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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P01008: Variant p.Pro73Leu

Antithrombin-III
Gene: SERPINC1
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Variant information Variant position: help 73 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 Proline (P) to Leucine (L) at position 73 (P73L, p.Pro73Leu). 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 Similar physico-chemical property. Both residues are medium size and hydrophobic. 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 AT3D; type-II; lacks heparin-binding ability. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 73 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 CIYRSPEKKATEDEGSEQKI P EATNRRVWELSKANSRFATT 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                         CIYRSPEKKATEDEGSEQKIPEATNRRVWELSKANSRFATT

Mouse                         CIYRSPGKKATEEDGSEQKVPEATNRRVWELSKANSRFATN

Bovine                        CIYRSSEKKATEGQGSEQKIPGATNRRVWELSKANSHFATA

Sheep                         CIYRSPEKKATEGEGSEQKIPGATNRRVWELSKANSHFATA
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
Binding site 81 – 81
Modified residue 63 – 63 Phosphothreonine; by FAM20C
Modified residue 68 – 68 Phosphoserine; by FAM20C
Disulfide bond 40 – 160
Disulfide bond 53 – 127



Literature citations
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 Basel. Identification of a Pro-Leu substitution in a hereditary abnormal antithrombin with impaired heparin cofactor activity.
Chang J.Y.; Tran T.H.;
J. Biol. Chem. 261:1174-1176(1986)
Cited for: VARIANT AT3D LEU-73; CHARACTERIZATION OF VARIANT AT3D LEU-73; The molecular basis of antithrombin deficiency in Belgian and Dutch families.
Jochmans K.; Lissens W.; Seneca S.; Capel P.; Chatelain B.; Meeus P.; Osselaer J.C.; Peerlinck K.; Seghers J.; Slacmeulder M.; Stibbe J.; van de Loo J.; Vermylen J.; Liebaers I.; De Waele M.;
Thromb. Haemost. 80:376-381(1998)
Cited for: VARIANTS AT3D ARG-32; LEU-73; CYS-79; HIS-198; ARG-257 AND ARG-412; Type II antithrombin deficiency caused by a founder mutation Pro73Leu in the Finnish population: clinical picture.
Puurunen M.; Salo P.; Engelbarth S.; Javela K.; Perola M.;
J. Thromb. Haemost. 11:1844-1849(2013)
Cited for: VARIANTS AT3D PHE-53; LEU-73; ASP-125; PRO-170; ASN-218; GLY-248; PRO-293; ARG-401; CYS-425; GLY-438 AND ALA-439; VARIANT GLU-30;
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.