中性粒细胞胞质因子1 (NCF1，也称为p47phox)是NADPH氧化酶(NOX2)复合物的一个组成部分，它由6个亚基组成(Groemping Y et al. 2003;El-Benna J et al. 2005)。其中两个亚基，p22phox和gp91phox，是完整的膜蛋白，并形成异二聚体黄细胞色素，构成酶的催化核心。氧化酶的其余成分驻留在胞质中，包括小的GTPase Rac，以及NCF4 (p40phox)、NCF1和NCF2 (p67phox)的复合物(Groemping Y et al. 2003;El-Benna J et al. 2005)。在静息状态下，NCF1 (p47phox)与p22phox的相互作用，以及由此产生的易位和NADPH氧化酶的激活，会被NCF1的自抑制构象所阻止(Groemping Y et al. 2003;Yuzawa S et al. 2004)。这被认为是由于NCF1的SH3结构域与c端自抑制区(AIR)(氨基酸292‐340)的分子内相互作用，以保持蛋白质的“锁定”(Groemping Y et al. 2003;El Benna J et al. 2016)。TNF-α或GM-CSF诱导的引物诱导NCF1在Ser345位点的磷酸化，激活脯氨酸异构酶PIN1, PIN1与NCF1结合诱导构象变化(Boussetta T et al. 2010)。 This process facilitates extensive phosphorylation of NCF1 by PKC on other sites and induces full opening of NCF1 (Boussetta T et al. 2010). Phosphorylation studies showed that p47phox is phosphorylated on serines located between Ser303 and Ser379 (El Benna J et al. 1994; 2009). Most of these sites correspond to PKC consensus phosphorylation sites, and PKCα, -β, -δ and -ζ were all shown to phosphorylate NCF1 (p47phox) in vitro or in human neutrophil‐like HL‐60 cells (Dang PM et al. 2001; Fontayne A et al. 2002; Belambri SA et al. 2018). In vitro studies also showed that phosphorylation of p47phox induced its binding to the proline rich region (PRR) of p22phox and enhanced the binding of NCF2 (p67phox) to gp91phox (Fontayne A et al. 2002; Dang PMC et al. 2002; Boussetta T et al. 2010).

Reactome事件描述了pkc介导的NCF1在Ser303, Ser304, Ser320, Ser328, Ser348上的磷酸化。然而，NCF1在多个位点上被PKCs磷酸化，位点的数量尚未确定。