SPPL2B

Signal peptide peptidase-like 2B, also known as SPPL2B, is a human gene.cite web | title = Entrez Gene: SPPL2B signal peptide peptidase-like 2B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=56928| accessdate = ]

PBB_Summary
section_title =
summary_text = This gene encodes a member of the GXGD family of aspartic proteases. The GXGD proteases are transmembrane proteins with two conserved catalytic motifs localized within the membrane-spanning regions. This enzyme localizes to endosomes, lysosomes, and the plasma membrane. It cleaves the transmembrane domain of tumor necrosis factor alpha to release the intracellular domain, which triggers cytokine expression in the innate and adaptive immunity pathways. Multiple transcript variants encoding different isoforms have been found for this gene.cite web | title = Entrez Gene: SPPL2B signal peptide peptidase-like 2B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=56928| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=
*cite journal | author=Nagase T, Kikuno R, Ishikawa K, "et al." |title=Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=7 |issue= 2 |pages= 143–50 |year= 2000 |pmid= 10819331 |doi=
*cite journal | author=Weihofen A, Binns K, Lemberg MK, "et al." |title=Identification of signal peptide peptidase, a presenilin-type aspartic protease. |journal=Science |volume=296 |issue= 5576 |pages= 2215–8 |year= 2002 |pmid= 12077416 |doi= 10.1126/science.1070925
*cite journal | author=Grigorenko AP, Moliaka YK, Korovaitseva GI, Rogaev EI |title=Novel class of polytopic proteins with domains associated with putative protease activity. |journal=Biochemistry Mosc. |volume=67 |issue= 7 |pages= 826–35 |year= 2003 |pmid= 12139484 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Grimwood J, Gordon LA, Olsen A, "et al." |title=The DNA sequence and biology of human chromosome 19. |journal=Nature |volume=428 |issue= 6982 |pages= 529–35 |year= 2004 |pmid= 15057824 |doi= 10.1038/nature02399
*cite journal | author=Friedmann E, Lemberg MK, Weihofen A, "et al." |title=Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins. |journal=J. Biol. Chem. |volume=279 |issue= 49 |pages= 50790–8 |year= 2005 |pmid= 15385547 |doi= 10.1074/jbc.M407898200
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Krawitz P, Haffner C, Fluhrer R, "et al." |title=Differential localization and identification of a critical aspartate suggest non-redundant proteolytic functions of the presenilin homologues SPPL2b and SPPL3. |journal=J. Biol. Chem. |volume=280 |issue= 47 |pages= 39515–23 |year= 2006 |pmid= 15998642 |doi= 10.1074/jbc.M501645200
*cite journal | author=Fluhrer R, Grammer G, Israel L, "et al." |title=A gamma-secretase-like intramembrane cleavage of TNFalpha by the GxGD aspartyl protease SPPL2b. |journal=Nat. Cell Biol. |volume=8 |issue= 8 |pages= 894–6 |year= 2006 |pmid= 16829951 |doi= 10.1038/ncb1450
*cite journal | author=Friedmann E, Hauben E, Maylandt K, "et al." |title=SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in activated dendritic cells to trigger IL-12 production. |journal=Nat. Cell Biol. |volume=8 |issue= 8 |pages= 843–8 |year= 2006 |pmid= 16829952 |doi= 10.1038/ncb1440

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