Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P37023: Variant p.Arg411Trp

Activin receptor type-1-like
Gene: ACVRL1
Feedback?
Variant information Variant position: help 411 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 Arginine (R) to Tryptophan (W) at position 411 (R411W, p.Arg411Trp). 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 (R) to large size and aromatic (W) 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 HHT2; loss of receptor activity in response to BMP9; predominantly retained in the endoplasmic reticulum. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 411 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 503 The length of the canonical sequence.
Location on the sequence: help ESYKWTDIWAFGLVLWEIAR R TIVNGIVEDYRPPFYDVVPN 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                         ESYKWTDIWAFGLVLWEIARRTIVNGIVEDYRPPFYDVVPN

Mouse                         ESYKWTDIWAFGLVLWEIARRTIINGIVEDYRPPFYDMVPN

Rat                           ESYKWTDIWAFGLVLWEIARRTIINGIVEDYRPPFYDMVPN
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 22 – 503 Activin receptor type-1-like
Topological domain 142 – 503 Cytoplasmic
Domain 202 – 492 Protein kinase



Literature citations
Clinical and molecular genetic features of pulmonary hypertension in patients with hereditary hemorrhagic telangiectasia.
Trembath R.C.; Thomson J.R.; Machado R.D.; Morgan N.V.; Atkinson C.; Winship I.; Simonneau G.; Galie N.; Loyd J.E.; Humbert M.; Nichols W.C.; Berg J.; Manes A.; McGaughran J.; Pauciulo M.; Wheeler L.; Morrell N.W.;
N. Engl. J. Med. 345:325-334(2001)
Cited for: VARIANTS HHT2 ASP-254 DEL; TRP-411 AND TRP-484; Molecular screening of ALK1/ACVRL1 and ENG genes in hereditary hemorrhagic telangiectasia in France.
Lesca G.; Plauchu H.; Coulet F.; Lefebvre S.; Plessis G.; Odent S.; Riviere S.; Leheup B.; Goizet C.; Carette M.-F.; Cordier J.-F.; Pinson S.; Soubrier F.; Calender A.; Giraud S.;
Hum. Mutat. 23:289-299(2004)
Cited for: VARIANTS HHT2 ARG-48; LYS-215; ARG-223; ARG-229; SER-233 DEL; PHE-285; PRO-306; TYR-314; PRO-337; PRO-347; GLN-374; VAL-376; LYS-379; GLY-397; TRP-411; PRO-411; GLN-411; LEU-425; LEU-479; VAL-482 AND TRP-484; Hepatic manifestation is associated with ALK1 in hereditary hemorrhagic telangiectasia: identification of five novel ALK1 and one novel ENG mutations.
Kuehl H.K.A.; Caselitz M.; Hasenkamp S.; Wagner S.; El-Harith E.-H.A.; Manns M.P.; Stuhrmann M.;
Hum. Mutat. 25:320-320(2005)
Cited for: VARIANTS HHT2 TRP-67; TRP-374; LYS-379; ASP-407; TRP-411; VAL-425 AND PHE-425 DEL; Functional and splicing defect analysis of 23 ACVRL1 mutations in a cohort of patients affected by hereditary hemorrhagic telangiectasia.
Alaa El Din F.; Patri S.; Thoreau V.; Rodriguez-Ballesteros M.; Hamade E.; Bailly S.; Gilbert-Dussardier B.; Abou Merhi R.; Kitzis A.;
PLoS ONE 10:E0132111-E0132111(2015)
Cited for: VARIANTS HHT2 GLY-41; TYR-41; GLY-46; PRO-47; TYR-66; PHE-77; ASP-211; SER-211; VAL-245; PRO-306; VAL-313; TYR-314; SER-378; ASP-379; LYS-379; GLY-404; TRP-411; MET-441 AND TYR-443; VARIANTS ASP-111 AND PHE-417; CHARACTERIZATION OF VARIANTS HHT2 GLY-41; TYR-41; GLY-46; PRO-47; TYR-66; PHE-77; ASP-211; SER-211; VAL-245; PRO-306; VAL-313; TYR-314; SER-378; ASP-379; LYS-379; GLY-404; TRP-411; MET-441 AND TYR-443; CHARACTERIZATION OF VARIANTS ASP-111 AND PHE-417; FUNCTION; 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.