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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P01008: Variant p.Ala414Thr

Antithrombin-III
Gene: SERPINC1
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Variant information Variant position: help 414 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 Alanine (A) to Threonine (T) at position 414 (A414T, p.Ala414Thr). 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 small size and hydrophobic (A) to medium size and polar (T) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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 AT3D; type-II; Hamilton/Glasgow-2; reduces interaction with thrombin by 90%. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 414 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 464 The length of the canonical sequence.
Location on the sequence: help LYVSDAFHKAFLEVNEEGSE A AASTAVVIAGRSLNPNRVTF 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                         LYVSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPNRVTF

Mouse                         LYVSDAFHKAFLEVNEEGSEAAASTSVVITGRSLNPNRVTF

Bovine                        LYVSDAFHKAFLEVNEEGSEAAASTVISIAGRSLNSDRVTF

Sheep                         LYVSDAFHKAFLEVNEEGSEAAASTVISIAGRSLNLNRVTF
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 33 – 464 Antithrombin-III
Disulfide bond 279 – 462
Mutagenesis 414 – 414 A -> K. Reduces interaction with thrombin by 99%.
Mutagenesis 414 – 414 A -> Q. Reduces interaction with thrombin by 80%.



Literature citations
Antithrombin-TRI (Ala382 to Thr) causing severe thromboembolic tendency undergoes the S-to-R transition and is associated with a plasma-inactive high-molecular-weight complex of aggregated antithrombin.
Lindo V.S.; Kakkar V.V.; Learmonth M.; Melissari E.; Zappacosta F.; Panico M.; Morris H.R.;
Br. J. Haematol. 89:589-601(1995)
Cited for: PROTEIN SEQUENCE OF 371-425; MASS SPECTROMETRY; VARIANT AT3D THR-414; Antithrombin mutation database: 2nd (1997) update.
Lane D.A.; Bayston T.; Olds R.J.; Fitches A.C.; Cooper D.N.; Millar D.S.; Jochmans K.; Perry D.J.; Okajima K.; Thein S.L.; Emmerich J.;
Thromb. Haemost. 77:197-211(1997)
Cited for: VARIANTS AT3D SER-17; PRO-23; ASN-39; CYS-56; LEU-73; CYS-79; HIS-79; SER-79; ASN-87 DEL; CYS-89; LEU-90; CYS-95; SER-95; PRO-98; THR-112; PHE-131; VAL-131; LYS-133; 138-PHE-LYS-139 DEL; PRO-148; PRO-150; PRO-158; TYR-160; GLN-161; CYS-198; HIS-198; ILE-218 DEL; ASP-219; LYS-219; ARG-257; LYS-269; ILE-283; ASN-316; LYS-334; ARG-412; THR-414; PRO-416; SER-416; VAL-419; ASP-424; CYS-425; HIS-425; PRO-425; LEU-426; CYS-434; LEU-434; SER-434; THR-436; LYS-437; GLY-438; MET-438; LEU-439; THR-439; THR-453; ARG-456; THR-457; ASP-459; LEU-461 AND PHE-462; VARIANTS GLU-30; THR-52 AND CYS-190; Antithrombin-III-Hamilton: a gene with a point mutation (guanine to adenine) in codon 382 causing impaired serine protease reactivity.
Devrak-Kizuk R.; Chui D.H.K.; Prochownik E.V.; Carter C.J.; Ofosu F.A.; Blajchman M.A.;
Blood 72:1518-1523(1988)
Cited for: VARIANT AT3D THR-414; Site-directed mutagenesis of alanine-382 of human antithrombin III.
Austin R.C.; Rachubinski R.A.; Blachjman M.A.;
FEBS Lett. 280:254-258(1991)
Cited for: CHARACTERIZATION OF VARIANT AT3D THR-414; MUTAGENESIS OF ALA-414;
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.