Peptidyl-Prolyl Cis/Trans-Isomerase - rHuPIN-1 - EC 5.2.1.8

Human Pin 1 is a peptidyl-prolyl cis/trans isomerase (PPIase) that interacts with NIMA and essential for cell cycle regulation Pin1 is nuclear PPIase containing a WW protein interaction domain, and is structurally and functionally related to Ess1/Ptf1, an essential protein in budding yeast. PPIase activity is necessary for Ess1/Pin1 function in yeast. Pin1 is thus an essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity.

Substrates of Pin1 include the mitotic regulators (Cdc25 phosphatase and NIMA, PLK I, Wee, and Myt1 kinases), several transcription factors like b-Catenin, c-Jun, and the tumor suppressor protein p53, and some specific proteins like the RNA Pol II, the cytoskeleton protein tau, and the G1/S protein Cyclin D1..

Human recombinant PPIase from E.Coli is a single, non-glycosylated polypeptide of 163 amino acids and a molecular mass of 18.2 kDa. 

The specific activity is >330 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1µmol of suc-AAFP-pNA per minute at 25°C in Tris/HCl pH8.0 using chymotrypsin.

Sequence of human Pin 1:
MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGN SSSGGKNGQG EPARVRCSHL LVKHSQSRRP SSWRQEKITR TKEEALELIN GYIQKIKSGE EDFESLASQF SDCSSAKARG DLGAFSRGQM QKPFEDASFA LRTGEMSGPV FTDSGIHIIL RTE

Synonym: DOD, NIMA-interacting protein 1, PPIase Pin1, Rotamase Pin1, UBL5