PIN1
| Peptidylprolyl cis/trans isomerase, NIMA-interacting 1 |
PDB rendering based on 1f8a. |
| Available structures |
| PDB |
1F8A, 1I6C, 1I8G, 1I8H, 1NMV, 1NMW, 1PIN, 1ZCN, 2F21, 2ITK, 2KBU, 2KCF, 2Q5A, 2ZQS, 2ZQT, 2ZQU, 2ZQV, 2ZR4, 2ZR5, 2ZR6, 3I6C, 3IK8, 3IKD, 3IKG, 3JYJ, 3KAB, 3KAC, 3KAD, 3KAF, 3KAG, 3KAH, 3KAI, 3KCE, 3ODK |
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| Identifiers |
| Symbols |
PIN1; DOD; FLJ40239; FLJ77628; MGC10717; UBL5 |
| External IDs |
OMIM: 601052 MGI: 1346036 HomoloGene: 4531 GeneCards: PIN1 Gene |
| EC number |
5.2.1.8 |
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| RNA expression pattern |
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| More reference expression data |
| Orthologs |
| Species |
Human |
Mouse |
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| Entrez |
5300 |
23988 |
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| Ensembl |
ENSG00000127445 |
ENSMUSG00000032171 |
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| UniProt |
Q13526 |
Q3UTI7 |
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| RefSeq (mRNA) |
NM_006221.3 |
NM_023371.3 |
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| RefSeq (protein) |
NP_006212 |
NP_075860.1 |
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| Location (UCSC) |
Chr 19:
9.95 – 9.96 Mb |
Chr 9:
20.4 – 20.42 Mb |
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| PubMed search |
[1] |
[2] |
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Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 is an enzyme that in humans is encoded by the PIN1 gene.[1][2]
Interactions
PIN1 has been shown to interact with CSNK2A2,[3] Casein kinase 2, alpha 1,[3] Wee1-like protein kinase,[4] FOXO4,[5] CDC25C,[4][6][7] CDC27,[4][7] MYT1,[8] PLK1,[4][7] MPHOSPH1,[9] DAB2,[10] P53,[11][12] PKMYT1,[4] C-jun,[13] SUPT5H,[14] Mothers against decapentaplegic homolog 3[15] and Mothers against decapentaplegic homolog 2.[15]
References
- ^ Lu KP, Hanes SD, Hunter T (May 1996). "A human peptidyl-prolyl isomerase essential for regulation of mitosis". Nature 380 (6574): 544–7. doi:10.1038/380544a0. PMID 8606777.
- ^ "Entrez Gene: PIN1 Protein (peptidylprolyl cis/trans isomerase) NIMA-interacting 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5300.
- ^ a b Messenger, Moira M; Saulnier Ronald B, Gilchrist Andrew D, Diamond Phaedra, Gorbsky Gary J, Litchfield David W (June 2002). "Interactions between protein kinase CK2 and Pin1. Evidence for phosphorylation-dependent interactions". J. Biol. Chem. (United States) 277 (25): 23054–64. doi:10.1074/jbc.M200111200. ISSN 0021-9258. PMID 11940573.
- ^ a b c d e Shen, M; Stukenberg P T, Kirschner M W, Lu K P (March 1998). "The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins". Genes Dev. (UNITED STATES) 12 (5): 706–20. doi:10.1101/gad.12.5.706. ISSN 0890-9369. PMC 316589. PMID 9499405. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=316589.
- ^ Brenkman, Arjan B; de Keizer Peter L J, van den Broek Niels J F, van der Groep Petra, van Diest Paul J, van der Horst Armando, Smits Alida M M, Burgering Boudewijn M T (September 2008). "The peptidyl-isomerase Pin1 regulates p27kip1 expression through inhibition of Forkhead box O tumor suppressors". Cancer Res. (United States) 68 (18): 7597–605. doi:10.1158/0008-5472.CAN-08-1059. PMID 18794148.
- ^ Goldstrohm, A C; Albrecht T R, Suñé C, Bedford M T, Garcia-Blanco M A (November 2001). "The transcription elongation factor CA150 interacts with RNA polymerase II and the pre-mRNA splicing factor SF1". Mol. Cell. Biol. (United States) 21 (22): 7617–28. doi:10.1128/MCB.21.22.7617-7628.2001. ISSN 0270-7306. PMC 99933. PMID 11604498. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=99933.
- ^ a b c Lu, P J; Zhou X Z, Shen M, Lu K P (February 1999). "Function of WW domains as phosphoserine- or phosphothreonine-binding modules". Science (UNITED STATES) 283 (5406): 1325–8. doi:10.1126/science.283.5406.1325. ISSN 0036-8075. PMID 10037602.
- ^ Wells, N J; Watanabe N, Tokusumi T, Jiang W, Verdecia M A, Hunter T (October 1999). "The C-terminal domain of the Cdc2 inhibitory kinase Myt1 interacts with Cdc2 complexes and is required for inhibition of G(2)/M progression". J. Cell. Sci.. 112 (ENGLAND) ( Pt 19): 3361–71. ISSN 0021-9533. PMID 10504341.
- ^ Kamimoto, T; Zama T, Aoki R, Muro Y, Hagiwara M (October 2001). "Identification of a novel kinesin-related protein, KRMP1, as a target for mitotic peptidyl-prolyl isomerase Pin1". J. Biol. Chem. (United States) 276 (40): 37520–8. doi:10.1074/jbc.M106207200. ISSN 0021-9258. PMID 11470801.
- ^ He, Junqi; Xu Jianguo, Xu Xiang-Xi, Hall Randy A (July 2003). "Cell cycle-dependent phosphorylation of Disabled-2 by cdc2". Oncogene (England) 22 (29): 4524–30. doi:10.1038/sj.onc.1206767. ISSN 0950-9232. PMID 12881709.
- ^ Wulf, Gerburg M; Liou Yih-Cherng, Ryo Akihide, Lee Sam W, Lu Kun Ping (December 2002). "Role of Pin1 in the regulation of p53 stability and p21 transactivation, and cell cycle checkpoints in response to DNA damage". J. Biol. Chem. (United States) 277 (50): 47976–9. doi:10.1074/jbc.C200538200. ISSN 0021-9258. PMID 12388558.
- ^ Zacchi, Paola; Gostissa Monica, Uchida Takafumi, Salvagno Clio, Avolio Fabio, Volinia Stefano, Ronai Ze'ev, Blandino Giovanni, Schneider Claudio, Del Sal Giannino (October 2002). "The prolyl isomerase Pin1 reveals a mechanism to control p53 functions after genotoxic insults". Nature (England) 419 (6909): 853–7. doi:10.1038/nature01120. ISSN 0028-0836. PMID 12397362.
- ^ Wulf, G M; Ryo A, Wulf G G, Lee S W, Niu T, Petkova V, Lu K P (July 2001). "Pin1 is overexpressed in breast cancer and cooperates with Ras signaling in increasing the transcriptional activity of c-Jun towards cyclin D1". EMBO J. (England) 20 (13): 3459–72. doi:10.1093/emboj/20.13.3459. ISSN 0261-4189. PMC 125530. PMID 11432833. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125530.
- ^ Lavoie, S B; Albert A L, Handa H, Vincent M, Bensaude O (September 2001). "The peptidyl-prolyl isomerase Pin1 interacts with hSpt5 phosphorylated by Cdk9". J. Mol. Biol. (England) 312 (4): 675–85. doi:10.1006/jmbi.2001.4991. ISSN 0022-2836. PMID 11575923.
- ^ a b Nakano, Ayako; Koinuma Daizo, Miyazawa Keiji, Uchida Takafumi, Saitoh Masao, Kawabata Masahiro, Hanai Jun-ichi, Akiyama Hirotada, Abe Masahiro, Miyazono Kohei, Matsumoto Toshio, Imamura Takeshi (March 2009). "Pin1 down-regulates transforming growth factor-beta (TGF-beta) signaling by inducing degradation of Smad proteins". J. Biol. Chem. (United States) 284 (10): 6109–15. doi:10.1074/jbc.M804659200. ISSN 0021-9258. PMID 19122240.
Further reading
- Lu KP, Liou YC, Zhou XZ (2002). "Pinning down proline-directed phosphorylation signaling.". Trends Cell Biol. 12 (4): 164–72. doi:10.1016/S0962-8924(02)02253-5. PMID 11978535.
- Wulf G, Finn G, Suizu F, Lu KP (2005). "Phosphorylation-specific prolyl isomerization: is there an underlying theme?". Nat. Cell Biol. 7 (5): 435–41. doi:10.1038/ncb0505-435. PMID 15867923.
- Etzkorn FA (2007). "Pin1 flips Alzheimer's switch.". ACS Chem. Biol. 1 (4): 214–6. doi:10.1021/cb600171g. PMID 17163675.
- Balastik M, Lim J, Pastorino L, Lu KP (2007). "Pin1 in Alzheimer's disease: multiple substrates, one regulatory mechanism?". Biochim. Biophys. Acta 1772 (4): 422–9. doi:10.1016/j.bbadis.2007.01.006. PMC 1868500. PMID 17317113. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1868500.
- Maleszka R, Hanes SD, Hackett RL, et al. (1996). "The Drosophila melanogaster dodo (dod) gene, conserved in humans, is functionally interchangeable with the ESS1 cell division gene of Saccharomyces cerevisiae.". Proc. Natl. Acad. Sci. U.S.A. 93 (1): 447–51. doi:10.1073/pnas.93.1.447. PMC 40255. PMID 8552658. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=40255.
- Ranganathan R, Lu KP, Hunter T, Noel JP (1997). "Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent.". Cell 89 (6): 875–86. doi:10.1016/S0092-8674(00)80273-1. PMID 9200606.
- Campbell HD, Webb GC, Fountain S, Young IG (1997). "The human PIN1 peptidyl-prolyl cis/trans isomerase gene maps to human chromosome 19p13 and the closely related PIN1L gene to 1p31.". Genomics 44 (2): 157–62. doi:10.1006/geno.1997.4854. PMID 9299231.
- Crenshaw DG, Yang J, Means AR, Kornbluth S (1998). "The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1.". EMBO J. 17 (5): 1315–27. doi:10.1093/emboj/17.5.1315. PMC 1170480. PMID 9482729. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170480.
- Shen M, Stukenberg PT, Kirschner MW, Lu KP (1998). "The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins.". Genes Dev. 12 (5): 706–20. doi:10.1101/gad.12.5.706. PMC 316589. PMID 9499405. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=316589.
- Lu PJ, Zhou XZ, Shen M, Lu KP (1999). "Function of WW domains as phosphoserine- or phosphothreonine-binding modules.". Science 283 (5406): 1325–8. doi:10.1126/science.283.5406.1325. PMID 10037602.
- Lu PJ, Wulf G, Zhou XZ, et al. (1999). "The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein.". Nature 399 (6738): 784–8. doi:10.1038/21650. PMID 10391244.
- Albert A, Lavoie S, Vincent M (1999). "A hyperphosphorylated form of RNA polymerase II is the major interphase antigen of the phosphoprotein antibody MPM-2 and interacts with the peptidyl-prolyl isomerase Pin1.". J. Cell. Sci.. 112 ( Pt 15): 2493–500. PMID 10393805.
- Wells NJ, Watanabe N, Tokusumi T, et al. (1999). "The C-terminal domain of the Cdc2 inhibitory kinase Myt1 interacts with Cdc2 complexes and is required for inhibition of G(2)/M progression.". J. Cell. Sci.. 112 ( Pt 19): 3361–71. PMID 10504341.
- Gerez L, Mohrmann K, van Raak M, et al. (2000). "Accumulation of rab4GTP in the cytoplasm and association with the peptidyl-prolyl isomerase pin1 during mitosis.". Mol. Biol. Cell 11 (7): 2201–11. PMC 14913. PMID 10888662. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=14913.
- Verdecia MA, Bowman ME, Lu KP, et al. (2000). "Structural basis for phosphoserine-proline recognition by group IV WW domains.". Nat. Struct. Biol. 7 (8): 639–43. doi:10.1038/77929. PMID 10932246.
- Rippmann JF, Hobbie S, Daiber C, et al. (2000). "Phosphorylation-dependent proline isomerization catalyzed by Pin1 is essential for tumor cell survival and entry into mitosis.". Cell Growth Differ. 11 (7): 409–16. PMID 10939594.
- Liu W, Youn HD, Zhou XZ, et al. (2001). "Binding and regulation of the transcription factor NFAT by the peptidyl prolyl cis-trans isomerase Pin1.". FEBS Lett. 496 (2-3): 105–8. doi:10.1016/S0014-5793(01)02411-5. PMID 11356192.
- Wulf GM, Ryo A, Wulf GG, et al. (2001). "Pin1 is overexpressed in breast cancer and cooperates with Ras signaling in increasing the transcriptional activity of c-Jun towards cyclin D1.". EMBO J. 20 (13): 3459–72. doi:10.1093/emboj/20.13.3459. PMC 125530. PMID 11432833. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125530.
- Kamimoto T, Zama T, Aoki R, et al. (2001). "Identification of a novel kinesin-related protein, KRMP1, as a target for mitotic peptidyl-prolyl isomerase Pin1.". J. Biol. Chem. 276 (40): 37520–8. doi:10.1074/jbc.M106207200. PMID 11470801.
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PDB gallery
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1f8a: STRUCTURAL BASIS FOR THE PHOSPHOSERINE-PROLINE RECOGNITION BY GROUP IV WW DOMAINS
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1i6c: SOLUTION STRUCTURE OF PIN1 WW DOMAIN
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1i8g: SOLUTION STRUCTURE OF PIN1 WW DOMAIN COMPLEXED WITH CDC25 PHOSPHOTHREONINE PEPTIDE
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1i8h: SOLUTION STRUCTURE OF PIN1 WW DOMAIN COMPLEXED WITH HUMAN TAU PHOSPHOTHREONINE PEPTIDE
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1nmv: Solution structure of human Pin1
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1nmw: Solution structure of the PPIase domain of human Pin1
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1pin: PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM HOMO SAPIENS
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1zcn: human Pin1 Ng mutant
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2f21: human Pin1 Fip mutant
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2itk: human Pin1 bound to D-PEPTIDE
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