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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9BXJ7: Variant p.Met69Lys

Protein amnionless
Gene: AMN
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Variant information Variant position: help 69 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 Methionine (M) to Lysine (K) at position 69 (M69K, p.Met69Lys). 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 hydrophobic (M) to large size and basic (K) 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 IGS2; loss of interaction with CUBN; strongly reduced CUBN expression at the cell surface. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 69 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 453 The length of the canonical sequence.
Location on the sequence: help EFPADKMVSVLVQEGHAVSD M LLPLDGELVLASGAGFGVSD 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                         EFPADKMVSVLVQEGHAVSDM--------------------------------------------------------LLPLDGELVLASGAGFGVSD

                              QFPADKAVSVVVRASHGFSDM--------------------

Mouse                         QFPADKMVSVLVRDSHAISDM--------------------

Pig                           KFPADKMVSVLVREGHSISDMEELQDRKRENIHSFIHCSFI

Drosophila                    VFPEYYPALLPLPEDISIDGL--------------------
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 20 – 453 Protein amnionless
Topological domain 20 – 357 Extracellular
Region 67 – 87 Interaction with CUBN
Disulfide bond 43 – 96
Mutagenesis 59 – 59 L -> P. Loss of interaction with CUBN and strongly reduced CUBN expression at the cell surface.
Beta strand 62 – 70



Literature citations
Novel compound heterozygous mutations in AMN cause Imerslund-Graesbeck syndrome in two half-sisters: a case report.
Montgomery E.; Sayer J.A.; Baines L.A.; Hynes A.M.; Vega-Warner V.; Johnson S.; Goodship J.A.; Otto E.A.;
BMC Med. Genet. 16:35-35(2015)
Cited for: VARIANT IGS2 LYS-69; FUNCTION; Amnionless-mediated glycosylation is crucial for cell surface targeting of cubilin in renal and intestinal cells.
Udagawa T.; Harita Y.; Miura K.; Mitsui J.; Ode K.L.; Morishita S.; Urae S.; Kanda S.; Kajiho Y.; Tsurumi H.; Ueda H.R.; Tsuji S.; Saito A.; Oka A.;
Sci. Rep. 8:2351-2351(2018)
Cited for: FUNCTION; INTERACTION WITH CUBN; SUBCELLULAR LOCATION; TISSUE SPECIFICITY; CHARACTERIZATION OF VARIANTS IGS2 ILE-41; LYS-69 AND PHE-234; MUTAGENESIS OF LEU-59 AND GLY-254;
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.