Literature summary for 5.2.1.8 extracted from

Ettelaie, C.; Collier, M.E.W.; Featherby, S.; Greenman, J.; Maraveyas, A.
Peptidyl-prolyl isomerase 1 (Pin1) preserves the phosphorylation state of tissue factor and prolongs its release within microvesicles (2018), Biochim. Biophys. Acta, 1865, 12-24 .

Search for more literature for 5.2.1.8

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q13526	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
HCAEC cell	-	Homo sapiens	-
MDA-MB-231 cell	-	Homo sapiens	-

General Information

General Information	Comment	Organism
physiological function	Pin1 interacts with the cytoplasmic domain of tissue factor. Pin1 is able to bind wild-type and mutant forms of overexpressed tissue factor-tGFP fusion proteins. Pin1 coimmunoprecipitates with overexpressed wild-type tissue factor-tGFP but not Ser258Ala or Pro259Ala substituted mutants. Pin1 is capable of interfering with the ubiquitination and dephosphorylation of tissue factor-derived peptides	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)