PIN1

From Wikipedia, the free encyclopedia

Protein (peptidylprolyl cis/trans isomerase) NIMA-interacting 1

PDB rendering based on 1f8a.

Available structures: 1f8a, 1i6c, 1i8g, 1i8h, 1nmv, 1nmw, 1pin, 1zcn, 2f21, 2iti, 2itk

Identifiers

Symbol(s)

PIN1; DOD; UBL5

External IDs

OMIM: 601052 MGI: 1346036 HomoloGene: 4531

Gene ontology
Molecular Function:	• peptidyl-prolyl cis-trans isomerase activity • protein binding • isomerase activity
Cellular Component:	• nucleus
Biological Process:	• protein folding • cell cycle • regulation of mitosis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006221 (mRNA)
NP_006212 (protein)

NM_023371 (mRNA)
NP_075860 (protein)

Location

Chr 19: 9.81 - 9.82 Mb

Chr 9: 20.4 - 20.42 Mb

Pubmed search

[1]

[2]

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

[edit] References

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

[edit] 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.