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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02647: Variant p.Gly50Arg

Apolipoprotein A-I
Gene: APOA1
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Variant information Variant position: help 50 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 Glycine (G) to Arginine (R) at position 50 (G50R, p.Gly50Arg). 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 glycine (G) to large size and basic (R) 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 AMYLD3. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 50 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 267 The length of the canonical sequence.
Location on the sequence: help SPWDRVKDLATVYVDVLKDS G RDYVSQFEGSALGKQLNLKL 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                         SPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKL

Gorilla                       SPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKL

                              SPWDRVKDLATVYVDAVKDSGRDYVAQFEASALGKQLNLKL

Rhesus macaque                TPWDRVKDLVTVYVEALKDSGKDYVSQFEGSALGKQLNLKL

Chimpanzee                    SPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKL

Mouse                         SQWDKVKDFANVYVDAVKDSGRDYVSQFESSSLGQQLNLNL

Rat                           SQWDRVKDFATVYVDAVKDSGRDYVSQFESSTLGKQLNLNL

Pig                           SPWDRVKDFATVYVDAIKDSGRDYVAQFEASALGKHLNLKL

Bovine                        SSWDRVKDFATVYVEAIKDSGRDYVAQFEASALGKQLNLKL

Rabbit                        SSWDKIKDFATVYVDTVKDSGREYVAQFEASAFGKQLNLKL

Chicken                       TPLDRIRDMVDVYLETVKASGKDAIAQFESSAVGKQLDLKL

Zebrafish                     TQLEHYKAAALVYLNQVKDQAEKALDNLDGTDY-EQYKLQL
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 19 – 267 Proapolipoprotein A-I
Chain 25 – 267 Apolipoprotein A-I
Chain 25 – 266 Truncated apolipoprotein A-I
Modified residue 53 – 53 3'-chlorotyrosine; alternate
Modified residue 53 – 53 3'-nitrotyrosine; alternate
Mutagenesis 42 – 42 Y -> F. Abolished chlorination and nitration without preventing inhibition in presence of myeloproxidase; when associated with F-53, F-124, F-139, F-190, F-216 and F-260.
Mutagenesis 53 – 53 Y -> F. Abolished chlorination and nitration without preventing inhibition in presence of myeloproxidase; when associated with F-42, F-124, F-139, F-190, F-216 and F-260.
Helix 45 – 59



Literature citations
Variant apolipoprotein AI as a major constituent of a human hereditary amyloid.
Nichols W.C.; Dwulet F.E.; Liepnieks J.; Benson M.D.;
Biochem. Biophys. Res. Commun. 156:762-768(1988)
Cited for: PROTEIN SEQUENCE OF 25-107; VARIANT AMYLD3 ARG-50;
A mutation in apolipoprotein A-I in the Iowa type of familial amyloidotic polyneuropathy.
Nichols W.C.; Gregg R.E.; Brewer H.B. Jr.; Benson M.D.;
Genomics 8:318-323(1990)
Cited for: VARIANT AMYLD3 ARG-50; INVOLVEMENT IN AMYLD3;
Familial nephropathic systemic amyloidosis caused by apolipoprotein AI variant Arg26.
Vigushin D.M.; Gough J.; Allan D.; Alguacil A.; Penner B.; Pettigrew N.M.; Quinonez G.; Bernstein K.; Booth S.E.; Booth D.R.; Soutar A.K.; Hawkins P.N.; Pepys M.B.;
Q. J. Med. 87:149-154(1994)
Cited for: VARIANT AMYLD3 ARG-50; INVOLVEMENT IN AMYLD3;
Misdiagnosis of hereditary amyloidosis as AL (primary) amyloidosis.
Lachmann H.J.; Booth D.R.; Booth S.E.; Bybee A.; Gilbertson J.A.; Gillmore J.D.; Pepys M.B.; Hawkins P.N.;
N. Engl. J. Med. 346:1786-1791(2002)
Cited for: VARIANTS AMYLD3 ARG-50 AND PRO-199; INVOLVEMENT IN AMYLD3;
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.