Literature summary for 3.4.17.20 extracted from

Valnickova, Z.; Christensen, T.; Skottrup, P.; Th?gersen, I.B.; H?jrup, P.; Enghild, J.J.
Post-translational modifications of human thrombin-activatable fibrinolysis inhibitor (TAFI): evidence for a large shift in the isoelectric point and reduced solubility upon activation (2006), Biochemistry, 45, 1525-1535.

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General Stability

General Stability	Organism
the activated enzyme TAFIa is highly unstable and less soluble compared to inactive TAFI, which is not due to posttranslational modifications, but to a loss of 80% of the attached glycans and a shift in pI of TAFIa, overview	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q96IY4	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	5 N-glycosylation sites at Asn22, Asn51, Asn63, Asn86, and Asn219, detailed carbohydrate analysis, overview, no O-glycosylation	Homo sapiens
proteolytic modification	Ca2+-dependent activation by thrombin/thrombumodulin or plasmin by cleavage of the activation peptide, in vitro activation by trypsin at 37°C and pH 7.5	Homo sapiens

Synonyms

Synonyms	Comment	Organism
TAFI	-	Homo sapiens
thrombin-activatable fibrinolysis inhibitor	-	Homo sapiens

pI Value

Organism	Comment	pI Value Maximum	pI Value
Homo sapiens	about, inactive TAFI, isoelectric focusing	-	5
Homo sapiens	about, active TAFIa, isoelectric focusing	-	8

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Release 2023.1 (January 2023)