PIN1
Protein (peptidylprolyl cis/trans isomerase) NIMA-interacting 1 | |||||||||||||
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File:PBB Protein PIN1 image.jpg PDB rendering based on 1f8a. | |||||||||||||
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Identifiers | |||||||||||||
Symbols | PIN1 ; DOD; UBL5 | ||||||||||||
External IDs | Template:OMIM5 Template:MGI HomoloGene: 4531 | ||||||||||||
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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
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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