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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P03950: Variant p.Lys41Ile

Angiogenin
Gene: ANG
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Variant information Variant position: help 41 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 Isoleucine (I) at position 41 (K41I, p.Lys41Ile). 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 large size and basic (K) to medium size and hydrophobic (I) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 ALS9; loss of angiogenic activity; reduced ribonucleolytic activity; retains nuclear translocation. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 41 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 147 The length of the canonical sequence.
Location on the sequence: help PTLAQDNSRYTHFLTQHYDA K PQGRDDRYCESIMRRRGLTS 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.
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 25 – 147 Angiogenin
Active site 37 – 37 Proton acceptor
Modified residue 25 – 25 Pyrrolidone carboxylic acid
Mutagenesis 29 – 29 R -> A. Significantly decreases binding affinity for RNH1.
Mutagenesis 32 – 32 H -> A. Significantly decreases binding affinity for RNH1.
Mutagenesis 36 – 36 Q -> A. Slightly decreases binding affinity for RNH1.
Mutagenesis 59 – 59 L -> P. Homodimerization is similar to wild-type; causes mislocalization in the cytoplasm; strongly reduces ribonucleolytic activity.



Literature citations
ANG mutations segregate with familial and 'sporadic' amyotrophic lateral sclerosis.
Greenway M.J.; Andersen P.M.; Russ C.; Ennis S.; Cashman S.; Donaghy C.; Patterson V.; Swingler R.; Kieran D.; Prehn J.; Morrison K.E.; Green A.; Acharya K.R.; Brown R.H. Jr.; Hardiman O.;
Nat. Genet. 38:411-413(2006)
Cited for: VARIANTS ALS9 LEU-36; ILE-41; GLU-41; LYS-55; TRP-63 AND ILE-64; VARIANT VAL-70; Angiogenin loss-of-function mutations in amyotrophic lateral sclerosis.
Wu D.; Yu W.; Kishikawa H.; Folkerth R.D.; Iafrate A.J.; Shen Y.; Xin W.; Sims K.; Hu G.-F.;
Ann. Neurol. 62:609-617(2007)
Cited for: VARIANTS ALS9 SER-20; ILE-41; ASN-52 AND LEU-136; CHARACTERIZATION OF VARIANTS ALS9 ILE-41; ASN-52 AND LEU-136; TISSUE SPECIFICITY; Characterization of human angiogenin variants implicated in amyotrophic lateral sclerosis.
Crabtree B.; Thiyagarajan N.; Prior S.H.; Wilson P.; Iyer S.; Ferns T.; Shapiro R.; Brew K.; Subramanian V.; Acharya K.R.;
Biochemistry 46:11810-11818(2007)
Cited for: CHARACTERIZATION OF VARIANTS ALS9 LEU-36; ILE-41; GLU-41; LYS-55; TRP-63 AND ILE-64; CHARACTERIZATION OF VARIANT VAL-70; SOD1, ANG, TARDBP and FUS mutations in amyotrophic lateral sclerosis: a United States clinical testing lab experience.
Brown J.A.; Min J.; Staropoli J.F.; Collin E.; Bi S.; Feng X.; Barone R.; Cao Y.; O'Malley L.; Xin W.; Mullen T.E.; Sims K.B.;
Amyotroph. Lateral Scler. 13:217-222(2012)
Cited for: VARIANTS ALS9 HIS-38; ILE-41 AND GLY-46;
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.