Spindlin family member 4 (SPIN4)

Spindlin family member 4 (SPIN4) is a nuclear protein belonging to the spindlin family, distinguished by containing three tandem Tudor-like domains that enable it to bind methylated lysine and arginine residues on histones, particularly H3K4me3 and H4K20me3[3][1][4]. SPIN4 operates primarily as an **epigenetic reader**, recognizing specific chromatin marks to mediate downstream gene regulation and cellular processes[1][3]. It is predominantly localized to chromatin and the nucleus[1][3]. Its best-defined biological roles include acting as a negative regulator of cell proliferation, promoting canonical Wnt/β-catenin signaling in certain contexts, and restraining somatic and organ growth, as demonstrated by the overgrowth phenotype seen in SPIN4 loss-of-function mutants in both human and mouse models[1]. SPIN4 does not appear to be a therapeutic target (e.g., receptor, enzyme, transporter) nor are there known drugs that act directly on SPIN4[3][1][4]. There is no current evidence for biomarker usage or specific safety concerns related to direct SPIN4 targeting. The mutant loss of SPIN4 is newly implicated in X-linked generalized overgrowth syndrome in humans, marking it as the first epigenetic reader gene implicated in such a disorder[1].

Other names

Spindlin-4FLJ44984TDRD28LJBSspindlin-4SPIN4