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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02144: Variant p.His98Tyr

Myoglobin
Gene: MB
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Variant information Variant position: help 98 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] 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 Histidine (H) to Tyrosine (Y) at position 98 (H98Y, p.His98Tyr). 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 medium size and polar (H) to large size and aromatic (Y) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 2 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 MYOSB; decreased oxygen binding; changed oxygen carrier activity; exhibits a higher tendency to form high-molecular-weight aggregates; more prone to heme bleaching. Any additional useful information about the variant.


Sequence information Variant position: help 98 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 154 The length of the canonical sequence.
Location on the sequence: help KKKGHHEAEIKPLAQSHATK H KIPVKYLEFISECIIQVLQS 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                         KKKGHHEAEIKPLAQSHATKHKIPVKYLEFISECIIQVLQS

                              KKKGHHEAELKPLAQSHATKHKIPVKYLEFISDAIIQVLQS

Chimpanzee                    KKKGHHEAEIKPLAQSHATKHKIPVKYLEFISECIIQVLHS

Mouse                         KKKGQHAAEIQPLAQSHATKHKIPVKYLEFISEIIIEVLKK

Rat                           KKKGQHAAEIQPLAQSHATKHKIPVKYLEFISEVIIQVLKK

Pig                           KKKGHHEAELTPLAQSHATKHKIPVKYLEFISEAIIQVLQS

Bovine                        KKKGHHEAEVKHLAESHANKHKIPVKYLEFISDAIIHVLHA

Rabbit                        KKKGHHEAEIKPLAQSHATKHKIPVKYLEFISEAIIHVLHS

Goat                          KKKGHHEAEVKHLAESHANKHKIPVKYLEFISDAIIHVLHA

Sheep                         KKKGHHEAEVKHLAESHANKHKIPVKYLEFISDAIIHVLHA

Horse                         KKKGHHEAELKPLAQSHATKHKIPIKYLEFISDAIIHVLHS

Chicken                       KQKGNHESELKPLAQTHATKHKIPVKYLEFISEVIIKVIAE

Zebrafish                     KAKGDHAALLKPLANTHANIHKVALNNFRLITEVLVKVMAE
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 – 154 Myoglobin
Domain 2 – 148 Globin
Binding site 94 – 94 proximal binding residue



Literature citations
Myoglobinopathy is an adult-onset autosomal dominant myopathy with characteristic sarcoplasmic inclusions.
Olive M.; Engvall M.; Ravenscroft G.; Cabrera-Serrano M.; Jiao H.; Bortolotti C.A.; Pignataro M.; Lambrughi M.; Jiang H.; Forrest A.R.R.; Benseny-Cases N.; Hofbauer S.; Obinger C.; Battistuzzi G.; Bellei M.; Borsari M.; Di Rocco G.; Viola H.M.; Hool L.C.; Cladera J.; Lagerstedt-Robinson K.; Xiang F.; Wredenberg A.; Miralles F.; Baiges J.J.; Malfatti E.; Romero N.B.; Streichenberger N.; Vial C.; Claeys K.G.; Straathof C.S.M.; Goris A.; Freyer C.; Lammens M.; Bassez G.; Kere J.; Clemente P.; Sejersen T.; Udd B.; Vidal N.; Ferrer I.; Edstroem L.; Wedell A.; Laing N.G.;
Nat. Commun. 10:1396-1396(2019)
Cited for: INVOLVEMENT IN MYOSB; VARIANT MYOSB TYR-98; CHARACTERIZATION OF VARIANT MYOSB TYR-98; FUNCTION; SUBCELLULAR LOCATION; Pseudoperoxidase activity, conformational stability, and aggregation propensity of the His98Tyr myoglobin variant: implications for the onset of myoglobinopathy.
Hofbauer S.; Pignataro M.; Borsari M.; Bortolotti C.A.; Di Rocco G.; Ravenscroft G.; Furtmueller P.G.; Obinger C.; Sola M.; Battistuzzi G.;
FEBS J. 289:1105-1117(2022)
Cited for: CHARACTERIZATION OF VARIANT MYOSB TYR-98; FUNCTION; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES; Myoglobinopathy affecting facial and oropharyngeal muscles.
Hama Y.; Mori-Yoshimura M.; Aizawa K.; Oya Y.; Nakamura H.; Inoue M.; Iida A.; Sato N.; Nonaka I.; Nishino I.; Takahashi Y.;
Neuromuscul. Disord. 32:516-520(2022)
Cited for: VARIANT MYOSB TYR-98;
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.