2m8j

Structure of Pin1 WW domain phospho-mimic S16EStructure of Pin1 WW domain phospho-mimic S16E

FunctionFunction

[PIN1_HUMAN] Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzes pSer/Thr-Pro cis/trans isomerizations. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation.^[1] ^[2] ^[3]

About this StructureAbout this Structure

2m8j is a 1 chain structure. Full experimental information is available from OCA.

ReferenceReference

^{[xtra 1]}

↑ Luh LM, Hansel R, Lohr F, Kirchner DK, Krauskopf K, Pitzius S, Schafer B, Tufar P, Corbeski I, Guntert P, Dotsch V. Molecular crowding drives active Pin1 into nonspecific complexes with endogenous proteins prior to substrate recognition. J Am Chem Soc. 2013 Sep 18;135(37):13796-803. doi: 10.1021/ja405244v. Epub 2013, Sep 6. PMID:23968199 doi:http://dx.doi.org/10.1021/ja405244v

↑ Dougherty MK, Muller J, Ritt DA, Zhou M, Zhou XZ, Copeland TD, Conrads TP, Veenstra TD, Lu KP, Morrison DK. Regulation of Raf-1 by direct feedback phosphorylation. Mol Cell. 2005 Jan 21;17(2):215-24. PMID:15664191 doi:10.1016/j.molcel.2004.11.055
↑ Yu L, Mohamed AJ, Vargas L, Berglof A, Finn G, Lu KP, Smith CI. Regulation of Bruton tyrosine kinase by the peptidylprolyl isomerase Pin1. J Biol Chem. 2006 Jun 30;281(26):18201-7. Epub 2006 Apr 27. PMID:16644721 doi:10.1074/jbc.M603090200
↑ Lee TH, Chen CH, Suizu F, Huang P, Schiene-Fischer C, Daum S, Zhang YJ, Goate A, Chen RH, Zhou XZ, Lu KP. Death-associated protein kinase 1 phosphorylates Pin1 and inhibits its prolyl isomerase activity and cellular function. Mol Cell. 2011 Apr 22;42(2):147-59. doi: 10.1016/j.molcel.2011.03.005. Epub 2011 , Apr 14. PMID:21497122 doi:10.1016/j.molcel.2011.03.005

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OCA

[4] Luh LM, Hansel R, Lohr F, Kirchner DK, Krauskopf K, Pitzius S, Schafer B, Tufar P, Corbeski I, Guntert P, Dotsch V. Molecular crowding drives active Pin1 into nonspecific complexes with endogenous proteins prior to substrate recognition. J Am Chem Soc. 2013 Sep 18;135(37):13796-803. doi: 10.1021/ja405244v. Epub 2013, Sep 6. PMID:23968199 doi:http://dx.doi.org/10.1021/ja405244v

[1] Dougherty MK, Muller J, Ritt DA, Zhou M, Zhou XZ, Copeland TD, Conrads TP, Veenstra TD, Lu KP, Morrison DK. Regulation of Raf-1 by direct feedback phosphorylation. Mol Cell. 2005 Jan 21;17(2):215-24. PMID:15664191 doi:10.1016/j.molcel.2004.11.055

[2] Yu L, Mohamed AJ, Vargas L, Berglof A, Finn G, Lu KP, Smith CI. Regulation of Bruton tyrosine kinase by the peptidylprolyl isomerase Pin1. J Biol Chem. 2006 Jun 30;281(26):18201-7. Epub 2006 Apr 27. PMID:16644721 doi:10.1074/jbc.M603090200

[3] Lee TH, Chen CH, Suizu F, Huang P, Schiene-Fischer C, Daum S, Zhang YJ, Goate A, Chen RH, Zhou XZ, Lu KP. Death-associated protein kinase 1 phosphorylates Pin1 and inhibits its prolyl isomerase activity and cellular function. Mol Cell. 2011 Apr 22;42(2):147-59. doi: 10.1016/j.molcel.2011.03.005. Epub 2011 , Apr 14. PMID:21497122 doi:10.1016/j.molcel.2011.03.005

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