About   Help   FAQ
Gene Ontology Classifications
presenilin 2

Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Psen2. (This text reflects annotations as of Tuesday, May 26, 2015.) MGI curation of this mouse gene is considered complete, including annotations derived from the biomedical literature as of January 25, 2008. If you know of any additional information regarding this mouse gene please let us know. Please supply mouse gene symbol and a PubMed ID.
Summary from NCBI RefSeq

This gene encodes a member of the presenilin family. Presenilins are catalytic components of the multi-subunit gamma-secretase complex, which mediates critical cellular processes through cleavage of type I transmembrane proteins including Notch receptors and the amyloid precursor protein. The encoded protein contains eight transmembrane domains and is localized to the endoplasmic reticulum, where it may play a role in calcium homeostasis. Following assembly of the gamma-secretase complex, the encoded protein is cleaved into N- and C-terminal fragments and the activated complex is released from the endoplasmic reticulum. Inactivation of this gene results in impaired synaptic function in a mouse model for Alzheimer's disease. Alternatively spliced transcript variants have been observed for this gene. [provided by RefSeq, Apr 2011]
Summary text based on GO annotations supported by experimental evidence in mouse
Summary text based on GO annotations supported by experimental evidence in other organisms
Summary text based on GO annotations supported by structural data
Summary text for additional MGI annotations
  1. Annaert WG et al. (2001) Interaction with telencephalin and the amyloid precursor protein predicts a ring structure for presenilins. Neuron, 32:579-89. (PubMed:11719200)
  2. Apert C et al. (1998) Profiles of amyloid precursor and presenilin 2-like proteins are correlated during development of the mouse hypothalamus. J Neuroendocrinol, 10:101-9. (PubMed:9535056)
  3. Blanchard V et al. (1997) Immunohistochemical analysis of presenilin 2 expression in the mouse brain: distribution pattern and co-localization with presenilin 1 protein. Brain Res, 758:209-17. (PubMed:9203550)
  4. Chan SL et al. (2002) Presenilin-1 mutations sensitize neurons to DNA damage-induced death by a mechanism involving perturbed calcium homeostasis and activation of calpains and caspase-12. Neurobiol Dis, 11:2-19. (PubMed:12460542)
  5. Chen F et al. (2003) Presenilin 1 and presenilin 2 have differential effects on the stability and maturation of nicastrin in Mammalian brain. J Biol Chem, 278:19974-9. (PubMed:12646573)
  6. Dong S et al. (2007) Environment enrichment rescues the neurodegenerative phenotypes in presenilins-deficient mice. Eur J Neurosci, 26:101-12. (PubMed:17614943)
  7. Donoviel DB et al. (1999) Mice lacking both presenilin genes exhibit early embryonic patterning defects. Genes Dev, 13:2801-10. (PubMed:10557208)
  8. Ezratty EJ et al. (2011) A Role for the Primary Cilium in Notch Signaling and Epidermal Differentiation during Skin Development. Cell, 145:1129-41. (PubMed:21703454)
  9. Feng R et al. (2004) Forebrain degeneration and ventricle enlargement caused by double knockout of Alzheimer's presenilin-1 and presenilin-2. Proc Natl Acad Sci U S A, 101:8162-7. (PubMed:15148382)
  10. Ferjentsik Z et al. (2009) Notch is a critical component of the mouse somitogenesis oscillator and is essential for the formation of the somites. PLoS Genet, 5:e1000662. (PubMed:19779553)
  11. Gowrishankar K et al. (2004) Release of a membrane-bound death domain by {gamma}-secretase processing of the p75NTR homolog NRADD. J Cell Sci, 117:4099-4111. (PubMed:15280425)
  12. Haks MC et al. (1999) Cell-fate decisions in early T cell development: regulation by cytokine receptors and the pre-TCR. Semin Immunol, 11:23-37. (PubMed:9950750)
  13. Hebert SS et al. (2004) Coordinated and widespread expression of gamma-secretase in vivo: evidence for size and molecular heterogeneity. Neurobiol Dis, 17:260-72. (PubMed:15474363)
  14. Herreman A et al. (1999) Presenilin 2 deficiency causes a mild pulmonary phenotype and no changes in amyloid precursor protein processing but enhances the embryonic lethal phenotype of presenilin 1 deficiency. Proc Natl Acad Sci U S A, 96:11872-7. (PubMed:10518543)
  15. Kim JS et al. (2006) Presenilin-1 inhibits delta-catenin-induced cellular branching and promotes delta-catenin processing and turnover. Biochem Biophys Res Commun, 351:903-8. (PubMed:17097608)
  16. Lai MT et al. (2003) Presenilin-1 and presenilin-2 exhibit distinct yet overlapping gamma-secretase activities. J Biol Chem, 278:22475-81. (PubMed:12684521)
  17. Laky K et al. (2007) Presenilins regulate alphabeta T cell development by modulating TCR signaling. J Exp Med, 204:2115-29. (PubMed:17698590)
  18. Leem JY et al. (2002) Presenilin 1 is required for maturation and cell surface accumulation of nicastrin. J Biol Chem, 277:19236-40. (PubMed:11943765)
  19. Liu Q et al. (2007) Amyloid precursor protein regulates brain apolipoprotein E and cholesterol metabolism through lipoprotein receptor LRP1. Neuron, 56:66-78. (PubMed:17920016)
  20. Pan Y et al. (2004) gamma-secretase functions through Notch signaling to maintain skin appendages but is not required for their patterning or initial morphogenesis. Dev Cell, 7:731-43. (PubMed:15525534)
  21. Pan Y et al. (2005) Notch1 and 2 cooperate in limb ectoderm to receive an early Jagged2 signal regulating interdigital apoptosis. Dev Biol, 286:472-82. (PubMed:16169548)
  22. Qyang Y et al. (2004) Myeloproliferative disease in mice with reduced presenilin gene dosage: effect of gamma-secretase blockage. Biochemistry, 43:5352-9. (PubMed:15122901)
  23. Rocher-Ros V et al. (2010) Presenilin modulates EGFR signaling and cell transformation by regulating the ubiquitin ligase Fbw7. Oncogene, 29:2950-61. (PubMed:20208556)
  24. Saura CA et al. (2004) Loss of presenilin function causes impairments of memory and synaptic plasticity followed by age-dependent neurodegeneration. Neuron, 42:23-36. (PubMed:15066262)
  25. Sawamura N et al. (2000) Mutant presenilin 2 transgenic mice. A large increase in the levels of Abeta 42 is presumably associated with the low density membrane domain that contains decreased levels of blycerophospholipids and sphingomyelin. J Biol Chem, 275:27901-8. (PubMed:10846187)
  26. Suzuki Y et al. (2009) An alternative spliced mouse presenilin-2 mRNA encodes a novel gamma-secretase inhibitor. FEBS Lett, 583:1403-8. (PubMed:19376115)
  27. Takeda T et al. (2005) Presenilin 2 regulates the systolic function of heart by modulating Ca2+ signaling. FASEB J, 19:2069-71. (PubMed:16204356)
  28. Vetrivel KS et al. (2005) Spatial segregation of gamma-secretase and substrates in distinct membrane domains. J Biol Chem, 280:25892-900. (PubMed:15886206)
  29. Vito P et al. (1997) Generation of anti-apoptotic presenilin-2 polypeptides by alternative transcription, proteolysis, and caspase-3 cleavage. J Biol Chem, 272:28315-20. (PubMed:9353287)
  30. Vito P et al. (1996) Requirement of the familial Alzheimer's disease gene PS2 for apoptosis. Opposing effect of ALG-3. J Biol Chem, 271:31025-8. (PubMed:8940094)
  31. Zhang YW et al. (2007) Presenilin/{gamma}-secretase-dependent processing of beta-amyloid precursor protein regulates EGF receptor expression. Proc Natl Acad Sci U S A, 104:10613-8. (PubMed:17556541)

Go Annotations in Tabular Form (Text View) (GO Graph)

Filter Markers by: Category  Evidence Code 


Gene Ontology Evidence Code Abbreviations:

  EXP Inferred from experiment
  IAS Inferred from ancestral sequence
  IBA Inferred from biological aspect of ancestor
  IBD Inferred from biological aspect of descendant
  IC Inferred by curator
  IDA Inferred from direct assay
  IEA Inferred from electronic annotation
  IGI Inferred from genetic interaction
  IKR Inferred from key residues
  IMP Inferred from mutant phenotype
  IMR Inferred from missing residues
  IPI Inferred from physical interaction
  IRD Inferred from rapid divergence
  ISS Inferred from sequence or structural similarity
  ISO Inferred from sequence orthology
  ISA Inferred from sequence alignment
  ISM Inferred from sequence model
  NAS Non-traceable author statement
  ND No biological data available
  RCA Reviewed computational analysis
  TAS Traceable author statement


Contributing Projects:
Mouse Genome Database (MGD), Gene Expression Database (GXD), Mouse Tumor Biology (MTB), Gene Ontology (GO), MouseCyc
Citing These Resources
Funding Information
Warranty Disclaimer & Copyright Notice
Send questions and comments to User Support.
last database update
MGI 6.0
The Jackson Laboratory