PIN1

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Protein (peptidylprolyl cis/trans isomerase) NIMA-interacting 1
File:PBB Protein PIN1 image.jpg
PDB rendering based on 1f8a.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols PIN1 ; DOD; UBL5
External IDs Template:OMIM5 Template:MGI HomoloGene4531
RNA expression pattern
File:PBB GE PIN1 202927 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Protein (peptidylprolyl cis/trans isomerase) NIMA-interacting 1, also known as PIN1, is a human gene.[1]


References

  1. "Entrez Gene: PIN1 Protein (peptidylprolyl cis/trans isomerase) NIMA-interacting 1".

Further reading

  • Lu KP, Liou YC, Zhou XZ (2002). "Pinning down proline-directed phosphorylation signaling". Trends Cell Biol. 12 (4): 164–72. 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. PMID 17317113.
  • 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. PMID 8552658.
  • Lu KP, Hanes SD, Hunter T (1996). "A human peptidyl-prolyl isomerase essential for regulation of mitosis". Nature. 380 (6574): 544–7. doi:10.1038/380544a0. PMID 8606777.
  • 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. 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. PMID 9482729.
  • 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. PMID 9499405.
  • Lu PJ, Zhou XZ, Shen M, Lu KP (1999). "Function of WW domains as phosphoserine- or phosphothreonine-binding modules". Science. 283 (5406): 1325–8. 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. PMID 10888662.
  • 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. 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. PMID 11432833.
  • 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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