| Structural highlights
6dcx is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Gene: | PPP1CA, PPP1A (HUMAN), PPP1R13L, IASPP, NKIP1, PPP1R13BL, RAI (HUMAN) |
| Activity: | Phosphoprotein phosphatase, with EC number 3.1.3.16 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[PP1A_HUMAN] Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development.[1] [IASPP_HUMAN] Regulator that plays a central role in regulation of apoptosis and transcription via its interaction with NF-kappa-B and p53/TP53 proteins. Blocks transcription of HIV-1 virus by inhibiting the action of both NF-kappa-B and SP1. Also inhibits p53/TP53 function, possibly by preventing the association between p53/TP53 and ASPP1 or ASPP2, and therefore suppressing the subsequent activation of apoptosis.[2] [3] [4] [5]
References
- ↑ Mi J, Guo C, Brautigan DL, Larner JM. Protein phosphatase-1alpha regulates centrosome splitting through Nek2. Cancer Res. 2007 Feb 1;67(3):1082-9. PMID:17283141 doi:10.1158/0008-5472.CAN-06-3071
- ↑ Slee EA, Gillotin S, Bergamaschi D, Royer C, Llanos S, Ali S, Jin B, Trigiante G, Lu X. The N-terminus of a novel isoform of human iASPP is required for its cytoplasmic localization. Oncogene. 2004 Dec 2;23(56):9007-16. PMID:15489900 doi:https://dx.doi.org/1208088
- ↑ Yang JP, Hori M, Sanda T, Okamoto T. Identification of a novel inhibitor of nuclear factor-kappaB, RelA-associated inhibitor. J Biol Chem. 1999 May 28;274(22):15662-70. PMID:10336463
- ↑ Takada N, Sanda T, Okamoto H, Yang JP, Asamitsu K, Sarol L, Kimura G, Uranishi H, Tetsuka T, Okamoto T. RelA-associated inhibitor blocks transcription of human immunodeficiency virus type 1 by inhibiting NF-kappaB and Sp1 actions. J Virol. 2002 Aug;76(16):8019-30. PMID:12134007
- ↑ Bergamaschi D, Samuels Y, O'Neil NJ, Trigiante G, Crook T, Hsieh JK, O'Connor DJ, Zhong S, Campargue I, Tomlinson ML, Kuwabara PE, Lu X. iASPP oncoprotein is a key inhibitor of p53 conserved from worm to human. Nat Genet. 2003 Feb;33(2):162-7. Epub 2003 Jan 13. PMID:12524540 doi:https://dx.doi.org/10.1038/ng1070
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