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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q12891: Variant p.Lys148Arg

Hyaluronidase-2
Gene: HYAL2
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Variant information Variant position: help 148 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 Lysine (K) to Arginine (R) at position 148 (K148R, p.Lys148Arg). 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 Similar physico-chemical property. Both residues are large size and basic. 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 MCCS; likely pathogenic. Any additional useful information about the variant.


Sequence information Variant position: help 148 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 473 The length of the canonical sequence.
Location on the sequence: help GLAVIDWEDWRPVWVRNWQD K DVYRRLSRQLVASRHPDWPP 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                         GLAVIDWEDWRPVWVRNWQDKDVYRRLSRQLVASRHPDWPP

Mouse                         GLAVIDWEEWRPVWVRNWQEKDVYRQSSRQLVASRHPDWPS

Rat                           GLAVIDWEEWRPVWVRNWQEKDVYRQSSRQLVASRHPDWPS

Bovine                        GLAVIDWEDWRPVWVRNWQDKDVYRRLSRHLVAIRHPDWPP

Sheep                         GLAVIDWEDWRPVWVRNWQDKDVYRRLSRQLVASHHPDWPP
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 21 – 448 Hyaluronidase-2
Active site 135 – 135 Proton donor
Disulfide bond 47 – 340



Literature citations
Mutations in HYAL2, Encoding Hyaluronidase 2, Cause a Syndrome of Orofacial Clefting and Cor Triatriatum Sinister in Humans and Mice.
Muggenthaler M.M.; Chowdhury B.; Hasan S.N.; Cross H.E.; Mark B.; Harlalka G.V.; Patton M.A.; Ishida M.; Behr E.R.; Sharma S.; Zahka K.; Faqeih E.; Blakley B.; Jackson M.; Lees M.; Dolinsky V.; Cross L.; Stanier P.; Salter C.; Baple E.L.; Alkuraya F.S.; Crosby A.H.; Triggs-Raine B.; Chioza B.A.;
PLoS Genet. 13:e1006470-e1006470(2017)
Cited for: INVOLVEMENT IN MCCS; VARIANTS MCCS ARG-148 AND LEU-250;
Elucidating the clinical spectrum and molecular basis of HYAL2 deficiency.
Fasham J.; Lin S.; Ghosh P.; Radio F.C.; Farrow E.G.; Thiffault I.; Kussman J.; Zhou D.; Hemming R.; Zahka K.; Chioza B.A.; Rawlins L.E.; Wenger O.K.; Gunning A.C.; Pizzi S.; Onesimo R.; Zampino G.; Barker E.; Osawa N.; Rodriguez M.C.; Neuhann T.M.; Zackai E.H.; Keena B.; Capasso J.; Levin A.V.; Bhoj E.; Li D.; Hakonarson H.; Wentzensen I.M.; Jackson A.; Chandler K.E.; Coban-Akdemir Z.H.; Posey J.E.; Banka S.; Lupski J.R.; Sheppard S.E.; Tartaglia M.; Triggs-Raine B.; Crosby A.H.; Baple E.L.;
Genet. Med. 24:631-644(2022)
Cited for: INVOLVEMENT IN MCCS; VARIANTS MCCS THR-64; 65-SER--LEU-473 DEL; ARG-148; ALA-204; ARG-238; CYS-277; 295-ARG--LEU-473 DEL; CYS-378 AND VAL-425; CHARACTERIZATION OF VARIANTS MCCS ALA-204; ARG-238; CYS-277 AND VAL-425; SUBCELLULAR LOCATION;
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.