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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P00488: Variant p.Leu530Pro

Coagulation factor XIII A chain
Gene: F13A1
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Variant information Variant position: help 530 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 Leucine (L) to Proline (P) at position 530 (L530P, p.Leu530Pro). 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 FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; loss of fibrin gamma chain cross-linking activity; decreased clot fiber thickness. Any additional useful information about the variant.


Sequence information Variant position: help 530 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 732 The length of the canonical sequence.
Location on the sequence: help EGVMKSRSNVDMDFEVENAV L GKDFKLSITFRNNSHNRYTI 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                         EGVMKSRSNVDMDFEVENAVLGKDFKLSITFRNNSHNRYTI

Mouse                         EGVVKSRSDVTMNFDVENAVLGKDFKVTITFQNNSSNLYTI

Rat                           EGMVKSSSDVDMNFDVENAVLGKDFRVTITFQNNSSNLYTI
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 39 – 732 Coagulation factor XIII A chain



Literature citations
Eight novel F13A1 gene missense mutations in patients with mild FXIII deficiency: in silico analysis suggests changes in FXIII-A subunit structure/function.
Biswas A.; Ivaskevicius V.; Thomas A.; Varvenne M.; Brand B.; Rott H.; Haussels I.; Ruehl H.; Scholz U.; Klamroth R.; Oldenburg J.;
Ann. Hematol. 93:1665-1676(2014)
Cited for: VARIANTS FA13AD LEU-167; GLN-172; TYR-343; ARG-416; PRO-530; LYS-602; GLN-704 AND GLY-716; Coagulation factor XIIIA subunit missense mutations affect structure and function at the various steps of factor XIII action.
Thomas A.; Biswas A.; Dodt J.; Philippou H.; Hethershaw E.; Ensikat H.J.; Ivaskevicius V.; Oldenburg J.;
Hum. Mutat. 37:1030-1041(2016)
Cited for: CHARACTERIZATION OF VARIANTS FA13AD GLN-38; LEU-167; CYS-168; GLN-172; ARG-290; TYR-343; ARG-416; PRO-530; GLN-541; SER-593; LYS-602; HIS-612; GLY-669; GLN-704 AND GLY-716; FUNCTION; CATALYTIC ACTIVITY;
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.