Peptidyl Prolyl Cis/Trans Isomerase NIMA Interacting Protein 1 (PIN1)

DOD; Protein(Peptidyl-Prolyl Cis/Trans Isomerase)NIMA-Interacting 1; Peptidyl-prolyl cis-trans isomerase Pin1; Rotamase Pin1

SPN	S566
HGNC	8988
MGI	1346036
PubMed	21454638
RGD	1310299
UniProt	Q13526
Wiki	Pin1

Peptidyl-prolyl cis/trans isomerases (PPIases; EC 5.2.1.8), such as PIN1, catalyze the cis/trans isomerization of peptidyl-prolyl peptide bonds. PIN1 is the only PPIase that specifically binds to phosphorylated ser/thr-pro motifs to catalytically regulate the post-phosphorylation conformation of its substrates. PIN1-catalyzed conformational regulation has a profound impact on key proteins involved in the regulation of cell growth, genotoxic and other stress responses, the immune response, germ cell development, neuronal differentiation, and survival. Both Drosophila and human DOD contain a WW domain for protein-protein interactions and a peptidylprolyl cis-trans isomerase (PPIase) domain, and they are related to the Ess1 cell division gene of Saccharomyces cerevisiae.

Reference

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Nature 380:544-547(1996) [PubMed] [Europe PMC] [Abstract]

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Mol. Cell 17:215-224(2005) [PubMed] [Europe PMC] [Abstract]

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Nat. Immunol. 8:1132-1139(2007) [PubMed] [Europe PMC] [Abstract]

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Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]

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PLoS ONE 3:E2686-E2686(2008) [PubMed] [Europe PMC] [Abstract]

"Protein kinase-X interacts with Pin-1 and Polycystin-1 during mouse kidney development."
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Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]

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BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]

"Mitogen-activated protein kinase extracellular signal-regulated kinase 2 phosphorylates and promotes Pin1 protein-dependent promyelocytic leukemia protein turnover."
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Mol. Cell 42:147-159(2011) [PubMed] [Europe PMC] [Abstract]

"Negative regulation of the stability and tumor suppressor function of Fbw7 by the Pin1 prolyl isomerase."
Mol. Cell 46:771-783(2012) [PubMed] [Europe PMC] [Abstract]

"Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent."
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