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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P33947: Variant p.His12Asp

ER lumen protein-retaining receptor 2
Gene: KDELR2
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Variant information Variant position: help 12 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 Aspartate (D) at position 12 (H12D, p.His12Asp). 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 medium size and acidic (D) 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 OI21; changed maintenance of protein localization in endoplasmic reticulum; SERPINH1 is not retained in the endoplasmic reticulum and secreted; leads to a loss of fiber formation of the bones connective tissue; no effect on protein abundance. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 12 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 212 The length of the canonical sequence.
Location on the sequence: help MNIFRLTGDLS H LAAIVILLLKIWKTRSCAGI 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                         MNIFRLTGDLSHLAAIVILLLKIWKTRSCAGI

Mouse                         MNIFRLTGDLSHLAAIVILLLKIWKTRSCAGI

Rat                           MNIFRLTGDLSHLAAIVILLLKIWKTRSCAGI

Bovine                        MNIFRLTGDLSHLAAIVILLLKIWKTRSCAGI

Chicken                       MNIFRLTGDLSHLAAIIILLLKIWKSRSCAGI

Xenopus laevis                MNVFRLSGDLCHLAAIIILLLKIWNSRSCAGI

Xenopus tropicalis            MNVFRLSGDLSHLAAIIILLLKIWKSRSCAGI

Zebrafish                     MNIFRLTGDLSHLAAIIILLLKIWKSRSCAGI

Caenorhabditis elegans        MNIFRISADMSHLLAIIILLLKIWKSRSCSGI
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 1 – 212 ER lumen protein-retaining receptor 2
Transmembrane 5 – 24 Helical
Site 5 – 5 Interaction with the K-D-E-L motif on target proteins



Literature citations
Interaction between KDELR2 and HSP47 as a Key Determinant in Osteogenesis Imperfecta Caused by Bi-allelic Variants in KDELR2.
van Dijk F.S.; Semler O.; Etich J.; Koehler A.; Jimenez-Estrada J.A.; Bravenboer N.; Claeys L.; Riesebos E.; Gegic S.; Piersma S.R.; Jimenez C.R.; Waisfisz Q.; Flores C.L.; Nevado J.; Harsevoort A.J.; Janus G.J.M.; Franken A.A.M.; van der Sar A.M.; Meijers-Heijboer H.; Heath K.E.; Lapunzina P.; Nikkels P.G.J.; Santen G.W.E.; Nuechel J.; Plomann M.; Wagener R.; Rehberg M.; Hoyer-Kuhn H.; Eekhoff E.M.W.; Pals G.; Moergelin M.; Newstead S.; Wilson B.T.; Ruiz-Perez V.L.; Maugeri A.; Netzer C.; Zaucke F.; Micha D.;
Am. J. Hum. Genet. 107:989-999(2020)
Cited for: INVOLVEMENT IN OI21; VARIANTS OI21 ASP-12; 120-TRP--ALA-212 DEL AND LEU-133; CHARACTERIZATION OF VARIANTS OI21 ASP-12 AND 120-TRP--ALA-212 DEL; FUNCTION;
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.