High impact information on SGPP2

• We propose that SPP-1 and SPP-2 are factors that participate in the recognition of 5' splice sites [1].
• Together, these results indicate that the chromatin-bound B-subunit in association with origin recognition complex mediates recruiting Polalpha-primase complex onto replication origins in G1 pre-Start through an interaction with primase Spp2/p58 subunit [2].
• Identification and characterization of a novel human sphingosine-1-phosphate phosphohydrolase, hSPP2 [3].
• In this study we have identified a second human S1P phosphohydrolase, SPP2, based on sequence homology to human SPP1 [3].
• Immunofluorescence microscopic analysis demonstrated that SPP2 is localized to the endoplasmic reticulum [3].

Anatomical context of SGPP2

• Complexes containing both polypeptides also contained U1 snRNPs, suggesting that SPP-1 and SPP-2 are a part of the functional spliceosome [1].
• While the SGPP-1 and SGPP-3 transcripts were most abundant in fat body from crowd-reared males, corresponding to significantly higher levels than in isolated-reared males, the SGPP-2 transcript was detected most abundantly in brain from crowd-reared male locusts [4].
• Furthermore, SGPP-2 transcript levels in brain, testes, fat body, and accessory glands from crowd-reared males significantly exceeded the levels in solitary locusts [4].

Associations of SGPP2 with chemical compounds

• SPP2 exhibited high phosphohydrolase activity against S1P and dihydrosphingosine 1-phosphate [3].
• The dihydrosphingosine-1-phosphate phosphohydrolase activity was efficiently inhibited by excess S1P but not by lysophosphatidic acid, phosphatidic acid, or glycerol 3-phosphate, indicating that SPP2 is highly specific to sphingoid base 1-phosphates [3].

References