Variant position: 425 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 464 The length of the canonical sequence.
Location on the sequence:
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: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human LEVNEEGSEAAASTAVVIAG RSLNPNRVTFKANRPFLVFIR
Mouse LEVNEEGSEAAASTSVVITG RSLNPNRVTFKANRPFLVLIR
Bovine LEVNEEGSEAAASTVISIAG RSLNSDRVTFKANRPILVLIR
Sheep LEVNEEGSEAAASTVISIAG RSLNLNRVTFQANRPFLVLIR
Sequence annotation in neighborhood: 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.
Type Positions Description
33 – 464 Antithrombin-III
425 – 426 Reactive bond
279 – 462
414 – 414 A -> K. Reduces interaction with thrombin by 99%.
414 – 414 A -> Q. Reduces interaction with thrombin by 80%.
423 – 426
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; PHE-138-139-LYS 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;
Single amino acid substitutions in the reactive site of antithrombin leading to thrombosis. Congenital substitution of arginine 393 to cysteine in antithrombin Northwick Park and to histidine in antithrombin Glasgow.
Erdjument H.; Laned D.A.; Panico M.; di Marzo V.; Morris H.R.;
J. Biol. Chem. 263:5589-5593(1988)
Cited for: VARIANTS AT3D CYS-425 AND HIS-425;
Antithrombin Chicago, amino acid substitution of arginine 393 to histidine.
Erdjument H.; Lane D.A.; Panico M.; di Marzo V.; Morris H.R.; Bauer K.; Rosenberg R.D.;
Thromb. Res. 54:613-619(1989)
Cited for: VARIANT AT3D HIS-425;
Antithrombin III Kumamoto II; a single mutation at Arg393-His increased the affinity of antithrombin III for heparin.
Okajima K.; Abe H.; Wagatsuma M.; Okabe H.; Takatsuki K.;
Am. J. Hematol. 48:12-18(1995)
Cited for: VARIANT AT3D HIS-425;
Five novel and four recurrent point mutations in the antithrombin gene causing venous thrombosis.
Nagaizumi K.; Inaba H.; Amano K.; Suzuki M.; Arai M.; Fukutake K.;
Int. J. Hematol. 78:79-83(2003)
Cited for: VARIANTS AT3D LYS-121; HIS-178; CYS-425; HIS-425 AND PRO-441;
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