BMP2K is an uncharacterized member of NAK family. Structural similarities of kinase domains (75% identical) and in vitro inhibition profiles categorized BMP2K as the closest homolog of AAK1. BMP2K was originally identified as a serine-threonine kinase regulating osteoblast differentiation whose gene product is sharply upregulated by BMP-2 stimulation. Later, various genetic and proteomic screens linked BMP2K to HIV entry, developmental dysplasia of the hip, myopia, leukemia, breast cancer metastasis and so on. Recent multivariate proteomic profiling approaches identified BMP2K as a component of purified CCV from HeLa cells. BMP2K can phosphorylate AP-2 in vitro and in vivo. Functional impairment of BMP2K impedes AP-2 phosphorylation leading to defects in clathrin-coated pit (CCP) morphology and cargo internalization. BMP2K engages AP-2 via its extended C-terminus and this interaction is important for its CCP localization and function (PMID: 34480404).