of the canonical sequence.
Location on the sequence: help TFATLSELHCDKLHVDPENF R LLGNVLVCVLAHHFGKEFTP 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.
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 – 147 Hemoglobin subunit beta
Domain 3 – 147 Globin
Binding site 93 – 93 proximal binding residue
Site 96 – 96 Not glycated
Site 105 – 106 (Microbial infection) Cleavage; by N.americanus apr-2
Modified residue 88 – 88 Phosphothreonine
Modified residue 94 – 94 S-nitrosocysteine
Glycosylation 121 – 121 N-linked (Glc) (glycation) lysine
Helix 102 – 119

Literature citations
A new haemoglobin variant, haemoglobin Camperdown (beta 104 (G6) arginine->serine).
Wilkinson T.; Chua C.G.; Carrell R.W.; Robin H.; Exner T.; Lee K.M.; Kronenberg H.;
Biochim. Biophys. Acta 393:195-200(1975)
Cited for: VARIANT CAMPERDOWN SER-105; Two new human hemoglobin variants caused by unusual mutational events: Hb Zaire contains a five residue repetition within the alpha-chain and Hb Duino has two residues substituted in the beta-chain.
Wajcman H.; Blouquit Y.; Vasseur C.; le Querrec A.; Laniece M.; Melevendi C.; Rasore A.; Galacteros F.;
Hum. Genet. 89:676-680(1992)
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.