Biology:PPEF1
 Generic protein structure example |
Serine/threonine-protein phosphatase with EF-hands 1 is an enzyme that in humans is encoded by the PPEF1 gene.[1][2][3]
Function
This gene encodes a member of the serine/threonine protein phosphatase with EF-hand motif family. The protein contains a protein phosphatase catalytic domain, and at least two EF-hand calcium-binding motifs in its C terminus. Although its substrate(s) is unknown, the encoded protein has been suggested to play a role in specific sensory neuron function and/or development. This gene shares high sequence similarity with the Drosophila retinal degeneration C (rdgC) gene. Several alternatively spliced transcript variants, each encoding a distinct isoform, have been described.[3]
Interactions
PPEF1 has been shown to interact with Calmodulin 1.[4]
References
- ↑ "A novel human serine-threonine phosphatase related to the Drosophila retinal degeneration C (rdgC) gene is selectively expressed in sensory neurons of neural crest origin". Human Molecular Genetics 6 (7): 1137–45. Jul 1997. doi:10.1093/hmg/6.7.1137. PMID 9215685.
- ↑ "Identification and characterization of a conserved family of protein serine/threonine phosphatases homologous to Drosophila retinal degeneration C". Proceedings of the National Academy of Sciences of the United States of America 94 (21): 11639–44. Oct 1997. doi:10.1073/pnas.94.21.11639. PMID 9326663.
- ↑ 3.0 3.1 "Entrez Gene: PPEF1 protein phosphatase, EF-hand calcium binding domain 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5475.
- ↑ "Protein Ser/Thr phosphatases PPEF interact with calmodulin". Biochemical and Biophysical Research Communications 293 (3): 1047–52. May 2002. doi:10.1016/S0006-291X(02)00338-8. PMID 12051765.
Further reading
- "Effects of serine/threonine protein phosphatases on ion channels in excitable membranes". Physiological Reviews 80 (1): 173–210. Jan 2000. doi:10.1152/physrev.2000.80.1.173. PMID 10617768.
- "Molecular cloning, expression, and characterization of a novel human serine/threonine protein phosphatase, PP7, that is homologous to Drosophila retinal degeneration C gene product (rdgC)". The Journal of Biological Chemistry 273 (3): 1462–8. Jan 1998. doi:10.1074/jbc.273.3.1462. PMID 9430683.
- "Normal light response, photoreceptor integrity, and rhodopsin dephosphorylation in mice lacking both protein phosphatases with EF hands (PPEF-1 and PPEF-2)". Molecular and Cellular Biology 21 (24): 8605–14. Dec 2001. doi:10.1128/MCB.21.24.8605-8614.2001. PMID 11713293.
- "Protein Ser/Thr phosphatases PPEF interact with calmodulin". Biochemical and Biophysical Research Communications 293 (3): 1047–52. May 2002. doi:10.1016/S0006-291X(02)00338-8. PMID 12051765.
- "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology 21 (5): 566–9. May 2003. doi:10.1038/nbt810. PMID 12665801.
- "An unappreciated role for RNA surveillance". Genome Biology 5 (2): R8. 2005. doi:10.1186/gb-2004-5-2-r8. PMID 14759258.
- "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. Oct 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
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